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2.A.6 The Resistance-Nodulation-Cell Division (RND) Superfamily

Characterized members of the RND superfamily all probably catalyze substrate efflux via an H+ antiport mechanism.These proteins are found ubiquitously in bacteria, archaea and eukaryotes (see Nikaido 2018 for a review of RND transporters). They fall into ten recognized phylogenetic families, three primary phylogenetic families that are restricted largely to Gram-negative bacteria (families 1-3, see below), the SecDF family (family 4) that is represented in both Gram-negative and Gram-positive bacteria as well as archaea, the HAE2 family (family 5) that is restricted to Gram-positive bacteria, one very diverse eukaryotic family (family 6), one archaeal plus spirochete family (family 7) (Tseng et al., 1999), a recently identified family that includes a probable pigment exporter in Gram-negative bacteria (TC #2.A.6.8.1; Goel et al., 2002), Dispatched (family 9), an exporter of the amino terminal portion (19 kDa) of Hedgehog which has a C-terminal cholesterol covanlent linkage that may be recognized by Dispatched (Nikaido 2018), and the uncharacterized family 10 from Actinobacteria. For mechanistic considerations, see Murakami et al. 2020 and Simsir et al. 2020.  Additionally, the structural basis of substrate recognition of RND pumps and the molecular mechanisms underlying multidrug extrusion has been reviewed (Klenotic and Yu 2024).

Clustering patterns in the Gram-negative bacterial families of the RND superfamily correlate with substrate specificity with family 1 catalyzing export of heavy metals, family 2 catalyzing export of multiple drugs, cluster 3 probably catalyzing export of lipooligosaccharides concerned with plant nodulation for the purpose of symbiotic nitrogen fixation, cluster 4 corresponding to the SecDF proteins, and cluster 8 catalyzing pigment export. Within family 2, MdtABC, consisting of an MFP (TC #8.A.1) and two RND family proteins (MdtB [TC #2.A.6.2.12] and MdtC [TC #2.A.6.2.14]) may form a complex exhibiting broader specificity than either MdtAB or MdtAC (Baranova and Nikaido, 2002; Nagakubo et al., 2002). The ActII3 protein, one of the two partially characterized member of family 5, has been implicated in drug resistance. The MmpL7 protein, also of this family, catalyzes export of an outer membrane lipid, phthiocerol dimycocerosate (PDIM) in M. tuberculosis. The SecDF proteins (family 4) function as nonessential constituents of the IISP protein secretory system (TC #3.A.5). They seem to allow coupling of substrate protein translocation to the proton motive force by facilitating deinsertion of the SecA component of the IISP system, thus rendering this system partially ATP-independent.

Nies (2003) subdivied the HME-RND proteins (2.A.6.1) into subgroups according to substrate specificity.  HME1 (Zn2+, Co2+, Cd2+), HME2 (Co2+, Ni2+), HME3a (divalent cations), HME3b (monovalent cations) HME4 (Cu+ or Ag+) and HME5 (Ni2+).  Kim et al. (2011) have proposed two models for the extrusion of heavy metals (2.A.6.1) from the periplasm to the extracellular medium, the 'switch' and the 'funnel' mechanisms. The funnel model involves the shuttling of periplasmic substrate from the membrane fusion protein to the RND transporter and further on through the outer membrane factor to the extracellular space. Conversely, the switch model requires substrate binding to the membrane fusion protein, inducing a conformational change and creating an open-access state of the tripartite protein complex. They favor the switch mechanism.

Some or all of the eukaryotic proteins (family 6) may function in cholesterol/lipid/steroid hormone transport, reception, regulation or catalysis. One such protein complex includes the RND family disease protein, Niemann-Pick C1, which may function in the export of cholesterol and lipids from lysosomes in conjunction with a soluble lysosomal protein with cholesterol binding properties, NPC2 (TC #2.A.6.6.1; Sleat et al., 2004). The disorder is typified by inhibited egress of cholesterol and glycosphingolipids from endosomal and lysosomal compartments. In the majority of NPC patients, mutations in the NPC1 gene can be identified, but about 5% of patients show mutations in the NPC2 gene. Many different mutations can cause NPC disease, and multiple variants not associated with the disease are known in both genes. There is an NPC disease gene variation database (NPC-db; Non-transporter homologues possess the sterol recognition domain and do not exhibit the typical RND family internal duplication (see below). The functions of the archaeal and spirochete proteins of family 7 have not been investigated.

Water-soluble Niemann-Pick C2 (NPC2) and membrane-bound NPC1 are cholesterol-binding lysosomal proteins required for export of lipoprotein-derived cholesterol from lysosomes. The binding site in NPC1 is located in its N-terminal domain (NTD), which projects into the lysosomal lumen. Transfer of cholesterol from NPC2 to NPC1 requires three residues that form a patch on the surface of NPC2. Wang et al. (2010) previously identified a patch of residues on the surface of NPC1(NTD) that is required for transfer. They presented a model in which these two surface patches on NPC2 and NPC1(NTD) interact, thereby opening an entry pore on NPC1(NTD) and allowing cholesterol to transfer without passing through the water phase. They referred to this transfer as a hydrophobic handoff and hypothesized that this handoff is essential for cholesterol export from lysosomes (Wang et al., 2010).

Most of the RND superfamily transport systems consist of large polypeptide chains (700-1300 amino acyl residues long). These proteins possess a single transmembrane spanner (TMS) at their N-termini followed by a large extracytoplasmic domain, then six additional TMSs, a second large extracytoplasmic domain, and five final C-terminal TMSs. In the case of one system (NolGHI) the system may consist of three distinct polypeptide chains, and most of the SecDF homologues consist of two polypeptide chains. Most others probably consist of a single polypeptide chain. The first halves of RND family proteins are homologous to the second halves, and the proteins therefore probably arose as a result of an intragenic tandem duplication event that occurred in the primordial system prior to divergence of the family members. One protein homologue from Methanococcus jannaschii is of half size and has no internal duplication. It can be postulated to function as a homo- or heterodimer in the membrane. The same is true of the eukaryotic RND family homologues that do not appear to function in transport. Some of the eukaryotic proteins have hydrophilic C-terminal domains.

Crystal structures of the RND drug exporter of E. coli, AcrB (TC #2.A.6.2.2), have been solved at 3.5 Å and 2.8 Å resolution (Murakami et al., 2002, 2006). Three AcrB protomers are organized as a homotrimer in the shape of a jellyfish. Each protomer consists of a 50 Å thick transmembrane domain and a 70 Å headpiece, protruding from the external membrane surface. The top of the headpiece opens like a funnel, and this may be a site of interaction with the MFP, AcrA (TC #8.A.1.6.1) and the OMF, TolC (TC #1.B.17.1.1). A pore formed by the three α-helices connects the funnel with a central cavity at the bottom of the headpiece. The 12 TMSs in the membrane domain are visible. Substrates are presumably successively transported through the channels of AcrB and TolC (Murakami et al., 2002). An MFP such as MexF of P. aeruginosa facilitates proper assembly of the RND permease as well as stabilization of the OMF such as OprN (Maseda et al., 2002). Vestibules are part of substrate path in AcrB multidrug efflux transporter of Escherichia coli (Husain et al., 2011). Pagès et al. (2011) have described several classes of efflux pump inhibitors that counteract MDR.

The large external cavity is of 5000 cubic angstroms. Several different hydrophobic and amphipathic ligands can bind in different positions within the cavity simultaneously. Binding involves hydrophobic forces, aromatic (π) stacking and van der Waals interactions (Yu et al., 2003). Crystallographic studies of the asymmetric trimer of AcrB suggest that each protomer in the trimeric assembly goes through a cycle of conformational changes during drug export. The external large cleft in the periplasmic domain of AcrB appears to be closed in the crystal structure of one of the three protomers. Conformational changes, including the closure of the external cleft in the periplasmic domain, are apparently required for drug transport by AcrB (Takatsuka and Nikaido, 2007; Takatsuka et al., 2010).

Murakami et al. (2006) have described crystal structures of AcrB with and without substrates. The AcrB-drug complex consists of three protomers, each of which has a different conformation corresponding to one of the three functional states of the transport cycle. Bound substrate was found in the periplasmic domain of one of the three protomers. The voluminous binding pocket is aromatic and allows multi-site binding. The structures indicate that drugs are exported by a three-step functionally rotating mechanism in which substrates undergo ordered binding change. A crystal structure at 2.9 Å resolution of trimeric AcrB was reported by Seeger et al. (2006) and shows asymmetry of the monomers. This structure reveals three different monomer conformations representing consecutive states in a transport cycle. The structural data imply an alternating access mechanism and a novel peristaltic mode of drug transport by this type of transporter.

The RND members of families 1-3 function in conjunction with a 'membrane fusion protein' (MFP; TC #8.A.1) and an 'outer membrane factor' (OMF; TC #1.B.17) to effect efflux across both membranes of the Gram-negative bacterial cell envelope in a single energy-coupled step. They may also pump hydrophobic substances from the cytoplasmic membrane, and toxic hydrophilic substances (i.e., heavy metals) from the periplasm to the external medium. The large periplasmic domains of RND pumps are involved in substrate recognition and form a cavity that can accommodate multiple drugs simultaneously (Mao et al., 2002). A comprehensive review of the classes of efflux pump inhibitors from various sources, highlighting their structure-activity relationships, which can be useful for medicinal chemists in the pursuit of novel efflux pump inhibitors, has appeared (Durães et al. 2018). Pyridylpiperazine-based allosteric inhibitors of RND-type multidrug efflux pumps have been studied (Plé et al. 2022).

Symmons et al., 2009 showed that the adaptor termini assemble a beta-roll structure forming the final domain adjacent to the inner membrane. The completed structure enabled in vivo cross-linking to map intermolecular contacts between the adaptor AcrA and the transporter AcrB, defining a periplasmic interface between several transporter subdomains and the contiguous beta-roll, beta-barrel, and lipoyl domains of the adaptor. The flexible linear topology of the adaptor allowed a multidomain docking approach to model the transporter-adaptor complex, revealing that the adaptor docks to a transporter region of comparative stability distinct from those key to the proposed rotatory pump mechanism, putative drug-binding pockets, and the binding site of inhibitory DARPins. AcrA(3)-AcrB(3)-TolC(3) is a 610 KDa, 270-A-long efflux pump crossing the entire bacterial cell envelope (Symmons et al., 2009).

RND transporters such as AcrD of E. coli can capture drugs such as aminoglycosides, from the periplasm and maybe from the cytoplasm (Aires and Nikaido, 2005). The latter process has been referred to as periplasmic vacuuming where, in this case, AcrD is the periplasmic vacuum cleaner (Lomovskaya and Totrov, 2005). This allows Gram-negative bacteria to protect themselves against cell wall biosynthetic inhibitors (drugs) that act in the periplasm. It also explains why HAE1 family members are largely restricted to Gram-negative bacteria. They are rarely found in Gram-positive bacteria or archaea.

A novel member of the RND superfamily, very distantly related to other established members of the superfamily, was shown to be a pigment (xanthomonadin) exporter in Xanthomonas oryzae (Goel et al., 2002). This protein (TC #2.A.6.8.1) has close homologues in various species of Xanthomonas as well as Xylella, Ralstonia and E. coli (AAG58596). These proteins comprise the eighth recognized family in the RND superfamily.

Protein translocation across the bacterial membrane, mediated by the secretory translocon SecYEG and the SecA ATPase, is enhanced by the proton motive force and membrane-integrated SecDF, which associates with SecYEG. The role of SecDF has been shown to function in late stages of protein secretion and membrane protein biogenesis. Tsukazaki et al. (2011) determined the crystal structure of Thermus thermophilus SecDF TC# 2.A.6.4.3) at 3.3 Å resolution, revealing a pseudo-symmetrical, 12-helix transmembrane domain belonging to the RND superfamily and two major periplasmic domains, P1 and P4. Higher-resolution analysis of the periplasmic domains suggested that P1, which binds an unfolded protein, undergoes functionally important conformational changes. In vitro analyses identified an ATP-independent step of protein translocation that requires both SecDF and the proton motive force. Electrophysiological analyses revealed that SecDF conducts protons in a manner dependent on pH and the presence of an unfolded protein, with conserved Asp and Arg residues at the transmembrane interface between SecD and SecF playing essential roles in the movements of protons and preproteins. Therefore, Tsukazaki et al. (2011) proposed that SecDF functions as a membrane-integrated chaperone, powered by the proton motive force, to achieve ATP-independent protein translocation. Furukawa et al. 2018  reported the crystal structure of SecDF in a form named the super-membrane-facing form, demonstrating a beta-barrel architecture instead of the previously reported beta-sheet structure. A remote coupling model was proposed in which a structural change of the transmembrane region drives a functional, extracytoplasmic conformational transition.

AcrB actively exports a wide variety of noxious compounds using the proton-motive force for energy. AcrB adopts an asymmetric structure of three protomers with different conformations that are sequentially converted during drug export; these cyclic conformational changes during drug export are referred to as functional rotation. Using different protonation states for the titratable residues in the middle of the transmembrane domain, simulations revealed a correlation between the specific protonation states and the side-chain configurations. Changing the protonation state for Asp408 induced a spontaneous structural transition, which suggests that the proton translocation stoichiometry may be one proton per functional rotation cycle.  Simulations also demonstrate that alternating the protonation states in the transmembrane domain induces functional rotation in the porter domain, which is coupled to drug transport (Yamane et al. 2013).  A mechanism involving two remote alternating-access conformational cycles within each protomer, namely one for protons in the transmembrane region and another for drugs in the periplasmic domain, 50 A apart, has been proposed (Eicher et al. 2014). Each of these cycles entails two distinct types of collective motions of two structural repeats, coupled by flanking α-helices that project from the membrane. Cross-talk among protomers across the trimerization interface might lead to a more kinetically efficient efflux system.

The generalized transport reaction catalyzed by functionally characterized RND proteins is:

Substrates (in) + nH+ (out) → Substrates (out) + nH+ (in).

Substrates: (a) heavy metals, (e.g., Co2+, Zn2+, Cd2+, Ni2+, Cu+ and Ag+; family 1); (b) multiple drugs (e.g., tetracycline, chloramphenicol, fluoroquinolones, β-lactams, etc.; family 2); (c) lipooligosaccharides (nodulation factors; family 3); (d) unfolded proteins as for the SecDF-mediated translocation of substrate proteins (Family 4), (e) lipids and possibly antibiotic drugs in Gram positive bacteria (e.g., outer membrane mycolic acid-containing lipids in actinobacteria and  actinorhodin; family 5), (f) possibly sterols in eukaryotes (family 6), (g) fused pentacyclic ring compounds such a hopanoids in bacteria (family 7), (h) pigments (family 8), and (i) cholesterol-modified peptides such as 'hedgehog', a sterol sensor in animals (family 9).

References associated with 2.A.6 family:

and Rayasam GV. (2014). MmpL3 a potential new target for development of novel anti-tuberculosis drugs. Expert Opin Ther Targets. 18(3):247-56. 24325728
Abi-Mosleh, L., R.E. Infante, A. Radhakrishnan, J.L. Goldstein, and M.S. Brown. (2009). Cyclodextrin overcomes deficient lysosome-to-endoplasmic reticulum transport of cholesterol in Niemann-Pick type C cells. Proc. Natl. Acad. Sci. USA 106: 19316-19321. 19884502
Aires, J.R. and H. Nikaido. (2005). Aminoglycosides are captured from both periplasm and cytoplasm by the AcrD multidrug efflux transporter of Escherichia coli. J. Bacteriol. 187: 1923-1929. 15743938
Al-Marzooq, F., A. Ghazawi, L. Daoud, and S. Tariq. (2023). Boosting the Antibacterial Activity of Azithromycin on Multidrug-Resistant by Efflux Pump Inhibition Coupled with Outer Membrane Permeabilization Induced by Phenylalanine-Arginine β-Naphthylamide. Int J Mol Sci 24:. 37240007
Alonso, A. and J.L. Martínez. (2000). Cloning and characterization of SmeDEF, a novel multidrug efflux pump from Stenotrophomonas maltophilia. Antimicrob. Agents Chemother. 44: 3079-3086. 11036026
AlQumaizi, K.I., S. Kumar, R. Anwer, and S. Mustafa. (2022). Differential Gene Expression of Efflux Pumps and Porins in Clinical Isolates of MDR. Life (Basel) 12:. 35330171
Altmann, S.W., H.R. Davis, Jr., L.-J. Zhu, X. Yao, L.M. Hoos, G. Tetzloff, S.P.N. Iyer, M. Maguire, A. Golovko, M. Zeng, L. Wang, N. Murgolo, and M.P. Graziano. (2004). Niemann-Pick C1 like 1 protein is critical for intestinal cholesterol absorption. Science 303: 1201-1204. 14976318
Anderson, J., G. Walker, and J. Pu. (2022). BORC-ARL8-HOPS ensemble is required for lysosomal cholesterol egress through NPC2. Mol. Biol. Cell 33: ar81. 35653304
Ansell, T.B., R.A. Corey, L.V. Viti, M. Kinnebrew, R. Rohatgi, C. Siebold, and M.S.P. Sansom. (2023). The Energetics and Ion Coupling of Cholesterol Transport Through Patched1. bioRxiv. 36824746
Ardourel, M., N. Demont, F. Debellé, F. Maillet, F. de Billy, J.C. Promé, J. Dénarié, and G. Truchet. (1994). Rhizobium meliloti lipooligosaccharide nodulation factors: different structural requirements for bacterial entry into target root hair cells and induction of plant symbiotic developmental responses. Plant Cell 6: 1357-1374. 7994171
Avchalumov, Y., T. Kirschstein, J. Lukas, J. Luo, A. Wree, A. Rolfs, and R. Köhling. (2012). Increased excitability and compromised long-term potentiation in the neocortex of NPC1(-/-) mice. Brain Res 1444: 20-26. 22325094
Baev, N., G. Endre, G. Petrovics, Z. Banfalvi, and A. Kondorosi. (1991). Six nodulation genes of nod box locus 4 in Rhizobium meliloti are involved in nodulation signal production: nodM codes for D-glucosamine synthetase. Mol. Gen. Genet. 228: 113-124. 1909418
Bagai, I., W. Liu, C. Rensing, N.J. Blackburn, and M.M. McEvoy. (2007). Substrate-linked Conformational Change in the Periplasmic Component of a Cu(I)/Ag(I) Efflux System. J. Biol. Chem. 282(49): 35695-35702.
Bailo, R., A. Bhatt, and J.A. Aínsa. (2015). Lipid transport in Mycobacterium tuberculosis and its implications in virulence and drug development. Biochem Pharmacol 96: 159-167. 25986884
Baranova, N. and H. Nikaido. (2002). The BaeSR two-component regulatory system activates transcription of the yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and increases its resistance to novobiocin and deoxycholate. J. Bacteriol. 184: 4168-4176. 12107134
Begic, S., and E.A. Worobec (2008). The role of the Serratia marcescens SdeAB multidrug efflux pump and TolC homologue in fluoroquinolone resistance studied via gene-knockout mutagenesis. Microbiology 154: 454-61. 18227249
Belardinelli, J.M. and M. Jackson. (2017). Green Fluorescent Protein as a protein localization and topological reporter in mycobacteria. Tuberculosis (Edinb) 105: 13-17. 28610783
Belardinelli, J.M., A. Yazidi, L. Yang, L. Fabre, W. Li, B. Jacques, S.K. Angala, I. Rouiller, H.I. Zgurskaya, J. Sygusch, and M. Jackson. (2016). Structure-Function Profile of MmpL3, the Essential Mycolic Acid Transporter from Mycobacterium tuberculosis. ACS Infect Dis 2: 702-713. 27737557
Bergmiller, T., A.M.C. Andersson, K. Tomasek, E. Balleza, D.J. Kiviet, R. Hauschild, G. Tkačik, and C.C. Guet. (2017). Biased partitioning of the multidrug efflux pump AcrAB-TolC underlies long-lived phenotypic heterogeneity. Science 356: 311-315. 28428424
Bernut, A., A. Viljoen, C. Dupont, G. Sapriel, M. Blaise, C. Bouchier, R. Brosch, C. de Chastellier, J.L. Herrmann, and L. Kremer. (2016). Insights into the smooth-to-rough transitioning in Mycobacterium bolletii unravels a functional Tyr residue conserved in all mycobacterial MmpL family members. Mol. Microbiol. 99: 866-883. 26585558
Betters JL. and Yu L. (2010). NPC1L1 and cholesterol transport. FEBS Lett. 584(13):2740-7. 20307540
Bialek-Davenet, S., J.P. Lavigne, K. Guyot, N. Mayer, R. Tournebize, S. Brisse, V. Leflon-Guibout, and M.H. Nicolas-Chanoine. (2015). Differential contribution of AcrAB and OqxAB efflux pumps to multidrug resistance and virulence in Klebsiella pneumoniae. J Antimicrob Chemother 70: 81-88. 25193085
Bina, X.R., C.L. Lavine, M.A. Miller, and J.E. Bina. (2008). The AcrAB RND efflux system from the live vaccine strain of Francisella tularensis is a multiple drug efflux system that is required for virulence in mice. FEMS Microbiol. Lett. 279: 226-233. 18179581
Bina, X.R., D. Provenzano, N. Nguyen, and J.E. Bina. (2008). Vibrio cholerae RND family efflux systems are required for antimicrobial resistance, optimal virulence factor production, and colonization of the infant mouse small intestine. Infect. Immun. 76: 3595-3605. 18490456
Bolaños, J., A. Betanzos, R. Javier-Reyna, G. García-Rivera, M. Huerta, J. Pais-Morales, A. González-Robles, M.A. Rodríguez, M. Schnoor, and E. Orozco. (2016). EhNPC1 and EhNPC2 Proteins Participate in Trafficking of Exogenous Cholesterol in Entamoeba histolytica Trophozoites: Relevance for Phagocytosis. PLoS Pathog 12: e1006089. 28002502
Bolhuis, A., C.P. Broekhuizen, A. Sorokin, M.L. van Roosmalen, G. Venema, S. Bron, W.J. Quax, and J.M. van Dijl. (1998). SecDF of Bacillus subtilis, a molecular siamese twin required for the efficient secretion of proteins. J. Biol. Chem. 273: 21217-21224. 9694879
Bradwell, K.R., V.N. Koparde, A.V. Matveyev, M.G. Serrano, J.M.P. Alves, H. Parikh, B. Huang, V. Lee, O. Espinosa-Alvarez, P.A. Ortiz, A.G. Costa-Martins, M.M.G. Teixeira, and G.A. Buck. (2018). Genomic comparison of Trypanosoma conorhini and Trypanosoma rangeli to Trypanosoma cruzi strains of high and low virulence. BMC Genomics 19: 770. 30355302
Briffotaux, J., W. Huang, X. Wang, and B. Gicquel. (2017). MmpS5/MmpL5 as an efflux pump in Mycobacterium species. Tuberculosis (Edinb) 107: 13-19. 29050760
Brown, D.G., J.K. Swanson, and C. Allen. (2007). Two host-induced Ralstonia solanacearum genes, acrA and dinF, encode multidrug efflux pumps and contribute to bacterial wilt virulence. Appl. Environ. Microbiol. 73: 2777-2786. 17337552
Bunikis, I., K. Denker, Y. Ostberg, C. Andersen, R. Benz, and S. Bergström. (2008). An RND-type efflux system in Borrelia burgdorferi is involved in virulence and resistance to antimicrobial compounds. PLoS Pathog 4: e1000009. 18389081
Carbone, J., N.J. Paradis, L. Bennet, M.C. Alesiani, K.R. Hausman, and C. Wu. (2023). Inhibition Mechanism of Anti-TB Drug SQ109: Allosteric Inhibition of TMM Translocation of Mycobacterium Tuberculosis MmpL3 Transporter. J Chem Inf Model 63: 5356-5374. 37589273
Carstea, E.D., J.A. Morris, K.G. Coleman, S.K. Loftus, D. Zhang, C. Cummings, J. Gu, M.A. Rosenfeld, W.J. Pavan, D.B. Krizman et al. (1997). Niemann-Pick C1 disease gene: homology to mediators of cholesterol homeostasis. Science 277: 228-231. 9211849
Castellano, B.M., A.M. Thelen, O. Moldavski, M. Feltes, R.E. van der Welle, L. Mydock-McGrane, X. Jiang, R.J. van Eijkeren, O.B. Davis, S.M. Louie, R.M. Perera, D.F. Covey, D.K. Nomura, D.S. Ory, and R. Zoncu. (2017). Lysosomal cholesterol activates mTORC1 via an SLC38A9-Niemann-Pick C1 signaling complex. Science 355: 1306-1311. 28336668
Chacon KN., Mealman TD., McEvoy MM. and Blackburn NJ. (2014). Tracking metal ions through a Cu/Ag efflux pump assigns the functional roles of the periplasmic proteins. Proc Natl Acad Sci U S A. 111(43):15373-8. 25313055
Chacón, K.N., J. Perkins, Z. Mathe, K. Alwan, E.N. Ho, M.N. Ucisik, K.M. Merz, and N.J. Blackburn. (2018). Trapping intermediates in metal transfer reactions of the CusCBAF export pump of. Commun Biol 1: 192. 30456313
Chan, Y.Y. and K.L. Chua. (2005). The Burkholderia pseudomallei BpeAB-OprB efflux pump: expression and impact on quorum sensing and virulence. J. Bacteriol. 187: 4707-4719. 15995185
Chan, Y.Y., H.S. Bian, T.M. Tan, M.E. Mattmann, G.D. Geske, J. Igarashi, T. Hatano, H. Suga, H.E. Blackwell, and K.L. Chua. (2007). Control of quorum sensing by a Burkholderia pseudomallei multidrug efflux pump. J. Bacteriol. 189: 4320-4324. 17384185
Chan, Y.Y., T.M. Tan, Y.M. Ong, and K.L. Chua. (2004). BpeAB-OprB, a multidrug efflux pump in Burkholderia pseudomallei. Antimicrob. Agents Chemother. 48: 1128-1135. 15047512
Chau, S.L., Y.W. Chu, and E.T. Houang. (2004). Novel resistance-nodulation-cell division efflux system AdeDE in Acinetobacter genomic DNA group 3. Antimicrob. Agents Chemother. 48: 4054-4055. 15388479
Chen, C.H., C.C. Huang, T.C. Chung, R.M. Hu, Y.W. Huang, and T.C. Yang. (2011). Contribution of resistance-nodulation-division efflux pump operon smeU1-V-W-U2-X to multidrug resistance of Stenotrophomonas maltophilia. Antimicrob. Agents Chemother. 55: 5826-5833. 21930878
Chen, H., Y. Liu, and X. Li. (2020). Structure of human Dispatched-1 provides insights into Hedgehog ligand biogenesis. Life Sci Alliance 3:. 32646883
Chen, K., X. Zhang, H. Peng, F. Huang, G. Sun, Q. Xu, L. Liao, Z. Xing, Y. Zhong, Z. Fang, M. Liao, S. Luo, W. Chen, and M. Dong. (2023). Exploring the diagnostic value, prognostic value, and biological functions of NPC gene family members in hepatocellular carcinoma based on a multi-omics analysis. Funct Integr Genomics 23: 264. 37541978
Chitsaz, M., V. Gupta, B. Harris, M.L. O''Mara, and M.H. Brown. (2021). A Unique Sequence Is Essential for Efficient Multidrug Efflux Function of the MtrD Protein of. mBio 12: e0167521. 34465021
Cho, H.H., J.Y. Sung, K.C. Kwon, and S.H. Koo. (2012). Expression of Sme efflux pumps and multilocus sequence typing in clinical isolates of Stenotrophomonas maltophilia. Ann Lab Med 32: 38-43. 22259777
Chuanchuen, R., C.T. Narasaki, and H.P. Schweizer. (2002). The MexJK efflux pump of Pseudomonas aeruginosa requires OprM for antibiotic efflux but not for efflux of triclosan. J. Bacteriol. 184: 5036-5044. 12193619
Cohen, J.D., C.E. Cadena Del Castillo, N.D. Serra, A. Kaech, A. Spang, and M.V. Sundaram. (2021). The Caenorhabditis elegans Patched domain protein PTR-4 is required for proper organization of the precuticular apical extracellular matrix. Genetics 219:. 34740248
Conroy O., Kim EH., McEvoy MM. and Rensing C. (2010). Differing ability to transport nonmetal substrates by two RND-type metal exporters. FEMS Microbiol Lett. 308(2):115-22. 20497225
Cox, J.S., B. Chen, M. McNeil, and W.R. Jacobs Jr. (1999). Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice. Nature 402: 79-83. 10573420
Coyne, S., N. Rosenfeld, T. Lambert, P. Courvalin, and B. Périchon. (2010). Overexpression of resistance-nodulation-cell division pump AdeFGH confers multidrug resistance in Acinetobacter baumannii. Antimicrob. Agents Chemother. 54: 4389-4393. 20696879
Damier-Piolle, L., S. Magnet, S. Brémont, T. Lambert, and P. Courvalin (2008). AdeIJK, a resistance-nodulation-cell division pump effluxing multiple antibiotics in Acinetobacter baumannii. Antimicrob. Agents Chemother. 52: 557-562. 18086852
Davies, J.P., C. Scott, K. Oishi, A. Liapis, and Y.A. Ioannou. (2005). Inactivation of NPC1L1 causes multiple lipid transport defects and protects against diet-induced hypercholesterolemia. J. Biol. Chem. 280: 12710-12720. 15671032
De Angelis, F., J.K. Lee, J.D. O'Connell, 3rd, L.J. Miercke, K.H. Verschueren, V. Srinivasan, C. Bauvois, C. Govaerts, R.A. Robbins, J.M. Ruysschaert, R.M. Stroud, and G. Vandenbussche. (2010). Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems. Proc. Natl. Acad. Sci. USA 107: 11038-11043. 20534468
Delmar, J.A., C.C. Su, and E.W. Yu. (2013). Structural mechanisms of heavy-metal extrusion by the Cus efflux system. Biometals 26: 593-607. 23657864
Delmar, J.A., C.C. Su, and E.W. Yu. (2014). Bacterial multidrug efflux transporters. Annu Rev Biophys 43: 93-117. 24702006
Deshayes, C., H. Bach, D. Euphrasie, R. Attarian, M. Coureuil, W. Sougakoff, F. Laval, Y. Av-Gay, M. Daffé, G. Etienne, and J.M. Reyrat. (2010). MmpS4 promotes glycopeptidolipids biosynthesis and export in Mycobacterium smegmatis. Mol. Microbiol. 78: 989-1003. 21062372
Dinh, D., I.T. Paulsen, and M.H. Saier, Jr. (1994). A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of Gram-negative bacteria. J. Bacteriol. 176: 3825-3831. 8021163
Dixit, S.S., D.E. Sleat, A.M. Stock, and P. Lobel. (2007). Do mammalian NPC1 and NPC2 play a role in intestinal cholesterol absorption? Biochem. J. 408: 1-5. 17880278
Dofini Magnini, R., F. Pedinielli, J. Vergalli, N. Ouedraogo, S. Remy, A. Hilou, J.M. Brunel, J.M. Pagès, and A. Davin-Regli. (2023). Budmunchiamines as a Potential Adjuvant for Rejuvenating Phenicol Activities towards -Resistant Strains. Int J Mol Sci 24:. 37240134
Domenech, P., M.B. Reed, C.S. Dowd, C. Manca, G. Kaplan, and C.E. Barry, III. (2004). The role of MmpL8 in sulfatide biogenesis and virulence of Mycobacterium tuberculosis. J. Biol. Chem. 279: 21257-21265. 15001577
Doughty, D.M., M.L. Coleman, R.C. Hunter, A.L. Sessions, R.E. Summons, and D.K. Newman. (2011). The RND-family transporter, HpnN, is required for hopanoid localization to the outer membrane of Rhodopseudomonas palustris TIE-1. Proc. Natl. Acad. Sci. USA 108: E1045-1051. 21873238
Du, D., J. Voss, Z. Wang, W. Chiu, and B.F. Luisi. (2015). The pseudo-atomic structure of an RND-type tripartite multidrug efflux pump. Biol Chem 396: 1073-1082. 25803077
Du, D., Z. Wang, W. Chiu, and B.F. Luisi. (2018). Purification of AcrAB-TolC Multidrug Efflux Pump for Cryo-EM Analysis. Methods Mol Biol 1700: 71-81. 29177826
Dubey, V., B. Bozorg, D. Wüstner, and H. Khandelia. (2020). Cholesterol binding to the sterol-sensing region of Niemann Pick C1 protein confines dynamics of its N-terminal domain. PLoS Comput Biol 16: e1007554. 33021976
Dunlop, M.J., Z.Y. Dossani, H.L. Szmidt, H.C. Chu, T.S. Lee, J.D. Keasling, M.Z. Hadi, and A. Mukhopadhyay. (2011). Engineering microbial biofuel tolerance and export using efflux pumps. Mol Syst Biol 7: 487. 21556065
Echizen, Y., T. Tsukazaki, N. Dohmae, R. Ishitani, and O. Nureki. (2011). Crystallization and preliminary X-ray diffraction of the first periplasmic domain of SecDF, a translocon-associated membrane protein, from Thermus thermophilus. Acta Crystallogr Sect F Struct Biol Cryst Commun 67: 1367-1370. 22102233
Eicher, T., M.A. Seeger, C. Anselmi, W. Zhou, L. Brandstätter, F. Verrey, K. Diederichs, J.D. Faraldo-Gómez, and K.M. Pos. (2014). Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump AcrB. Elife 3:. 25248080
Elghobashi-Meinhardt, N. (2019). Computational Tools Unravel Putative Sterol Binding Sites in the Lysosomal NPC1 Protein. J Chem Inf Model. [Epub: Ahead of Print] 30942586
Elghobashi-Meinhardt, N. (2020). Cholesterol Transport in Wild-Type NPC1 and P691S: Molecular Dynamics Simulations Reveal Changes in Dynamical Behavior. Int J Mol Sci 21:. 32331453
Elkins, C.A. and L.B. Mullis. (2006). Mammalian steroid hormones are substrates for the major RND- and MFS-type tripartite multidrug efflux pumps of Escherichia coli. J. Bacteriol. 188: 1191-1195. 16428427
Evans, K., L. Passador, R. Srikumar, E. Tsang, J. Nezezon, and K. Poole. (1998). Influence of the MexAB-OprM multidrug efflux system on quorum sensing in Pseudomonas aeruginosa. J. Bacteriol. 180: 5443-5447. 9765578
Fairweather, S.J., V. Gupta, M. Chitsaz, L. Booth, M.H. Brown, and M.L. O''Mara. (2021). Coordination of Substrate Binding and Protonation in the MtrD Efflux Pump Controls the Functionally Rotating Transport Mechanism. ACS Infect Dis 7: 1833-1847. 33980014
Fernandez-Morena, M.A., J.L. Caballero, D.A. Hopwood, and F. Malpartida. (1991). The act cluster contains regulatory and antibiotic export genes, direct targets for translational control by the bldA tRNA gene of Streptomyces. Cell 66: 769-780. 1878971
Fernando, D.M., W. Xu, P.C. Loewen, G.G. Zhanel, and A. Kumar. (2014). Triclosan can select for an AdeIJK-overexpressing mutant of Acinetobacter baumannii ATCC 17978 that displays reduced susceptibility to multiple antibiotics. Antimicrob. Agents Chemother. 58: 6424-6431. 25136007
Ferrada, E. and G. Superti-Furga. (2022). A structure and evolutionary-based classification of solute carriers. iScience 25: 105096. 36164651
Ficici, E., D. Jeong, and I. Andricioaei. (2017). Electric-Field-Induced Protein Translocation via a Conformational Transition in SecDF: An MD Study. Biophys. J. 112: 2520-2528. 28636909
Fleet, A.J. and P.A. Hamel. (2018). Protein-specific activities of the transmembrane modules of Ptch1 and Ptch2 are determined by their adjacent protein domains. J. Biol. Chem. [Epub: Ahead of Print] 30166346
Franke, S., G. Grass, and D.H. Nies. (2001). The product of the ybdE gene of the Escherichia coli chromosome is involved in detoxification of silver ions. Microbiology 147: 965-972. 11283292
Franke, S., G. Grass, and D.H. Nies. (2003). Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli. J. Bacteriol. 185: 3804-3812. 12813074
Furukawa, A., S. Nakayama, K. Yoshikaie, Y. Tanaka, and T. Tsukazaki. (2018). Remote Coupled Drastic β-Barrel to β-Sheet Transition of the Protein Translocation Motor. Structure 26: 485-489.e2. 29398525
Ge, L., J. Wang, W. Qi, H.H. Miao, J. Cao, Y.X. Qu, B.L. Li, and B.L. Song. (2008). The cholesterol absorption inhibitor ezetimibe acts by blocking the sterol-induced internalization of NPC1L1. Cell Metab 7: 508-519. 18522832
Goel, A.K., L. Rajagopal, N. Nagesh, and R.V. Sonti. (2002). Genetic locus encoding functions involved in biosynthesis and outer membrane localization of xanthomonadin in Xanthomonas oryzae pv. oryzae. J. Bacteriol. 184: 3539-3548. 12057948
Goldberg, M., T. Pribyl, S. Juhnke, and D. Nies. (1999). Energetics and topology of CzcA, a cation/proton antiporter of the resistance-nodulation-cell division protein family. J. Biol. Chem. 274: 26065-26070. 10473554
Gong, X., H. Qian, X. Zhou, J. Wu, T. Wan, P. Cao, W. Huang, X. Zhao, X. Wang, P. Wang, Y. Shi, G.F. Gao, Q. Zhou, and N. Yan. (2016). Structural Insights into the Niemann-Pick C1 (NPC1)-Mediated Cholesterol Transfer and Ebola Infection. Cell 165: 1467-1478. 27238017
Gould VC., Okazaki A. and Avison MB. (2013). Coordinate hyperproduction of SmeZ and SmeJK efflux pumps extends drug resistance in Stenotrophomonas maltophilia. Antimicrob Agents Chemother. 57(1):655-7. 23147729
Gould, V.C. and M.B. Avison. (2006). SmeDEF-mediated antimicrobial drug resistance in Stenotrophomonas maltophilia clinical isolates having defined phylogenetic relationships. J Antimicrob Chemother 57: 1070-1076. 16597633
Grass, G. and C. Rensing. (2001). Genes involved in copper homeostasis in Escherichia coli. J. Bacteriol. 183: 2145-2147. 11222619
Grass, G., C. Grosse, and D.H. Nies. (2000). Regulation of the cnr cobalt and nickel resistance determinant from Ralstonia sp. strain CH34. J. Bacteriol. 182: 1390-1398. 10671463
Gregson, B.H., G. Metodieva, M.V. Metodiev, P.N. Golyshin, and B.A. McKew. (2018). Differential Protein Expression During Growth on Medium Versus Long-Chain Alkanes in the Obligate Marine Hydrocarbon-Degrading Bacterium MIL-1. Front Microbiol 9: 3130. 30619200
Gristwood, T., M.B. McNeil, J.S. Clulow, G.P. Salmond, and P.C. Fineran. (2011). PigS and PigP regulate prodigiosin biosynthesis in Serratia via differential control of divergent operons, which include predicted transporters of sulfur-containing molecules. J. Bacteriol. 193: 1076-1085. 21183667
Guan, L., M. Ehrmann, H. Yoneyama, and T. Nakae. (1999). Membrane topology of the xenobiotic-exporting subunit, MexB, of the MexA,B-OprM extrusion pump in Pseudomonas aeruginosa. J. Biol. Chem. 274: 10517-10522. 10187844
Gupta, A., K. Matsui, J.-F. Lo, and S. Silver. (1999). Molecular basis for resistance to silver cations in Salmonella. Nature Med. 5: 183-188. 9930866
Gupta, K.R., C.M. Gwin, K.C. Rahlwes, K.J. Biegas, C. Wang, J.H. Park, J. Liu, B.M. Swarts, Y.S. Morita, and E.H. Rego. (2022). An essential periplasmic protein coordinates lipid trafficking and is required for asymmetric polar growth in mycobacteria. Elife 11:. [Epub: Ahead of Print] 36346214
H. Runz, D. Dolle, A.M. Schlitter, and J. Zschocke. (2008). NPC-db, a Niemann-Pick type C disease gene variation database. Hum. Mutat. 29: 345-350. 18081003
Hagman, K.E., C.E. Lucas, J.T. Balthazar, L. Snyder, M. Nilles, R.C. Judd, and W.M. Shafer. (1997). The MtrD protein of Neisseria gonorrhoeae is a member of the resistance/nodulation/division protein family constituting part of an efflux system. Microbiology 143: 2117-2125. 9245801
Hassan, K.A., A.J. Brzoska, N.L. Wilson, B.A. Eijkelkamp, M.H. Brown, and I.T. Paulsen. (2011). Roles of DHA2 family transporters in drug resistance and iron homeostasis in Acinetobacter spp. J. Mol. Microbiol. Biotechnol. 20: 116-124. 21430390
Hassan, M.T., D. van der Lelie, D. Springael, U. Römling, N. Ahmed, and M. Mergeay. (1999). Identification of a gene cluster, czr, involved in cadmium and zinc resistance in Pseudomonas aeruginosa. Gene 238: 417-425. 10570969
He, F., Y. Fu, Q. Chen, Z. Ruan, X. Hua, H. Zhou, and Y. Yu. (2015). Tigecycline susceptibility and the role of efflux pumps in tigecycline resistance in KPC-producing Klebsiella pneumoniae. PLoS One 10: e0119064. 25734903
Hearn, E.M., J.J. Dennis, M.R. Gray, and J.M. Foght. (2003). Identification and characterization of the emhABC efflux system for polycyclic aromatic hydrocarbons in Pseudomonas fluorescens cLP6a. J. Bacteriol. 185: 6233-6240. 14563857
Hearn, E.M., M.R. Gray, and J.M. Foght. (2006). Mutations in the central cavity and periplasmic domain affect efflux activity of the resistance-nodulation-division pump EmhB from Pseudomonas fluorescens cLP6a. J. Bacteriol. 188: 115-123. 16352827
Hernando-Amado, S., P. Laborda, and J.L. Martínez. (2023). Tackling antibiotic resistance by inducing transient and robust collateral sensitivity. Nat Commun 14: 1723. 36997518
Higgins, C.F. (2007). Multiple molecular mechanisms for multidrug resistance transporters. Nature 446: 749-757. 17429392
Hobbs, E.C., X. Yin, B.J. Paul, J.L. Astarita, and G. Storz. (2012). Conserved small protein associates with the multidrug efflux pump AcrB and differentially affects antibiotic resistance. Proc. Natl. Acad. Sci. USA 109: 16696-16701. 23010927
Hu, T., X. Yang, F. Liu, S. Sun, Z. Xiong, J. Liang, X. Yang, H. Wang, X. Yang, L.W. Guddat, H. Yang, Z. Rao, and B. Zhang. (2022). Structure-based design of anti-mycobacterial drug leads that target the mycolic acid transporter MmpL3. Structure. [Epub: Ahead of Print] 35981536
Hua, X., A. Nohturfft, J.L. Goldstein, and M.S. Brown. (1996). Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein. Cell 87: 415-426. 8898195
Huang, Y.Q., G.R. Huang, M.H. Wu, H.Y. Tang, Z.S. Huang, X.H. Zhou, W.Q. Yu, J.W. Su, X.Q. Mo, B.P. Chen, L.J. Zhao, X.F. Huang, H.Y. Wei, and L.D. Wei. (2015). Inhibitory effects of emodin, baicalin, schizandrin and berberine on hefA gene: treatment of Helicobacter pylori-induced multidrug resistance. World J Gastroenterol 21: 4225-4231. 25892872
Hughes, I., M. Saito, P.H. Schlesinger, and D.M. Ornitz. (2007). Otopetrin 1 activation by purinergic nucleotides regulates intracellular calcium. Proc. Natl. Acad. Sci. USA 104: 12023-12028. 17606897
Husain F., Bikhchandani M. and Nikaido H. (2011). Vestibules are part of the substrate path in the multidrug efflux transporter AcrB of Escherichia coli. J Bacteriol. 193(20):5847-9. 21856849
Husain, F. and H. Nikaido. (2010). Substrate path in the AcrB multidrug efflux pump of Escherichia coli. Mol. Microbiol. 78: 320-330. 20804453
Igarashi, M., T. Hirokawa, Y. Takadate, and A. Takada. (2021). Structural Insights into the Interaction of Filovirus Glycoproteins with the Endosomal Receptor Niemann-Pick C1: A Computational Study. Viruses 13:. 34069246
Infante, R.E., A. Radhakrishnan, L. Abi-Mosleh, L.N. Kinch, M.L. Wang, N.V. Grishin, J.L. Goldstein, and M.S. Brown. (2008). Purified NPC1 protein: II. Localization of sterol binding to a 240-amino acid soluble luminal loop. J. Biol. Chem. 283: 1064-1075. 17989072
Infante, R.E., L. Abi-Mosleh, A. Radhakrishnan, J.D. Dale, M.S. Brown, and J.L. Goldstein. (2008). Purified NPC1 protein. I. Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein. J. Biol. Chem. 283: 1052-1063. 17989073
Janganan, T.K., L. Zhang, V.N. Bavro, D. Matak-Vinkovic, N.P. Barrera, M.F. Burton, P.G. Steel, C.V. Robinson, M.I. Borges-Walmsley, and A.R. Walmsley. (2011). Opening of the outer membrane protein channel in tripartite efflux pumps is induced by interaction with the membrane fusion partner. J. Biol. Chem. 286: 5484-5493. 21115481
Jeannot, K., M.L. Sobel, F. El Garch, K. Poole, and P. Plesiat. (2005). Induction of the MexXY efflux pump in Pseudomonas aeruginosa is dependent on drug-ribosome interaction. J Bacteriol. 187: 5341-5346. 16030228
Jesin, J.A., T.A. Stone, C.J. Mitchell, E. Reading, and C.M. Deber. (2020). Peptide-Based Approach to Inhibition of the Multidrug Resistance Efflux Pump AcrB. Biochemistry 59: 3973-3981. 33026802
Jewel, Y., Q. Van Dinh, J. Liu, and P. Dutta. (2020). Substrate-dependent transport mechanism in AcrB of multidrug resistant bacteria. Proteins 88: 853-864. 31998988
Jia L., Betters JL. and Yu L. (2011). Niemann-pick C1-like 1 (NPC1L1) protein in intestinal and hepatic cholesterol transport. Annu Rev Physiol. 73:239-59. 20809793
Kamal, N., C. Rouquette-Loughlin, and W.M. Shafer. (2007). The TolC-Like Protein of Neisseria Meningitidis Is Required for Extracellular Production of the Repeats-in-Toxin Toxin FrpC but Not for Resistance to Antimicrobials Recognized by the Mtr Efflux Pump System. Infect. Immun. 75(12):6008-6012. 17923520
Kang, H. and D.C. Gross. (2005). Characterization of a resistance-nodulation-cell division transporter system associated with the syr-syp genomic island of Pseudomonas syringae pv. syringae. Appl. Environ. Microbiol. 71: 5056-5065. 16151087
Kapoor, V. and D. Wendell. (2013). Engineering bacterial efflux pumps for solar-powered bioremediation of surface waters. Nano Lett 13: 2189-2193. 23581993
Ke, X.X., H. Chao, M.N. Abbas, S. Kausar, I. Gul, H. Ji, L. Yang, and H. Cui. (2020). Niemann-Pick type C1 regulates cholesterol transport and metamorphosis in silkworm, Bombyx mori (Dazao). Int J Biol Macromol 152: 525-534. 32112844
Kennedy, B.E., C.T. Madreiter, N. Vishnu, R. Malli, W.F. Graier, and B. Karten. (2014). Adaptations of energy metabolism associated with increased levels of mitochondrial cholesterol in Niemann-Pick type C1-deficient cells. J. Biol. Chem. 289: 16278-16289. 24790103
Khan, M.T., T.A. Khan, I. Ahmad, S. Muhammad, and D.Q. Wei. (2022). Diversity and novel mutations in membrane transporters of Mycobacterium tuberculosis. Brief Funct Genomics. [Epub: Ahead of Print] 35868449
Khanam, S., M. Guragain, D.L. Lenaburg, R. Kubat, and M.A. Patrauchan. (2017). Calcium induces tobramycin resistance in Pseudomonas aeruginosa by regulating RND efflux pumps. Cell Calcium 61: 32-43. 28034459
Kieboom, J. and J.A.M. de Bont. (2001). Identification and molecular characterization of an efflux system involved in Pseudomonas putida S12 multidrug resistance. Microbiology 147: 43-51. 11160799
Kieboom, J., J.J. Dennis, J.A. de Bont, and G.J. Zylstra. (1998). Identification and molecular characterization of an efflux pump involved in Pseudomonas putida S12 solvent tolerance. J. Biol. Chem. 273: 85-91. 9417051
Kim, E.H., D.H. Nies, M.M. McEvoy, and C. Rensing. (2011). Switch or funnel: how RND-type transport systems control periplasmic metal homeostasis. J. Bacteriol. 193: 2381-2387. 21398536
Kim, H.S. and H. Nikaido. (2012). Different functions of MdtB and MdtC subunits in the heterotrimeric efflux transporter MdtB(2)C complex of Escherichia coli. Biochemistry 51: 4188-4197. 22559837
Kim, H.S., D. Nagore, and H. Nikaido. (2010). Multidrug Efflux Pump MdtBC of Escherichia coli Is Active Only as a B2C Heterotrimer. J. Bacteriol. 192: 1377-1386. 20038594
Kim, J., J.G. Kim, Y. Kang, J.Y. Jang, G.J. Jog, J.Y. Lim, S. Kim, H. Suga, T. Nagamatsu, and I. Hwang. (2004). Quorum sensing and the LysR-type transcriptional activator ToxR regulate toxoflavin biosynthesis and transport in Burkholderia glumae. Mol. Microbiol. 54: 921-934. 15522077
Kim, J.S., H. Jeong, S. Song, H.Y. Kim, K. Lee, J. Hyun, and N.C. Ha. (2015). Structure of the tripartite multidrug efflux pump AcrAB-TolC suggests an alternative assembly mode. Mol. Cells 38: 180-186. 26013259
Kinnebrew, M., G. Luchetti, R. Sircar, S. Frigui, L.V. Viti, T. Naito, F. Beckert, Y. Saheki, C. Siebold, A. Radhakrishnan, and R. Rohatgi. (2021). Patched 1 reduces the accessibility of cholesterol in the outer leaflet of membranes. Elife 10:. [Epub: Ahead of Print] 34698632
Kinnebrew, M., K.A. Johnson, A. Radhakrishnan, and R. Rohatgi. (2022). Measuring and Manipulating Membrane Cholesterol for the Study of Hedgehog Signaling. Methods Mol Biol 2374: 73-87. 34562244
Klenotic, P.A. and E.W. Yu. (2024). Structural analysis of resistance-nodulation cell division transporters. Microbiol. Mol. Biol. Rev. e0019823. [Epub: Ahead of Print] 38551344
Kober, D.L., A. Radhakrishnan, J.L. Goldstein, M.S. Brown, L.D. Clark, X.C. Bai, and D.M. Rosenbaum. (2021). Scap structures highlight key role for rotation of intertwined luminal loops in cholesterol sensing. Cell. [Epub: Ahead of Print] 34139175
Kohler, T., Michea-Hamzehpour, M., Henze, U., Gotoh, N., Curty, L.K., and Pechere, J.C. (1997). Characterization of MexE-MexF-OprN, a positively regulated multidrug efflux system of Pseudomonas aeruginosa. Mol. Microbiol. 23: 345-354. 9044268
Kui, X., D. Qiu, W. Wang, N. Li, P. Tong, X. Sun, L. Jin, W. Deng, J. Dai, and C. Lu. (2021). Molecular cloning and characterization of NPC1L1 in the Chinese tree shrew (Tupaia belangeri chinensis). Mol Biol Rep 48: 7975-7984. 34716864
Kumar, N., C.C. Su, T.H. Chou, A. Radhakrishnan, J.A. Delmar, K.R. Rajashankar, and E.W. Yu. (2017). Crystal structures of the hopanoid transporter HpnN. Proc. Natl. Acad. Sci. USA 114: 6557-6562. 28584102
Lau, S.Y. and H.I. Zgurskaya. (2005). Cell division defects in Escherichia coli deficient in the multidrug efflux transporter AcrEF-TolC. J. Bacteriol. 187: 7815-7825. 16267305
Leedjärv, A., A. Ivask, and M. Virta. (2008). Interplay of different transporters in the mediation of divalent heavy metal resistance in Pseudomonas putida KT2440. J. Bacteriol. 190: 2680-2689. 18065533
Lei, H.T., T.H. Chou, C.C. Su, J.R. Bolla, N. Kumar, A. Radhakrishnan, F. Long, J.A. Delmar, S.V. Do, K.R. Rajashankar, W.M. Shafer, and E.W. Yu. (2014). Crystal structure of the open state of the Neisseria gonorrhoeae MtrE outer membrane channel. PLoS One 9: e97475. 24901251
Li W., Upadhyay A., Fontes FL., North EJ., Wang Y., Crans DC., Grzegorzewicz AE., Jones V., Franzblau SG., Lee RE., Crick DC. and Jackson M. (2014). Novel insights into the mechanism of inhibition of MmpL3, a target of multiple pharmacophores in Mycobacterium tuberculosis. Antimicrob Agents Chemother. 58(11):6413-23. 25136022
Li, R., Y. Han, Y. Zhou, Z. Du, H. Wu, J. Wang, and Y. Chen. (2016). Tigecycline Susceptibility and Molecular Resistance Mechanisms Among Clinical Klebsiella pneumoniae Strains Isolated During Non-Tigecycline Treatment. Microb Drug Resist. [Epub: Ahead of Print] 27219271
Li, W., C.M. Stevens, A.N. Pandya, Z. Darzynkiewicz, P. Bhattarai, W. Tong, M. Gonzalez-Juarrero, E.J. North, H.I. Zgurskaya, and M. Jackson. (2019). Direct Inhibition of MmpL3 by Novel Antitubercular Compounds. ACS Infect Dis. [Epub: Ahead of Print] 30882198
Li, X., H. Yang, D. Zhang, X. Li, H. Yu, and Z. Shen. (2015). Overexpression of specific proton motive force-dependent transporters facilitate the export of surfactin in Bacillus subtilis. J Ind Microbiol Biotechnol 42: 93-103. 25366377
Li, X., J. Wang, E. Coutavas, H. Shi, Q. Hao, and G. Blobel. (2016). Structure of human Niemann-Pick C1 protein. Proc. Natl. Acad. Sci. USA. [Epub: Ahead of Print] 27307437
Li, X., S. Eda, and T. Nakae. (2006). Organic solvent-selective domain of the resistance-nodulation-division-type xenobiotic-antibiotic transporters of Pseudomonas aeruginosa. Microbiol Immunol 50: 53-56. 16428873
Li, Y., A. Acharya, L. Yang, J. Liu, E. Tajkhorshid, H.I. Zgurskaya, M. Jackson, and J.C. Gumbart. (2023). Insights into substrate transport and water permeation in the mycobacterial transporter MmpL3. Biophys. J. [Epub: Ahead of Print] 36926696
Li, Y., T. Mima, Y. Komori, Y. Morita, T. Kuroda, T. Mizushima, and T. Tsuchiya. (2003). A new member of the tripartite multidrug efflux pumps, MexVW-OprM, in Pseudomonas aeruginosa. J Antimicrob Chemother 52: 572-575. 12951344
Lin, J., C. Cagliero, B. Guo, Y.-W. Barton, M.-C. Maurel, S. Payot, and Q. Zhang. (2005). Bile salts modulate expression of the CmeABC multidrug efflux pump in Campylobacter jejuni. J. Bacteriol. 187: 7417-7424. 16237025
Liscum, L. (2007). A role for NPC1 and NPC2 in intestinal cholesterol absorption--the hypothesis gutted. Biochem. J. 408: 1-5.
Liu, R., P. Lu, J.W. Chu, and F.J. Sharom. (2009). Characterization of fluorescent sterol binding to purified human NPC1. J. Biol. Chem. 284: 1840-1852. 19029290
Liu, Z.Q., P.Y. Zheng, and P.C. Yang. (2008). Efflux pump gene hefA of Helicobacter pylori plays an important role in multidrug resistance. World J Gastroenterol 14: 5217-5222. 18777600
Loftus, S.K., J.A. Morris, E.D. Carstea, J.Z. Gu, C. Cummings, A. Brown, J. Ellison, K. Ohno, M.A. Rosenfeld, D.A. Tagle et al. (1997). Murine model of Niemann-Pick C disease: mutation in a cholesterol homeostasis gene. Science 277: 232-235. 9211850
Lomovskaya, O. and M. Totrov. (2005). Vacuuming the periplasm. J. Bacteriol. 187: 1879-1883. 15743933
Long, F., C.C. Su, M.T. Zimmermann, S.E. Boyken, K.R. Rajashankar, R.L. Jernigan, and E.W. Yu. (2010). Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport. Nature 467: 484-488. 20865003
Long, T., X. Qi, A. Hassan, Q. Liang, J.K. De Brabander, and X. Li. (2020). Structural basis for itraconazole-mediated NPC1 inhibition. Nat Commun 11: 152. 31919352
Long, T., Y. Liu, Y. Qin, R.A. DeBose-Boyd, and X. Li. (2021). Structures of dimeric human NPC1L1 provide insight into mechanisms for cholesterol absorption. Sci Adv 7:. 34407950
Lorusso, A.B., J.A. Carrara, C.D.N. Barroso, F.F. Tuon, and H. Faoro. (2022). Role of Efflux Pumps on Antimicrobial Resistance in. Int J Mol Sci 23:. 36555423
Luo, Y., G. Wan, X. Zhang, X. Zhou, Q. Wang, J. Fan, H. Cai, L. Ma, H. Wu, Q. Qu, Y. Cong, Y. Zhao, and D. Li. (2021). Cryo-EM study of patched in lipid nanodisc suggests a structural basis for its clustering in caveolae. Structure. [Epub: Ahead of Print] 34174188
Ma, Y., A. Erkner, R. Gong, S. Yao, J. Taipale, K. Basler, and P.A. Beachy. (2002) Hedgehog-mediated patterning of the mammalian embryo requires transporter-like function of dispatched. Cell 111: 63-75. 12372301
Malathi, K., K. Higaki, A.H. Tinkelenberg, D.A. Balderes, D. Almanzar-Paramio, L.J. Wilcox, N. Erdeniz, F. Redican, M. Padamsee, Y. Liu, S. Khan, F. Alcantara, E.D. Carstea, J.A. Morris, and S.L. Sturley. (2004). Mutagenesis of the putative sterol-sensing domain of yeast Niemann Pick C-related protein reveals a primordial role in subcellular sphingolipid distribution. J. Cell Biol. 164: 547-556. 14970192
Malwal, S.R. and E. Oldfield. (2021). Mycobacterial membrane protein Large 3-like-family proteins in bacteria, protozoa, fungi, plants, and animals: A bioinformatics and structural investigation. Proteins. [Epub: Ahead of Print] 34739144
Mao, W., M.S. Warren, D.S. Black, T. Satou, T. Murata, T. Nishino, N. Gotoh, and O. Lomovskaya. (2002). On the mechanism of substrate specificity by resistance nodulation division (RND)-type multidrug resistance pumps: the large periplasmic loops of MexD from Pseudomonas aeruginosa are involved in substrate recognition. Mol. Microbiol. 46: 889-901. 12410844
Martínez-Archundia, M., T.G. Hernández Mojica, J. Correa-Basurto, S. Montaño, and A. Camacho-Molina. (2020). Molecular dynamics simulations reveal structural differences among wild-type NPC1 protein and its mutant forms. J Biomol Struct Dyn 38: 3527-3532. 31506030
Martins, T.S., R.S. Costa, R. Vilaça, C. Lemos, V. Teixeira, C. Pereira, and V. Costa. (2023). Iron Limitation Restores Autophagy and Increases Lifespan in the Yeast Model of Niemann-Pick Type C1. Int J Mol Sci 24:. 37047194
Maseda, H., M. Kitao, S. Eda, E. Yoshihara, and T. Nakae. (2002). A novel assembly process of the multicomponent xenobiotic efflux pump in Pseudomonas aeruginosa. Mol. Microbiol. 46: 677-686. 12410825
Masi, M., J.M. Pages, C. Villard, and E. Pradel. (2005). The eefABC multidrug efflux pump operon is repressed by H-NS in Enterobacter aerogenes. J. Bacteriol. 187: 3894-3897. 15901719
Masi, M., N. Saint, G. Molle, and J.M. Pagès. (2007). The Enterobacter aerogenes outer membrane efflux proteins TolC and EefC have different channel properties. Biochim. Biophys. Acta. 1768: 2559-2567. 17658457
Matsunaga, Y., T. Yamane, T. Terada, K. Moritsugu, H. Fujisaki, S. Murakami, M. Ikeguchi, and A. Kidera. (2018). Energetics and conformational pathways of functional rotation in the multidrug transporter AcrB. Elife 7:. 29506651
Matsuo, T., K. Hayashi, Y. Morita, M. Koterasawa, W. Ogawa, T. Mizushima, T. Tsuchiya, and T. Kuroda. (2007). VmeAB, an RND-type multidrug efflux transporter in Vibrio parahaemolyticus. Microbiology. 153:4129-4137. 18048926
Matsuo, T., K. Nakamura, T. Kodama, T. Mikami, H. Hiyoshi, T. Tsuchiya, W. Ogawa, and T. Kuroda. (2013). Characterization of all RND-type multidrug efflux transporters in Vibrio parahaemolyticus. Microbiologyopen 2: 725-742. 23894076
Mehrabadi, J.F., M. Sirous, N.E. Daryani, S. Eshraghi, B. Akbari, and M.H. Shirazi. (2011). Assessing the role of the RND efflux pump in metronidazole resistance of Helicobacter pylori by RT-PCR assay. J Infect Dev Ctries 5: 88-93. 21389587
Middlemiss, J.K. and K. Poole. (2004). Differential impact of MexB mutations on substrate selectivity of the MexAB-OprM multidrug efflux pump of Pseudomonas aeruginosa. J. Bacteriol. 186: 1258-1269. 14973037
Mima, T., N. Kohira, Y. Li, H. Sekiya, W. Ogawa, T. Kuroda, and T. Tsuchiya. (2009). Gene cloning and characteristics of the RND-type multidrug efflux pump MuxABC-OpmB possessing two RND components in Pseudomonas aeruginosa. Microbiology 155: 3509-3517. 19713238
Mima, T., S. Joshi, M. Gomez-Escalada, and H.P. Schweizer. (2007). Identification and characterization of TriABC-OpmH, a triclosan efflux pump of Pseudomonas aeruginosa requiring two membrane fusion proteins. J. Bacteriol. 189: 7600-7609. 17720796
Mio, K., T. Tsukazaki, H. Mori, M. Kawata, T. Moriya, Y. Sasaki, R. Ishitani, K. Ito, O. Nureki, and C. Sato. (2014). Conformational variation of the translocon enhancing chaperone SecDF. J Struct Funct Genomics 15: 107-115. 24368747
Moolla, N., R. Bailo, R. Marshall, V.N. Bavro, and A. Bhatt. (2021). Structure-function analysis of MmpL7-mediated lipid transport in mycobacteria. Cell Surf 7: 100062. 34522829
Moore, R.A., D. DeShazer, S. Reckseidler, A. Weissman, and D.E. Woods. (1999). Efflux-mediated aminoglycoside and macrolide resistance in Burkholderia pseudomallei. Antimicrob. Agents Chemother. 43: 465-470. 10049252
Moraleda-Muñoz, A., J. Pérez, A.L. Extremera, and J. Muñoz-Dorado. (2010). Differential regulation of six heavy metal efflux systems in the response of Myxococcus xanthus to copper. Appl. Environ. Microbiol. 76: 6069-6076. 20562277
Morgan, C.E., P. Glaza, I.V. Leus, A. Trinh, C.C. Su, M. Cui, H.I. Zgurskaya, and E.W. Yu. (2021). Cryoelectron Microscopy Structures of AdeB Illuminate Mechanisms of Simultaneous Binding and Exporting of Substrates. mBio 12:. 33622726
Murakami, S., R. Nakashima, E. Yamashita, and A. Yamaguchi. (2002). Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419: 587-593. 12374972
Murakami, S., R. Nakashima, E. Yamashita, T. Matsumoto, and A. Yamaguchi. (2006). Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature 443: 173-179. 16915237
Murakami, S., U. Okada, and H.W. van Veen. (2020). Tripartite transporters as mechano-transmitters in periplasmic alternating-access mechanisms. FEBS Lett. [Epub: Ahead of Print] 32936941
Musalkova, D., F. Majer, L. Kuchar, O. Luksan, B. Asfaw, H. Vlaskova, G. Storkanova, M. Reboun, H. Poupetova, H. Jahnova, H. Hulkova, J. Ledvinova, L. Dvorakova, J. Sikora, M. Jirsa, M.T. Vanier, and M. Hrebicek. (2020). Transcript, protein, metabolite and cellular studies in skin fibroblasts demonstrate variable pathogenic impacts of NPC1 mutations. Orphanet J Rare Dis 15: 85. 32248828
Myers, B.R., L. Neahring, Y. Zhang, K.J. Roberts, and P.A. Beachy. (2017). Rapid, direct activity assays for Smoothened reveal Hedgehog pathway regulation by membrane cholesterol and extracellular sodium. Proc. Natl. Acad. Sci. USA. [Epub: Ahead of Print] 29229834
Nagakubo, S., K. Nishino, T. Hirata, and A. Yamaguchi. (2002). The putative response regulator BaeR stimulates multidrug resistance of Escherichia coli via a novel multidrug exporter system, MdtABC. J. Bacteriol. 184: 4161-4167. 12107133
Nagano, K. and H. Nikaido. (2009). Kinetic behavior of the major multidrug efflux pump AcrB of Escherichia coli. Proc. Natl. Acad. Sci. USA 106: 5854-5858. 19307562
Nakano, Y., H.R. Kim, A. Kawakami, S. Roy, A.F. Schier, and P.W. Ingham. (2004). Inactivation of dispatched 1 by the chameleon mutation disrupts Hedgehog signalling in the zebrafish embryo. Biol. 269: 381-92. 15110707
Nakase, Y., A. Hamada, N. Kitamura, T. Hata, S. Toratani, T. Yamamoto, and T. Okamoto. (2020). Novel PTCH1 mutations in Japanese familial nevoid basal cell carcinoma syndrome. Hum Genome Var 7: 38. 33298892
Naseer, N., J.A. Shapiro, and M. Chander. (2014). RNA-Seq analysis reveals a six-gene SoxR regulon in Streptomyces coelicolor. PLoS One 9: e106181. 25162599
Nehme D., Poole K. (2007). Assembly of the MexAB-OprM multidrug pump of Pseudomonas aeruginosa: component interactions defined by the study of pump mutant suppressors. J Bacteriol. 189: 6118-6127. 17586626
Nielsen, L.E., E.C. Snesrud, F. Onmus-Leone, Y.I. Kwak, R. Avilés, E.D. Steele, D.E. Sutter, P.E. Waterman, and E.P. Lesho. (2014). IS5 element integration, a novel mechanism for rapid in vivo emergence of tigecycline nonsusceptibility in Klebsiella pneumoniae. Antimicrob. Agents Chemother. 58: 6151-6156. 25092708
Nies, D.H. (2003). Efflux-mediated heavy metal resistance in prokaryotes. FEMS Microbiol. Rev. 27: 313-339. 12829273
Nihei, W., M. Nagafuku, H. Hayamizu, Y. Odagiri, Y. Tamura, Y. Kikuchi, L. Veillon, H. Kanoh, K.I. Inamori, K. Arai, K. Kabayama, K. Fukase, and J.I. Inokuchi. (2018). NPC1L1-dependent intestinal cholesterol absorption requires ganglioside GM3 in membrane microdomains. J Lipid Res 59: 2181-2187. 30242108
Nikaido, H. (2018). RND transporters in the living world. Res. Microbiol. [Epub: Ahead of Print] 29577985
Nikaido, H. and Y. Takatsuka. (2009). Mechanisms of RND multidrug efflux pumps. Biochim. Biophys. Acta. 1794: 769-781. 19026770
Nishino, K. and A. Yamaguchi. (2001). Analysis of a complete library of putative drug transporter genes in Escherichia coli. J. Bacteriol. 183: 5803-5812. 11566977
Nishino,K., E. Nikaido, and A. Yamaguchi. (2007). Regulation of Multidrug Efflux Systems Involved in Multidrug and Metal Resistance of Salmonella enterica Serovar Typhimurium. J. Bacteriol. 189: 9066-9075. 17933888
Nishiyama, K., A. Fukuda, K. Morita, and H. Tokuda. (1999). Membrane deinsertion of SecA underlying proton motive force-dependent stimulation of protein translocation. EMBO J. 18: 1049-1058. 10022846
Nolivos, S., J. Cayron, A. Dedieu, A. Page, F. Delolme, and C. Lesterlin. (2019). Role of AcrAB-TolC multidrug efflux pump in drug-resistance acquisition by plasmid transfer. Science 364: 778-782. 31123134
Ohene-Agyei, T., J.D. Lea, and H. Venter. (2012). Mutations in MexB that affect the efflux of antibiotics with cytoplasmic targets. FEMS Microbiol. Lett. 333: 20-27. 22568688
Ohgami, N., D.C. Ko, M. Thomas, M.P. Scott, C.C. Chang, and T.Y. Chang. (2004). Binding between the Niemann-Pick C1 protein and a photoactivatable cholesterol analog requires a functional sterol-sensing domain. Proc. Natl. Acad. Sci. USA 101: 12473-12478. 15314240
Olshvang, E., S. Fritsch, O.C. Scholtyssek, I.J. Schalk, and N. Metzler-Nolte. (2023). Vectorization via Siderophores Increases Antibacterial Activity of K(RW) Peptides against Pseudomonas aeruginosa. Chemistry e202300364. [Epub: Ahead of Print] 37541431
Oswald, C., H.K. Tam, and K.M. Pos. (2016). Transport of lipophilic carboxylates is mediated by transmembrane helix 2 in multidrug transporter AcrB. Nat Commun 7: 13819. 27982032
Ouled Amar Bencheikh, B., K. Senkevich, U. Rudakou, E. Yu, K. Mufti, J.A. Ruskey, F. Asayesh, S.B. Laurent, D. Spiegelman, S. Fahn, C. Waters, O. Monchi, Y. Dauvilliers, A.J. Espay, N. Dupré, L. Greenbaum, S. Hassin-Baer, G.A. Rouleau, R.N. Alcalay, E.A. Fon, and Z. Gan-Or. (2020). Variants in the Niemann-Pick type C gene NPC1 are not associated with Parkinson''s disease. Neurobiol Aging 93: 143.e1-143.e4. 32371106
Owens, C.P., N. Chim, and C.W. Goulding. (2013). Insights on how the Mycobacterium tuberculosis heme uptake pathway can be used as a drug target. Future Med Chem 5: 1391-1403. 23919550
Padilla-Benavides, T., A.M. George Thompson, M.M. McEvoy, and J.M. Argüello. (2014). Mechanism of ATPase-mediated Cu+ Export and Delivery to Periplasmic Chaperones: THE INTERACTION OF ESCHERICHIA COLI CopA AND CusF. J. Biol. Chem. 289: 20492-20501. 24917681
Pagès, J.M., L. Amaral, and S. Fanning. (2011). An original deal for new molecule: reversal of efflux pump activity, a rational strategy to combat gram-negative resistant bacteria. Curr. Med. Chem. 18: 2969-2980. 21651484
Pak, J.E., E.N. Ekendé, E.G. Kifle, J.D. O'Connell, 3rd, F. De Angelis, M.B. Tessema, K.M. Derfoufi, Y. Robles-Colmenares, R.A. Robbins, E. Goormaghtigh, G. Vandenbussche, and R.M. Stroud. (2013). Structures of intermediate transport states of ZneA, a Zn(II)/proton antiporter. Proc. Natl. Acad. Sci. USA 110: 18484-18489. 24173033
Pal, R., S. Hameed, and Z. Fatima. (2018). Altered drug efflux under iron deprivation unveils abrogated MmpL3 driven mycolic acid transport and fluidity in mycobacteria. Biometals. [Epub: Ahead of Print] 30430296
Palumbo, J.D., C.I. Kado, and D.A. Phillips. (1998). An isoflavonoid-inducible efflux pump in Agrobacterium tumefaciens is involved in competitive colonization of roots. J. Bacteriol. 180: 3107-3113. 9620959
Pamp, S.J., M. Gjermansen, H.K. Johansen, and T. Tolker-Nielsen. (2008). Tolerance to the antimicrobial peptide colistin in Pseudomonas aeruginosa biofilms is linked to metabolically active cells, and depends on the pmr and mexAB-oprM genes. Mol. Microbiol. 68: 223-240. 18312276
Pantel, L., P. Juarez, M. Serri, L. Boucinha, E. Lessoud, A. Lanois, A. Givaudan, E. Racine, and M. Gualtieri. (2021). Missense Mutations in the CrrB Protein Mediate Odilorhabdin Derivative Resistance in. Antimicrob. Agents Chemother. [Epub: Ahead of Print] 33685902
Papadopoulos, C.J., C.F. Carson, B.J. Chang, and T.V. Riley. (2008). Role of the MexAB-OprM efflux pump of Pseudomonas aeruginosa in tolerance to tea tree (Melaleuca alternifolia) oil and its monoterpene components terpinen-4-ol, 1,8-cineole, and α-terpineol. Appl. Environ. Microbiol. 74(6): 1932-1935. 18192403
Pasca, M.R., P. Guglierame, E. De Rossi, F. Zara, and G. Riccardi. (2005). mmpL7 gene of Mycobacterium tuberculosis is responsible for isoniazid efflux in Mycobacterium smegmatis. Antimicrob. Agents Chemother. 49: 4775-4777. 16251328
Paulsen, I.T., M.H. Brown, and R.A. Skurray. (1996). Proton-dependent multidrug efflux pumps. Microbiol. Rev. 60: 575-608. 8987357
Peake KB. and Vance JE. (2010). Defective cholesterol trafficking in Niemann-Pick C-deficient cells. FEBS Lett. 584(13):2731-9. 20416299
Pearson, J.P., C. van Delden, and B.H. Iglewski. (1999). Active efflux and diffusion are involved in transport of Pseudomonas aeruginosa cell-to-cell signals. J. Bacteriol. 181: 1203-1210. 9973347
Peleg, A.Y., J. Adams, and D.L. Paterson. (2007). Tigecycline Efflux as a Mechanism for Nonsusceptibility in Acinetobacter baumannii. Antimicrob. Agents Chemother. 51: 2065-2069. 17420217
Petrova, A., Y. Feodorova, T. Miteva-Katrandzhieva, M. Petrov, and M. Murdjeva. (2019). First detected OXA-50 carbapenem-resistant clinical isolates from Bulgaria and interplay between the expression of main efflux pumps, OprD and intrinsic AmpC. J. Med. Microbiol. 68: 1723-1731. 31746726
Petukh, M. and I.B. Zhulin. (2018). Comparative study of the effect of disease causing and benign mutations in position Q92 on cholesterol binding by the NPC1 n-terminal domain. Proteins 86: 1165-1175. 30183109
Pfrieger, F.W. (2023). The Niemann-Pick type diseases - A synopsis of inborn errors in sphingolipid and cholesterol metabolism. Prog Lipid Res 101225. [Epub: Ahead of Print] 37003582
Pirillo, A., A.L. Catapano, and G.D. Norata. (2016). Niemann-Pick C1-Like 1 (NPC1L1) Inhibition and Cardiovascular Diseases. Curr. Med. Chem. 23: 983-999. 26923679
Plé, C., H.K. Tam, A. Vieira Da Cruz, N. Compagne, J.C. Jiménez-Castellanos, R.T. Müller, E. Pradel, W.E. Foong, G. Malloci, A. Ballée, M.A. Kirchner, P. Moshfegh, A. Herledan, A. Herrmann, B. Deprez, N. Willand, A.V. Vargiu, K.M. Pos, M. Flipo, and R.C. Hartkoorn. (2022). Pyridylpiperazine-based allosteric inhibitors of RND-type multidrug efflux pumps. Nat Commun 13: 115. 35013254
Pletzer, D. and H. Weingart. (2014). Characterization of AcrD, a resistance-nodulation-cell division-type multidrug efflux pump from the fire blight pathogen Erwinia amylovora. BMC Microbiol 14: 13. 24443882
Pontel, L.B., M.E. Audero, M. Espariz, S.K. Checa, and F.C. Soncini. (2007). GolS controls the response to gold by the hierarchical induction of Salmonella-specific genes that include a CBA efflux-coding operon. Mol. Microbiol. 66: 814-825. 17919284
Poole, K.  (2008).   Bacterial multidrug efflux pumps serve other functions.  Microbe 3: 179-185. 
Pos, K.M. (2009). Drug transport mechanism of the AcrB efflux pump. Biochim. Biophys. Acta. 1794: 782-793. 19166984
Provasi Cardoso, J., R. Cayô, R. Girardello, and A.C. Gales. (2016). Diversity of mechanisms conferring resistance to β-lactams among OXA-23-producing Acinetobacter baumannii clones. Diagn Microbiol Infect Dis. [Epub: Ahead of Print] 26971181
Pumbwe, L., A. Chang, R.L. Smith, and H.M. Wexler. (2007). BmeRABC5 is a multidrug efflux system that can confer metronidazole resistance in Bacteroides fragilis. Microb Drug Resist 13: 96-101. 17650960
Pumbwe, L., L.P. Randall, M.J. Woodward, and L.J. Piddock. (2005). Evidence for multiple-antibiotic resistance in Campylobacter jejuni not mediated by CmeB or CmeF. Antimicrob. Agents Chemother. 49: 1289-1293. 15793099
Qi, X., P. Schmiege, E. Coutavas, and X. Li. (2018). Two Patched molecules engage distinct sites on Hedgehog yielding a signaling-competent complex. Science 362:. 30139912
Qian, H., X. Wu, X. Du, X. Yao, X. Zhao, J. Lee, H. Yang, and N. Yan. (2020). Structural Basis of Low-pH-Dependent Lysosomal Cholesterol Egress by NPC1 and NPC2. Cell. [Epub: Ahead of Print] 32544384
Qiu, W., Z. Fu, G.G. Xu, R.A. Grassucci, Y. Zhang, J. Frank, W.A. Hendrickson, and Y. Guo. (2018). Structure and activity of lipid bilayer within a membrane-protein transporter. Proc. Natl. Acad. Sci. USA. [Epub: Ahead of Print] 30509977
Rahman, M.M., T. Matsuo, W. Ogawa, M. Koterasawa, T. Kuroda, and T. Tsuchiya (2007). Molecular Cl- oning and Characterization of All RND-Type Efflux Transporters in Vibrio cholerae Non-O1. Microbiol Immunol 51: 1061-70. 18037783
Reboul, E. (2013). Absorption of vitamin A and carotenoids by the enterocyte: focus on transport proteins. Nutrients 5: 3563-3581. 24036530
Recht J, A. Martinez, S. Torello, and R. Kolter. (2000). Genetic analysis of sliding motility in Mycobacterium smegmatis. J. Bacteriol. 182: 4348-4351. 10894747
Robertson, G.T., T.B. Doyle, Q. Du, L. Duncan, K.E. Mdluli, and A.S. Lynch. (2007). A Novel indole compound that inhibits Pseudomonas aeruginosa growth by targeting MreB is a substrate for MexAB-OprM. J. Bacteriol. 189: 6870-6881. 17644596
Rojas, A., E. Duque, G. Mosqueda, G. Golden, A. Hurtado, J.L. Ramos, and A. Segura. (2001). Three efflux pumps are required to provide efficient tolerance to toluene in Pseudomonas putida DOT-T1E. J. Bacteriol. 183: 3967-3973. 11395460
Rosenberg, E.Y., D. Ma, and H. Nikaido. (2000). AcrD of Escherichia coli is an aminoglycoside efflux pump. J. Bacteriol. 182: 1754-1756. 10692383
Rouquette, C., J.B. Harmon, and W.M. Shafer. (1999). Induction of the mtrCDE-encoded efflux pump system of Neisseria gonorrhoeae requires MtrA, an AraC-like protein. Mol. Micobiol. 33: 651-658. 10417654
Saier, M.H., Jr., R. Tam, A. Reizer, and J. Reizer. (1994). Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport. Mol. Microbiol. 11: 841-847. 8022262
Schmidt, T. and H.G. Schlegel. (1994). Combined nickel-cobalt-cadmium resistance encoded by the ncc locus of Alcaligenes xylosoxidans 31A. J. Bacteriol. 176: 7045-7054. 7961470
Schultz, M.L., K.J. Schache, R.D. Azaria, E.Q. Kuiper, S. Erwood, E.A. Ivakine, N.Y. Farhat, F.D. Porter, K.C. Pathmasiri, S.M. Cologna, M.D. Uhler, and A.P. Lieberman. (2022). Species-specific differences in NPC1 protein trafficking govern therapeutic response in Niemann-Pick type C disease. JCI Insight 7:. 36301667
Schultz, M.L., K.L. Krus, and A.P. Lieberman. (2016). Lysosome and endoplasmic reticulum quality control pathways in Niemann-Pick type C disease. Brain Res 1649: 181-188. 27026653
Schultz, M.L., K.L. Krus, S. Kaushik, D. Dang, R. Chopra, L. Qi, V.G. Shakkottai, A.M. Cuervo, and A.P. Lieberman. (2018). Coordinate regulation of mutant NPC1 degradation by selective ER autophagy and MARCH6-dependent ERAD. Nat Commun 9: 3671. 30202070
Schuster, S., M. Vavra, D.A.N. Wirth, and W.V. Kern. (2024). Comparative reassessment of AcrB efflux inhibitors reveals differential impact of specific pump mutations on the activity of potent compounds. Microbiol Spectr 12: e0304523. 38170977
Seeger, M.A., A. Schiefner, T. Eicher, F. Verrey, K. Diederichs, and K.M. Pos. (2006). Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science 313: 1295-1298. 16946072
Seeliger, J.C., C.M. Holsclaw, M.W. Schelle, Z. Botyanszki, S.A. Gilmore, S.E. Tully, M. Niederweis, B.F. Cravatt, J.A. Leary, and C.R. Bertozzi. (2012). Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem. 287: 7990-8000. 22194604
Sennhauser, G., M.A. Bukowska, C. Briand, and M.G. Grütter. (2009). Crystal structure of the multidrug exporter MexB from Pseudomonas aeruginosa. J. Mol. Biol. 389: 134-145. 19361527
Serra, C., B. Bouharkat, A. Tir Touil-Meddah, S. Guénin, and C. Mullié. (2019). MexXY Multidrug Efflux System Is More Frequently Overexpressed in Ciprofloxacin Resistant French Clinical Isolates Compared to Hospital Environment Ones. Front Microbiol 10: 366. 30863391
Simsir, M., I. Broutin, I. Mus-Veteau, and F. Cazals. (2020). Studying dynamics without explicit dynamics: a structure-based study of the export mechanism by AcrB. Proteins. [Epub: Ahead of Print] 32960482
Skov, M., C.K. Tønnesen, G.H. Hansen, and E.M. Danielsen. (2011). Dietary cholesterol induces trafficking of intestinal Niemann-Pick Type C1 Like 1 from the brush border to endosomes. Am. J. Physiol. Gastrointest Liver Physiol 300: G33-40. 21051527
Sleat, D.E., J.A. Wiseman, M. El-Banna, S.M. Price, L. Verot, M.M. Shen, G.S. Tint, M.T. Vanier, S.U. Walkley, and P. Lobel. (2004). Genetic evidence for nonredundant functional cooperativity between NPC1 and NPC2 in lipid transport. Proc. Natl. Acad. Sci. USA 101: 5886-5891. 15071184
Sommer, A. and M.A. Lemmon. (2018). Smoothening out the patches. Science 362: 26-27. 30287647
Stähler, F.N., S. Odenbreit, R. Haas, J. Wilrich, A.H. Van Vliet, J.G. Kusters, M. Kist, and S. Bereswill. (2006). The novel Helicobacter pylori CznABC metal efflux pump is required for cadmium, zinc, and nickel resistance, urease modulation, and gastric colonization. Infect. Immun. 74: 3845-3852. 16790756
Su, C.C., A. Radhakrishnan, N. Kumar, F. Long, J.R. Bolla, H.T. Lei, J.A. Delmar, S.V. Do, T.H. Chou, K.R. Rajashankar, Q. Zhang, and E.W. Yu. (2014). Crystal structure of the Campylobacter jejuni CmeC outer membrane channel. Protein. Sci. 23: 954-961. 24753291
Su, C.C., F. Long, and E.W. Yu. (2011). The Cus efflux system removes toxic ions via a methionine shuttle. Protein. Sci. 20: 6-18. 20981744
Su, C.C., F. Long, M.T. Zimmermann, K.R. Rajashankar, R.L. Jernigan, and E.W. Yu. (2011). Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli. Nature 470: 558-562. 21350490
Su, C.C., F. Yang, F. Long, D. Reyon, M.D. Routh, D.W. Kuo, A.K. Mokhtari, J.D. Van Ornam, K.L. Rabe, J.A. Hoy, Y.J. Lee, K.R. Rajashankar, and E.W. Yu. (2009). Crystal structure of the membrane fusion protein CusB from Escherichia coli. J. Mol. Biol. 393: 342-355. 19695261
Su, C.C., M. Li, R. Gu, Y. Takatsuka, G. McDermott, H. Nikaido, and E.W. Yu. (2006). Conformation of the AcrB multidrug efflux pump in mutants of the putative proton relay pathway. J. Bacteriol. 188: 7290-7296. 17015668
Su, C.C., P.A. Klenotic, M. Cui, M. Lyu, C.E. Morgan, and E.W. Yu. (2021). Structures of the mycobacterial membrane protein MmpL3 reveal its mechanism of lipid transport. PLoS Biol 19: e3001370. [Epub: Ahead of Print] 34383749
Symmons, M.F., E. Bokma, E. Koronakis, C. Hughes, and V. Koronakis. (2009). The assembled structure of a complete tripartite bacterial multidrug efflux pump. Proc. Natl. Acad. Sci. USA 106: 7173-7178. 19342493
Taherpour, A. and A. Hashemi. (2013). Detection of OqxAB efflux pumps, OmpK35 and OmpK36 porins in extended-spectrum-β-lactamase-producing Klebsiella pneumoniae isolates from Iran. Hippokratia 17: 355-358. 25031516
Tahlan, K., R. Wilson, D.B. Kastrinsky, K. Arora, V. Nair, E. Fischer, S.W. Barnes, J.R. Walker, D. Alland, C.E. Barry, 3rd, and H.I. Boshoff. (2012). SQ109 targets MmpL3, a membrane transporter of trehalose monomycolate involved in mycolic acid donation to the cell wall core of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 56: 1797-1809. 22252828
Taipale, J., M.K. Cooper, T. Maiti, and P.A. Beachy. (2002). Patched acts catalytically to suppress the activity of Smoothened. Nature 418: 892-897. 12192414
Takahashi, T., F. Friedmacher, J. Zimmer, and P. Puri. (2018). Expression of dispatched RND transporter family member 1 is decreased in the diaphragmatic and pulmonary mesenchyme of nitrofen-induced congenital diaphragmatic hernia. Pediatr Surg Int. [Epub: Ahead of Print] 30382378
Takatsuka, Y. and H. Nikaido. (2006). Threonine-978 in the transmembrane segment of the multidrug efflux pump AcrB of Escherichia coli is crucial for drug transport as a probable component of the proton relay network. J. Bacteriol. 188: 7284-7289. 17015667
Takatsuka, Y. and H. Nikaido. (2007). Site-Directed Disulfide Cross-Linking Shows that Cleft Flexibility in the Periplasmic Domain Is Needed for the Multidrug Efflux Pump AcrB of Escherichia coli. J. Bacteriol. 189(23):8677-8684.
Takatsuka, Y. and H. Nikaido. (2009). Covalently linked trimer of the AcrB multidrug efflux pump provides support for the functional rotating mechanism. J. Bacteriol. 191: 1729-1737. 19060146
Takatsuka, Y., C. Chen, and H. Nikaido. (2010). Mechanism of recognition of compounds of diverse structures by the multidrug efflux pump AcrB of Escherichia coli. Proc. Natl. Acad. Sci. USA 107: 6559-6565. 20212112
Tam, H.K., V.N. Malviya, W.E. Foong, A. Herrmann, G. Malloci, P. Ruggerone, A.V. Vargiu, and K.M. Pos. (2019). Binding and transport of carboxylated drugs by the multidrug transporter AcrB. J. Mol. Biol. [Epub: Ahead of Print] 31881208
Tam, H.K., W.E. Foong, C. Oswald, A. Herrmann, H. Zeng, and K.M. Pos. (2021). Allosteric drug transport mechanism of multidrug transporter AcrB. Nat Commun 12: 3889. 34188038
Teh, A.H.T., S.M. Lee, and G.A. Dykes. (2017). Identification of potential Campylobacter jejuni genes involved in biofilm formation by EZ-Tn5 Transposome mutagenesis. BMC Res Notes 10: 182. 28499399
Terán, W., A. Felipe, S. Fillet, M.E. Guazzaroni, T. Krell, R. Ruiz, J.L. Ramos, and M.T. Gallegos. (2007). Complexity in efflux pump control: cross-regulation by the paralogues TtgV and TtgT. Mol. Microbiol. 66(6):1416-1428. 17986203
Tibazarwa, C., S. Wuertz, M. Mergeay, L. Wyns, and D. van Der Lelie. (2000). Regulation of the cnr cobalt and nickel resistance determinant of Ralstonia eutropha (Alcaligenes eutrophus) CH34. J. Bacteriol. 182: 1399-1409. 10671464
Törnroth-Horsefield, S., P. Gourdon, R. Horsefield, L. Brive, N. Yamamoto, H. Mori, A. Snijder, and R. Neutze. (2007). Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twist. Structure 15: 1663-1673. 18073115
Trinh, M.N., M.S. Brown, J. Seemann, J.L. Goldstein, and F. Lu. (2018). Lysosomal cholesterol export reconstituted from fragments of Niemann-Pick C1. Elife 7:. 30047864
Tseng, T.-T., K.S. Gratwick, J. Kollman, D. Park, D.H. Nies, A. Goffeau, and M.H. Saier, Jr. (1999). The RND permease superfamily: an ancient, ubiquitous and diverse family that includes human disease and development proteins. J. Mol. Microbiol. Biotechnol. 1: 107-125. 10941792
Tsukazaki, T. (2018). Structure-based working model of SecDF, a proton-driven bacterial protein translocation factor. FEMS Microbiol. Lett. 365:. 29718185
Tsukazaki, T. and O. Nureki. (2011). The mechanism of protein export enhancement by the SecDF membrane component. Biophysics (Nagoya-shi) 7: 129-133. 27857601
Tsukazaki, T., H. Mori, Y. Echizen, R. Ishitani, S. Fukai, T. Tanaka, A. Perederina, D.G. Vassylyev, T. Kohno, A.D. Maturana, K. Ito, and O. Nureki. (2011). Structure and function of a membrane component SecDF that enhances protein export. Nature 474: 235-238. 21562494
Tullius, M.V., C.A. Harmston, C.P. Owens, N. Chim, R.P. Morse, L.M. McMath, A. Iniguez, J.M. Kimmey, M.R. Sawaya, J.P. Whitelegge, M.A. Horwitz, and C.W. Goulding. (2011). Discovery and characterization of a unique mycobacterial heme acquisition system. Proc. Natl. Acad. Sci. USA 108: 5051-5056. 21383189
Valencia, E.Y., V.S. Braz, C. Guzzo, and M.V. Marques. (2013). Two RND proteins involved in heavy metal efflux in Caulobacter crescentus belong to separate clusters within proteobacteria. BMC Microbiol 13: 79. 23578014
Vieira Da Cruz, A., J.C. Jiménez-Castellanos, C. Börnsen, L. Van Maele, N. Compagne, E. Pradel, R.T. Müller, V. Meurillon, D. Soulard, C. Piveteau, A. Biela, J. Dumont, F. Leroux, B. Deprez, N. Willand, K.M. Pos, A.S. Frangakis, R.C. Hartkoorn, and M. Flipo. (2024). Pyridylpiperazine efflux pump inhibitor boosts in vivo antibiotic efficacy against K. pneumoniae. EMBO Mol Med 16: 93-111. 38177534
Walkley, S.U. and K. Suzuki. (2004). Consequences of NPC1 and NPC2 loss of function in mammalian neurons. Biochim. Biophys. Acta. 1685: 48-62. 15465426
Wang, B., J. Weng, and W. Wang. (2015). Substrate binding accelerates the conformational transitions and substrate dissociation in multidrug efflux transporter AcrB. Front Microbiol 6: 302. 25918513
Wang, C., S.M. Scott, S. Sun, P. Zhao, D.M. Hutt, H. Shao, J.E. Gestwicki, and W.E. Balch. (2020). Individualized management of genetic diversity in Niemann-Pick C1 through modulation of the Hsp70 chaperone system. Hum Mol Genet 29: 1-19. 31509197
Wang, L.J. and B.L. Song. (2012). Niemann-Pick C1-Like 1 and cholesterol uptake. Biochim. Biophys. Acta. 1821: 964-972. 22480541
Wang, M.L., M. Motamed, R.E. Infante, L. Abi-Mosleh, H.J. Kwon, M.S. Brown, and J.L. Goldstein. (2010). Identification of surface residues on Niemann-Pick C2 essential for hydrophobic handoff of cholesterol to NPC1 in lysosomes. Cell Metab 12: 166-173. 20674861
Wang, Q., D.E. Asarnow, K. Ding, R.K. Mann, J. Hatakeyama, Y. Zhang, Y. Ma, Y. Cheng, and P.A. Beachy. (2021). Dispatched uses Na flux to power release of lipid-modified Hedgehog. Nature 599: 320-324. 34707294
Weiss, L.E., L. Milenkovic, J. Yoon, T. Stearns, and W.E. Moerner. (2019). Motional dynamics of single Patched1 molecules in cilia are controlled by Hedgehog and cholesterol. Proc. Natl. Acad. Sci. USA 116: 5550-5557. 30819883
Wells, R.M., C.M. Jones, Z. Xi, A. Speer, O. Danilchanka, K.S. Doornbos, P. Sun, F. Wu, C. Tian, and M. Niederweis. (2013). Discovery of a siderophore export system essential for virulence of Mycobacterium tuberculosis. PLoS Pathog 9: e1003120. 23431276
White, D.G., J.D. Goldman, B. Demple, and S.B. Levy. (1997). The acrAB locus in organic solvent tolerance meditated by expression of marA, soxS, or robA in Escherichia coli. J. Bacteriol. 179: 6122-6126. 9324261
Williams, J.T. and R.B. Abramovitch. (2023). Molecular Mechanisms of MmpL3 Function and Inhibition. Microb Drug Resist. [Epub: Ahead of Print] 36809064
Winkler, M.B.L., R.T. Kidmose, M. Szomek, K. Thaysen, S. Rawson, S.P. Muench, D. Wüstner, and B.P. Pedersen. (2019). Structural Insight into Eukaryotic Sterol Transport through Niemann-Pick Type C Proteins. Cell. [Epub: Ahead of Print] 31543266
Xie, C., Z.S. Zhou, N. Li, Y. Bian, Y.J. Wang, L.J. Wang, B.L. Li, and B.L. Song. (2012). Ezetimibe blocks the internalization of NPC1L1 and cholesterol in mouse small intestine. J Lipid Res 53: 2092-2101. 22811412
Xiong, L.B., H.H. Liu, L.Q. Xu, W.J. Sun, F.Q. Wang, and D.Z. Wei. (2017). Improving the production of 22-hydroxy-23,24-bisnorchol-4-ene-3-one from sterols in Mycobacterium neoaurum by increasing cell permeability and modifying multiple genes. Microb Cell Fact 16: 89. 28532497
Xu, Z., V.A. Meshcheryakov, G. Poce, and S.S. Chng. (2017). MmpL3 is the flippase for mycolic acids in mycobacteria. Proc. Natl. Acad. Sci. USA 114: 7993-7998. 28698380
Yamada, S., N. Awano, K. Inubushi, E. Maeda, S. Nakamori, K. Nishino, A. Yamaguchi, and H. Takagi. (2006). Effect of drug transporter genes on cysteine export and overproduction in Escherichia coli. Appl. Environ. Microbiol. 72: 4735-4742. 16820466
Yamane T., Murakami S. and Ikeguchi M. (2013). Functional rotation induced by alternating protonation states in the multidrug transporter AcrB: all-atom molecular dynamics simulations. Biochemistry. 52(43):7648-58. 24083838
Yan, R., P. Cao, W. Song, H. Qian, X. Du, H.W. Coates, X. Zhao, Y. Li, S. Gao, X. Gong, X. Liu, J. Sui, J. Lei, H. Yang, A.J. Brown, Q. Zhou, C. Yan, and N. Yan. (2021). A structure of human Scap bound to Insig-2 suggests how their interaction is regulated by sterols. Science 371:. 33446483
Yañez, M.J., T. Marín, E. Balboa, A.D. Klein, A.R. Alvarez, and S. Zanlungo. (2020). Finding pathogenic commonalities between Niemann-Pick type C and other lysosomal storage disorders: Opportunities for shared therapeutic interventions. Biochim. Biophys. Acta. Mol Basis Dis 1866: 165875. 32522631
Yang, L., S. Lu, J. Belardinelli, E. Huc-Claustre, V. Jones, M. Jackson, and H.I. Zgurskaya. (2014). RND transporters protect Corynebacterium glutamicum from antibiotics by assembling the outer membrane. Microbiologyopen 3: 484-496. 24942069
Yang, S., C.R. Lopez, and E.L. Zechiedrich. (2006). Quorum sensing and multidrug transporters in Escherichia coli. Proc. Natl. Acad. Sci. USA 103: 2386-2391. 16467145
Yang, X., T. Hu, X. Yang, W. Xu, H. Yang, L.W. Guddat, B. Zhang, and Z. Rao. (2020). Structural Basis for the Inhibition of Mycobacterial MmpL3 by NITD-349 and SPIRO. J. Mol. Biol. [Epub: Ahead of Print] 32512002
Yao, X., X. Fan, and N. Yan. (2020). Cryo-EM analysis of a membrane protein embedded in the liposome. Proc. Natl. Acad. Sci. USA 117: 18497-18503. 32680969
Yasuda, N., T. Fujita, T. Fujioka, M. Tagawa, N. Kohira, K. Torimaru, S. Shiota, T. Kumagai, D. Morita, W. Ogawa, T. Tsuchiya, and T. Kuroda. (2023). Effects of the order of exposure to antimicrobials on the incidence of multidrug-resistant Pseudomonas aeruginosa. Sci Rep 13: 8826. 37258635
Ye C., Wang Z., Lu W., Zhong M., Chai Q. and Wei Y. (2014). Correlation between AcrB trimer association affinity and efflux activity. Biochemistry. 53(23):3738-46. 24854514
Yoon, J., C.J. Comerci, L.E. Weiss, L. Milenkovic, T. Stearns, and W.E. Moerner. (2019). Revealing Nanoscale Morphology of the Primary Cilium Using Super-Resolution Fluorescence Microscopy. Biophys. J. 116: 319-329. 30598282
Yu, E.W., G. McDermott, H.I. Zgurskaya, H. Nikaido, and D.E. Koshland, Jr. (2003). Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump. Science 300: 976-980. 12738864
Yu, E.W., J.R. Aires, and H. Nikaido. (2003). AcrB multidrug efflux pump of Escherichia coli: composite substrate-binding cavity of exceptional flexibility generates its extremely wide substrate specificity. J. Bacteriol. 185: 5657-5664. 13129936
Yu, L. (2008). The structure and function of Niemann-Pick C1-like 1 protein. Curr Opin Lipidol 19: 263-269. 18460917
Yu, T. and A.P. Lieberman. (2013). Npc1 acting in neurons and glia is essential for the formation and maintenance of CNS myelin. PLoS Genet 9: e1003462. 23593041
Yu, T., C. Chung, D. Shen, H. Xu, and A.P. Lieberman. (2012). Ryanodine receptor antagonists adapt NPC1 proteostasis to ameliorate lipid storage in Niemann-Pick type C disease fibroblasts. Hum Mol Genet 21: 3205-3214. 22505584
Yue, Z., W. Chen, H.I. Zgurskaya, and J. Shen. (2017). Constant pH Molecular Dynamics Reveals How Proton Release Drives the Conformational Transition of a Transmembrane Efflux Pump. J Chem Theory Comput. [Epub: Ahead of Print] 29117682
Yuhan, Y., Y. Ziyun, Z. Yongbo, L. Fuqiang, and Z. Qinghua. (2016). Over expression of AdeABC and AcrAB-TolC efflux systems confers tigecycline resistance in clinical isolates of Acinetobacter baumannii and Klebsiella pneumoniae. Rev Soc Bras Med Trop 49: 165-171. 27192584
Zgurskaya, H.I. and H. Nikaido. (2000). Cross-linked complex between oligomeric periplasmic lipoprotein AcrA and the inner-membrane-associated multidrug efflux pump AcrB from Escherichia coli. J. Bacteriol. 182: 4264-4267. 10894736
Zhang, B., J. Li, X. Yang, L. Wu, J. Zhang, Y. Yang, Y. Zhao, L. Zhang, X. Yang, X. Yang, X. Cheng, Z. Liu, B. Jiang, H. Jiang, L.W. Guddat, H. Yang, and Z. Rao. (2019). Crystal Structures of Membrane Transporter MmpL3, an Anti-TB Drug Target. Cell 176: 636-648.e13. 30682372
Zhang, X.C., M. Liu, and L. Han. (2017). Energy coupling mechanisms of AcrB-like RND transporters. Biophys Rep 3: 73-84. 29238744
Zhang, Y., D.P. Bulkley, Y. Xin, K.J. Roberts, D.E. Asarnow, A. Sharma, B.R. Myers, W. Cho, Y. Cheng, and P.A. Beachy. (2018). Structural Basis for Cholesterol Transport-like Activity of the Hedgehog Receptor Patched. Cell 175: 1352-1364.e14. 30415841
Zhang, Y., K.M. Lee, L.N. Kinch, L. Clark, N.V. Grishin, D.M. Rosenbaum, M.S. Brown, J.L. Goldstein, and A. Radhakrishnan. (2016). Direct Demonstration that Loop1 of Scap Binds to Loop7, a crucial event in cholesterol homeostasis. J. Biol. Chem. [Epub: Ahead of Print] 27068746
Zwama, M., A. Yamaguchi, and K. Nishino. (2019). Phylogenetic and functional characterisation of the multidrug efflux pump AcrB. Commun Biol 2: 340. 31531401
Zwama, M., K. Hayashi, K. Sakurai, R. Nakashima, K. Kitagawa, K. Nishino, and A. Yamaguchi. (2017). Hoisting-Loop in Bacterial Multidrug Exporter AcrB Is a Highly Flexible Hinge That Enables the Large Motion of the Subdomains. Front Microbiol 8: 2095. 29118749