Molecular mechanisms of antibiotic resistance revisited
Abstract
Antibiotic resistance is a global health emergency, with resistance detected to all antibiotics currently in clinical use and only a few novel drugs in the pipeline. Understanding the molecular mechanisms that bacteria use to resist the action of antimicrobials is critical to recognize global patterns of resistance and to improve the use of current drugs, as well as for the design of new drugs less susceptible to resistance development and novel strategies to combat resistance. In this Review, we explore recent advances in understanding how resistance genes contribute to the biology of the host, new structural details of relevant molecular events underpinning resistance, the identification of new resistance gene families and the interactions between different resistance mechanisms. Finally, we discuss how we can use this information to develop the next generation of antimicrobial therapies.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Efflux pumps were prevalent across multiple strains, particularly within Escherichia and Klebsiella.
“Efflux pumps, which facilitate multidrug resistance by expelling a broad range of antibiotics41, were also prevalent across multiple strains, particularly within Escherichia and Klebsiella, further complicating treatment options for infections by these pathogens in preterm infants.”
From Impact of early life antibiotic and probiotic treatment on gut microbiome and resistome of very-low-birth-weight preterm infants. (2025) · cites this paper as [41]
Cites
Liu, Y.-Y., Wang, Y., Walsh, T., Yi, L.-X., Zhang, R., Spencer, J., Doi, Y., Tian, G.-B., Dong, B.-L., Huang, X.-H., et al. (2016) · Lancet. Infectious Diseases (Print) · doi:10.1016/s1473-3099(15)00424-7 · Cited by 4,920 · see citing works
Molecular Basis of Bacterial Outer Membrane Permeability Revisited
Nikaido, H. (2003) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.67.4.593-656.2003 · Cited by 4,316 · see citing works
Molecular mechanisms of antibiotic resistance
Blair, J. M. A., Webber, M. A., Baylay, A. J., Ogbolu, D. O., & Piddock, L. J. V. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3380 · Cited by 4,092 · see citing works
Self-citationJ Antimicrob Chemother 1994; 33: 350–351
O’Shaughnessy, E. M., & DAS, S. S. (1994) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/33.2.350 · Cited by 3,746 · see citing works
Yong, D., Toleman, M. A., Giske, C. G., Cho, H. S., Sundman, K., Lee, K., & Walsh, T. R. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00774-09 · Cited by 2,531 · see citing works
Carbapenemases: the Versatile β-Lactamases
Queenan, A. M., & Bush, K. (2007) · Clinical Microbiology Reviews · doi:10.1128/cmr.00001-07 · Cited by 2,504 · see citing works
Updated Functional Classification of β-Lactamases
Bush, K., & Jacoby, G. A. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01009-09 · Cited by 2,367 · see citing works
Methicillin-resistant Staphylococcus aureus clinical strain with reduced vancomycin susceptibility
Hiramatsu, K. (1997) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/40.1.135 · Cited by 1,984 · see citing works
Ambler, R. P. (1980) · Philosophical transactions of the Royal Society of London. Series B, Biological sciences · doi:10.1098/rstb.1980.0049 · Cited by 1,839 · see citing works
Aminoglycoside modifying enzymes
Ramirez, M. S., & Tolmasky, M. E. (2010) · Drug Resistance Updates · doi:10.1016/j.drup.2010.08.003 · Cited by 1,504 · see citing works
Definitions and guidelines for research on antibiotic persistence
Balaban, N. Q., Helaine, S., Lewis, K., Ackermann, M., Aldridge, B., Andersson, D. I., Brynildsen, M. P., Bumann, D., Camilli, A., Collins, J. J., et al. (2019) · Nature Reviews Microbiology · doi:10.1038/s41579-019-0196-3 · Cited by 1,313 · see citing works
Antibiotic tolerance facilitates the evolution of resistance
Levin-Reisman, I., Ronin, I., Gefen, O., Braniss, I., Noam Shoresh, F., & Balaban, N. Q. (2017) · Science · doi:10.1126/science.aaj2191 · Cited by 1,229 · see citing works
Tolerance and resistance of microbial biofilms
Ciofu, O., Moser, C. E., Jensen, P. Ø., & Høiby, N. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00682-4 · Cited by 1,153 · see citing works
Multidrug efflux pumps: structure, function and regulation
Du, D., Wang‐Kan, X., Neuberger, A., van Veen, H. W., Pos, K. M., Piddock, L. J. V., & Luisi, B. F. (2018) · Nature Reviews Microbiology · doi:10.1038/s41579-018-0048-6 · Cited by 1,063 · see citing works
β-Lactamases and β-Lactamase Inhibitors in the 21st Century
Tooke, C. L., Hinchliffe, P., Bragginton, É. C., Colenso, C. K., Hirvonen, V. H. A., Takebayashi, Y., & SPENCER, J. M. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.04.002 · Cited by 1,033 · see citing works
Crystal structure of bacterial multidrug efflux transporter AcrB
Murakami, S., Nakashima, R., Yamashita, E., & Yamaguchi, A. (2002) · Nature · doi:10.1038/nature01050 · Cited by 987 · see citing works
Adaptive and Mutational Resistance: Role of Porins and Efflux Pumps in Drug Resistance
Fernández, L., & Hancock, R. E. W. (2012) · Clinical Microbiology Reviews · doi:10.1128/cmr.00043-12 · Cited by 905 · see citing works
Bacterial resistance to antibiotics: Enzymatic degradation and modification
WRIGHT, G. (2005) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2005.04.002 · Cited by 897 · see citing works
The importance of efflux pumps in bacterial antibiotic resistance
Webber, M. A. (2002) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkg050 · Cited by 856 · see citing works
Self-citationMoffatt, J. H., Harper, M., Harrison, P. F., Hale, J. D. F., VINOGRADOV, E. V., Seemann, T., Henry, R., Crane, B., Michael, F. S., Cox, A. D., et al. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00834-10 · Cited by 817 · see citing works
Mechanisms of antibiotic resistance in enterococci
Miller, W. R., Munita, J. M., & Arias, C. A. (2014) · Expert Review of Anti-infective Therapy · doi:10.1586/14787210.2014.956092 · Cited by 772 · see citing works
Emergence of plasmid-mediated high-level tigecycline resistance genes in animals and humans
He, T., Wang, R., Liu, D., et al. (2019) · Nature Microbiology · doi:10.1038/s41564-019-0445-2 · Cited by 711 · see citing works
Long, K. S., Poehlsgaard, J., Kehrenberg, C., Schwarz, Š., & Vester, B. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00131-06 · Cited by 710 · see citing works
Beta-lactamase database (BLDB) – structure and function
Naas, T., Oueslati, S., Bonnin, R. A., Dabos, L., Zavala, A. J., Dortet, L., Retailleau, P., & Iorga, B. I. (2017) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2017.1344235 · Cited by 708 · see citing works
Penicillin-binding proteins and β-lactam resistance
Zapun, A., Contreras‐Martel, C., & Vernet, T. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00095.x · Cited by 690 · see citing works
β-lactam antibiotics: An overview from a medicinal chemistry perspective
Lima, L. M., da Silva, B. N. M., Barbosa, G., & Barreiro, E. J. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112829 · Cited by 669 · see citing works
Structure of the AcrAB–TolC multidrug efflux pump
Du, D., Wang, Z., James, N. R., Voss, J. E., Klimont, E., Ohene‐Agyei, T., Venter, H., Chiu, W., & Luisi, B. F. (2014) · Nature · doi:10.1038/nature13205 · Cited by 664 · see citing works
Sulfonamide resistance: mechanisms and trends.
Sköld, O. (2000) · Drug Resistance Updates · doi:10.1054/drup.2000.0146 · Cited by 647 · see citing works
Emergence of antibiotic resistance Pseudomonas aeruginosa in intensive care unit; a critical review
Pachori, P., Gothalwal, R., & Gandhi, P. (2019) · Genes & Diseases · doi:10.1016/j.gendis.2019.04.001 · Cited by 636 · see citing works
The bacterial ribosome as a target for antibiotics
Poehlsgaard, J., & Douthwaite, S. R. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1265 · Cited by 604 · see citing works
Mechanisms of vancomycin resistance in Staphylococcus aureus
Gardete, S., & Tomasz, A. (2014) · Journal of Clinical Investigation · doi:10.1172/jci68834 · Cited by 565 · see citing works
The Oxazolidinone Linezolid Inhibits Initiation of Protein Synthesis in Bacteria
Swaney, S. M., Aoki, H., GANOZA, M. C., et al. (1998) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.42.12.3251 · Cited by 557 · see citing works
RifamycinMode of Action, Resistance, and Biosynthesis
Floss, H. G., & Yu, T.-W. (2005) · Chemical Reviews · doi:10.1021/cr030112j · Cited by 547 · see citing works
ATP-Dependent Persister Formation in <i>Escherichia coli</i>
Shan, Y., Brown Gandt, A., Rowe, S. E., Deisinger, J. P., Conlon, B. P., & Lewis, K. (2017) · mBio · doi:10.1128/mbio.02267-16 · Cited by 508 · see citing works
Role of bacterial efflux pumps in biofilm formation
Alav, I., Sutton, J. M., & Rahman, K. M. (2018) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dky042 · Cited by 504 · see citing works
Self-citationResistance to Trimethoprim-Sulfamethoxazole
Eliopoulos, G. M., & Huovinen, P. (2001) · Clinical Infectious Diseases · doi:10.1086/320532 · Cited by 500 · see citing works
Plasmid-encoded tet(X) genes that confer high-level tigecycline resistance in Escherichia coli
Sun, J. G., Chen, C., Cui, C., Zhang, Y., Liu, X., Cui, Z.-H., Ma, X.-Y., Feng, Y., Fang, L., Lian, X.-L., et al. (2019) · Nature Microbiology · doi:10.1038/s41564-019-0496-4 · Cited by 487 · see citing works
Vancomycin-Resistant Staphylococcus aureus in the United States, 2002-2006
Sievert, D. M., Rudrik, J. T., Patel, J. B., McDonald, L. C., Wilkins, M. J., & Hageman, J. C. (2008) · Clinical Infectious Diseases · doi:10.1086/527392 · Cited by 483 · see citing works
Efflux pump inhibitors for bacterial pathogens
Sharma, A., Gupta, V., & Pathania, R. (2019) · The Indian Journal of Medical Research · doi:10.4103/ijmr.ijmr_2079_17 · Cited by 458 · see citing works
Quinolones: Mechanism, Lethality and Their Contributions to Antibiotic Resistance
Bush, N. G., Díez-Santos, I., Abbott, L. R., & Maxwell, A. (2020) · Molecules · doi:10.3390/molecules25235662 · Cited by 431 · see citing works
Bacterial resistance to antibiotics: Modified target sites
Lambert, P. A. (2005) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2005.04.003 · Cited by 427 · see citing works
Methicillin Resistance in Staphylococcus Aureus: Mechanisms and Modulation
Stapleton, P. D., & Taylor, P. W. (2002) · Science Progress · doi:10.3184/003685002783238870 · Cited by 418 · see citing works
How Macrolide Antibiotics Work
Vázquez‐Laslop, N., & Mankin, A. S. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.06.011 · Cited by 414 · see citing works
Glycopeptide resistance in enterococci
Arthur, M., REYNOLDS, P., & Courvalin, P. M. (1996) · Trends in Microbiology · doi:10.1016/0966-842x(96)10063-9 · Cited by 412 · see citing works
Johnson, A. P., & Woodford, N. (2013) · Journal of Medical Microbiology · doi:10.1099/jmm.0.052555-0 · Cited by 411 · see citing works
Liu, C. G., Green, S. I., Min, L., Clark, J. R., Salazar, K. C., Terwilliger, A. L., Kaplan, H. B., Trautner, B. W., Ramig, R. F., & Maresso, A. W. (2020) · mBio · doi:10.1128/mbio.01462-20 · Cited by 411 · see citing works
Alarming β-lactamase-mediated resistance in multidrug-resistant Enterobacteriaceae
Bush, K. (2010) · Current Opinion in Microbiology · doi:10.1016/j.mib.2010.09.006 · Cited by 398 · see citing works
Colistin kills bacteria by targeting lipopolysaccharide in the cytoplasmic membrane
Sabnis, A., Hagart, K. L., Klöckner, A., Becce, M., Evans, L. E., Furniss, R. C. D., Mavridou, D. A. I., Murphy, R. A., Stevens, M. M., Davies, J. C., et al. (2021) · eLife · doi:10.7554/elife.65836 · Cited by 393 · see citing works
Roberts, M. C. (2008) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2008.01145.x · Cited by 392 · see citing works
Molecular mechanisms of vancomycin resistance
Stogios, P. J., & Savchenko, A. V. (2020) · Protein Science · doi:10.1002/pro.3819 · Cited by 388 · see citing works
Structure, function and regulation of Pseudomonas aeruginosa porins
Chevalier, S., Bouffartigues, E., Bodilis, J., Maillot, O., Lesouhaitier, O., Feuilloley, M., Orange, N., Dufour, A., & Cornelis, P. (2017) · FEMS Microbiology Reviews · doi:10.1093/femsre/fux020 · Cited by 370 · see citing works
Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket
Nakashima, R., Sakurai, K., Yamasaki, S., Nishino, K., & Yamaguchi, A. (2011) · Nature · doi:10.1038/nature10641 · Cited by 348 · see citing works
Doi, Y., Wachino, J.-I., & Arakawa, Y. (2016) · Infectious Disease Clinics of North America · doi:10.1016/j.idc.2016.02.011 · Cited by 344 · see citing works
Mechanisms of quinolone action and resistance: where do we stand?
Correia, S., Poeta, P. A. C. Q. D., Hébraud, M., Capelo, J. L., & Igrejas, G. (2017) · Journal of Medical Microbiology · doi:10.1099/jmm.0.000475 · Cited by 332 · see citing works
Pratt, L. A., Hsing, W., Gibson, K. E., & Silhavy, T. J. (1996) · Molecular Microbiology · doi:10.1111/j.1365-2958.1996.tb02532.x · Cited by 318 · see citing works
Bermingham, A., & Derrick, J. P. (2002) · BioEssays · doi:10.1002/bies.10114 · Cited by 295 · see citing works
Emergence of methicillin resistance predates the clinical use of antibiotics
Larsen, J., Raisen, C. L., Ba, X., Sadgrove, N. J., Padilla-González, G. F., Simmonds, M. S. J., Loncaric, I., Kerschner, H., Apfalter, P., Hartl, R., et al. (2022) · Nature · doi:10.1038/s41586-021-04265-w · Cited by 295 · see citing works
Davis, B. D., Chen, L. L., & Tai, P. C. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.16.6164 · Cited by 294 · see citing works
Halat, D. H., & Moubareck, C. A. (2020) · Antibiotics · doi:10.3390/antibiotics9040186 · Cited by 291 · see citing works
Colistin Update on Its Mechanism of Action and Resistance, Present and Future Challenges
Andrade, F. F., Silva, D., Rodrigues, A. G., et al. (2020) · Microorganisms · doi:10.3390/microorganisms8111716 · Cited by 287 · see citing works
RND-type drug efflux pumps from Gram-negative bacteria: molecular mechanism and inhibition
Venter, H., Mowla, R., Ohene‐Agyei, T., & Ma, S. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00377 · Cited by 286 · see citing works
The Growing Genetic and Functional Diversity of Extended Spectrum Beta-Lactamases
Rahman, S. U., Ali, T., Ali, I., Khan, N. A., Han, B., & Gao, J. (2018) · BioMed Research International · doi:10.1155/2018/9519718 · Cited by 285 · see citing works
ABC-F Proteins Mediate Antibiotic Resistance through Ribosomal Protection
Sharkey, L. K. R., Edwards, T. A., & O’Neill, A. J. (2016) · mBio · doi:10.1128/mbio.01975-15 · Cited by 281 · see citing works
Lin, L. Y.-C., Nonejuie, P., Munguia, J., Hollands, A., Olson, J., Dam, Q., Kumaraswamy, M., Rivera, H., Corriden, R., Rohde, M., et al. (2015) · EBioMedicine · doi:10.1016/j.ebiom.2015.05.021 · Cited by 278 · see citing works
An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump
Wang, Z., Fan, G., Hryc, C. F., Blaza, J. N., Serysheva, I. I., Schmid, M. F., Chiu, W., Luisi, B. F., & Du, D. (2017) · eLife · doi:10.7554/elife.24905 · Cited by 274 · see citing works
Proximate and ultimate causes of the bactericidal action of antibiotics
Baquero, F., & Levin, B. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-020-00443-1 · Cited by 270 · see citing works
Cephalosporinase over-expression resulting from insertion of ISAba1 in Acinetobacter baumannii
Héritier, C., Poirel, L., & Nordmann, P. (2006) · Clinical Microbiology and Infection · doi:10.1111/j.1469-0691.2005.01320.x · Cited by 266 · see citing works
Luthra, S., Rominski, A., & Sander, P. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02179 · Cited by 261 · see citing works
Role of AcrAB-TolC multidrug efflux pump in drug-resistance acquisition by plasmid transfer
Nolivos, S., Cayron, J., Berne-Dedieu, A., Page, A., Delolme, F., & Lesterlin, C. (2019) · Science · doi:10.1126/science.aav6390 · Cited by 257 · see citing works
MicC, a Second Small-RNA Regulator of Omp Protein Expression inEscherichia coli
Chen, S., Zhang, A., Blyn, L. B., & Storz, G. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.20.6689-6697.2004 · Cited by 246 · see citing works
Plasmids in Gram negatives: Molecular typing of resistance plasmids
Carattoli, A. (2011) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2011.09.003 · Cited by 245 · see citing works
Heterogeneity in efflux pump expression predisposes antibiotic-resistant cells to mutation
Meouche, I. E., & Dunlop, M. J. (2018) · Science · doi:10.1126/science.aar7981 · Cited by 240 · see citing works
Crystal Structure of Osmoporin OmpC from E. coli at 2.0 Å
Baslé, A., Rummel, G., Storici, P., Rosenbusch, J. P., & Schirmer, T. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.08.002 · Cited by 236 · see citing works
Mechanisms of drug resistance: daptomycin resistance
Tran, T. T., Munita, J. M., & Arias, C. A. (2015) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12948 · Cited by 236 · see citing works
Alav, I., Kobylka, J., Kuth, M. S., Pos, K. M., Picard, M., Blair, J. M. A., & Bavro, V. N. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00055 · Cited by 233 · see citing works
Self-citationHobbs, E. C., Yin, X., Paul, B. J., Astarita, J. L., & Storz, G. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1210093109 · Cited by 220 · see citing works
Delihas, N., & Forst, S. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5029 · Cited by 220 · see citing works
Lincosamides: Chemical structure, biosynthesis, mechanism of action, resistance, and applications
Spížek, J., & Řezanka, T. (2016) · Biochemical Pharmacology · doi:10.1016/j.bcp.2016.12.001 · Cited by 220 · see citing works
Target protection as a key antibiotic resistance mechanism
Wilson, D. N., Hauryliuk, V., Atkinson, G. C., & O’Neill, A. J. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-020-0386-z · Cited by 213 · see citing works
Approved Glycopeptide Antibacterial Drugs: Mechanism of Action and ResistancePreprint
Zeng, D., Debabov, D. V., Hartsell, T. L., Cano, R. J., Adams, S. M., Schuyler, J. A., McMillan, R. K., & Pace, J. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026989 · Cited by 212 · see citing works
Yang, Q., Li, M., Spiller, O. B., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02149-0 · Cited by 211 · see citing works
Antibiotic Resistance by Enzymatic Modification of Antibiotic Targets
Schaenzer, A. J., & Wright, G. D. (2020) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2020.05.001 · Cited by 198 · see citing works
Gasparrini, A. J., Markley, J. L., Kumar, H., Wang, B., Fang, L., Irum, S., Symister, C. T., Wallace, M. A., Burnham, C. D., Andleeb, S., et al. (2020) · Communications Biology · doi:10.1038/s42003-020-0966-5 · Cited by 196 · see citing works
Mobile Oxazolidinone Resistance Genes in Gram-Positive and Gram-Negative Bacteria
Schwarz, Š., Zhang, W., Du, X., Krüger, H., Feßler, A. T., Ma, S., Zhu, Y., Wu, C., Shen, J., & Wang, Y. (2021) · Clinical Microbiology Reviews · doi:10.1128/cmr.00188-20 · Cited by 190 · see citing works
Tetracycline-Inactivating Enzymes
Markley, J. L., & Wencewicz, T. A. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01058 · Cited by 188 · see citing works
OmpK36-mediated Carbapenem resistance attenuates ST258 Klebsiella pneumoniae in vivo
Wong, J. L. C., Romanò, M., Kerry, L. E., Kwong, H.-S., Low, W. W., Brett, S. J., Clements, A., Beis, K., & Frankel, G. M. (2019) · Nature Communications · doi:10.1038/s41467-019-11756-y · Cited by 187 · see citing works
Wadsworth, C. B., Arnold, B., Sater, M., & Grad, Y. H. (2018) · mBio · doi:10.1128/mbio.01419-18 · Cited by 182 · see citing works
The Tetracycline Destructases: A Novel Family of Tetracycline-Inactivating Enzymes
Forsberg, K. J., Patel, S., Wencewicz, T. A., & Dantas, G. A. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.05.017 · Cited by 181 · see citing works
Veal, W. L., Nicholas, R. A., & Shafer, W. M. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.20.5619-5624.2002 · Cited by 176 · see citing works
Permeability barriers of Gram‐negative pathogens
Zgurskaya, H. I., & Rybenkov, V. V. (2019) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14134 · Cited by 175 · see citing works
Wang, L., Liu, D., Lv, Y., et al. (2019) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01326-19 · Cited by 174 · see citing works
Dunn, S. J., Connor, C. H., & McNally, A. (2019) · Current Opinion in Microbiology · doi:10.1016/j.mib.2019.06.004 · Cited by 172 · see citing works
Gleckman, R. A., Blagg, N. A., & Joubert, D. W. (1981) · Pharmacotherapy The Journal of Human Pharmacology and Drug Therapy · doi:10.1002/j.1875-9114.1981.tb03548.x · Cited by 170 · see citing works
Mishra, N. N., Bayer, A. S., Tran, T. T., Shamoo, Y. E., Mileykovskaya, E., Dowhan, W., Guan, Z., & Arias, C. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043958 · Cited by 168 · see citing works
Wróbel, A., Arciszewska, K., Maliszewski, D., & Drozdowska, D. (2019) · The Journal of Antibiotics · doi:10.1038/s41429-019-0240-6 · Cited by 168 · see citing works
AcrB: a mean, keen, drug efflux machine
Kobylka, J., Kuth, M. S., Müller, R. T., Geertsma, E. R., & Pos, K. M. (2019) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14239 · Cited by 167 · see citing works
Efflux pump activity potentiates the evolution of antibiotic resistance across S. aureus isolates
Papkou, A., Hedge, J., Kapel, N., Young, B., & MacLean, R. C. (2020) · Nature Communications · doi:10.1038/s41467-020-17735-y · Cited by 167 · see citing works
Hugonnet, J., Mengin‐Lecreulx, D., Silva, A. M., den Blaauwen, T., Carbonnelle, É., Veckerlé, C., Brun, Y. V., VanNieuwenhze, M. S., Bouchier, C., Tu, K., et al. (2016) · eLife · doi:10.7554/elife.19469 · Cited by 161 · see citing works
Antibiotics: Combatting Tolerance To Stop Resistance
Windels, E. M., Michiels, J. E., den Bergh, B. V., Fauvart, M., & Michiels, J. J. (2019) · mBio · doi:10.1128/mbio.02095-19 · Cited by 158 · see citing works
Efflux pump inhibitors: targeting mycobacterial efflux systems to enhance TB therapy
Pule, C. M., Sampson, S. L., Warren, R. M., et al. (2015) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkv316 · Cited by 155 · see citing works
Bacterial persisters are a stochastically formed subpopulation of low-energy cells
Manuse, S., Shan, Y., Cañas-Duarte, S. J., Bakshi, S., Sun, W.-S. W., Mori, H., Paulsson, J., & Lewis, K. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001194 · Cited by 154 · see citing works
Transferable Mechanisms of Quinolone Resistance from 1998 Onward
Ruiz, J. (2019) · Clinical Microbiology Reviews · doi:10.1128/cmr.00007-19 · Cited by 149 · see citing works
Getting Drugs into Gram-Negative Bacteria: Rational Rules for Permeation through General Porins
Acosta‐Gutiérrez, S., Ferrara, L., Pathania, M., Masi, M., Wang, J., Bodrenko, I. V., Zahn, M., Winterhalter, M., Stavenger, R. A., Pagès, J., et al. (2018) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.8b00108 · Cited by 148 · see citing works
Meyer, B., & Cookson, B. (2010) · Journal of Hospital Infection · doi:10.1016/j.jhin.2010.05.020 · Cited by 147 · see citing works
Schwarz, Š., Shen, J., Kadlec, K., Wang, Y., Michael, G. B., Feßler, A. T., & Vester, B. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a027037 · Cited by 147 · see citing works
Lou, H., Chen, M., Black, S. S., Bushell, S. R., Ceccarelli, M., Mach, T., Beis, K., Low, A. S., Bamford, V. A., Booth, I. R., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025825 · Cited by 145 · see citing works
Decreased Azithromycin Susceptibility of Neisseria gonorrhoeae Due to mtrR Mutations
Zarantonelli, L., Borthagaray, G., Lee, E. H., & Shafer, W. M. (1999) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.43.10.2468 · Cited by 144 · see citing works
(p)ppGpp and Its Role in Bacterial Persistence: New Challenges
Pacios, O., Blasco, L., Bleriot, I., Fernández-García, L., Ambroa, A., López, M. C., Bou, G., Cantón, R., García‐Contreras, R., Wood, T. K., et al. (2020) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01283-20 · Cited by 144 · see citing works
Tsutsumi, K., Yonehara, R., Ishizaka-Ikeda, E., Miyazaki, N., Maeda, S., Iwasaki, K., Nakagawa, A., & Yamashita, E. (2019) · Nature Communications · doi:10.1038/s41467-019-09463-9 · Cited by 135 · see citing works
Sequential Mechanism of Assembly of Multidrug Efflux Pump AcrAB-TolC
Tikhonova, E. B., Yamada, Y. M. A., & Zgurskaya, H. I. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.02.011 · Cited by 134 · see citing works
Duval, V. (2013) · International Journal of Biotechnology for Wellness Industries · doi:10.6000/1927-3037.2013.02.03.2 · Cited by 134 · see citing works
Sharma, P., Haycocks, J. R. J., Middlemiss, A. D., Kettles, R. A., Sellars, L. E., Ricci, V., Piddock, L. J. V., & Grainger, D. C. (2017) · Nature Communications · doi:10.1038/s41467-017-01405-7 · Cited by 134 · see citing works
The outer parts of the mycobacterial envelope as permeability barriers
Draper, P. (1998) · Frontiers in bioscience · doi:10.2741/a360 · Cited by 132 · see citing works
Fang, L., Chen, C., Cui, C., Li, X., Zhang, Y., Liao, X., Sun, J. G., & Liu, Y. (2020) · BioEssays · doi:10.1002/bies.202000014 · Cited by 132 · see citing works
Ude, J., Tripathi, V., Buyck, J. M., Söderholm, S., Cunrath, O., Fanous, J., Claudi, B., Egli, A., Schleberger, C., Hiller, S., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2107644118 · Cited by 132 · see citing works
Rominski, A., Roditscheff, A., Selchow, P., Böttger, E. C., & Sander, P. (2016) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkw466 · Cited by 130 · see citing works
Gomez‐Simmonds, A., & Uhlemann, A. (2017) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiw378 · Cited by 130 · see citing works
Ricci, V., Tzakas, P., Buckley, A. M., Coldham, N. G., & Piddock, L. J. V. (2005) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.50.1.38-42.2006 · Cited by 129 · see citing works
The History of Colistin Resistance Mechanisms in Bacteria: Progress and Challenges
Hamel, M., Rolain, J., & Baron, S. A. (2021) · Microorganisms · doi:10.3390/microorganisms9020442 · Cited by 128 · see citing works
The impact of genetic diversity on gene essentiality within the Escherichia coli species
Rousset, F., Cabezas-Caballero, J., Piastra-Facon, F., Fernández-Rodríguez, J., Clermont, O., Denamur, É., Rocha, E. P. C., & Bikard, D. (2021) · Nature Microbiology · doi:10.1038/s41564-020-00839-y · Cited by 127 · see citing works
Emergence of trimethoprim-sulfamethoxazole resistance in the AIDS era.
Martin, J. N., Rose, D. A., Hadley, W. K., Perdreau‐Remington, F., Lam, P. K., & Gerberding, J. L. (1999) · The Journal of Infectious Diseases · doi:10.1086/315132 · Cited by 126 · see citing works
Look and Outlook on Enzyme-Mediated Macrolide Resistance
Golkar, T., Zieliński, M., & Berghuis, A. M. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01942 · Cited by 126 · see citing works
Substrate Specificity within a Family of Outer Membrane Carboxylate Channels
Eren, E., Vijayaraghavan, J., Liu, J., Cheneke, B. R., Touw, D. S., Lepore, B. W., Indic, M., Movileanu, L., & van den Berg, B. (2012) · PLoS Biology · doi:10.1371/journal.pbio.1001242 · Cited by 124 · see citing works
Abdali, N., Parks, J. M., Haynes, K. M., et al. (2016) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.6b00167 · Cited by 124 · see citing works
Nepal, K., Pant, N. D., Neupane, B., Belbase, A., Baidhya, R., Shrestha, R. K., Lekhak, B., Bhatta, D. R., & Jha, B. (2017) · Annals of Clinical Microbiology and Antimicrobials · doi:10.1186/s12941-017-0236-7 · Cited by 120 · see citing works
Multiple entry pathways within the efflux transporter AcrB contribute to multidrug recognition
Zwama, M., Yamasaki, S., Nakashima, R., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02493-1 · Cited by 118 · see citing works
Synthetic group A streptogramin antibiotics that overcome Vat resistance
Li, Q., Pellegrino, J., Lee, D. J., et al. (2020) · Nature · doi:10.1038/s41586-020-2761-3 · Cited by 118 · see citing works
First case of infection with vancomycin-resistant Staphylococcus aureus in Europe
Melo‐Cristino, J., Resina, C., Manuel, V., Lito, L., & Ramirez, M. (2013) · The Lancet · doi:10.1016/s0140-6736(13)61219-2 · Cited by 116 · see citing works
Efflux Pump Inhibitors: A Novel Approach to Combat Efflux-Mediated Drug Resistance in Bacteria
Wang, Y., Venter, H., & Ma, S. (2015) · Current Drug Targets · doi:10.2174/1389450116666151001103948 · Cited by 116 · see citing works
A cell wall recycling shortcut that bypasses peptidoglycan de novo biosynthesis
Gisin, J., Schneider, A., Nägele, B., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1289 · Cited by 113 · see citing works
Dissemination of blaNDM-5 gene via an IncX3-type plasmid among non-clonal Escherichia coli in China
Li, X., Fu, Y., Shen, M., et al. (2018) · Antimicrobial Resistance and Infection Control · doi:10.1186/s13756-018-0349-6 · Cited by 113 · see citing works
Parallel Evolution of Tobramycin Resistance across Species and Environments
Scribner, M. R., Santos-López, A., Marshall, C. W., et al. (2020) · mBio · doi:10.1128/mbio.00932-20 · Cited by 113 · see citing works
Zimmermann, S., Klinger-Strobel, M., Bohnert, J. A., Wendler, S., Rödel, J., Pletz, M. W., Löffler, B., & Tuchscherr, L. P. N. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02762 · Cited by 110 · see citing works
Huang, J., Li, C., Song, J., Velkov, T., Wang, L., Zhu, Y., & Li, J. (2020) · Future Microbiology · doi:10.2217/fmb-2019-0322 · Cited by 109 · see citing works
micF RNA binds to the 5' end of ompF mRNA and to a protein from Escherichia coli
Andersen, J., & Delihas, N. (1990) · Biochemistry · doi:10.1021/bi00491a020 · Cited by 105 · see citing works
Synthetic lipopeptides: a novel class of anti-infectives
Jerala, R. (2007) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.16.8.1159 · Cited by 105 · see citing works
Ribosome protection by antibiotic resistance ATP-binding cassette protein
Su, W., Kumar, V., Ding, Y., Ero, R., Serra, A., Lee, B. S. T., Wong, A. S. W., Shi, J. R., Sze, S. K., Yang, L., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1803313115 · Cited by 103 · see citing works
An Evolutionarily Conserved Mechanism for Intrinsic and Transferable Polymyxin Resistance
Xu, Y., Wei, W., Lei, S., et al. (2018) · mBio · doi:10.1128/mbio.02317-17 · Cited by 102 · see citing works
Mechanisms of Resistance to Trimethoprim, the Sulfonamides, and Trimethoprim-Sulfamethoxazole
Then, R. L. (1982) · Clinical Infectious Diseases · doi:10.1093/clinids/4.2.261 · Cited by 101 · see citing works
Antibiotic resistance by enzyme inactivation: From mechanisms to solutions
De Pascale, G., & Wright, G. D. (2010) · ChemBioChem · doi:10.1002/cbic.201000067 · Cited by 94 · see citing works
Stewart, P. S., White, B., Boegli, L., Hamerly, T., Williamson, K. S., Franklin, M. J., Bothner, B. B., James, G. A., Fisher, S. T., Vital-Lopez, F. G., et al. (2019) · Journal of Bacteriology · doi:10.1128/jb.00307-19 · Cited by 91 · see citing works
Glavier, M., Puvanendran, D., Salvador, D., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18770-5 · Cited by 91 · see citing works
Broad-Spectrum Peptide Inhibitors of Aminoglycoside Antibiotic Resistance Enzymes
Boehr, D. D., Draker, K.-A., Koteva, K. K., Bains, M., Hancock, R. E. W., & Wright, G. D. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00026-7 · Cited by 90 · see citing works
Ever-Adapting RND Efflux Pumps in Gram-Negative Multidrug-Resistant Pathogens: A Race against Time
Zwama, M., & Nishino, K. (2021) · Antibiotics · doi:10.3390/antibiotics10070774 · Cited by 90 · see citing works
A rifamycin inactivating phosphotransferase family shared by environmental and pathogenic bacteria
Spanogiannopoulos, P., Waglechner, N., Koteva, K. K., & Wright, G. D. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402358111 · Cited by 89 · see citing works
Allosteric drug transport mechanism of multidrug transporter AcrB
Tam, H.-K., Foong, W. E., Oswald, C., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24151-3 · Cited by 88 · see citing works
The secondary resistome of multidrug-resistant Klebsiella pneumoniae
Jana, B., Cain, A. K., Doerrler, W. T., Boinett, C. J., Fookes, M. C., Parkhill, J., & Guardabassi, L. (2017) · Scientific Reports · doi:10.1038/srep42483 · Cited by 87 · see citing works
Novotna, G. B., & Janata, J. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00799-06 · Cited by 84 · see citing works
Crowe‐McAuliffe, C., Murina, V., Turnbull, K. J., Kasari, M., Mohamad, M., Polte, C., Takada, H., Vaitkevicius, K., Johansson, J., Ignatova, Z., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23753-1 · Cited by 84 · see citing works
Chatterjee, S., Datta, S., Roy, S., et al. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.01126 · Cited by 83 · see citing works
Structure of the Tripartite Multidrug Efflux Pump AcrAB-TolC Suggests an Alternative Assembly Mode
Kim, J., Jeong, H., Song, S., et al. (2015) · Molecules and Cells · doi:10.14348/molcells.2015.2277 · Cited by 82 · see citing works
Sequence-Specific Targeting of Bacterial Resistance Genes Increases Antibiotic Efficacy
Ayhan, D. H., Tamer, Y. T., Akbar, M. A., Bailey, S. M., Wong, M., Daly, S. M., Greenberg, D. E., & Toprak, E. (2016) · PLoS Biology · doi:10.1371/journal.pbio.1002552 · Cited by 82 · see citing works
Wachino, J.-I., Doi, Y., & Arakawa, Y. (2020) · Infectious Disease Clinics of North America · doi:10.1016/j.idc.2020.06.002 · Cited by 82 · see citing works
Cell Wall Deficiency as a Coping Strategy for Stress
Claessen, D., & Errington, J. (2019) · Trends in Microbiology · doi:10.1016/j.tim.2019.07.008 · Cited by 81 · see citing works
Buckner, M. M. C., Saw, H. T. H., Osagie, R. N., McNally, A., Ricci, V., Wand, M. E., Woodford, N., Ivens, A. C., Webber, M. A., & Piddock, L. J. V. (2018) · mBio · doi:10.1128/mbio.02303-17 · Cited by 80 · see citing works
Self-citationBacteria's different ways to recycle their own cell wall
Mayer, C. A., Kluj, R. M., Mühleck, M., et al. (2019) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2019.06.006 · Cited by 78 · see citing works
Du, D., Neuberger, A., Orr, M. W., Newman, C. E., Hsu, P., Samsudin, F., Harris, A., Ramos, L. M., Debela, M., Khalid, S., et al. (2020) · Structure · doi:10.1016/j.str.2020.03.013 · Cited by 77 · see citing works
Machado, D., Coelho, T. S., Perdigão, J., et al. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00711 · Cited by 76 · see citing works
Gerson, S., Nowak, J., Zander, E., et al. (2018) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dky083 · Cited by 76 · see citing works
The molecular basis of pyrazinamide activity on Mycobacterium tuberculosis PanD
Sun, Q., Li, X., Pérez, L. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-14238-3 · Cited by 76 · see citing works
Monahan, L. G., Turnbull, L., Osvath, S. R., Birch, D., Charles, I. G., & Whitchurch, C. B. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01901-13 · Cited by 75 · see citing works
Rox, a Rifamycin Resistance Enzyme with an Unprecedented Mechanism of Action
Koteva, K. K., Cox, G., Kelso, J., et al. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.01.009 · Cited by 74 · see citing works
Murina, V., Kasari, M., Hauryliuk, V., & Atkinson, G. C. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky050 · Cited by 74 · see citing works
Spatiotemporal dynamics of multidrug resistant bacteria on intensive care unit surfaces
D’Souza, A. W., Potter, R. F., Wallace, M. A., Shupe, A., Patel, S., Sun, X., Gul, D., Kwon, J. H., Andleeb, S., Burnham, C. D., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12563-1 · Cited by 72 · see citing works
First Report of NDM-1-Producing Acinetobacter baumannii Sequence Type 25 in Brazil
Pillonetto, M., Arend, L. N. V. S., Vespero, E. C., et al. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.03444-14 · Cited by 71 · see citing works
Xu, Z., Li, M., Li, Y., Cao, H., Lu, M., Xu, Z., Higuchi, Y., Yamasaki, S., Nishino, K., Woo, P. C. Y., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.10.006 · Cited by 71 · see citing works
Periasamy, H., Joshi, P., Palwe, S. R., Shrivastava, R., Bhagwat, S., & Patel, M. V. (2020) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkaa021 · Cited by 71 · see citing works
The Role of Efflux Pumps in the Transition from Low-Level to Clinical Antibiotic Resistance
Ebbensgaard, A. E., Løbner‐Olesen, A., & Frimodt-Møller, J. (2020) · Antibiotics · doi:10.3390/antibiotics9120855 · Cited by 70 · see citing works
Liao, W., Cui, Y., Quan, J., Zhao, D., Han, X., Shi, Q., Wang, Q. Q., Jiang, Y., Du, X., Li, X., et al. (2022) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2022.106573 · Cited by 69 · see citing works
Issa, K. H. B., Phan, G., & Broutin, I. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00057 · Cited by 66 · see citing works
Morgan, C. E., Glaza, P., Leus, I. V., Trinh, A., Su, C., Cui, M., Zgurskaya, H. I., & Yu, E. W. (2021) · mBio · doi:10.1128/mbio.03690-20 · Cited by 66 · see citing works
Molecular mechanisms of AcrB-mediated multidrug export
Zwama, M., & Yamaguchi, A. (2018) · Research in Microbiology · doi:10.1016/j.resmic.2018.05.005 · Cited by 65 · see citing works
Saw, H. T. H., Webber, M. A., Mushtaq, S., Woodford, N., & Piddock, L. J. V. (2016) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkw028 · Cited by 64 · see citing works
Self-citationCryo-EM structure of multidrug efflux pump MexAB-OprM (0 degree state)
Tsutsumi, K., Yonehara, R., Nakagawa, A., et al. (2018) · Worldwide Protein Data Bank · doi:10.2210/pdb6iok/pdb · Cited by 64 · see citing works
Oswald, C., Tam, H.-K., & Pos, K. M. (2016) · Nature Communications · doi:10.1038/ncomms13819 · Cited by 63 · see citing works
Adler, M., Anjum, M., Andersson, D. I., & Sandegren, L. (2012) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dks368 · Cited by 62 · see citing works
Architecture and roles of periplasmic adaptor proteins in tripartite efflux assemblies
Symmons, M. F., Marshall, R. L., & Bavro, V. N. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00513 · Cited by 61 · see citing works
Spanogiannopoulos, P., Thaker, M., Koteva, K. K., Waglechner, N., & Wright, G. D. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01166-12 · Cited by 61 · see citing works
Rifampin phosphotransferase is an unusual antibiotic resistance kinase
Stogios, P. J., Cox, G., Spanogiannopoulos, P., Pillon, M. C., Waglechner, N., Skarina, T., Koteva, K. K., Guarné, A., Savchenko, A. V., & Wright, G. D. (2016) · Nature Communications · doi:10.1038/ncomms11343 · Cited by 60 · see citing works
Ribosome protection by ABC‐F proteins—Molecular mechanism and potential drug design
Ero, R., Kumar, V., Su, W., et al. (2019) · Protein Science · doi:10.1002/pro.3589 · Cited by 60 · see citing works
Structure of the Ligand-blocked Periplasmic Entrance of the Bacterial Multidrug Efflux Protein TolC
Higgins, M. K., Eswaran, J., Edwards, P. C., Schertler, G. F. X., Hughes, C., & Koronakis, V. E. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.088 · Cited by 59 · see citing works
Binding and Transport of Carboxylated Drugs by the Multidrug Transporter AcrB
Tam, H.-K., Malviya, V. N., Foong, W. E., Herrmann, A., Malloci, G., Ruggerone, P., Vargiu, A. V., & Pos, K. M. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.025 · Cited by 59 · see citing works
The role of potentiating mutations in the evolution of pandemic Escherichia coli clones
Cummins, E., Snaith, A. E., McNally, A., & Hall, R. J. (2021) · European Journal of Clinical Microbiology & Infectious Diseases · doi:10.1007/s10096-021-04359-3 · Cited by 58 · see citing works
Structural insight into YcbB-mediated beta-lactam resistance in Escherichia coli
Caveney, N. A., Caballero, G., Voedts, H., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09507-0 · Cited by 56 · see citing works
Castanheira, M., Doyle, T. B., Smith, C. J., et al. (2019) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkz243 · Cited by 56 · see citing works
Handing, J. W., Ragland, S. A., Bharathan, U. V., et al. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02688 · Cited by 55 · see citing works
Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid
Cox, G., Thompson, G. S., Jenkins, H. T., Peske, F., Savelsbergh, A., Rodnina, M. V., Wintermeyer, W., Homans, S. W., Edwards, T. A., & O’Neill, A. J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117275109 · Cited by 54 · see citing works
The hydrophobic trap—the Achilles heel of RND efflux pumps
Aron, Z. D., & Opperman, T. J. (2017) · Research in Microbiology · doi:10.1016/j.resmic.2017.11.001 · Cited by 54 · see citing works
Yasir, M., Turner, A. K., Bastkowski, S., Baker, D., Page, A. J., Telatin, A., Phan, M., Monahan, L. G., Savva, G. M., Darling, A. E., et al. (2020) · Genome Research · doi:10.1101/gr.254391.119 · Cited by 54 · see citing works
Self-citationPorter domain opening and closing motions in the multi-drug efflux transporter AcrB
Fischer, N., & Kandt, C. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.10.016 · Cited by 53 · see citing works
Crystal structure of the multidrug resistance regulator RamR complexed with bile acids
Yamasaki, S., Nakashima, R., Sakurai, K., et al. (2019) · Scientific Reports · doi:10.1038/s41598-018-36025-8 · Cited by 51 · see citing works
In situ structure of the AcrAB-TolC efflux pump at subnanometer resolution
Chen, M., Shi, X., Yu, Z., Fan, G., Serysheva, I. I., Baker, M. L., Luisi, B. F., Ludtke, S. J., & Wang, Z. (2021) · Structure · doi:10.1016/j.str.2021.08.008 · Cited by 51 · see citing works
Grimsey, E. M., Weston, N., Ricci, V., et al. (2020) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02460-19 · Cited by 49 · see citing works
Cha, H.-J., Müller, R. T., & Pos, K. M. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02733-13 · Cited by 48 · see citing works
MDR Pumps as Crossroads of Resistance: Antibiotics and Bacteriophages
Nazarov, P. A. (2022) · Antibiotics · doi:10.3390/antibiotics11060734 · Cited by 47 · see citing works
Dynamics of Intact MexAB-OprM Efflux Pump: Focusing on the MexA-OprM Interface
López, C. A., Travers, T. S., Pos, K. M., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-16497-w · Cited by 45 · see citing works
Mobile lincosamide resistance genes in staphylococci
Feßler, A. T., Wang, Y., Wu, C., et al. (2018) · Plasmid · doi:10.1016/j.plasmid.2018.06.002 · Cited by 42 · see citing works
McNeil, H. E., Alav, I., Corona-Torres, R., et al. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1008101 · Cited by 42 · see citing works
Self-citationThe Enzymes of the Rifamycin Antibiotic Resistome
Surette, M. D., Spanogiannopoulos, P., & Wright, G. D. (2021) · Accounts of Chemical Research · doi:10.1021/acs.accounts.1c00048 · Cited by 42 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Tackling the outer membrane: facilitating compound entry into Gram-negative bacterial pathogens
Saxena, D., Maitra, R., Bormon, R., Czekanska, M., Meiers, J., Titz, A., Verma, S., & Chopra, S. (2023) · npj Antimicrobials and Resistance · doi:10.1038/s44259-023-00016-1 · Cited by 217 · see citing works
Nanozybiotics: advancing antimicrobial strategies through biomimetic mechanisms
Zhou, C., Wang, Q., Cao, H., Jiang, J., & Gao, L. (2024) · Advanced Materials · doi:10.1002/adma.202403362 · Cited by 114 · see citing works
Fu, Y., Dou, Q., Smalla, K., Wang, Y., Johnson, T. A., Brandt, K. K., Mei, Z., Liao, M., Hashsham, S. A., Schäffer, A., et al. (2023) · mLife · doi:10.1002/mlf2.12101 · Cited by 65 · see citing works
Kiu, R., Darby, E. M., Alcon-Giner, C., Acuna-Gonzalez, A., Camargo, A., Lamberte, L. E., Phillips, S., Sim, K., Shaw, A. G., Clarke, P., et al. (2025) · Nature communications · doi:10.1038/s41467-025-62584-2 · Cited by 36 · see citing works
“Ef fl ux pumps, which facilitate multidrug resistance by expelling a broad range of antibiotics 41 , were also prevalent across multiple strains, particularly within Escherichia and Klebsiella , further complicating treatment options for infections by these pathogens in preterm infants.”
Self-citationEl Meouche, I., Jain, P., Jolly, M. K., & Capp, J.-P. (2024) · Translational Oncology · doi:10.1016/j.tranon.2024.102069 · Cited by 22 · see citing works
Grabeck, J., Mayer, J., Miltz, A., Casoria, M., Quagliata, M., Meinberger, D., Klatt, A. R., Wielert, I., Maier, B., Papini, A. M., et al. (2024) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.4c00078 · Cited by 7 · see citing works
Extensive natural variation in bacterial ribosomal drug-binding sites
Ekemezie, C. L., Chan, L. I., Brown, C. R., Helena-Bueno, K., Williams, T. A., & Melnikov, S. V. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115878 · Cited by 2 · see citing works
- Authors
- Darby, E. M., Trampari, E., Siasat, P., Gaya, M. S., Alav, I., Webber, M. A., & Blair, J. M. A.
- Affiliations
- University of Birmingham (GB)
- Quadram Institute (GB)
- University of East Anglia (GB)
- Corresponding author
- Webber, Mark A.
- Blair, Jessica M. A.
- ORCID
- Venue
- Nature Reviews Microbiology
- Published
- 2022-11-21
- Volume
- 21
- Issue
- 5
- Pages
- 280-295
- ISSN
- 1740-1526 (ISSN-L)
- 1740-1534
- OpenAlex
- W4309666648
- Cited by
- 1,398
- References
- 235
- Citations by year
- 2026: 369 · 2025: 497 · 2024: 382 · 2023: 146 · 2022: 2 · 2021: 1
- FWCI
- 19.01
- Type
- journal article
- Language
- en
- Update notices
- correction (2024-02-02)
- Open access
- closed
- Licence
- Locations
- Nature Reviews Microbiology (publishedVersion)
- PubMed (publishedVersion)
- University of Birmingham Research Portal (University of Birmingham) (submittedVersion)
- UEA Digital Repository (University of East Anglia) (submittedVersion)
- Funders
- Medical Research Council (2438035)
- Biotechnology and Biological Sciences Research Council (BBS/E/F/00044426, BBS/E/F/000PR10349)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Antibiotic Resistance in Bacteria
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
- Keywords
- antibiotic resistance, molecular mechanisms of resistance, resistance genes, antibiotic efflux, drug modification
- MeSH terms
- Anti-Bacterial Agents, Bacteria, Drug Resistance, Microbial, Global Health
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review