Molecular mechanisms of antibiotic resistance revisited

Emergence of plasmid-mediated colistin resistance mechanism MCR-1 in animals and human beings in China: a microbiological and molecular biological study.

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

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

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

J 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 3,758

Carbapenemases: the Versatile β-Lactamases

Queenan, A. M., & Bush, K. (2007) · Clinical Microbiology Reviews · doi:10.1128/cmr.00001-07 · Cited by 2,609

Characterization of a New Metallo-β-Lactamase Gene, bla NDM-1 , and a Novel Erythromycin Esterase Gene Carried on a Unique Genetic Structure in Klebsiella pneumoniae Sequence Type 14 from India

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

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

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

The structure of β-lactamases

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

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

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

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

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 1,227

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 1,117

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 1,062

Crystal structure of bacterial multidrug efflux transporter AcrB

Murakami, S., Nakashima, R., Yamashita, E., & Yamaguchi, A. (2002) · Nature · doi:10.1038/nature01050 · Cited by 1,018

The EnteroBase user's guide, with case studies on Salmonella transmissions, Yersinia pestis phylogeny, and Escherichia core genomic diversity

(2019) · doi:10.1101/gr.251678.119 · Cited by 976

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

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

Colistin Resistance in Acinetobacter baumannii Is Mediated by Complete Loss of Lipopolysaccharide Production

Moffatt, 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 858

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

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

Emergence of plasmid-mediated high-level tigecycline resistance genes in animals and humans

He, T., Wang, R., Liu, D., Walsh, T. R., Zhang, R., Lv, Y., Ke, Y., Ji, Q., Wei, R., Liu, Z., et al. (2019) · Nature Microbiology · doi:10.1038/s41564-019-0445-2 · Cited by 713

The Cfr rRNA Methyltransferase Confers Resistance to Phenicols, Lincosamides, Oxazolidinones, Pleuromutilins, and Streptogramin A Antibiotics

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

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

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 702

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

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

Sulfonamide resistance: mechanisms and trends.

Sköld, O. (2000) · Drug Resistance Updates · doi:10.1054/drup.2000.0146 · Cited by 647

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

The bacterial ribosome as a target for antibiotics

Poehlsgaard, J., & Douthwaite, S. R. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1265 · Cited by 618

Mechanisms of vancomycin resistance in Staphylococcus aureus

Gardete, S., & Tomasz, A. (2014) · Journal of Clinical Investigation · doi:10.1172/jci68834 · Cited by 565

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

RifamycinMode of Action, Resistance, and Biosynthesis

Floss, H. G., & Yu, T.-W. (2005) · Chemical Reviews · doi:10.1021/cr030112j · Cited by 547

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 529

ATP-Dependent Persister Formation in Escherichia coli

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

Resistance to Trimethoprim-Sulfamethoxazole

Eliopoulos, G. M., & Huovinen, P. (2001) · Clinical Infectious Diseases · doi:10.1086/320532 · Cited by 500

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 492

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

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 460

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

Structure, function and regulation of Pseudomonas aeruginosa porins

Chevalier, S., Bouffartigues, E., Bodilis, J., Maillot, O., Lesouhaitier, O., Feuilloley, M. G. J., Orange, N., Dufour, A., & Cornélis, P. (2017) · FEMS Microbiology Reviews · doi:10.1093/femsre/fux020 · Cited by 456

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 452

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

Methicillin Resistance in Staphylococcus Aureus: Mechanisms and Modulation

Stapleton, P. D., & Taylor, P. W. (2002) · Science Progress · doi:10.3184/003685002783238870 · Cited by 418

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

Global spread of antibiotic resistance: the example of New Delhi metallo-β-lactamase (NDM)-mediated carbapenem resistance

Johnson, A. P., & Woodford, N. (2013) · Journal of Medical Microbiology · doi:10.1099/jmm.0.052555-0 · Cited by 411

Phage-Antibiotic Synergy Is Driven by a Unique Combination of Antibacterial Mechanism of Action and Stoichiometry

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

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

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

Update on macrolide-lincosamide-streptogramin, ketolide, and oxazolidinone resistance genes: MLSKO genes

Roberts, M. C. (2008) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2008.01145.x · Cited by 392

Molecular mechanisms of vancomycin resistance

Stogios, P. J., & Savchenko, A. V. (2020) · Protein Science · doi:10.1002/pro.3819 · Cited by 388

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 361

Aminoglycoside Resistance

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

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

Proximate and ultimate causes of the bactericidal action of antibiotics

Baquero, F., & Levin, B. R. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-020-00443-1 · Cited by 328

From acids to osmZ: multiple factors influence synthesis of the OmpF and OmpC porins in Escherichia coli

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

Colistin Update on Its Mechanism of Action and Resistance, Present and Future Challenges

Andrade, F. F., Silva, D., Rodrigues, A. G., & Pina‐Vaz, C. (2020) · Microorganisms · doi:10.3390/microorganisms8111716 · Cited by 303

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 297

The folic acid biosynthesis pathway in bacteria: evaluation of potential for antibacterial drug discovery

Bermingham, A., & Derrick, J. P. (2002) · BioEssays · doi:10.1002/bies.10114 · Cited by 295

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

Misread protein creates membrane channels: an essential step in the bactericidal action of aminoglycosides.

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

The Current Burden of Carbapenemases: Review of Significant Properties and Dissemination among Gram-Negative Bacteria

Halat, D. H., & Moubareck, C. A. (2020) · Antibiotics · doi:10.3390/antibiotics9040186 · Cited by 291

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

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

Azithromycin Synergizes with Cationic Antimicrobial Peptides to Exert Bactericidal and Therapeutic Activity Against Highly Multidrug-Resistant Gram-Negative Bacterial Pathogens

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

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

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

The Role of Antibiotic-Target-Modifying and Antibiotic-Modifying Enzymes in Mycobacterium abscessus Drug Resistance

Luthra, S., Rominski, A., & Sander, P. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02179 · Cited by 265

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

Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria

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 249

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

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

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 242

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

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 239

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 232

MicF : an antisense RNA gene involved in response of Escherichia coli to global stress factors 1 1Edited by D. Draper

Delihas, N., & Forst, S. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5029 · Cited by 228

Conserved small protein associates with the multidrug efflux pump AcrB and differentially affects antibiotic resistance

Hobbs, 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

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

Balancing mcr-1 expression and bacterial survival is a delicate equilibrium between essential cellular defence mechanisms

Yang, Q., Li, M., Spiller, O. B., Andrey, D. O., Hinchliffe, P., Li, H., MacLean, R. C., Niumsup, P. R., Powell, L. C., Pritchard, M., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02149-0 · Cited by 213

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

Tetracycline-Inactivating Enzymes

Markley, J. L., & Wencewicz, T. A. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01058 · Cited by 207

Tetracycline-inactivating enzymes from environmental, human commensal, and pathogenic bacteria cause broad-spectrum tetracycline resistance

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 204

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

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

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 187

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

Azithromycin Resistance through Interspecific Acquisition of an Epistasis-Dependent Efflux Pump Component and Transcriptional Regulator in Neisseria gonorrhoeae

Wadsworth, C. B., Arnold, B., Sater, M., & Grad, Y. H. (2018) · mBio · doi:10.1128/mbio.01419-18 · Cited by 180

Overexpression of the MtrC-MtrD-MtrE Efflux Pump Due to an mtrR Mutation Is Required for Chromosomally Mediated Penicillin Resistance in Neisseria gonorrhoeae

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

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

Trimethoprim and other nonclassical antifolates an excellent template for searching modifications of dihydrofolate reductase enzyme inhibitors

Wróbel, A., Arciszewska, K., Maliszewski, D., & Drozdowska, D. (2019) · The Journal of Antibiotics · doi:10.1038/s41429-019-0240-6 · Cited by 175

Novel Plasmid-Mediated tet (X5) Gene Conferring Resistance to Tigecycline, Eravacycline, and Omadacycline in a Clinical Acinetobacter baumannii Isolate

Wang, L., Liu, D., Lv, Y., et al. (2019) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01326-19 · Cited by 174

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 174

The evolution and transmission of multi-drug resistant Escherichia coli and Klebsiella pneumoniae: the complexity of clones and plasmids

Dunn, S. J., Connor, C. H., & McNally, A. (2019) · Current Opinion in Microbiology · doi:10.1016/j.mib.2019.06.004 · Cited by 172

Trimethoprim: Mechanisms of Action, Antimicrobial Activity, Bacterial Resistance, Pharmacokinetics, Adverse Reactions, and Therapeutic Indications

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

Daptomycin Resistance in Enterococci Is Associated with Distinct Alterations of Cell Membrane Phospholipid Content

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

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 168

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

Lincosamides, Streptogramins, Phenicols, and Pleuromutilins: Mode of Action and Mechanisms of ResistancePreprint

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 162

Factors essential for L,D-transpeptidase-mediated peptidoglycan cross-linking and β-lactam resistance in Escherichia coli

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

Efflux pump inhibitors: targeting mycobacterial efflux systems to enhance TB therapy

Pule, C. M., Sampson, S. L., Warren, R. M., Black, P. A., van Helden, P. D., Victor, T. C., & Louw, G. (2015) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkv316 · Cited by 157

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

(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 151

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 150

Transferable Mechanisms of Quinolone Resistance from 1998 Onward

Ruiz, J. (2019) · Clinical Microbiology Reviews · doi:10.1128/cmr.00007-19 · Cited by 149

Does microbial resistance or adaptation to biocides create a hazard in infection prevention and control?

Meyer, B., & Cookson, B. (2010) · Journal of Hospital Infection · doi:10.1016/j.jhin.2010.05.020 · Cited by 147

Altered Antibiotic Transport in OmpC Mutants Isolated from a Series of Clinical Strains of Multi-Drug Resistant E. coli

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

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

Outer membrane permeability: Antimicrobials and diverse nutrients bypass porins in Pseudomonas aeruginosa

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 141

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 140

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 136

Structures of the wild-type MexAB–OprM tripartite pump reveal its complex formation and drug efflux mechanism

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

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

MarA, SoxS and Rob of Escherichia coli – Global Regulators of Multidrug Resistance, Virulence and Stress Response

Duval, V. (2013) · International Journal of Biotechnology for Wellness Industries · doi:10.6000/1927-3037.2013.02.03.2 · Cited by 134

The multiple antibiotic resistance operon of enteric bacteria controls DNA repair and outer membrane integrity

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

The outer parts of the mycobacterial envelope as permeability barriers

Draper, P. (1998) · Frontiers in bioscience · doi:10.2741/a360 · Cited by 132

Emerging High‐Level Tigecycline Resistance: Novel Tetracycline Destructases Spread via the Mobile Tet(X)

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

Intrinsic rifamycin resistance of Mycobacterium abscessus is mediated by ADP-ribosyltransferase MAB_0591

Rominski, A., Roditscheff, A., Selchow, P., Böttger, E. C., & Sander, P. (2016) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkw466 · Cited by 130

Clinical Implications of Genomic Adaptation and Evolution of Carbapenem-Resistant Klebsiella pneumoniae

Gomez‐Simmonds, A., & Uhlemann, A. (2017) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiw378 · Cited by 130

Ciprofloxacin-Resistant Salmonella enterica Serovar Typhimurium Strains Are Difficult To Select in the Absence of AcrB and TolC

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

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

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

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

Reviving Antibiotics: Efflux Pump Inhibitors That Interact with AcrA, a Membrane Fusion Protein of the AcrAB-TolC Multidrug Efflux Pump

Abdali, N., Parks, J. M., Haynes, K. M., et al. (2016) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.6b00167 · Cited by 124

Extended spectrum beta-lactamase and metallo beta-lactamase production among Escherichia coli and Klebsiella pneumoniae isolated from different clinical samples in a tertiary care hospital in Kathmandu, Nepal

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

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

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

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

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

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

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

Clinically Approved Drugs Inhibit the Staphylococcus aureus Multidrug NorA Efflux Pump and Reduce Biofilm Formation

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

Regulating Polymyxin Resistance in Gram-Negative Bacteria: Roles of Two-Component Systems PhoPQ and PmrAB

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

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 108

Parallel Evolution of Tobramycin Resistance across Species and Environments

Scribner, M. R., Santos-López, A., Marshall, C. W., Deitrick, C., & Cooper, V. S. (2020) · mBio · doi:10.1128/mbio.00932-20 · Cited by 107

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

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

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 104

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

Antibiotic export by MexB multidrug efflux transporter is allosterically controlled by a MexA-OprM chaperone-like complex

Glavier, M., Puvanendran, D., Salvador, D., Décossas, M., Phan, G., Garnier, C., Frezza, E., Cece, Q., Schoehn, G., Picard, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18770-5 · Cited by 102

Conceptual Model of Biofilm Antibiotic Tolerance That Integrates Phenomena of Diffusion, Metabolism, Gene Expression, and Physiology

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 96

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

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

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

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

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

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

Structural basis of ABCF-mediated resistance to pleuromutilin, lincosamide, and streptogramin A antibiotics in Gram-positive pathogens

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 86

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 85

A New Evolutionary Variant of the Streptogramin A Resistance Protein, Vga(A) LC , from Staphylococcus haemolyticus with Shifted Substrate Specificity towards Lincosamides

Novotna, G. B., & Janata, J. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00799-06 · Cited by 84

Interactions of a Bacterial RND Transporter with a Transmembrane Small Protein in a Lipid Environment

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 84

Carbapenem Resistance in Acinetobacter baumannii and Other Acinetobacter spp. Causing Neonatal Sepsis: Focus on NDM-1 and Its Linkage to ISAba125

Chatterjee, S., Datta, S., Roy, S., et al. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.01126 · Cited by 83

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

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

Aminoglycoside Resistance

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

Clinically Relevant Plasmid-Host Interactions Indicate that Transcriptional and Not Genomic Modifications Ameliorate Fitness Costs of Klebsiella pneumoniae Carbapenemase-Carrying Plasmids

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

Bacteria'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

Interplay between Mutations and Efflux in Drug Resistant Clinical Isolates of Mycobacterium tuberculosis

Machado, D., Coelho, T. S., Perdigão, J., et al. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00711 · Cited by 76

Diversity of mutations in regulatory genes of resistance-nodulation-cell division efflux pumps in association with tigecycline resistance in Acinetobacter baumannii

Gerson, S., Nowak, J., Zander, E., et al. (2018) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dky083 · Cited by 76

Antibiotic resistance ABCF proteins reset the peptidyl transferase centre of the ribosome to counter translational arrest

Murina, V., Kasari, M., Hauryliuk, V., & Atkinson, G. C. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky050 · Cited by 76

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

Rapid Conversion of Pseudomonas aeruginosa to a Spherical Cell Morphotype Facilitates Tolerance to Carbapenems and Penicillins but Increases Susceptibility to Antimicrobial Peptides

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

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 75

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

Functional Mechanism of the Efflux Pumps Transcription Regulators From Pseudomonas aeruginosa Based on 3D Structures

Issa, K. H. B., Phan, G., & Broutin, I. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00057 · Cited by 74

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

Native CRISPR-Cas-Mediated Genome Editing Enables Dissecting and Sensitizing Clinical Multidrug-Resistant P. aeruginosa

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

High prevalence of Escherichia coli clinical isolates in India harbouring four amino acid inserts in PBP3 adversely impacting activity of aztreonam/avibactam

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

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

High prevalence of colistin resistance and mcr-9/10 genes in Enterobacter spp. in a tertiary hospital over a decade

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

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 68

Cryoelectron Microscopy Structures of AdeB Illuminate Mechanisms of Simultaneous Binding and Exporting of Substrates

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 67

Influence of acquired -lactamases on the evolution of spontaneous carbapenem resistance in Escherichia coli

Adler, M., Anjum, M., Andersson, D. I., & Sandegren, L. (2012) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dks368 · Cited by 65

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

Inactivation or inhibition of AcrAB-TolC increases resistance of carbapenemase-producing Enterobacteriaceae to carbapenems

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

Cryo-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

Transport of lipophilic carboxylates is mediated by transmembrane helix 2 in multidrug transporter AcrB

Oswald, C., Tam, H.-K., & Pos, K. M. (2016) · Nature Communications · doi:10.1038/ncomms13819 · Cited by 63

Structural insight into YcbB-mediated beta-lactam resistance in Escherichia coli

Caveney, N. A., Caballero, G., Voedts, H., Niciforovic, A. P., Worrall, L. J., Vuckovic, M., Fonvielle, M., Hugonnet, J., Arthur, M., & Strynadka, N. C. J. (2019) · Nature Communications · doi:10.1038/s41467-019-09507-0 · Cited by 63

Characterization of a Rifampin-Inactivating Glycosyltransferase from a Screen of Environmental Actinomycetes

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 62

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 61

Ribosome protection by ABC‐F proteins—Molecular mechanism and potential drug design

Ero, R., Kumar, V., Su, W., & Gao, Y. (2019) · Protein Science · doi:10.1002/pro.3589 · Cited by 60

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

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

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

Combination of MexAB-OprM overexpression and mutations in efflux regulators, PBPs and chaperone proteins is responsible for ceftazidime/avibactam resistance in Pseudomonas aeruginosa clinical isolates from US hospitals

Castanheira, M., Doyle, T. B., Smith, C. J., et al. (2019) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkz243 · Cited by 56

The MtrCDE Efflux Pump Contributes to Survival of Neisseria gonorrhoeae From Human Neutrophils and Their Antimicrobial Components

Handing, J. W., Ragland, S. A., Bharathan, U. V., et al. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02688 · Cited by 55

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

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

TraDIS-Xpress: a high-resolution whole-genome assay identifies novel mechanisms of triclosan action and resistancePreprint

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

Porter 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

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

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

Overexpression of RamA, Which Regulates Production of the Multidrug Resistance Efflux Pump AcrAB-TolC, Increases Mutation Rate and Influences Drug Resistance Phenotype

Grimsey, E. M., Weston, N., Ricci, V., et al. (2020) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02460-19 · Cited by 49

Switch-Loop Flexibility Affects Transport of Large Drugs by the Promiscuous AcrB Multidrug Efflux Transporter

Cha, H.-J., Müller, R. T., & Pos, K. M. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02733-13 · Cited by 48

MDR Pumps as Crossroads of Resistance: Antibiotics and Bacteriophages

Nazarov, P. A. (2022) · Antibiotics · doi:10.3390/antibiotics11060734 · Cited by 48

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

The 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 43

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

Identification of binding residues between periplasmic adapter protein (PAP) and RND efflux pumps explains PAP-pump promiscuity and roles in antimicrobial resistance

McNeil, H. E., Alav, I., Corona-Torres, R., et al. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1008101 · Cited by 42

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

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

Gut microbiota research nexus: One Health relationship between human, animal, and environmental resistomes

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

Impact of early life antibiotic and probiotic treatment on gut microbiome and resistome of very-low-birth-weight preterm infants.

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

Drug tolerance and persistence in bacteria, fungi and cancer cells: Role of non-genetic heterogeneity

El Meouche, I., Jain, P., Jolly, M. K., & Capp, J.-P. (2024) · Translational Oncology · doi:10.1016/j.tranon.2024.102069 · Cited by 22

A genetic platform to investigate the functions of bacterial drug efflux pumps

Teelucksingh, T., Thompson, L. K., Zhu, S., Kuehfuss, N. M., Goetz, J. A., Gilbert, S., MacNair, C. R., Geddes‐McAlister, J., Brown, E. D., & Cox, G. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01119-y · Cited by 46

Synthesis and evaluation of fluoroquinolone derivatives as substrate-based inhibitors of bacterial efflux pumps

German, N., Wei, P., Kaatz, G. W., & Kerns, R. J. (2008) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2008.01.042 · Cited by 68

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

Target (MexB)- and Efflux-Based Mechanisms Decreasing the Effectiveness of the Efflux Pump Inhibitor D13-9001 in Pseudomonas aeruginosa PAO1: Uncovering a New Role for MexMN-OprM in Efflux of β-Lactams and a Novel Regulatory Circuit (MmnRS) Controlling MexMN Expression

Ranjitkar, S., Jones, A. K., Mostafavi, M., Zwirko, Z., Iartchouk, O., Barnes, S. W., Walker, J. R., Willis, T. W., Lee, P. S., & Dean, C. R. (2018) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01718-18 · Cited by 23

Screening of medicinal plants of Himachal Pradesh for efflux pump inhibitory activity against Escherichia coli

Kumar, R., Jandaik, S., & Patial., P. (2016) · Journal of Pharmacognosy and Phytochemistry · Cited by 1