References

Efflux pumps of the resistance–nodulation–division family: a perspective of their structure, function, and regulation in gram-negative bacteria. wiley

10.1002/9780470920541.ch3 · ExternalCitation · doi-reference

Developments, applications, and prospects of cryo-electron microscopy

10.1002/pro.3805 · ExternalCitation · doi-reference

The translocation kinetics of antibiotics through porin OmpC: insights from structure-based solvation mapping using WaterMap

10.1002/prot.24185 · ExternalCitation · doi-reference

Artificial intelligence-based methods for protein structure prediction: a survey

10.1007/s10462-025-11325-4 · ExternalCitation · doi-reference

A deep learning approach to antibiotic discovery

10.1016/j.cell.2020.01.021 · ExternalCitation · doi-reference

Mutations inside rifampicin-resistance determining region of rpoB gene associated with rifampicin-resistance in Mycobacterium tuberculosis

10.1016/j.jiph.2018.04.005 · ExternalCitation · doi-reference

Structural mechanism for rifampicin inhibition of bacterial RNA polymerase

10.1016/s0092-8674(01)00286-0 · ExternalCitation · doi-reference

Access to effective antimicrobials: a worldwide challenge

10.1016/s0140-6736(15)00474-2 · ExternalCitation · doi-reference

Global burden of bacterial antimicrobial resistance in 2019: a systematic analysis

10.1016/s0140-6736(21)02724-0 · ExternalCitation · doi-reference

Global antibiotic consumption 2000 to 2010: an analysis of national pharmaceutical sales data

10.1016/s1473-3099(14)70780-7 · ExternalCitation · doi-reference

The epidemiology, pathogenesis, transmission, diagnosis, and management of multidrug-resistant, extensively drug-resistant, and incurable tuberculosis

10.1016/s2213-2600(17)30079-6 · ExternalCitation · doi-reference

Global antibiotic consumption and usage in humans, 2000–18: a spatial modelling study

10.1016/s2542-5196(21)00280-1 · ExternalCitation · doi-reference

How to enter a bacterium: bacterial porins and the permeation of antibiotics

10.1021/acs.chemrev.0c01213 · ExternalCitation · doi-reference

Role of Molecular Dynamics and Related Methods in Drug Discovery.

10.1021/acs.jmedchem.5b01684 · ExternalCitation · doi-reference

Mechanism of quinolone action and resistance

10.1021/bi5000564 · ExternalCitation · doi-reference

Role of the water-metal ion bridge in mediating interactions between quinolones and Escherichia coli topoisomerase IV

10.1021/bi500682e · ExternalCitation · doi-reference

Bacterial resistance to β-lactam antibiotics: compelling opportunism, compelling opportunity

10.1021/cr030102i · ExternalCitation · doi-reference

Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics

10.1038/35030019 · ExternalCitation · doi-reference

Structure of the AcrAB-TolC multidrug efflux pump

10.1038/nature13205 · ExternalCitation · doi-reference

Ribosome-targeting antibiotics and mechanisms of bacterial resistance

10.1038/nrmicro3155 · ExternalCitation · doi-reference

Molecular mechanisms of antibiotic resistance

10.1038/nrmicro3380 · ExternalCitation · doi-reference

Molecular mechanism of plasmid-borne resistance to sulfonamide antibiotics

10.1038/s41467-023-39778-7 · ExternalCitation · doi-reference

Accelerated antimicrobial discovery via deep generative models and molecular dynamics simulations

10.1038/s41551-021-00689-x · ExternalCitation · doi-reference

Methicillin-resistant Staphylococcus aureus: an overview of basic and clinical research

10.1038/s41579-018-0147-4 · ExternalCitation · doi-reference

Antibiotic resistance in the environment

10.1038/s41579-021-00649-x · ExternalCitation · doi-reference

Molecular mechanisms of antibiotic resistance revisited

10.1038/s41579-022-00820-y · ExternalCitation · doi-reference

Highly accurate protein structure prediction with AlphaFold

10.1038/s41586-021-03819-2 · ExternalCitation · doi-reference

Structure of Erm-modified 70S ribosome reveals the mechanism of macrolide resistance

10.1038/s41589-020-00715-0 · ExternalCitation · doi-reference

A structural biology community assessment of AlphaFold2 applications

10.1038/s41594-022-00849-w · ExternalCitation · doi-reference

Structure-guided functional studies of plasmid-encoded dihydrofolate reductases reveal a common mechanism of trimethoprim resistance in Gram-negative pathogens

10.1038/s42003-022-03384-y · ExternalCitation · doi-reference

Characterization of trimethoprim resistant E. coli dihydrofolate reductase mutants by mass spectrometry and inhibition by propargyl-linked antifolates

10.1039/c6sc05235e · ExternalCitation · doi-reference

Catalytic properties of class A beta-lactamases: efficiency and diversity

10.1042/bj3300581 · ExternalCitation · doi-reference

Structure and function of bacterial outer membrane proteins: Barrels in a nutshell

10.1046/j.1365-2958.2000.01983.x · ExternalCitation · doi-reference

Sulfonamide resistance: mechanisms and trends

10.1054/drup.2000.0146 · ExternalCitation · doi-reference

AcrB drug-binding pocket substitution confers clinically relevant resistance and altered substrate specificity

10.1073/pnas.1419939112 · ExternalCitation · doi-reference

Cryo-EM structure of the tetracycline resistance protein TetM in complex with a translating ribosome at 3.9-Å resolution

10.1073/pnas.1501775112 · ExternalCitation · doi-reference

Structure of chloramphenicol acetyltransferase at 1.75-A resolution

10.1073/pnas.85.12.4133 · ExternalCitation · doi-reference

Voltage gating of Escherichia coli porin channels: role of the constriction loop

10.1073/pnas.94.13.6741 · ExternalCitation · doi-reference

Penicillin binding proteins, β-lactams, and lactamases: offensives, attacks, and defensive countermeasures

10.1080/10408410091154228 · ExternalCitation · doi-reference

Mechanisms of resistance to trimethoprim, the sulfonamides, and trimethoprim-sulfamethoxazole

10.1093/clinids/4.2.261 · ExternalCitation · doi-reference

Metabolic pathways and antimicrobial peptide resistance in bacteria

10.1093/jac/dkae128 · ExternalCitation · doi-reference

AlphaFold protein structure database: massively expanding the structural coverage of protein-sequence space with high-accuracy models

10.1093/nar/gkab1061 · ExternalCitation · doi-reference

Role of bacterial efflux pumps in antibiotic resistance, virulence, and strategies to discover novel efflux pump inhibitors

10.1099/mic.0.001333 · ExternalCitation · doi-reference

Structural basis for rifamycin resistance of bacterial RNA polymerase by the three most clinically important RpoB mutations found in Mycobacterium tuberculosis

10.1111/mmi.13606 · ExternalCitation · doi-reference

Antibiotics for emerging pathogens

10.1126/science.1176667 · ExternalCitation · doi-reference

Catalysis and sulfa drug resistance in dihydropteroate synthase

10.1126/science.1214641 · ExternalCitation · doi-reference

The resolution revolution

10.1126/science.1251652 · ExternalCitation · doi-reference

Structure of the A site of Escherichia coli 16S ribosomal RNA complexed with an aminoglycoside antibiotic

10.1126/science.274.5291.1367 · ExternalCitation · doi-reference

Toward dynamic structural biology: two decades of single-molecule Förster resonance energy transfer

10.1126/science.aan1133 · ExternalCitation · doi-reference

Mobile genetic elements associated with antimicrobial resistance

10.1128/cmr.00088-17 · ExternalCitation · doi-reference

Machine learning for antimicrobial resistance prediction: current practice, limitations, and clinical perspective

10.1128/cmr.00179-21 · ExternalCitation · doi-reference

Expression of multidrug resistance efflux pump gene nora is iron responsive in Staphylococcus aureus

10.1128/jb.06582-11 · ExternalCitation · doi-reference

Bacterial metabolism shapes the host-pathogen interface

10.1128/microbiolspec.vmbf-0027-2015 · ExternalCitation · doi-reference

Lantibiotic resistance

10.1128/mmbr.00051-14 · ExternalCitation · doi-reference

Tackling antimicrobial resistance in low-income and middle-income countries

10.1136/bmjgh-2019-002104 · ExternalCitation · doi-reference

Ribosome-targeting antibiotics: modes of action, mechanisms of resistance, and implications for drug design

10.1146/annurev-biochem-062917-011942 · ExternalCitation · doi-reference

Antimicrobial resistance: a global multifaceted phenomenon

10.1179/2047773215y.0000000030 · ExternalCitation · doi-reference

Estimating the burden of antimicrobial resistance: a systematic literature review

10.1186/s13756-018-0336-y · ExternalCitation · doi-reference

High-resolution crystal structures of ribosome-bound chloramphenicol and erythromycin provide the ultimate basis for their competition

10.1261/rna.069260.118 · ExternalCitation · doi-reference

The gram-negative bacterial periplasm: size matters

10.1371/journal.pbio.2004935 · ExternalCitation · doi-reference

Molecular characterisation of trimethoprim resistance in Escherichia coli and Klebsiella pneumoniae during a two year intervention on trimethoprim use

10.1371/journal.pone.0009233 · ExternalCitation · doi-reference

Structure based in silico analysis of quinolone resistance in clinical isolates of Salmonella Typhi from India

10.1371/journal.pone.0126560 · ExternalCitation · doi-reference

Structures of gate loop variants of the AcrB drug efflux pump bound by erythromycin substrate

10.1371/journal.pone.0159154 · ExternalCitation · doi-reference

Daria Van Tyne, Interplay between porin deficiency, fitness, and virulence in carbapenem-non-susceptible Pseudomonas aeruginosa and Enterobacteriaceae

10.1371/journal.ppat.1012902 · ExternalCitation · doi-reference

Understanding antibiotic resistance via outer membrane permeability

10.2147/idr.s156995 · ExternalCitation · doi-reference

<p>Antimicrobial resistance: implications and costs</p>

10.2147/idr.s234610 · ExternalCitation · doi-reference

Understanding the structural mechanisms of antibiotic resistance sets the platform for new discovery

10.2217/fmb.15.78 · ExternalCitation · doi-reference

Global spread of carbapenemase-producing enterobacteriaceae

10.3201/eid1710.110655 · ExternalCitation · doi-reference

Molecular resistance mechanisms to newly approved antibiotics (2017–2025) in WHO priority pathogens

10.3389/fmicb.2025.1719798 · ExternalCitation · doi-reference

Mechanism of antibacterial resistance, strategies and next-generation antimicrobials to contain antimicrobial resistance: a review

10.3389/fphar.2024.1444781 · ExternalCitation · doi-reference

Bacterial resistance to antimicrobial agents

10.3390/antibiotics10050593 · ExternalCitation · doi-reference

Using machine learning to predict antimicrobial resistance―a literature review

10.3390/antibiotics12030452 · ExternalCitation · doi-reference

Outer membrane porins contribute to antimicrobial resistance in gram-negative bacteria

10.3390/microorganisms11071690 · ExternalCitation · doi-reference

Molecular docking and structure-based drug design strategies

10.3390/molecules200713384 · ExternalCitation · doi-reference

Artificial intelligence in virtual screening: transforming drug research and discovery—a review

10.34133/jbioxresearch.0041 · ExternalCitation · doi-reference

Multidrug resistance and major facilitator superfamily antimicrobial efflux pumps of the ESKAPEE pathogen Staphylococcus aureus

10.37349/eds.2025.100897 · ExternalCitation · doi-reference

The macrolides: erythromycin, clarithromycin, and azithromycin

10.4065/74.6.613 · ExternalCitation · doi-reference

Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump AcrB

10.7554/elife.03145 · ExternalCitation · doi-reference