Teixobactin kills bacteria by a two-pronged attack on the cell envelope

Polymorphic transitions in single crystals: A new molecular dynamics method

Parrinello, M., & Rahman, A. (1981) · Journal of Applied Physics · doi:10.1063/1.328693 · Cited by 19,668 · see citing works

Two dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots

Rouser, G., Fleischer, S., & Yamamoto, A. (1970) · Lipids · doi:10.1007/bf02531316 · Cited by 3,280 · see citing works

Attributable deaths and disability-adjusted life-years caused by infections with antibiotic-resistant bacteria in the EU and the European Economic Area in 2015: a population-level modelling analysis

Cassini, A., Högberg, L. D., Plachouras, D., Quattrocchi, A., Hoxha, A., Simonsen, G. S., Colomb-Cotinat, M., Kretzschmar, M., Devleesschauwer, B., Cecchini, M., et al. (2018) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(18)30605-4 · Cited by 2,951 · see citing works

The HADDOCK2.2 Web Server: User-Friendly Integrative Modeling of Biomolecular Complexes

van Zundert, G. C. P., Rodrigues, J. P. G. L. M., Trellet, M., Schmitz, C., Kastritis, P. L., Karaca, E., Melquiond, A. S. J., van Dijk, M., de Vries, S. J., & Bonvin, A. M. J. J. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.09.014 · Cited by 2,785 · see citing works

Definition and testing of the GROMOS force-field versions 54A7 and 54B7

Schmid, N., Eichenberger, A. P., Choutko, A., Riniker, S., Winger, M., Mark, A. E., & A, W. F. V. G. (2011) · European Biophysics Journal · doi:10.1007/s00249-011-0700-9 · Cited by 2,514 · see citing works

A new antibiotic kills pathogens without detectable resistance

Ling, L. L., Schneider, T., Peoples, A. J., Spoering, A. L., Engels, I., Conlon, B. P., Müller, A., Schäberle, T. F., Hughes, D. E., Epstein, S. S., et al. (2015) · Nature · doi:10.1038/nature14098 · Cited by 2,438 · see citing works

Antibacterial drug discovery in the resistance era

Brown, E. D., & Wright, G. D. (2016) · Nature · doi:10.1038/nature17042 · Cited by 2,265 · see citing works

An Automated Force Field Topology Builder (ATB) and Repository: Version 1.0

Malde, A. K., Zuo, L., Breeze, M., Stroet, M., Poger, D., Nair, P. C., Oostenbrink, C., & Mark, A. E. (2011) · Journal of Chemical Theory and Computation · doi:10.1021/ct200196m · Cited by 1,877 · see citing works

Persister cells

Lewis, K. (2010) · Annual Review of Microbiology · doi:10.1146/annurev.micro.112408.134306 · Cited by 1,858 · see citing works

Icy: an open bioimage informatics platform for extended reproducible research

de Chaumont, F., Dallongeville, S., Chenouard, N., Hervé, N., Pop, S., Provoost, T., Meas‐Yedid, V., Pankajakshan, P., Lecomte, T., Montagner, Y. L., et al. (2012) · Nature Methods · doi:10.1038/nmeth.2075 · Cited by 1,538 · see citing works

Drug-target residence time and its implications for lead optimization

Copeland, R. A., Pompliano, D. L., & Meek, T. D. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2082 · Cited by 1,464 · see citing works

Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks

Shen, Y., & Bax, A. (2013) · Journal of Biomolecular NMR · doi:10.1007/s10858-013-9741-y · Cited by 1,123 · see citing works

Video imaging of walking myosin V by high-speed atomic force microscopy

Kodera, N., Yamamoto, D., Ishikawa, R., & Ando, T. (2010) · Nature · doi:10.1038/nature09450 · Cited by 836 · see citing works

Use of the Cell Wall Precursor Lipid II by a Pore-Forming Peptide Antibiotic

Breukink, E. J., Wiedemann, I., van Kraaij, C., Kuipers, O. P., Sahl, H., & KRUIJFF, B. D. (1999) · Science · doi:10.1126/science.286.5448.2361 · Cited by 815 · see citing works

The Science of Antibiotic Discovery

Lewis, K. (2020) · Cell · doi:10.1016/j.cell.2020.02.056 · Cited by 812 · see citing works

Prediction of Hydrophobic (Lipophilic) Properties of Small Organic Molecules Using Fragmental Methods: An Analysis of ALOGP and CLOGP Methods

Ghose, A. K., Viswanadhan, V. N., & Wendoloski, J. J. (1998) · The Journal of Physical Chemistry A · doi:10.1021/jp980230o · Cited by 796 · see citing works

Lipid II as a target for antibiotics

Breukink, E. J., & KRUIJFF, B. D. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2004 · Cited by 702 · see citing works

Activated ClpP kills persisters and eradicates a chronic biofilm infection

Conlon, B. P., Nakayasu, E. S., Fleck, L. E., LaFleur, M. D., Isabella, V. M., Coleman, K., Leonard, S. N., Smith, R. D., Adkins, J., & Lewis, K. (2013) · Nature · doi:10.1038/nature12790 · Cited by 675 · see citing works

Bacterial viability and antibiotic susceptibility testing with SYTOX green nucleic acid stain

Roth, B. L., Poot, M., Yue, S. T., & Millard, P. J. (1997) · Applied and Environmental Microbiology · doi:10.1128/aem.63.6.2421-2431.1997 · Cited by 583 · see citing works

The nisin–lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics

Hsu, S. D., Breukink, E. J., Tischenko, E., Lutters, M., KRUIJFF, B. D., Kaptein, R., Bonvin, A. M. J. J., & van Nuland, N. A. J. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb830 · Cited by 550 · see citing works

Plectasin, a Fungal Defensin, Targets the Bacterial Cell Wall Precursor Lipid II

Schneider, T., Kruse, T., Wimmer, R., Wiedemann, I., Sass, V., Pag, U., Jansen, A., Nielsen, A. K., Mygind, P. H., Raventós, D., et al. (2010) · Science · doi:10.1126/science.1185723 · Cited by 549 · see citing works

Dysregulation of bacterial proteolytic machinery by a new class of antibiotics

Brötz-Oesterhelt, H., Beyer, D., Kroll, H.-P., Endermann, R., Ladel, C., Schroeder, W., Hinzen, B., Raddatz, S., Paulsen, H., Henninger, K., et al. (2005) · Nature Medicine · doi:10.1038/nm1306 · Cited by 505 · see citing works

Fix the antibiotics pipeline

Cooper, M. A., & Shlaes, D. M. (2011) · Nature · doi:10.1038/472032a · Cited by 475 · see citing works

Probability‐based protein secondary structure identification using combined NMR chemical‐shift data

Wang, Y., & Jardetzky, O. (2002) · Protein Science · doi:10.1110/ps.3180102 · Cited by 447 · see citing works

Interactions of Bacterial Cationic Peptide Antibiotics with Outer and Cytoplasmic Membranes of Pseudomonas aeruginosa

Zhang, L., Dhillon, P., Yan, H., Farmer, S., & Hancock, R. E. W. (2000) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.44.12.3317-3321.2000 · Cited by 349 · see citing works

RECOORD: A recalculated coordinate database of 500+ proteins from the PDB using restraints from the BioMagResBank

Nederveen, A. J., Doreleijers, J. F., Vranken, W., Miller, Z., Spronk, C. A. E. M., Nabuurs, S. B., Güntert, P., Livny, M., Markley, J. L., Nilges, M., et al. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20408 · Cited by 340 · see citing works

Lipid II Is an Intrinsic Component of the Pore Induced by Nisin in Bacterial Membranes

Breukink, E. J., van Heusden, H. E., Vollmerhaus, P. J., Świeżewska, E., Brunner, L., Walker, S., Heck, A. J. R., & KRUIJFF, B. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301463200 · Cited by 339 · see citing works

On the Validation of Molecular Dynamics Simulations of Saturated andcis-Monounsaturated Phosphatidylcholine Lipid Bilayers: A Comparison with Experiment

Poger, D., & Mark, A. E. (2009) · Journal of Chemical Theory and Computation · doi:10.1021/ct900487a · Cited by 305 · see citing works

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 · see citing works

Total Correlation Spectroscopy in the Solid State. The Use of Scalar Couplings to Determine the Through-Bond Connectivity

Baldus, M., & Meier, B. H. (1996) · Journal of Magnetic Resonance Series A · doi:10.1006/jmra.1996.0137 · Cited by 253 · see citing works

Vancomycin, a new antibiotic. I. Chemical and biologic properties.

Mh, M., Jm, M., PITTENGER, G. E., Pittenger, R. C., & Wm, S. (1955) · PubMed · Cited by 189 · see citing works

Computational analysis of local membrane properties

Gapsys, V., de Groot, B. L., & Briones, R. (2013) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-013-9684-0 · Cited by 178 · see citing works

Improved magnetization transfer in solid-state NMR with fast magic angle spinning

Weingarth, M. H., Demco, D. E., Bodenhausen, G., & Tékély, P. (2008) · Chemical Physics Letters · doi:10.1016/j.cplett.2008.12.084 · Cited by 152 · see citing works

High-resolution NMR studies of antibiotics in cellular membranes

Medeiros‐Silva, J., Jekhmane, S., Paioni, A. L., Gawarecka, K., Baldus, M., Świeżewska, E., Breukink, E. J., & Weingarth, M. H. (2018) · Nature Communications · doi:10.1038/s41467-018-06314-x · Cited by 142 · see citing works

Structural variations of the cell wall precursor lipid II in Gram-positive bacteria — Impact on binding and efficacy of antimicrobial peptides

Münch, D., & Sahl, H. (2015) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.04.014 · Cited by 122 · see citing works

Total synthesis of teixobactin

Jin, K., Sam, I. H., Po, K. H. L., Lin, D., Zadeh, E. H. G., Chen, S., Yuan, Y., & Li, X. (2016) · Nature Communications · doi:10.1038/ncomms12394 · Cited by 116 · see citing works

Mode of action of teixobactins in cellular membranes

Shukla, R., Medeiros‐Silva, J., Parmar, A., Vermeulen, B. J. A., Das, S. K., Paioni, A. L., Jekhmane, S., Lorent, J. H., Bonvin, A. M. J. J., Baldus, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16600-2 · Cited by 100 · see citing works

Elucidation of the Teixobactin Pharmacophore

Yang, H., Chen, K. H., & Nowick, J. S. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00295 · Cited by 98 · see citing works

1H‐Detected Solid‐State NMR Studies of Water‐Inaccessible Proteins In Vitro and In Situ

Medeiros‐Silva, J., Mance, D., Daniëls, M., Jekhmane, S., Houben, K., Baldus, M., & Weingarth, M. H. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201606594 · Cited by 94 · see citing works

Total Synthesis of Teixobactin

Giltrap, A. M., Dowman, L. J., Nagalingam, G., Ochoa, J. L., Linington, R. G., Britton, W. J., & Payne, R. J. (2016) · Organic Letters · doi:10.1021/acs.orglett.6b01324 · Cited by 93 · see citing works

Polyprenyl phosphates: synthesis and structure-activity relationship for a biosynthetic system of Salmonella anatum O-specific polysaccharide

Данилов, Л. Л., Druzhinina, T. N., Kalinchuk, N. A., Maltsev, S. D., & SHIBAEV, V. N. (1989) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(89)90006-6 · Cited by 90 · see citing works

Design and Syntheses of Highly Potent Teixobactin Analogues against Staphylococcus aureus, Methicillin-Resistant Staphylococcus aureus (MRSA), and Vancomycin-Resistant Enterococci (VRE) in Vitro and in Vivo

Parmar, A., Lakshminarayanan, R., Iyer, A., Mayandi, V., Goh, E. T. L., Lloyd, D. G., Chalasani, M. L. S., Verma, N. K., Prior, S. H., Beuerman, R. W., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01634 · Cited by 90 · see citing works

Synthesis and Biological Evaluation of a Teixobactin Analogue

Jad, Y. E., Acosta, G., Naicker, T., Ramtahal, M. A., El‐Faham, A., Govender, T., Kruger, H. G., de la Torre, B. G., & Alberício, F. (2015) · Organic Letters · doi:10.1021/acs.orglett.5b03176 · Cited by 85 · see citing works

Caught in the Act: Mechanistic Insight into Supramolecular Polymerization-Driven Self-Replication from Real-Time Visualization

Maity, S., Ottelé, J., Santiago, G. M., Frederix, P. W. J. M., Kroon, P., Markovitch, O., Stuart, M. C. A., Marrink, ‪. J., Otto, S., & Roos, W. H. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c02635 · Cited by 75 · see citing works

Low-power decoupling at high spinning frequencies in high static fields

Weingarth, M. H., Bodenhausen, G., & Tékély, P. (2009) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2009.04.015 · Cited by 70 · see citing works

Crystal structure of Staphylococcus aureus transglycosylase in complex with a lipid II analog and elucidation of peptidoglycan synthesis mechanism

Huang, C., Shih, H., Lin, L., Tien, Y.-W., Cheng, T.-J. R., Cheng, W., Wong, C., & Ma, C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1203900109 · Cited by 70 · see citing works

Shifts in the selectivity filter dynamics cause modal gating in K+ channels

Jekhmane, S., Medeiros‐Silva, J., Li, J., Kümmerer, F., Müller-Hermes, C., Baldus, M., Roux, B., & Weingarth, M. H. (2019) · Nature Communications · doi:10.1038/s41467-018-07973-6 · Cited by 70 · see citing works

One-step purification procedure for UDP-N-acetylmuramyl-peptide murein precursors fromBacillus cereus

Kohlrausch, U., & Höltje, J.-V. (1991) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1991.tb04451.x · Cited by 63 · see citing works

Broadband magnetization transfer using moderate radio-frequency fields for NMR with very high static fields and spinning speeds

Weingarth, M. H., Bodenhausen, G., & Tékély, P. (2010) · Chemical Physics Letters · doi:10.1016/j.cplett.2010.01.072 · Cited by 60 · see citing works

Teixobactin analogues reveal enduracididine to be non-essential for highly potent antibacterial activity and lipid II binding

Parmar, A., Iyer, A., Prior, S. H., Lloyd, D. G., Goh, E. T. L., Vincent, C. S., Palmai‐Pallag, T., Bachrati, C. Z., Breukink, E. J., Madder, A., et al. (2017) · Chemical Science · doi:10.1039/c7sc03241b · Cited by 59 · see citing works

NMR Determination of Protein Partitioning into Membrane Domains with Different Curvatures and Application to the Influenza M2 Peptide

Wang, T., Cady, S. D., & Hong, M. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.01.010 · Cited by 50 · see citing works

Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic Pathways

Valbuena, A., Maity, S., Mateu, M. G., & Roos, W. H. (2020) · ACS Nano · doi:10.1021/acsnano.0c03207 · Cited by 49 · see citing works

Enduracididine, a rare amino acid component of peptide antibiotics: Natural products and synthesis

Atkinson, D. J., Naysmith, B. J., Furkert, D. P., & Brimble, M. A. (2016) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.12.226 · Cited by 46 · see citing works

Gram-scale total synthesis of teixobactin promoting binding mode study and discovery of more potent antibiotics

Zong, Y., Fang, F., Meyer, K. J., Wang, L., Ni, Z., Gao, H., Lewis, K., Zhang, J., & Rao, Y. (2019) · Nature Communications · doi:10.1038/s41467-019-11211-y · Cited by 42 · see citing works

X-ray Crystallographic Structure of a Teixobactin Derivative Reveals Amyloid-like Assembly

Yang, H., Wierzbicki, M., Bois, D. R. D., & Nowick, J. S. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b07709 · Cited by 39 · see citing works

2D 1H–31P solid-state NMR studies of the dependence of inter-bilayer water dynamics on lipid headgroup structure and membrane peptides

Doherty, T., & Hong, M. (2008) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2008.10.001 · Cited by 36 · see citing works

Structural and Functional Characterization of MppR, an Enduracididine Biosynthetic Enzyme from Streptomyces hygroscopicus: Functional Diversity in the Acetoacetate Decarboxylase-like Superfamily

Burroughs, A. M., Hoppe, R. W., Goebel, N. C., Sayyed, B. H., Voegtline, T. J., Schwabacher, A. W., Zabriskie, T. M., & Silvaggi, N. R. (2013) · Biochemistry · doi:10.1021/bi400397k · Cited by 32 · see citing works

Structural studies suggest aggregation as one of the modes of action for teixobactin

Öster, C., Walkowiak, G. P., Hughes, D. E., Spoering, A. L., Peoples, A. J., Catherwood, A. C., Tod, J. A., Lloyd, A. J., Herrmann, T., Lewis, K., et al. (2018) · Chemical Science · doi:10.1039/c8sc03655a · Cited by 32 · see citing works

Investigation of the N-Terminus Amino Function of Arg10-Teixobactin

Monaim, S. A. H. A., Noki, S., Ramchuran, E. J., El‐Faham, A., Alberício, F., & de la Torre, B. G. (2017) · Molecules · doi:10.3390/molecules22101632 · Cited by 26 · see citing works

Structural dynamics of the cell wall precursor lipid II in the presence and absence of the lantibiotic nisin

Koch, D. C., Schmidt, T. H., Sahl, H., Kubitscheck, U., & Kandt, C. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.07.024 · Cited by 17 · see citing works

Design, Synthesis, and Study of Lactam and Ring-Expanded Analogues of Teixobactin

Yang, H., Pishenko, A. V., Li, X., & Nowick, J. S. (2019) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.9b02631 · Cited by 17 · see citing works

De Novo Resistance to Arg 10 -Teixobactin Occurs Slowly and Is Costly

Lloyd, D. G., Schofield, B. J., Goddard, M. R., & Taylor, E. J. (2020) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01152-20 · Cited by 16 · see citing works

Visualizing the mode of action and supramolecular assembly of teixobactin analogues in Bacillus subtilis

Morris, M. A., Vallmitjana, A., Grein, F., Schneider, T., Arts, M., Jones, C. R., Nguyen, B. T., Hashemian, M. H., Malek, M., Gratton, E., et al. (2022) · Chemical Science · doi:10.1039/d2sc01388f · Cited by 15 · see citing works

Teixobactin Provides Protection against Inhalation Anthrax in the Rabbit Model

Lawrence, W. S., Peel, J. E., Sivasubramani, S. K., Baze, W. B., Whorton, E. B., Beasley, D. W. C., Comer, J. E., Hughes, D. E., Ling, L. L., & Peterson, J. W. (2020) · Pathogens · doi:10.3390/pathogens9090773 · Cited by 10 · see citing works

Advance in peptide-based drug development: delivery platforms, therapeutics and vaccines

Xiao, W., Jiang, W., Chen, Z., Huang, Y., Mao, J., Zheng, W., Hu, Y., & Shi, J. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02107-5 · Cited by 449 · see citing works

An Overview of the Recent Advances in Antimicrobial Resistance

Oliveira, M. T. D. S., Antunes, W., MOTA, S. R. F., Madureira-Carvalho, Á., Dinis‐Oliveira, R. J., & da Silva, D. D. (2024) · Microorganisms · doi:10.3390/microorganisms12091920 · Cited by 295 · see citing works

The antibiotic resistance crisis and the development of new antibiotics

Brüssow, H. (2024) · Microbial Biotechnology · doi:10.1111/1751-7915.14510 · Cited by 209 · see citing works

An antibiotic from an uncultured bacterium binds to an immutable target

Shukla, R., Peoples, A. J., Ludwig, K. C., Maity, S., Derks, M. G. N., Benedetti, S. D., Krueger, A. M., Vermeulen, B. J. A., Harbig, T. A., Lavore, F., et al. (2023) · Cell · doi:10.1016/j.cell.2023.07.038 · Cited by 148 · see citing works

Sophisticated natural products as antibiotics

Lewis, K., Lee, R. E., Jr., Brötz‐Oesterhelt, H., Hiller, S., Rodnina, M. V., Schneider, T., Weingarth, M. H., & Wohlgemuth, I. (2024) · Nature · doi:10.1038/s41586-024-07530-w · Cited by 144 · see citing works

pH‐Triggered Size‐Transformable and Bioactivity‐Switchable Self‐Assembling Chimeric Peptide Nanoassemblies for Combating Drug‐Resistant Bacteria and Biofilms

Tan, P., Wu, C., Tang, Q., Wang, T., Zhou, C., Ding, Y., Fu, H., Xu, S., Feng, Y., Zhang, Y., et al. (2023) · Advanced Materials · doi:10.1002/adma.202210766 · Cited by 121 · see citing works

Tuning sterol extraction kinetics yields a renal-sparing polyene antifungal

Maji, A., Soutar, C. P., Zhang, J., Lewandowska, A., Uno, B. E., Su, Y. R., Shelke, Y. G., Murhade, G. M., Nimerovsky, E., Borcik, C. G., et al. (2023) · Nature · doi:10.1038/s41586-023-06710-4 · Cited by 108 · see citing works

A Review of Antibacterial Candidates with New Modes of Action

Butler, M. S., Vollmer, W., Goodall, E. C. A., Capon, R. J., Henderson, I. R., & Blaskovich, M. A. T. (2024) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.4c00218 · Cited by 102 · see citing works

Multitarget antibacterial drugs: An effective strategy to combat bacterial resistance

Jin, F., Zheng, Y., Ma, W., Ihsan, A., Hao, H., Cheng, G., & Wang, X. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108550 · Cited by 81 · see citing works

An Overview of Stimuli-Responsive Intelligent Antibacterial Nanomaterials

Zhang, J., Tang, W., Zhang, X., Song, Z., & Tong, T. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15082113 · Cited by 79 · see citing works

Vancomycin-resistant Enterococcus faecium: A current perspective on resilience, adaptation, and the urgent need for novel strategies

Almeida-Santos, A. C., Novais, C., Peixe, L. M. S. V., & Freitas, A. R. (2025) · Journal of Global Antimicrobial Resistance · doi:10.1016/j.jgar.2025.01.016 · Cited by 73 · see citing works

Current Promising Strategies against Antibiotic-Resistant Bacterial Infections

Ye, J.-Z., & Chen, X. (2022) · Antibiotics · doi:10.3390/antibiotics12010067 · Cited by 71 · see citing works

Cuproptosis to Cuproptosis‐Like: Therapeutic Strategies for Bacterial Infection

Wang, W., Gui, H., Wei, X., Liu, H., & Wang, X. (2025) · Advanced Materials · doi:10.1002/adma.202506119 · Cited by 68 · see citing works

Novel antimicrobial strategies to treat multi‐drug resistant Staphylococcus aureus infections

Douglas, E. J. A., Wulandari, S. W., Lovell, S., & Laabei, M. (2023) · Microbial Biotechnology · doi:10.1111/1751-7915.14268 · Cited by 70 · see citing works

A review of current antibiotic resistance and promising antibiotics with novel modes of action to combat antibiotic resistance

Lei, C., Kumar, S., & Wu, H. (2023) · Archives of Microbiology · doi:10.1007/s00203-023-03699-2 · Cited by 67 · see citing works

Five ways science is tackling the antibiotic resistance crisis

Dance, A. (2024) · Nature · doi:10.1038/d41586-024-02601-4 · Cited by 66 · see citing works

BODIPY‐Functionalized Natural Polymer Coatings for Multimodal Therapy of Drug‐Resistant Bacterial Infection

Zhang, L., Hu, C., Sun, M., Ding, X., Cheng, H., Duan, S., & Xu, F. (2023) · Advanced Science · doi:10.1002/advs.202300328 · Cited by 65 · see citing works

Connecting metabolome and phenotype: recent advances in functional metabolomics tools for the identification of bioactive natural products

Vitale, G. A., Geibel, C., Minda, V., Wang, M., Aron, A. T., & Petras, D. (2024) · Natural Product Reports · doi:10.1039/d3np00050h · Cited by 66 · see citing works

Antimicrobial Action Mechanisms of Natural Compounds Isolated from Endophytic Microorganisms

Eshboev, F., Mamadalieva, N. Z., Nazarov, P. A., Hussain, H., Katanaev, V. L., Egamberdieva, D., & Azimova, S. S. (2024) · Antibiotics · doi:10.3390/antibiotics13030271 · Cited by 69 · see citing works

Spatiotemporal resolution in high-speed atomic force microscopy for studying biological macromolecules in action

Umeda, K., McArthur, S. J., & Kodera, N. (2023) · Microscopy · doi:10.1093/jmicro/dfad011 · Cited by 49 · see citing works

Global health perspectives on antibacterial drug discovery and the preclinical pipeline

Theuretzbacher, U., Jumde, R. P., Hennessy, A. J., Cohn, J., & Piddock, L. J. V. (2025) · Nature Reviews Microbiology · doi:10.1038/s41579-025-01167-w · Cited by 49 · see citing works

Host defence peptide plectasin targets bacterial cell wall precursor lipid II by a calcium-sensitive supramolecular mechanism

Jekhmane, S., Derks, M. G. N., Maity, S., Slingerland, C. J., Tehrani, K. H. M. E., Medeiros‐Silva, J., Charitou, V., Ammerlaan, D., Fetz, C., Consoli, N. A., et al. (2024) · Nature Microbiology · doi:10.1038/s41564-024-01696-9 · Cited by 47 · see citing works

Efflux pump gene amplifications bypass necessity of multiple target mutations for resistance against dual-targeting antibiotic

Silva, K. P. T., Sundar, G., & Khare, A. (2023) · Nature Communications · doi:10.1038/s41467-023-38507-4 · Cited by 44 · see citing works

Synthesis and Biological Evaluation of Piperazine Hybridized Coumarin Indolylcyanoenones with Antibacterial Potential

Zeng, C., Avula, S. R., Meng, J. P., & Zhou, C. (2023) · Molecules · doi:10.3390/molecules28062511 · Cited by 41 · see citing works

Smart responsive materials for antibacterial therapy: Progress, opportunities, and challenges

Fu, J., Wang, C., Liu, X., Zhu, S., Zheng, Y., Li, Z., Cui, Z., Zhang, Y., Jiang, H., Cao, Y., et al. (2025) · Progress in Materials Science · doi:10.1016/j.pmatsci.2025.101532 · Cited by 42 · see citing works

Lateral membrane organization as target of an antimicrobial peptidomimetic compound

Melcrová, A., Maity, S., Melcr, J., de Kok, N. A. W., Gabler, M., van der Eyden, J., Stensen, W., Svendsen, J. S. M., Driessen, A. J. M., Marrink, ‪. J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39726-5 · Cited by 44 · see citing works

Proteolytic-resistant self-assembling peptide nanofibers combat specific bacterial infections via trap and kill

Yu, W., Zhao, M., Guo, X., Wang, X., Wang, J., Lyu, Y., & Shan, A. (2025) · Science Advances · doi:10.1126/sciadv.adx0153 · Cited by 40 · see citing works

Single Atom Engineered Antibiotics Overcome Bacterial Resistance

Panáček, D., Belza, J., Hochvaldová, L., Baďura, Z., Zoppellaro, G., Šrejber, M., Malina, T., Šedajová, V., Paloncýová, M., Langer, R., et al. (2024) · Advanced Materials · doi:10.1002/adma.202410652 · Cited by 37 · see citing works

Bacterial cell envelope-targeting antibiotics

Ntallis, C., Martin, N. I., Edwards, A. M., & Weingarth, M. H. (2025) · Nature Reviews Microbiology · doi:10.1038/s41579-025-01247-x · Cited by 40 · see citing works

Dipolar Recoupling in Rotating Solids

Ladizhansky, V., Palani, R. S., Mardini, M., & Griffin, R. G. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00373 · Cited by 34 · see citing works

Strategic re-engineering of antibiotics

Homer, J. A., Johnson, R. M., Koelln, R. A., Moorhouse, A. D., & Moses, J. E. (2024) · Nature Reviews Bioengineering · doi:10.1038/s44222-024-00250-w · Cited by 35 · see citing works

Novel antimicrobial peptides modified with fluorinated sulfono-γ-AA having high stability and targeting multidrug-resistant bacteria infections

Guo, X., Miao, X., An, Y., Yan, T., Jia, Y. X., Deng, B., Cai, J., Yang, W., Sun, W., Wang, R., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.116001 · Cited by 31 · see citing works

Copper‐Doped Prussian Blue Nanozymes: Targeted Starvation Therapy Against Gram‐Positive Bacteria via the ABC Transporter Inhibition

Zhang, W., Niu, Q., Cui, Y., Fan, K., & Wang, X. (2025) · Advanced Functional Materials · doi:10.1002/adfm.202507939 · Cited by 31 · see citing works

Solid-state NMR structure determination of a membrane protein in E. coli cellular inner membrane

Xie, H., Zhao, Y., Zhao, W., Chen, Y. J., Liu, M., & Yang, J. (2023) · Science Advances · doi:10.1126/sciadv.adh4168 · Cited by 30 · see citing works

Analyzing mechanisms of action of antimicrobial peptides on bacterial membranes requires multiple complimentary assays and different bacterial strains

Wang, X., van Beekveld, R. A. M., Xu, Y., Parmar, A., Das, S. K., Singh, I. S., & Breukink, E. J. (2023) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2023.184160 · Cited by 30 · see citing works

In situ captured antibacterial action of membrane-incising peptide lamellae

el Battioui, K., Chakraborty, S., Wacha, A., Molnár, D., Quemé‐Peña, M., Szigyártó, I. C., Szabó, C. L., Bodor, A., Horváti, K., Gyulai, G., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47708-4 · Cited by 28 · see citing works

Engineering the interaction of short antimicrobial peptides with bacterial barriers

Montis, C., Marelli, E., Valle, F., Bombelli, F. B., & Pigliacelli, C. (2024) · Molecular Systems Design & Engineering · doi:10.1039/d4me00021h · Cited by 25 · see citing works

Metabolic engineering approaches for the biosynthesis of antibiotics

Yook, G., Nam, J., Jo, Y.-M., Yoon, H. S., & Yang, D. (2025) · Microbial Cell Factories · doi:10.1186/s12934-024-02628-2 · Cited by 23 · see citing works

Recent Advances and Future Prospects in Biological-Membrane-Targeted Polymers

Chen, R., Liu, Y., Jiang, Y., Sun, M., Fan, Z., & Du, J. (2025) · Polymer science & technology. · doi:10.1021/polymscitech.5c00014 · Cited by 22 · see citing works

BroadAMP-GPT: AI-Driven generation of broad-spectrum antimicrobial peptides for combating multidrug-resistant ESKAPE pathogens

Li, Y., Xu, X., Zhang, X., Xu, Z., Zhao, J., Zhu, R., Wang, Z., Ran, W., Zhao, W., Yan, N., et al. (2025) · Gut Microbes · doi:10.1080/19490976.2025.2523811 · Cited by 25 · see citing works

Targeting membrane-bound bacterial cell wall precursors: a tried and true antibiotic strategy in nature and the clinic

Buijs, N. P., Matheson, E. J., Cochrane, S. A., & Martin, N. I. (2023) · Chemical Communications · doi:10.1039/d3cc01070h · Cited by 23 · see citing works

A critical view of antimicrobial peptides: exploring their potential and the barriers to realization

Dad, N., Elsawy, M. A., Humphreys, G. J., Pluen, A., Lu, J. R., & McBain, A. J. (2025) · Journal of Applied Microbiology · doi:10.1093/jambio/lxaf087 · Cited by 22 · see citing works

A Bioinspired Lipopeptide Surmounts Therapeutic Dilemmas of Gram-Positive and Gram-Negative Polymicrobial Infection

Zou, D., Deng, K., Zeng, Z., Gong, W., Guo, B., Liu, Y., Xie, Y., Li, Y., & Xu, X. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c10219 · Cited by 22 · see citing works

Screening and identification of antimicrobial peptides from the gut microbiome of cockroach Blattella germanica

Chen, S., Qi, H., Zhu, X., Liu, T., Teng, Y., Gong, Q., 贾藏芝, Liu, T., Chen, S., Qi, H., et al. (2024) · Microbiome · doi:10.1186/s40168-024-01985-9 · Cited by 21 · see citing works

Antibiotic candidates for Gram-positive bacterial infections induce multidrug resistance

Martins, A., Judák, F., Farkas, Z. J., Szili, P. É., Grézal, G., Csörgő, B., Czikkely, M. S., Maharramov, E., Daruka, L., Spohn, R., et al. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.adl2103 · Cited by 22 · see citing works

Vancomycin–Teixobactin Conjugates

Padilla, M. S. T. L., & Nowick, J. S. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c17175 · Cited by 20 · see citing works

Nanofiber Peptides for Bacterial Trapping: A Novel Approach to Antibiotic Alternatives in Wound Infections

Yang, H. L., Wang, J., Wang, X., Wang, S., Xu, J., Shan, Q., Wang, J., Ma, X., & Zhu, Y. (2024) · Advanced Healthcare Materials · doi:10.1002/adhm.202304657 · Cited by 20 · see citing works

Proton-Detected Solid-State NMR for Deciphering Structural Polymorphism and Dynamic Heterogeneity of Cellular Carbohydrates in Pathogenic Fungi

Yarava, J. R., Gautam, I., Jacob, A., Fu, R., & Wang, T. (2025) · bioRxiv · doi:10.1021/jacs.5c04054 · Cited by 21 · see citing works

Synthesis and structure–activity relationship studies of N-terminal analogues of the lipopeptide antibiotics brevicidine and laterocidine

Ballantine, R. D., Ayed, K. A., Bann, S. J., Hoekstra, M., Martin, N. I., & Cochrane, S. A. (2022) · RSC Medicinal Chemistry · doi:10.1039/d2md00281g · Cited by 19 · see citing works

Cellular Applications of DNP Solid‐State NMR – State of the Art and a Look to the Future

Beriashvili, D., Zhou, J., Liu, Y., Folkers, G. E., & Baldus, M. (2024) · Chemistry - A European Journal · doi:10.1002/chem.202400323 · Cited by 19 · see citing works

Monitoring the conformational ensemble and lipid environment of a mechanosensitive channel under cyclodextrin-induced membrane tension

Lane, B. J., Ma, Y., Yan, N., Wang, B., Ackermann, K., Karamanos, T. K., Bode, B. E., & Pliotas, C. (2024) · Structure · doi:10.1016/j.str.2024.02.020 · Cited by 18 · see citing works

NRPStransformer, an Accurate Adenylation Domain Specificity Prediction Algorithm for Genome Mining of Nonribosomal Peptides

Zhang, Z., Zhou, Y., Xie, S., Liu, R., Huang, Z., Kumar, P. S., Feng, G., Yuan, F., & Zhang, L. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c08076 · Cited by 18 · see citing works

Medium-sized peptides from microbial sources with potential for antibacterial drug development

Chen, J., Wang, W., Hu, X., Yue, Y., Lu, X., Wang, C., Wei, B., Zhang, H., & Wang, H. (2024) · Natural Product Reports · doi:10.1039/d4np00002a · Cited by 18 · see citing works

Plasma Membrane-Cell Wall Feedback in Bacteria

García‐Heredia, A. (2023) · Journal of Bacteriology · doi:10.1128/jb.00433-22 · Cited by 17 · see citing works

Returning to Nature for the Next Generation of Antimicrobial Therapeutics

MacNair, C. R., Tsai, C. N., Rutherford, S. T., & Tan, M. (2023) · Antibiotics · doi:10.3390/antibiotics12081267 · Cited by 19 · see citing works

Overcoming Nanosilver Resistance: Resensitizing Bacteria and Targeting Evolutionary Mechanisms

Sun, R. Q., Cui, Y., Wu, Y., Gao, M., Xue, S., Li, R., Zbořil, R., & Zhang, C. (2024) · ACS Nano · doi:10.1021/acsnano.4c15607 · Cited by 17 · see citing works

Pseudo-Phosphorylated Tau Forms Paired Helical Filaments in the Presence of High-Curvature Cholesterol-Containing Lipid Membranes

Mammeri, N. E., Duan, P., & Hong, M. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c13772 · Cited by 16 · see citing works

Combinatorial Screening of Cationic Lipidoids Reveals How Molecular Conformation Affects Membrane-Targeting Antimicrobial Activity

Jennings, J., Ašćerić, D., Semeraro, E. F., Lohner, K., Malanović, N., & Pabst, G. (2023) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.3c05481 · Cited by 16 · see citing works

Real-Time Biosynthetic Reaction Monitoring Informs the Mechanism of Action of Antibiotics

Oluwole, A. O., Hernández‐Rocamora, V. M., Cao, Y., Li, X., Vollmer, W., Robinson, C. V., & Bolla, J. R. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c00081 · Cited by 16 · see citing works

Functional Materials to Overcome Bacterial Barriers and Models to Advance Their Development

Bali, A., Kamal, M. A. M., Mulla, G., Loretz, B., & Lehr, C. (2023) · Advanced Functional Materials · doi:10.1002/adfm.202304370 · Cited by 15 · see citing works

Biomolecular NMR in the AI-assisted structural biology era: Old tricks and new opportunities

Karamanos, T. K., & Matthews, S. (2023) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2023.140949 · Cited by 15 · see citing works

Arg-biodynamers as antibiotic potentiators through interacting with Gram-negative outer membrane lipopolysaccharides

Kamal, M. A. M., Bassil, J., Loretz, B., Hirsch, A. K. H., Lee, S., & Lehr, C. (2024) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2024.114336 · Cited by 15 · see citing works

An Update Review of Approaches to Multiple Action-Based Antibacterials

Bremner, J. B. (2023) · Antibiotics · doi:10.3390/antibiotics12050865 · Cited by 14 · see citing works

The opening dynamics of the lateral gate regulates the activity of rhomboid proteases

Bohg, C., Öster, C., Türkaydin, B., Lisurek, M., Sanchez-Carranza, P., Lange, S., Utesch, T., Sun, H., & Lange, A. (2023) · Science Advances · doi:10.1126/sciadv.adh3858 · Cited by 14 · see citing works

The two‐component system CroRS acts as a master regulator of cell envelope homeostasis to confer antimicrobial tolerance in the bacterial pathogen Enterococcus faecalis

Rose, F. O. T., Darnell, R. L., Morris, S. M., Rose, O. E., Paxie, O., Campbell, G., Cook, G. M., & Gebhard, S. (2023) · Molecular Microbiology · doi:10.1111/mmi.15128 · Cited by 14 · see citing works

Specific Lipid Studies in Complex Membranes by Solid‐State NMR Spectroscopy

van Beekveld, R. A. M., Derks, M. G. N., Kumar, R., Smid, L., Maaß, T., Medeiros‐Silva, J., Breukink, E. J., & Weingarth, M. H. (2022) · Chemistry - A European Journal · doi:10.1002/chem.202202472 · Cited by 14 · see citing works

Chimeric Peptidomimetic Antibiotic Efficiently Neutralizes Lipopolysaccharides (LPS) and Bacteria-Induced Activation of RAW Macrophages

Javed, A., Slingerland, C. J., Wood, T. M., Martin, N. I., Broere, F., Weingarth, M. H., & Veldhuizen, E. J. A. (2023) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.2c00518 · Cited by 14 · see citing works

Discovery of novel xanthotoxin-pyridine quaternary ammonium derivatives with membrane-targeting mode of action as potential antimicrobials against methicillin-resistant Staphylococcus aureus

Xu, S., Zhang, M., Xie, X., Tian, Y., Wang, Y., Wang, X., Yang, R., & Guo, Y. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.118139 · Cited by 13 · see citing works

Exploring the antibiotic potential of cultured ‘unculturable’ bacteria

Wang, X., Deng, Z., & Gao, J. (2023) · Trends in Microbiology · doi:10.1016/j.tim.2023.11.012 · Cited by 13 · see citing works

In Bacterial Membranes Lipid II Changes the Stability of Pores Formed by the Antimicrobial Peptide Nisin

Sheridan, M. S., Pandey, P., & Hansmann, U. H. E. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.4c01249 · Cited by 13 · see citing works

Lipopeptide antibiotics disrupt interactions of undecaprenyl phosphate with UptA

Oluwole, A. O., Kalmankar, N. V., Guida, M., Bennett, J. L., Poce, G., Bolla, J. R., & Robinson, C. V. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2408315121 · Cited by 13 · see citing works

Escherichia coli has an undiscovered ability to inhibit the growth of both Gram-negative and Gram-positive bacteria

Kastrat, E., & Cheng, H. (2024) · Scientific Reports · doi:10.1038/s41598-024-57996-x · Cited by 12 · see citing works

Solid-State NMR 13C sensitivity at high magnetic field

Han, R., Borcik, C. G., Wang, S., Warmuth, O. A., Geohring, K., Mullen, C. G., Incitti, M., Stringer, J. A., & Rienstra, C. M. (2024) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2024.107709 · Cited by 12 · see citing works

Novel antimicrobial strategies for diabetic foot infections: addressing challenges and resistance

Alenazi, F., & Khan, M. S. (2025) · Acta Diabetologica · doi:10.1007/s00592-024-02438-3 · Cited by 12 · see citing works

Systematic Determination of the Impact of Structural Edits on Peptide Accumulation into Mycobacteria

Dash, R., Liu, Z., Lepori, I., Chordia, M. D., Ocius, K. L., Holsinger, K. A., Zhang, H., Kenyon, R., Im, W., Siegrist, M. S., et al. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.5c00330 · Cited by 12 · see citing works

Membrane-Active Antibiotics Affect Domains in Bacterial Membranes as the First Step of Their Activity

Melcrová, A., Klein, C., & Roos, W. H. (2024) · Nano Letters · doi:10.1021/acs.nanolett.4c01873 · Cited by 11 · see citing works

Synthesis and Stereochemical Determination of the Peptide Antibiotic Novo29

Krumberger, M., Li, X., Kreutzer, A. G., Peoples, A. J., Nitti, A. G., Cunningham, V. A., Jones, C. R., Achorn, C., Ling, L. L., Hughes, D. E., et al. (2023) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.2c02648 · Cited by 11 · see citing works

A historical, economic, and technical-scientific approach to the current crisis in the development of antibacterial drugs: Promising role of antibacterial peptides in this scenario

Guevara, Y. A. S., Santos, M. H. C., Gomes, F. Í. R., Sheheryar, S., Mesquita, F. P., & Souza, P. F. N. (2023) · Microbial Pathogenesis · doi:10.1016/j.micpath.2023.106108 · Cited by 11 · see citing works

Total Synthesis of Auriculatin and Millexatin F and Discovery of Their Antibacterial Mechanism

Che, Y., Wang, Q., Hou, Z., Xie, J., Mei, L., Peng, T., Zhang, C., Song, T., & Dong, H. (2025) · ACS Omega · doi:10.1021/acsomega.4c10340 · Cited by 10 · see citing works

Revolutionizing agroindustry: Towards the industrial application of antimicrobial peptides against pathogens and pests

Bermúdez-Puga, S., Mendes, B. D. S., Ramos-Galarza, J. P., de Azevedo, P. O. D. S., Converti, A., Molinari, F., Moore, S. J., Almeida, J. R., & Oliveira, R. P. D. S. (2025) · Biotechnology Advances · doi:10.1016/j.biotechadv.2025.108605 · Cited by 9 · see citing works

Solid-state NMR spectroscopy for structural studies of polypeptides and lipids in extended physiological membranes

Saad, A., & Bechinger, B. (2023) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2023.184162 · Cited by 10 · see citing works

Guarding the walls: the multifaceted roles of Bce modules in cell envelope stress sensing and antimicrobial resistance

George, N. L., Bennett, E., & Orlando, B. J. (2024) · Journal of Bacteriology · doi:10.1128/jb.00123-24 · Cited by 9 · see citing works

Structure–Activity Relationship Studies of the Peptide Antibiotic Clovibactin

Brunicardi, J. E. H., Griffin, J. H., Ferracane, M. J., Kreutzer, A. G., Small, J., Mendoza, A.-T., Ziller, J. W., & Nowick, J. S. (2024) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.4c01414 · Cited by 9 · see citing works

Metabolic profiling unveils enhanced antibacterial synergy of polymyxin B and teixobactin against multi-drug resistant Acinetobacter baumannii

Hussein, M. H., Kang, Z., Neville, S. L., Allobawi, R., Thrombare, V., Koh, A. J. J., Wilksch, J. J., Crawford, S., Mohammed, M. K., McDevitt, C. A., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-78769-6 · Cited by 9 · see citing works

OPTO: Automated Optimization for Solid-State NMR Spectroscopy

Borcik, C. G., DeZonia, B. E., Ravula, T., Harding, B. D., Garg, R., & Rienstra, C. M. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c13295 · Cited by 9 · see citing works

Streptococcus pneumoniae β-lactam resistance: epidemiological trends, molecular drivers, and innovative control strategies in the post-pandemic era

Li, J., Cheng, G., Qin, X., & Liu, J. (2025) · Clinical Microbiology Reviews · doi:10.1128/cmr.00082-25 · Cited by 10 · see citing works

Biomimetic antimicrobial peptides against gram-positive bacteria

Li, Y., Wei, T.-C., Yuan, J., Feng, J., Yang, P., Tang, S., Wang, L., & Wang, H. (2025) · Biomaterials · doi:10.1016/j.biomaterials.2025.123916 · Cited by 9 · see citing works

Fluoride permeation mechanism of the Fluc channel in liposomes revealed by solid-state NMR

Zhang, J., Song, D., Schackert, F. K., Li, J., Xiang, S., Tian, C., Gong, W., Carloni, P., Alfonso‐Prieto, M., & Shi, C. (2023) · Science Advances · doi:10.1126/sciadv.adg9709 · Cited by 9 · see citing works

Simulation-Guided Molecular Modeling of Nisin and Lipid II Assembly and Membrane Pore Formation

Perez, H. A., Wang, Z., Gerstman, B. S., He, J. M., & Chapagain, P. P. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01050 · Cited by 8 · see citing works

Antimicrobial Resistance: The Answers

Millar, B. C., Cates, M. J., Torrisi, M. S., Round, A. J., Warde, A., Lowery, C. J., & Moore, J. E. (2026) · British Journal of Biomedical Science · doi:10.3389/bjbs.2026.15559 · Cited by 9 · see citing works

Metagenomics for accelerated discovery of antimicrobial compounds: A review focused on bovine mastitis

Cerioli, M. F., Moliva, M. V., & Reinoso, E. (2024) · The Microbe · doi:10.1016/j.microb.2024.100177 · Cited by 8 · see citing works

Structural Mechanism of Insect Cuticular Protein Binding to Chitin Revealed by Solid-State NMR

Hu, S., Li, J., Yuan, F., Zhang, J., Cheng, X., Xiang, S., Tian, C., Gong, W., Liu, T., & Shi, C. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c05099 · Cited by 8 · see citing works

Isobactins: O -acyl isopeptide prodrugs of teixobactin and teixobactin derivatives

Jones, C. R., Guaglianone, G., Lai, G. H., & Nowick, J. S. (2022) · Chemical Science · doi:10.1039/d2sc02670h · Cited by 8 · see citing works

Teixobactin: A Resistance-Evading Antibiotic for Treating Anthrax

Lawrence, W. S., Peel, J. E., de Winter, R., Ling, L. L., Nitti, A. G., Peoples, A. J., Shukla, R., MacGillavry, H. D., Heine, H. S., Hensel, M. E., et al. (2025) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.4c00835 · Cited by 7 · see citing works

Machine Learning Accelerated Discovery of Antimicrobial Inorganic Nanomaterials

Gao, Y., Shang, L., Liu, J., & Zhu, Z. (2025) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.5c00865 · Cited by 7 · see citing works

Adapting antibacterial display to identify serum-active macrocyclic peptide antibiotics

Randall, J. R., Groover, K. E., O’Donnell, A. C., Garza, J. M., Cole, T. J., & Davies, B. W. (2023) · PNAS Nexus · doi:10.1093/pnasnexus/pgad270 · Cited by 7 · see citing works

Mechanism of action of pseudopteroxazole and pseudopterosin G: Diterpenes from marine origin

Janzing, N. B. M., Senges, C. H. R., Dietze, P., Haltli, B., Marchbank, D. H., Kerr, R. G., & Bandow, J. E. (2023) · PROTEOMICS · doi:10.1002/pmic.202300390 · Cited by 7 · see citing works

An Engineered Nisin Analogue with a Hydrophobic Moiety Attached at Position 17 Selectively Inhibits Enterococcus faecium Strains

Guo, L., Kuipers, O. P., & Broos, J. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.4c00337 · Cited by 7 · see citing works

Chemical genetic approaches for the discovery of bacterial cell wall inhibitors

Gupta, R., Singh, M., & Pathania, R. (2023) · RSC Medicinal Chemistry · doi:10.1039/d3md00143a · Cited by 7 · see citing works

Cell Wall-Binding Proteins-Armed Controlled-Release Nanodelivery System Enhances Nisin’s Efficacy against Streptococcus pneumoniae Infections

Zhao, X., Liu, J., Fan, X., Zhong, X., Wang, Y., Yang, S., Tan, H., Deng, J., Song, X., Xie, S., et al. (2025) · ACS Nano · doi:10.1021/acsnano.5c01115 · Cited by 6 · see citing works

Mode of action of teixobactins in cellular membranes

Shukla, R., Medeiros‐Silva, J., Parmar, A., Vermeulen, B. J. A., Das, S. K., Paioni, A. L., Jekhmane, S., Lorent, J. H., Bonvin, A. M. J. J., Baldus, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16600-2 · Cited by 100 · see citing works

Structural studies suggest aggregation as one of the modes of action for teixobactin

Öster, C., Walkowiak, G. P., Hughes, D. E., Spoering, A. L., Peoples, A. J., Catherwood, A. C., Tod, J. A., Lloyd, A. J., Herrmann, T., Lewis, K., et al. (2018) · Chemical Science · doi:10.1039/c8sc03655a · Cited by 32 · see citing works

Exploring Conformations of the Teixobactin-Lipid II Complex in Membrane

Wen, P., Vanegas, J. M., Rempe, S. B., & Tajkhorshid, E. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.11.2519

Revisiting lipid II binding by teixobactin oligomers using membrane MD simulations

Wen, P., Rempe, S. B., & Tajkhorshid, E. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2021.11.1921

Dissecting the Binding Interactions of Teixobactin with the Bacterial Cell‐Wall Precursor Lipid II

Chiorean, S., Antwi, I., Carney, D. W., Kotsogianni, I., Giltrap, A. M., Alexander, F. M., Cochrane, S. A., Payne, R. J., Martin, N. I., Henninot, A., et al. (2019) · ChemBioChem · doi:10.1002/cbic.201900504 · Cited by 30 · see citing works