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The multifaceted nature of antimicrobial peptides: current synthetic chemistry approaches and future directions
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This review discusses the diversity of structure and physicochemical properties of antimicrobial peptides and their derivatives, various chemical synthetic strategies that have been applied in their development, and how this links to their activity.
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Cites
Ror2 signaling regulates Golgi structure and transport through IFT20 for tumor invasiveness
Nishita, M., Park, S.-Y., Nishio, T., Kamizaki, K., Wang, Z., Tamada, K., Takumi, T., Hashimoto, R., Otani, H., Pazour, G. J., et al. (2017) · Scientific Reports · doi:10.1038/s41598-016-0028-x · Cited by 15,947
Magiorakos, A.-P., Srinivasan, A., Carey, R. B., Carmeli, Y., Falagas, M. E., Giske, C. G., Harbarth, S., Hindler, J. F., Kahlmeter, G., Olsson-Liljequist, B., et al. (2012) · Clinical Microbiology and Infection · doi:10.1111/j.1469-0691.2011.03570.x · Cited by 14,449
Solid Phase Peptide Synthesis. I. The Synthesis of a Tetrapeptide
Merrifield, R. B. (1963) · Journal of the American Chemical Society · doi:10.1021/ja00897a025 · Cited by 7,647
Structural absorption by barbule microstructures of super black bird of paradise feathers
McCoy, D. E., Feo, T., Harvey, T. A., & Prum, R. O. (2018) · Nature Communications · doi:10.1038/s41467-017-02088-w · Cited by 7,424
Acute Kidney Injury Network: report of an initiative to improve outcomes in acute kidney injury
Mehta, R. L., Kellum, J. A., Shah, S. V., Molitoris, B. A., Ronco, C., Warnock, D. G., Levin, A., & the Acute Kidney Injury Network (2007) · Critical Care · doi:10.1186/cc5713 · Cited by 7,048
Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829
Liu, Y.-Y., Wang, Y., Walsh, T. R., Yi, L.-X., Zhang, R., Spencer, J., Doi, Y., Tian, G., Dong, B., Huang, X., et al. (2016) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(15)00424-7 · Cited by 5,398
Meijer, L., Nelson, D. J., Riazanski, V., Gabdoulkhakova, A. G., Hery-Arnaud, G., Le Berre, R., Loaëc, N., Oumata, N., Galons, H., Nowak, E., et al. (2016) · Journal of Innate Immunity · doi:10.1159/000444256 · Cited by 4,992
A New Class of Polymers: Starburst-Dendritic Macromolecules
Tomalia, D. A., Baker, H., Dewald, J., Hall, M., Kallos, G., Martin, S., Roeck, J., Ryder, J., & Smith, P. (1985) · Polymer Journal · doi:10.1295/polymj.17.117 · Cited by 3,904
Mechanisms of Antimicrobial Peptide Action and Resistance
Yeaman, M. R., & Yount, N. Y. (2003) · Pharmacological Reviews · doi:10.1124/pr.55.1.2 · Cited by 3,001
Antibiotic resistance: a rundown of a global crisis
Aslam, B., Wang, W., Arshad, M. I., Khurshid, M., Muzammil, S., Rasool, M. H., Nisar, M. A., Alvi, R. F., Aslam, M. A., Qamar, M. U., et al. (2018) · Infection and Drug Resistance · doi:10.2147/idr.s173867 · Cited by 2,552
Jenssen, H., Hamill, P., & Hancock, R. E. W. (2006) · Clinical Microbiology Reviews · doi:10.1128/cmr.00056-05 · Cited by 2,518
Bacillus lipopeptides: versatile weapons for plant disease biocontrol
Ongena, M., & Jacques, P. (2008) · Trends in Microbiology · doi:10.1016/j.tim.2007.12.009 · Cited by 2,418
Hawker, C. J., & Frechet, J. M. J. (1990) · Journal of the American Chemical Society · doi:10.1021/ja00177a027 · Cited by 2,413
APD3: the antimicrobial peptide database as a tool for research and education
Wang, G., Li, X., & Wang, Z. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1278 · Cited by 2,388
Physiological heterogeneity in biofilms
Stewart, P. S., & Franklin, M. J. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1838 · Cited by 2,327
Antibacterial drug discovery in the resistance era
Brown, E. D., & Wright, G. D. (2016) · Nature · doi:10.1038/nature17042 · Cited by 2,247
Overview of the immune response
Chaplin, D. D. (2010) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2009.12.980 · Cited by 2,235
Arnison, P. G., Bibb, M. J., Bierbaum, G., Bowers, A. A., Bugni, T. S., Bulaj, G., Camarero, J. A., Campopiano, D. J., Challis, G. L., Clardy, J., et al. (2013) · Nat. Prod. Rep. · doi:10.1039/c2np20085f · Cited by 2,076
Efficient generation of mouse models of human diseases via ABE- and BE-mediated base editing
Liu, Z., Lu, Z., Yang, G., Huang, S., Li, G., Feng, S., Liu, Y., Li, J., Yu, W., Zhang, Y., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04768-7 · Cited by 2,074
Persister cells, dormancy and infectious disease
Lewis, K. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1557 · Cited by 2,052
Designing antimicrobial peptides: form follows function
Fjell, C. D., Hiss, J. A., Hancock, R. E. W., & Schneider, G. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3591 · Cited by 2,035
The third helix of the Antennapedia homeodomain translocates through biological membranes.
Derossi, D., Joliot, A. H., Chassaing, G., & Prochiantz, A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34080-2 · Cited by 2,034
Lewis, K. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.4.999-1007.2001 · Cited by 1,980
Emerging Strategies to Combat ESKAPE Pathogens in the Era of Antimicrobial Resistance: A Review
Mulani, M. S., Kamble, E. E., Kumkar, S. N., Tawre, M. S., & Pardesi, K. R. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00539 · Cited by 1,644
Hotchkiss, R. S., Moldawer, L. L., Opal, S. M., Reinhart, K., Turnbull, I. R., & Vincent, J.-L. (2016) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2016.45 · Cited by 1,620
Antimicrobial host defence peptides: functions and clinical potential
Mookherjee, N., Anderson, M. A., Haagsman, H. P., & Davidson, D. J. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0058-8 · Cited by 1,502
Nucleic acid-based approaches to investigate microbial-related cheese quality defects
O'Sullivan, D. J., Giblin, L., McSweeney, P. L. H., Sheehan, J. J., & Cotter, P. D. (2013) · Frontiers in Microbiology · doi:10.3389/fmicb.2013.00001 · Cited by 1,417
Membrane lipid homeostasis in bacteria
Zhang, Y.-M., & Rock, C. O. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1839 · Cited by 1,393
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
Studies on anticancer activities of antimicrobial peptides
Hoskin, D. W., & Ramamoorthy, A. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.11.008 · Cited by 1,296
LeVine, A. M., Kurak, K. E., Wright, J. R., Watford, W. T., Bruno, M. D., Ross, G. F., Whitsett, J. A., & Korfhagen, T. R. (1999) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.20.2.3303 · Cited by 1,273
Tam, J. P. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.15.5409 · Cited by 1,251
Kumar, P., Kizhakkedathu, J., & Straus, S. (2018) · Biomolecules · doi:10.3390/biom8010004 · Cited by 1,227
Boas, U., & Heegaard, P. M. H. (2004) · Chemical Society Reviews · doi:10.1039/b309043b · Cited by 1,175
The value of antimicrobial peptides in the age of resistance
Magana, M., Pushpanathan, M., Santos, A. L., Leanse, L., Fernandez, M., Ioannidis, A., Giulianotti, M. A., Apidianakis, Y., Bradfute, S., Ferguson, A. L., et al. (2020) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(20)30327-3 · Cited by 1,150
The antimicrobial peptides and their potential clinical applications.
Lei, J., Sun, L., Huang, S., Zhu, C., Li, P., He, J., Mackey, V., Coy, D. H., & He, Q. (2019) · PubMed · Cited by 1,116
The global threat of antimicrobial resistance: science for intervention.
Roca, I., Akova, M., Baquero, F., Carlet, J., Cavaleri, M., Coenen, S., Cohen, J., Findlay, D., Gyssens, I., Heure, O. E., et al. (2015) · New Microbes and New Infections · doi:10.1016/j.nmni.2015.02.007 · Cited by 1,106
Verkleij, A. J., Zwaal, R. F. A., Roelofsen, B., Comfurius, P., Kastelijn, D., & van Deenen, L. L. M. (1973) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(73)90143-0 · Cited by 1,106
Human β-Defensin-1 Is a Salt-Sensitive Antibiotic in Lung That Is Inactivated in Cystic Fibrosis
Goldman, M. J., Anderson, G. M., Stolzenberg, E. D., Kari, U. P., Zasloff, M., & Wilson, J. M. (1997) · Cell · doi:10.1016/s0092-8674(00)81895-4 · Cited by 1,080
Antimicrobial peptides: Application informed by evolution
Lazzaro, B. P., Zasloff, M., & Rolff, J. (2020) · Science · doi:10.1126/science.aau5480 · Cited by 1,069
Influence of pH on wound-healing: a new perspective for wound-therapy?
Schneider, L. A., Korber, A., Grabbe, S., & Dissemond, J. (2007) · Archives of Dermatological Research · doi:10.1007/s00403-006-0713-x · Cited by 1,066
Cystic Fibrosis Airway Epithelia Fail to Kill Bacteria Because of Abnormal Airway Surface Fluid
Smith, J. J., Travis, S. M., Greenberg, E. P., & Welsh, M. J. (1996) · Cell · doi:10.1016/s0092-8674(00)81099-5 · Cited by 1,039
Describing the Mechanism of Antimicrobial Peptide Action with the Interfacial Activity Model
Wimley, W. C. (2010) · ACS Chemical Biology · doi:10.1021/cb1001558 · Cited by 1,001
Glucose Metabolism Regulates T Cell Activation, Differentiation, and Functions
Palmer, C. S., Ostrowski, M., Balderson, B., Christian, N., & Crowe, S. M. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00001 · Cited by 988
Nonribosomal Peptide Synthesis—Principles and Prospects
Süssmuth, R. D., & Mainz, A. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201609079 · Cited by 958
APD2: the updated antimicrobial peptide database and its application in peptide design.
Wang, G., Li, X., & Wang, Z. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn823 · Cited by 941
Antibacterial agents based on the cyclic d,l-α-peptide architecture
Fernandez-Lopez, S., Kim, H.-S., Choi, E. C., Delgado, M., Granja, J. R., Khasanov, A., Kraehenbuehl, K., Long, G., Weinberger, D. A., Wilcoxen, K. M., et al. (2001) · Nature · doi:10.1038/35086601 · Cited by 938
Macrocyclic Peptides as Drug Candidates: Recent Progress and Remaining Challenges
Vinogradov, A. A., Yin, Y., & Suga, H. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b13178 · Cited by 848
Cruz, D. N., Antonelli, M., Fumagalli, R., Foltran, F., Brienza, N., Donati, A., Malcangi, V., Petrini, F., Volta, G., Bobbio Pallavicini, F. M., et al. (2009) · JAMA · doi:10.1001/jama.2009.856 · Cited by 832
Toxicity of polymyxins: a systematic review of the evidence from old and recent studies
Falagas, M. E., & Kasiakou, S. K. (2006) · Critical Care · doi:10.1186/cc3995 · Cited by 828
Lam, S. J., O'Brien-Simpson, N. M., Pantarat, N., Sulistio, A., Wong, E. H. H., Chen, Y.-Y., Lenzo, J. C., Holden, J. A., Blencowe, A., Reynolds, E. C., et al. (2016) · Nature Microbiology · doi:10.1038/nmicrobiol.2016.162 · Cited by 821
Binding of polymyxin B to the lipid A portion of bacterial lipopolysaccharides
Morrison, D. C., & Jacobs, D. M. (1976) · Immunochemistry · doi:10.1016/0019-2791(76)90181-6 · Cited by 819
Cell-penetrating peptides: classes, origin, and current landscape
Milletti, F. (2012) · Drug Discovery Today · doi:10.1016/j.drudis.2012.03.002 · Cited by 813
APD: the Antimicrobial Peptide Database
Wang, Z. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh025 · Cited by 808
Multidrug Tolerance of Biofilms and Persister Cells
Lewis, K. (2008) · Current Topics in Microbiology and Immunology · doi:10.1007/978-3-540-75418-3_6 · Cited by 804
Wiedemann, I., Breukink, E., van Kraaij, C., Kuipers, O. P., Bierbaum, G., de Kruijff, B., & Sahl, H.-G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006770200 · Cited by 790
New developments in RiPP discovery, enzymology and engineering
Montalbán-López, M., Scott, T. A., Ramesh, S., Rahman, I. R., van Heel, A. J., Viel, J. H., Bandarian, V., Dittmann, E., Genilloud, O., Goto, Y., et al. (2021) · Natural Product Reports · doi:10.1039/d0np00027b · Cited by 787
Structure−Activity Relationships of Polymyxin Antibiotics
Velkov, T., Thompson, P. E., Nation, R. L., & Li, J. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm900999h · Cited by 780
Xavier, B. B., Lammens, C., Ruhal, R., Kumar-Singh, S., Butaye, P., Goossens, H., & Malhotra-Kumar, S. (2016) · Eurosurveillance · doi:10.2807/1560-7917.es.2016.21.27.30280 · Cited by 779
Multicomponent therapeutics for networked systems
Keith, C. T., Borisy, A. A., & Stockwell, B. R. (2005) · Nature Reviews Drug Discovery · doi:10.1038/nrd1609 · Cited by 769
Role of Peptide Hydrophobicity in the Mechanism of Action of α-Helical Antimicrobial Peptides
Chen, Y., Guarnieri, M. T., Vasil, A. I., Vasil, M. L., Mant, C. T., & Hodges, R. S. (2007) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00925-06 · Cited by 757
An Introduction to Medicinal Chemistry
Patrick, G. L. (2023) · Oxford University Press eBooks · doi:10.1093/hesc/9780198866664.001.0001 · Cited by 756
Cyclic peptide therapeutics: past, present and future
Zorzi, A., Deyle, K., & Heinis, C. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.02.006 · Cited by 737
Pelay‐Gimeno, M., Glas, A., Koch, O., & Grossmann, T. N. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201412070 · Cited by 717
Control of cell selectivity of antimicrobial peptides
Matsuzaki, K. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.09.013 · Cited by 713
Role of lipids in the interaction of antimicrobial peptides with membranes
Teixeira, V., Feio, M. J., & Bastos, M. (2012) · Progress in Lipid Research · doi:10.1016/j.plipres.2011.12.005 · Cited by 692
RAD51B in Familial Breast Cancer
Pelttari, L. M., Khan, S., Vuorela, M., Kiiski, J. I., Vilske, S., Nevanlinna, V., Ranta, S., Schleutker, J., Winqvist, R., Kallioniemi, A., et al. (2016) · PLOS ONE · doi:10.1371/journal.pone.0153788 · Cited by 669
Molecular mechanisms of membrane targeting antibiotics
Epand, R. M., Walker, C., Epand, R. F., & Magarvey, N. A. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.10.018 · Cited by 666
Peptoids that mimic the structure, function, and mechanism of helical antimicrobial peptides
Chongsiriwatana, N. P., Patch, J. A., Czyzewski, A. M., Dohm, M. T., Ivankin, A., Gidalevitz, D., Zuckermann, R. N., & Barron, A. E. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708254105 · Cited by 657
Gunn, J. S., Lim, K. B., Krueger, J., Kim, K., Guo, L., Hackett, M., & Miller, S. I. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00757.x · Cited by 655
Facile synthesis of block copolypeptides of defined architecture
Deming, T. J. (1997) · Nature · doi:10.1038/37084 · Cited by 653
Spotlight on protein N-terminal acetylation
Ree, R., Varland, S., & Arnesen, T. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-018-0116-z · Cited by 646
Ion Concentration Polarization by Bifurcated Current Path
Kim, J., Cho, I., Lee, H., & Kim, S. J. (2017) · Scientific Reports · doi:10.1038/s41598-017-04646-0 · Cited by 644
Antibiotics: Actions, Origins, Resistance
Walsh, C. (2003) · Wiley eBooks · doi:10.1128/9781555817886 · Cited by 633
Sota, J., Insalaco, A., Cimaz, R., Alessio, M., Cattalini, M., Gallizzi, R., Maggio, M. C., Lopalco, G., La Torre, F., Fabiani, C., et al. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01526 · Cited by 616
Membrane Active Antimicrobial Peptides: Translating Mechanistic Insights to Design
Li, J., Koh, J.-J., Liu, S., Lakshminarayanan, R., Verma, C. S., & Beuerman, R. W. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00073 · Cited by 611
Chen, Y., Mant, C. T., Farmer, S. W., Hancock, R. E. W., Vasil, M. L., & Hodges, R. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413406200 · Cited by 600
Development and Challenges of Antimicrobial Peptides for Therapeutic Applications
Chen, C. H., & Lu, T. K. (2020) · Antibiotics · doi:10.3390/antibiotics9010024 · Cited by 598
Multidrug-Resistant Bacteria in the Community
van Duin, D., & Paterson, D. L. (2016) · Infectious Disease Clinics of North America · doi:10.1016/j.idc.2016.02.004 · Cited by 584
Molecular Medical Microbiology
(2015) · Elsevier eBooks · doi:10.1016/c2010-1-67744-9 · Cited by 579
Role of membranes in the activities of antimicrobial cationic peptides
Hancock, R. (2002) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(01)00480-3 · Cited by 574
Solid-Phase Peptide Synthesis. III. An Improved Synthesis of Bradykinin*
Merrifield, R. B. (1964) · Biochemistry · doi:10.1021/bi00897a032 · Cited by 572
Highly Efficient Synthesis of Covalently Cross-Linked Peptide Helices by Ring-Closing Metathesis
Blackwell, H. E., & Grubbs, R. H. (1998) · Angewandte Chemie International Edition · doi:10.1002/(sici)1521-3773(19981217)37:23<3281::aid-anie3281>3.0.co;2-v · Cited by 558
Rogosch, T., Kerzel, S., Hoi, K. H., Zhang, Z., Maier, R. F., Ippolito, G. C., & Zemlin, M. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00176 · Cited by 555
Peptidomimetic Antibiotics Target Outer-Membrane Biogenesis in Pseudomonas aeruginosa
Srinivas, N., Jetter, P., Ueberbacher, B. J., Werneburg, M., Zerbe, K., Steinmann, J., Van der Meijden, B., Bernardini, F., Lederer, A., Dias, R. L. A., et al. (2010) · Science · doi:10.1126/science.1182749 · Cited by 554
Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus -Derived Proteinases
Sieprawska-Lupa, M., Mydel, P., Krawczyk, K., Wójcik, K., Puklo, M., Lupa, B., Suder, P., Silberring, J., Reed, M., Pohl, J., et al. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.12.4673-4679.2004 · Cited by 551
Direct inactivation of viruses by human granulocyte defensins
Daher, K. A., Selsted, M. E., & Lehrer, R. I. (1986) · Journal of Virology · doi:10.1128/jvi.60.3.1068-1074.1986 · Cited by 533
Carattoli, A., Villa, L., Feudi, C., Curcio, L., Orsini, S., Luppi, A., Pezzotti, G., & Magistrali, C. F. (2017) · Eurosurveillance · doi:10.2807/1560-7917.es.2017.22.31.30589 · Cited by 533
Borowiak, M., Fischer, J., Hammerl, J. A., Hendriksen, R. S., Szabo, I., & Malorny, B. (2017) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkx327 · Cited by 533
Human Antimicrobial Peptides and Proteins
Wang, G. (2014) · Pharmaceuticals · doi:10.3390/ph7050545 · Cited by 528
Sato, H., & Feix, J. B. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.02.021 · Cited by 522
Broad-Spectrum Anti-biofilm Peptide That Targets a Cellular Stress Response
de la Fuente-Núñez, C., Reffuveille, F., Haney, E. F., Straus, S. K., & Hancock, R. E. W. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004152 · Cited by 521
Capsule Polysaccharide Mediates Bacterial Resistance to Antimicrobial Peptides
Campos, M. A., Vargas, M. A., Regueiro, V., Llompart, C. M., Albertí, S., & Bengoechea, J. A. (2004) · Infection and Immunity · doi:10.1128/iai.72.12.7107-7114.2004 · Cited by 518
Pazgier, M., Hoover, D. M., Yang, D., Lu, W., & Lubkowski, J. (2006) · Cellular and Molecular Life Sciences CMLS · doi:10.1007/s00018-005-5540-2 · Cited by 514
Antimicrobial Peptide Structure and Mechanism of Action: A Focus on the Role of Membrane Structure
Lee, T.-H., N. Hall, K., & Aguilar, M.-I. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150703121700 · Cited by 512
Carroll, L. M., Gaballa, A., Guldimann, C., Sullivan, G., Henderson, L. O., & Wiedmann, M. (2019) · mBio · doi:10.1128/mbio.00853-19 · Cited by 506
Jiang, Z., Vasil, A. I., Hale, J. D., Hancock, R. E. W., Vasil, M. L., & Hodges, R. S. (2008) · Peptide Science · doi:10.1002/bip.20911 · Cited by 505
QSAR-Based Virtual Screening: Advances and Applications in Drug Discovery
Neves, B. J., Braga, R. C., Melo-Filho, C. C., Moreira-Filho, J. T., Muratov, E. N., & Andrade, C. H. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01275 · Cited by 494
A New Era of Antibiotics: The Clinical Potential of Antimicrobial Peptides
Browne, K., Chakraborty, S., Chen, R., Willcox, M. D., Black, D. S., Walsh, W. R., & Kumar, N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197047 · Cited by 482
A Dose-Response Study of Antibiotic Resistance in Pseudomonas aeruginosa Biofilms
Brooun, A., Liu, S., & Lewis, K. (2000) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.44.3.640-646.2000 · Cited by 473
Sustainability Challenges in Peptide Synthesis and Purification: From R&D to Production
Isidro-Llobet, A., Kenworthy, M. N., Mukherjee, S., Kopach, M. E., Wegner, K., Gallou, F., Smith, A. G., & Roschangar, F. (2019) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.8b03001 · Cited by 473
Ultrashort antibacterial and antifungal lipopeptides
Makovitzki, A., Avrahami, D., & Shai, Y. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606129103 · Cited by 468
Emergence of a novel mobile colistin resistance gene, mcr-8 , in NDM-producing Klebsiella pneumoniae
Wang, X., Wang, Y., Zhou, Y., Li, J., Yin, W., Wang, S., Zhang, S., Shen, J., Shen, Z., & Wang, Y. (2018) · Emerging Microbes & Infections · doi:10.1038/s41426-018-0124-z · Cited by 460
de la Fuente-Núñez, C., Korolik, V., Bains, M., Nguyen, U., Breidenstein, E. B. M., Horsman, S., Lewenza, S., Burrows, L., & Hancock, R. E. W. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00064-12 · Cited by 459
Polymyxin: Alternative Mechanisms of Action and Resistance
Trimble, M. J., Mlynárčik, P., Kolář, M., & Hancock, R. E. W. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a025288 · Cited by 454
Estimation of Direct Healthcare Costs of Fungal Diseases in the United States
Benedict, K., Jackson, B. R., Chiller, T., & Beer, K. D. (2019) · Clinical Infectious Diseases · doi:10.1093/cid/ciy776 · Cited by 438
Local Epidemics Gone Viral: Evolution and Diffusion of the Italian HIV-1 Recombinant Form CRF60_BC
Lai, A., Simonetti, F. R., Brindicci, G., Bergna, A., Di Giambenedetto, S., Sterrantino, G., Mussini, C., Menzo, S., Bagnarelli, P., Zazzi, M., et al. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00769 · Cited by 436
Combating Multidrug‐Resistant Bacteria: Current Strategies for the Discovery of Novel Antibacterials
O'Connell, K. M. G., Hodgkinson, J. T., Sore, H. F., Welch, M., Salmond, G. P. C., & Spring, D. R. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201209979 · Cited by 435
Self-citationAntibiotic resistance: What is so special about multidrug-resistant Gram-negative bacteria?
Exner, M., Bhattacharya, S., Christiansen, B., Gebel, J., Goroncy‐Bermes, P., Hartemann, P., Heeg, P., Ilschner, C., Krämer, A., Larson, E., et al. (2017) · PubMed · doi:10.3205/dgkh000290 · Cited by 429
Moskowitz, S. M., Ernst, R. K., & Miller, S. I. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.2.575-579.2004 · Cited by 418
Macgregor, C. J., Thomas, C. D., Roy, D. B., Beaumont, M. A., Bell, J. R., Brereton, T., Bridle, J. R., Dytham, C., Fox, R., Gotthard, K., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12479-w · Cited by 414
Wall Teichoic Acid Function, Biosynthesis, and Inhibition
Swoboda, J. G., Campbell, J., Meredith, T. C., & Walker, S. (2010) · ChemBioChem · doi:10.1002/cbic.200900557 · Cited by 412
Gram-positive and gram-negative bacterial toxins in sepsis: A brief review
Ramachandran, G. (2014) · Virulence · doi:10.4161/viru.27024 · Cited by 411
Lasso Peptides: An Intriguing Class of Bacterial Natural Products
Hegemann, J. D., Zimmermann, M., Xie, X., & Marahiel, M. A. (2015) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5b00156 · Cited by 393
DRAMP 2.0, an updated data repository of antimicrobial peptides
Kang, X., Dong, F., Shi, C., Liu, S., Sun, J., Chen, J., Li, H., Xu, H., Lao, X., & Zheng, H. (2019) · Scientific Data · doi:10.1038/s41597-019-0154-y · Cited by 393
Veatch, W. R., Fossel, E. T., & Blout, E. R. (1974) · Biochemistry · doi:10.1021/bi00723a001 · Cited by 387
The gramicidin ion channel: A model membrane protein
Kelkar, D. A., & Chattopadhyay, A. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.05.011 · Cited by 380
Antimicrobial peptides under clinical investigation
Koo, H. B., & Seo, J. (2019) · Peptide Science · doi:10.1002/pep2.24122 · Cited by 376
Antimicrobial activity of synthetic magainin peptides and several analogues.
Zasloff, M., Martin, B., & Chen, H. C. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.3.910 · Cited by 373
Novel plasmid-mediated colistin resistance gene mcr-7.1 in Klebsiella pneumoniae
Yang, Y.-Q., Li, Y.-X., Lei, C.-W., Zhang, A.-Y., & Wang, H.-N. (2018) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dky111 · Cited by 367
Bacterial strategies of resistance to antimicrobial peptides
Joo, H.-S., Fu, C.-I., & Otto, M. (2016) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2015.0292 · Cited by 360
In Vitro Antibacterial Properties of Pexiganan, an Analog of Magainin
Ge, Y., MacDonald, D. L., Holroyd, K. J., Thornsberry, C., Wexler, H., & Zasloff, M. (1999) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.43.4.782 · Cited by 359
Reassessing the Host Defense Peptide Landscape
Haney, E. F., Straus, S. K., & Hancock, R. E. W. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00043 · Cited by 359
Carpenter, C. F., & Chambers, H. F. (2004) · Clinical Infectious Diseases · doi:10.1086/383472 · Cited by 358
Integrated evolutionary analysis reveals antimicrobial peptides with limited resistance
Spohn, R., Daruka, L., Lázár, V., Martins, A., Vidovics, F., Grézal, G., Méhi, O., Kintses, B., Számel, M., Jangir, P. K., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12364-6 · Cited by 358
Gottler, L. M., & Ramamoorthy, A. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.10.009 · Cited by 354
New Lipoglycopeptides: A Comparative Review of Dalbavancin, Oritavancin and Telavancin
Zhanel, G. G., Calic, D., Schweizer, F., Zelenitsky, S., Adam, H., Lagacé-Wiens, P. R. S., Rubinstein, E., Gin, A. S., Hoban, D. J., & Karlowsky, J. A. (2010) · Drugs · doi:10.2165/11534440-000000000-00000 · Cited by 352
Effectiveness of polymyxin B-immobilized fiber column in sepsis: a systematic review
Cruz, D. N., Perazella, M. A., Bellomo, R., de Cal, M., Polanco, N., Corradi, V., Lentini, P., Nalesso, F., Ueno, T., Ranieri, V. M., et al. (2007) · Critical Care · doi:10.1186/cc5780 · Cited by 347
Chemical space as a source for new drugs
Reymond, J.-L., van Deursen, R., Blum, L. C., & Ruddigkeit, L. (2010) · MedChemComm · doi:10.1039/c0md00020e · Cited by 347
Antiviral peptides as promising therapeutic drugs
Vilas Boas, L. C. P., Campos, M. L., Berlanda, R. L. A., de Carvalho Neves, N., & Franco, O. L. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03138-w · Cited by 336
Hollmann, A., Martinez, M., Maturana, P., Semorile, L. C., & Maffia, P. C. (2018) · Frontiers in Chemistry · doi:10.3389/fchem.2018.00204 · Cited by 334
Rasines Mazo, A., Allison-Logan, S., Karimi, F., Chan, N. J.-A., Qiu, W., Duan, W., O’Brien-Simpson, N. M., & Qiao, G. G. (2020) · Chemical Society Reviews · doi:10.1039/c9cs00738e · Cited by 329
Aliferis, T., Iatrou, H., & Hadjichristidis, N. (2004) · Biomacromolecules · doi:10.1021/bm0497217 · Cited by 327
de la Fuente-Núñez, C., Reffuveille, F., Mansour, S. C., Reckseidler-Zenteno, S. L., Hernández, D., Brackman, G., Coenye, T., & Hancock, R. E. W. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.01.002 · Cited by 323
Jin, T., Bokarewa, M., Foster, T., Mitchell, J., Higgins, J., & Tarkowski, A. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.2.1169 · Cited by 319
Capsule polysaccharide is a bacterial decoy for antimicrobial peptides
Llobet, E., Tomás, J. M., & Bengoechea, J. A. (2008) · Microbiology · doi:10.1099/mic.0.2008/022301-0 · Cited by 312
Diversity of endotoxin and its impact on pathogenesis
Trent, M. S., Stead, C. M., Tran, A. X., & Hankins, J. V. (2006) · Journal of Endotoxin Research · doi:10.1179/096805106x118825 · Cited by 311
Chimeric peptidomimetic antibiotics against Gram-negative bacteria
Luther, A., Urfer, M., Zahn, M., Müller, M., Wang, S.-Y., Mondal, M., Vitale, A., Hartmann, J.-B., Sharpe, T., Monte, F. L., et al. (2019) · Nature · doi:10.1038/s41586-019-1665-6 · Cited by 311
Recombinant production of antimicrobial peptides in Escherichia coli: A review
Li, Y. (2011) · Protein Expression and Purification · doi:10.1016/j.pep.2011.08.001 · Cited by 307
Glycopeptide antibiotics: Back to the future
Butler, M. S., Hansford, K. A., Blaskovich, M. A. T., Halai, R., & Cooper, M. A. (2014) · The Journal of Antibiotics · doi:10.1038/ja.2014.111 · Cited by 303
Delivery of antibiotics with polymeric particles
Xiong, M.-H., Bao, Y., Yang, X.-Z., Zhu, Y.-H., & Wang, J. (2014) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2014.02.002 · Cited by 302
Sepsis: Inflammation Is a Necessary Evil
Nedeva, C., Menassa, J., & Puthalakath, H. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00108 · Cited by 301
Will new generations of modified antimicrobial peptides improve their potential as pharmaceuticals?
Brogden, N. K., & Brogden, K. A. (2011) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2011.05.004 · Cited by 300
Mourtada, R., Herce, H. D., Yin, D. J., Moroco, J. A., Wales, T. E., Engen, J. R., & Walensky, L. D. (2019) · Nature Biotechnology · doi:10.1038/s41587-019-0222-z · Cited by 297
Antimicrobial peptide mimics for improved therapeutic properties
Rotem, S., & Mor, A. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.10.020 · Cited by 296
Antimicrobial Peptides: An Introduction
Haney, E. F., Mansour, S. C., & Hancock, R. E. W. (2017) · Methods in Molecular Biology · doi:10.1007/978-1-4939-6737-7_1 · Cited by 296
Mwangi, J., Yin, Y., Wang, G., Yang, M., Li, Y., Zhang, Z., & Lai, R. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1909585117 · Cited by 286
AbuOun, M., Stubberfield, E. J., Duggett, N. A., Kirchner, M., Dormer, L., Nunez-Garcia, J., Randall, L. P., Lemma, F., Crook, D. W., Teale, C., et al. (2017) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkx286 · Cited by 282
Bacterial Persisters and Infection: Past, Present, and Progressing
Gollan, B., Grabe, G., Michaux, C., & Helaine, S. (2019) · Annual Review of Microbiology · doi:10.1146/annurev-micro-020518-115650 · Cited by 280
Baker, B. J., Saw, J. H., Lind, A. E., Lazar, C. S., Hinrichs, K.-U., Teske, A. P., & Ettema, T. J. G. (2016) · Nature Microbiology · doi:10.1038/nmicrobiol.2016.32 · Cited by 277
Pickl, M., Winkler, C., Glueck, S., Fraaije, M., & Faber, K. (2017) · Molecules · doi:10.3390/molecules22122205 · Cited by 274
Palomo, J. M. (2014) · RSC Adv. · doi:10.1039/c4ra02458c · Cited by 273
Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds
McIntosh, J. A., Donia, M. S., & Schmidt, E. W. (2009) · Natural Product Reports · doi:10.1039/b714132g · Cited by 269
Antibiotics: from prehistory to the present day
Gould, K. (2016) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkv484 · Cited by 268
Recent advances in design of antimicrobial peptides and polypeptides toward clinical translation
Jiang, Y., Chen, Y., Song, Z., Tan, Z., & Cheng, J. (2021) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.12.016 · Cited by 267
Developments in Glycopeptide Antibiotics
Blaskovich, M. A. T., Hansford, K. A., Butler, M. S., Jia, Z., Mark, A. E., & Cooper, M. A. (2018) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.7b00258 · Cited by 265
Antibiotics in the clinical pipeline in October 2019
Butler, M. S., & Paterson, D. L. (2020) · The Journal of Antibiotics · doi:10.1038/s41429-020-0291-8 · Cited by 264
Antifungal Peptides as Therapeutic Agents
Fernández de Ullivarri, M., Arbulu, S., Garcia-Gutierrez, E., & Cotter, P. D. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.00105 · Cited by 264
Deslouches, B., Phadke, S. M., Lazarevic, V., Cascio, M., Islam, K., Montelaro, R. C., & Mietzner, T. A. (2005) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.49.1.316-322.2005 · Cited by 262
Advances in Development of Antimicrobial Peptidomimetics as Potential Drugs
Molchanova, N., Hansen, P., & Franzyk, H. (2017) · Molecules · doi:10.3390/molecules22091430 · Cited by 257
Effects of pH and salinity on the antimicrobial properties of clavanins
Lee, I. H., Cho, Y., & Lehrer, R. I. (1997) · Infection and Immunity · doi:10.1128/iai.65.7.2898-2903.1997 · Cited by 254
Jaradat, D. M. M. (2018) · Amino Acids · doi:10.1007/s00726-017-2516-0 · Cited by 253
Peptide Dendrimers as Artificial Enzymes, Receptors, and Drug-Delivery Agents
Darbre, T., & Reymond, J.-L. (2006) · Accounts of Chemical Research · doi:10.1021/ar050203y · Cited by 250
Cationic Antimicrobial Peptide Resistance in Neisseria meningitidis
Tzeng, Y.-L., Ambrose, K. D., Zughaier, S., Zhou, X., Miller, Y. K., Shafer, W. M., & Stephens, D. S. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.15.5387-5396.2005 · Cited by 249
Li, C., Harmanus, C., Zhu, D., Meng, X., Wang, S., Duan, J., Liu, S., Fu, C., Zhou, P., Liu, R., et al. (2018) · Emerging Microbes & Infections · doi:10.1038/s41426-018-0211-1 · Cited by 245
Exploitation of syndecan-1 shedding by Pseudomonas aeruginosa enhances virulence
Park, P. W., Pier, G. B., Hinkes, M. T., & Bernfield, M. (2001) · Nature · doi:10.1038/35075100 · Cited by 243
Targeted Killing of Streptococcus mutans by a Pheromone-Guided “Smart” Antimicrobial Peptide
Eckert, R., He, J., Yarbrough, D. K., Qi, F., Anderson, M. H., & Shi, W. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00622-06 · Cited by 238
Kovács, M., Halfmann, A., Fedtke, I., Heintz, M., Peschel, A., Vollmer, W., Hakenbeck, R., & Brückner, R. (2006) · Journal of Bacteriology · doi:10.1128/jb.00336-06 · Cited by 233
Computer-Aided Design of Antimicrobial Peptides: Are We Generating Effective Drug Candidates?
Cardoso, M. H., Orozco, R. Q., Rezende, S. B., Rodrigues, G., Oshiro, K. G. N., Cândido, E. S., & Franco, O. L. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.03097 · Cited by 232
Dewachter, L., Fauvart, M., & Michiels, J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.028 · Cited by 230
Helical antimicrobial polypeptides with radial amphiphilicity
Xiong, M., Lee, M. W., Mansbach, R. A., Song, Z., Bao, Y., Peek, R. M., Yao, C., Chen, L.-F., Ferguson, A. L., Wong, G. C. L., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1507893112 · Cited by 227
Delivery systems to increase the selectivity of antibiotics in phagocytic cells
Briones, E., Isabel Colino, C., & Lanao, J. M. (2008) · Journal of Controlled Release · doi:10.1016/j.jconrel.2007.10.027 · Cited by 224
Evolutionary causes and consequences of bacterial antibiotic persistence
Bakkeren, E., Diard, M., & Hardt, W.-D. (2020) · Nature Reviews Microbiology · doi:10.1038/s41579-020-0378-z · Cited by 224
A brief history of antibiotics and select advances in their synthesis
Nicolaou, K. C., & Rigol, S. (2018) · The Journal of Antibiotics · doi:10.1038/ja.2017.62 · Cited by 222
Peptide synthesis: chemical or enzymatic
Guzman, F., Barberis, S., & Illanes, A. (2007) · Electronic Journal of Biotechnology · doi:10.2225/vol10-issue2-fulltext-13 · Cited by 220
Human Antimicrobial Peptides as Therapeutics for Viral Infections
Ahmed, A., Siman-Tov, G., Hall, G., Bhalla, N., & Narayanan, A. (2019) · Viruses · doi:10.3390/v11080704 · Cited by 220
Salt-Resistant Alpha-Helical Cationic Antimicrobial Peptides
Friedrich, C., Scott, M. G., Karunaratne, N., Yan, H., & Hancock, R. E. W. (1999) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.43.7.1542 · Cited by 219
DADP: the database of anuran defense peptides
Novković, M., Simunić, J., Bojović, V., Tossi, A., & Juretić, D. (2012) · Bioinformatics · doi:10.1093/bioinformatics/bts141 · Cited by 218
RiPP antibiotics: biosynthesis and engineering potential
Hudson, G. A., & Mitchell, D. A. (2018) · Current Opinion in Microbiology · doi:10.1016/j.mib.2018.02.010 · Cited by 218
Invited review: Diversity of endotoxin and its impact on pathogenesis
Trent, M. S., Stead, C. M., Tran, A. X., & Hankins, J. V. (2006) · Journal of Endotoxin Research · doi:10.1177/09680519060120040201 · Cited by 211
Approved Glycopeptide Antibacterial Drugs: Mechanism of Action and Resistance
Zeng, D., Debabov, D., Hartsell, T. L., Cano, R. J., Adams, S., Schuyler, J. A., McMillan, R., & Pace, J. L. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026989 · Cited by 211
Mansour, S. C., de la Fuente‐Núñez, C., & Hancock, R. E. W. (2015) · Journal of Peptide Science · doi:10.1002/psc.2708 · Cited by 208
Current scenario of peptide-based drugs: the key roles of cationic antitumor and antiviral peptides
Mulder, K. C. L., Lima, L. A., Miranda, V. J., Dias, S. C., & Franco, O. L. (2013) · Frontiers in Microbiology · doi:10.3389/fmicb.2013.00321 · Cited by 207
Purification and characterization of eight peptides from Galleria mellonella immune hemolymph
Cytryńska, M., Mak, P., Zdybicka-Barabas, A., Suder, P., & Jakubowicz, T. (2007) · Peptides · doi:10.1016/j.peptides.2006.11.010 · Cited by 204
New Insights Into CRASP-Mediated Complement Evasion in the Lyme Disease Enzootic Cycle
Lin, Y.-P., Frye, A. M., Nowak, T. A., & Kraiczy, P. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.00001 · Cited by 204
Abou Alaiwa, M. H., Reznikov, L. R., Gansemer, N. D., Sheets, K. A., Horswill, A. R., Stoltz, D. A., Zabner, J., & Welsh, M. J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422091112 · Cited by 203
Intracellular pharmacodynamics of antibiotics
Carryn, S., Chanteux, H., Seral, C., Mingeot-Leclercq, M.-P., Van Bambeke, F., & Tulkens, P. M. (2003) · Infectious Disease Clinics of North America · doi:10.1016/s0891-5520(03)00066-7 · Cited by 201
Vancomycin Revisited – 60 Years Later
Rubinstein, E., & Keynan, Y. (2014) · Frontiers in Public Health · doi:10.3389/fpubh.2014.00217 · Cited by 200
Expression systems for heterologous production of antimicrobial peptides
Parachin, N. S., Mulder, K. C., Viana, A. A. B., Dias, S. C., & Franco, O. L. (2012) · Peptides · doi:10.1016/j.peptides.2012.09.020 · Cited by 197
Opal, S. M., Garber, G. E., LaRosa, S. P., Maki, D. G., Freebairn, R. C., Kinasewitz, G. T., Dhainaut, J.-F., Yan, S. B., Williams, M. D., Graham, D. E., et al. (2003) · Clinical Infectious Diseases · doi:10.1086/375593 · Cited by 194
Presentato, A., Piacenza, E., Anikovskiy, M., Cappelletti, M., Zannoni, D., & Turner, R. J. (2016) · Microbial Cell Factories · doi:10.1186/s12934-016-0602-8 · Cited by 191
Polymyxin B: similarities to and differences from colistin (polymyxin E)
Kwa, A., Kasiakou, S. K., Tam, V. H., & Falagas, M. E. (2007) · Expert Review of Anti-infective Therapy · doi:10.1586/14787210.5.5.811 · Cited by 190
Anticandida Activity Is Retained in P-113, a 12-Amino-Acid Fragment of Histatin 5
Rothstein, D. M., Spacciapoli, P., Tran, L. T., Xu, T., Roberts, F. D., Dalla Serra, M., Buxton, D. K., Oppenheim, F. G., & Friden, P. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.5.1367-1373.2001 · Cited by 188
Improved Methods for Classification, Prediction, and Design of Antimicrobial Peptides
Wang, G. (2015) · Methods in Molecular Biology · doi:10.1007/978-1-4939-2285-7_3 · Cited by 187
Dathe, M., Nikolenko, H., Klose, J., & Bienert, M. (2004) · Biochemistry · doi:10.1021/bi035948v · Cited by 186
Decoding the Membrane Activity of the Cyclotide Kalata B1
Henriques, S. T., Huang, Y.-H., Rosengren, K. J., Franquelim, H. G., Carvalho, F. A., Johnson, A., Sonza, S., Tachedjian, G., Castanho, M. A. R. B., Daly, N. L., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.253393 · Cited by 182
Metal binding and structure–activity relationship of the metalloantibiotic peptide bacitracin
Ming, L.-J., & Epperson, J. D. (2002) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(02)00464-6 · Cited by 181
Acetone‐Linked Peptides: A Convergent Approach for Peptide Macrocyclization and Labeling
Assem, N., Ferreira, D. J., Wolan, D. W., & Dawson, P. E. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201502607 · Cited by 181
Multitarget Approaches against Multiresistant Superbugs
Gray, D. A., & Wenzel, M. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00001 · Cited by 179
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Metadata
- Authors
- Gan, B. H., Gaynord, J., Rowe, S. M., Deingruber, T., & Spring, D. R.
- Venue
- Chemical Society Reviews
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2021
- Volume
- 50
- Issue
- 13
- Pages
- 7820-7880
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W3165052418
- Cited by
- 511
- References
- 457
- FWCI
- 13.39
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.