Antimicrobial peptides (AMPs): A promising class of antimicrobial compounds

Proceedings of the National Academy of Sciences of the United States of America

Dowling, J. E., & Wald, G. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1981.tb06752.x · Cited by 17,893

International Journal of Molecular Sciences

(2024) · International Journal of Molecular Sciences · doi:10.3390/ijms · Cited by 10,111

Antimicrobial peptides of multicellular organisms

Zasloff, M. (2002) · Nature · doi:10.1038/415389a · Cited by 8,457

Biochemical and Biophysical Research Communications

(1960) · Nature · doi:10.1038/186124d0 · Cited by 6,700

Biofilms: an emergent form of bacterial life

Flemming, H.-C., Wingender, J., Szewzyk, U., Steinberg, P., Rice, S. A., & Kjelleberg, S. (2016) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.94 · Cited by 5,979

Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829

Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies

Hancock, R. E. W., & Sahl, H.-G. (2006) · Nature Biotechnology · doi:10.1038/nbt1267 · Cited by 4,208

Philosophical Transactions of the Royal Society B: biological sciences

(2026) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb · Cited by 2,876

Antimicrobial agents and chemotherapy—1969

Parker, R. H. (1971) · Journal of Chronic Diseases · doi:10.1016/0021-9681(71)90113-5 · Cited by 2,504

Solid phase peptide synthesis utilizing 9‐fluorenylmethoxycarbonyl amino acids

FIELDS, G. B., & NOBLE, R. L. (1990) · International Journal of Peptide and Protein Research · doi:10.1111/j.1399-3011.1990.tb00939.x · Cited by 2,493

Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.

Zasloff, M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5449 · Cited by 2,305

Heterologous protein expression in the methylotrophic yeast Pichia pastoris

Cereghino, J. (2000) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(99)00029-7 · Cited by 2,039

Advances in Experimental Medicine and Biology

Lunt, G. G. (1986) · Neurochemistry International · doi:10.1016/0197-0186(86)90020-3 · Cited by 1,851

Cellular and Molecular Life Sciences

(2013) · Cellular and Molecular Life Sciences · doi:10.1007/18.1420-9071 · Cited by 1,805

Experimental and Therapeutic Medicine

(2026) · Experimental and Therapeutic Medicine · doi:10.3892/etm · Cited by 1,728

Bacterial biofilm and associated infections

Jamal, M., Ahmad, W., Andleeb, S., Jalil, F., Imran, M., Nawaz, M. A., Hussain, T., Ali, M., Rafiq, M., & Kamil, M. A. (2018) · Journal of the Chinese Medical Association · doi:10.1016/j.jcma.2017.07.012 · Cited by 1,642

Review of antimicrobial food packaging

Appendini, P., & Hotchkiss, J. H. (2002) · Innovative Food Science & Emerging Technologies · doi:10.1016/s1466-8564(02)00012-7 · Cited by 1,623

The expanding scope of antimicrobial peptide structures and their modes of action

Nguyen, L. T., Haney, E. F., & Vogel, H. J. (2011) · Trends in Biotechnology · doi:10.1016/j.tibtech.2011.05.001 · Cited by 1,604

Antimicrobial Peptides

Bahar, A., & Ren, D. (2013) · Pharmaceuticals · doi:10.3390/ph6121543 · Cited by 1,351

Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion

Xia, S., Liu, M., Wang, C., Xu, W., Lan, Q., Feng, S., Qi, F., Bao, L., Du, L., Liu, S., et al. (2020) · Cell Research · doi:10.1038/s41422-020-0305-x · Cited by 1,343

Untitled work

(2000) · Cited by 1,342

Antimicrobial Peptides: Diversity, Mechanism of Action and Strategies to Improve the Activity and Biocompatibility In Vivo

Kumar, P., Kizhakkedathu, J., & Straus, S. (2018) · Biomolecules · doi:10.3390/biom8010004 · Cited by 1,227

Barrel-Stave Model or Toroidal Model? A Case Study on Melittin Pores

Yang, L., Harroun, T. A., Weiss, T. M., Ding, L., & Huang, H. W. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)75802-x · Cited by 1,114

International Journal of Antimicrobial Agents

(2009) · International Journal of Antimicrobial Agents · doi:10.1016/s0924-8579(09)00446-4 · Cited by 1,085

Postharvest Biology and Technology

Sdol, E. (2009) · Cited by 991

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

Mechanism of Action of the Antimicrobial Peptide Buforin II: Buforin II Kills Microorganisms by Penetrating the Cell Membrane and Inhibiting Cellular Functions

Park, C. B., Kim, H. S., & Kim, S. C. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8159 · Cited by 896

Active Packaging Technologies with an Emphasis on Antimicrobial Packaging and its Applications

Suppakul, P., Miltz, J., Sonneveld, K., & Bigger, S. W. (2003) · Journal of Food Science · doi:10.1111/j.1365-2621.2003.tb05687.x · Cited by 882

Advances in Biochemical Engineering/Biotechnology

Chaplin, M. (1985) · Biochemical Education · doi:10.1016/0307-4412(85)90043-3 · Cited by 864

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

From antimicrobial to anticancer peptides. A review

Gaspar, D., Veiga, A. S., & Castanho, M. A. R. B. (2013) · Frontiers in Microbiology · doi:10.3389/fmicb.2013.00294 · Cited by 749

Antimicrobial Peptides: Mechanisms of Action and Resistance

Bechinger, B., & Gorr, S.-U. (2017) · Journal of Dental Research · doi:10.1177/0022034516679973 · Cited by 739

A Review of Antimicrobial Peptides and Their Therapeutic Potential as Anti-Infective Drugs

Gordon, Y. J., Romanowski, E. G., & McDermott, A. M. (2005) · Current Eye Research · doi:10.1080/02713680590968637 · Cited by 697

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

Amphipathic α helical antimicrobial peptides.: A systematic study of the effects of structural and physical properties on biological activity

Giangaspero, A., Sandri, L., & Tossi, A. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2001.02494.x · Cited by 636

Current Topics in Medicinal Chemistry

(2019) · Current Topics in Medicinal Chemistry · doi:10.2174/ctmc-15680266-615 · Cited by 629

Rational Design of α-Helical Antimicrobial Peptides with Enhanced Activities and Specificity/Therapeutic Index

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

Large-scale manufacture of peptide therapeutics by chemical synthesis

Bray, B. L. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd1133 · Cited by 598

Alpha-helical cationic antimicrobial peptides: relationships of structure and function

Huang, Y., Huang, J., & Chen, Y. (2010) · Protein & Cell · doi:10.1007/s13238-010-0004-3 · Cited by 575

A comprehensive summary of LL-37, the factotum human cathelicidin peptide

Vandamme, D., Landuyt, B., Luyten, W., & Schoofs, L. (2012) · Cellular Immunology · doi:10.1016/j.cellimm.2012.11.009 · Cited by 567

Macromolecular Rapid Communications

(2006) · Macromolecular Rapid Communications · doi:10.1002/(issn)1521-3927 · Cited by 564

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. S., et al. (2010) · Science · doi:10.1126/science.1185723 · Cited by 550

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

Hsu, S.-T. D., Breukink, E., Tischenko, E., Lutters, M. A. G., de Kruijff, B., Kaptein, R., Bonvin, A. M. J. J., & van Nuland, N. A. J. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb830 · Cited by 547

Peptide–membrane interactions and mechanisms of membrane destruction by amphipathic α-helical antimicrobial peptides

Sato, H., & Feix, J. B. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.02.021 · Cited by 522

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

Insect Antimicrobial Peptides: Structures, Properties and Gene Regulation

Bulet, P., & Stocklin, R. (2005) · Protein & Peptide Letters · doi:10.2174/0929866053406011 · Cited by 487

Antimicrobial peptides as therapeutic agents: opportunities and challenges

Mahlapuu, M., Björn, C., & Ekblom, J. (2020) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2020.1796576 · Cited by 484

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

Antimicrobial Peptides and Their Therapeutic Potential for Bacterial Skin Infections and Wounds

Pfalzgraff, A., Brandenburg, K., & Weindl, G. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00281 · Cited by 481

Fungal pathogen protection in potato by expression of a plant defensin peptide

Gao, A.-G., Hakimi, S. M., Mittanck, C. A., Wu, Y., Woerner, B. M., Stark, D. M., Shah, D. M., Liang, J., & Rommens, C. M. T. (2000) · Nature Biotechnology · doi:10.1038/82436 · Cited by 472

Developmental and comparative immunology

Ratcliffe, M. J. H. (1993) · Veterinary Immunology and Immunopathology · doi:10.1016/0165-2427(93)90131-m · Cited by 468

Overview on the recent study of antimicrobial peptides: Origins, functions, relative mechanisms and application

Li, Y., Xiang, Q., Zhang, Q., Huang, Y., & Su, Z. (2012) · Peptides · doi:10.1016/j.peptides.2012.07.001 · Cited by 462

Application of Edible Coatings on Meats, Poultry and Seafoods: A Review

Gennadios, A., Hanna, M. A., & Kurth, L. B. (1997) · LWT - Food Science and Technology · doi:10.1006/fstl.1996.0202 · Cited by 461

Inhibition of Bacterial Biofilm Formation and Swarming Motility by a Small Synthetic Cationic Peptide

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

Alpha-helical antimicrobial peptides—Using a sequence template to guide structure–activity relationship studies

Zelezetsky, I., & Tossi, A. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.03.021 · Cited by 439

Biotechnology and Applied Biochemistry

(2014) · Biotechnology and Applied Biochemistry · doi:10.1002/(issn)1470-8744 · Cited by 436

Plant antimicrobial peptides

Nawrot, R., Barylski, J., Nowicki, G., Broniarczyk, J., Buchwald, W., & Goździcka-Józefiak, A. (2014) · Folia Microbiologica · doi:10.1007/s12223-013-0280-4 · Cited by 431

Quorum Sensing Inhibitors as Anti-Biofilm Agents

Brackman, G., & Coenye, T. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140905114627 · Cited by 420

Selective Lysis of Bacteria but Not Mammalian Cells by Diastereomers of Melittin: Structure−Function Study

Oren, Z., & Shai, Y. (1997) · Biochemistry · doi:10.1021/bi962507l · Cited by 416

Natural antimicrobial peptides from bacteria: Characteristics and potential applications to fight against antibiotic resistance

Hassan, M., Kjos, M., Nes, I. F., Diep, D. B., & Lotfipour, F. (2012) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2012.05338.x · Cited by 402

Antimicrobial peptides and their interaction with biofilms of medically relevant bacteria

Batoni, G., Maisetta, G., & Esin, S. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.10.013 · Cited by 401

Innovative Food Science & Emerging Technologies

Dambolenaa, J. S., Zuninoa, M. P., Lópezb, A. G., Rubinsteinc, H. R., Zygadloa, J. A., Mwangi, J., Thoithi, G. N., Kibwage, I. O., Mwalukumbi, J. M., & Kariuki, S. (2011) · Cited by 394

Marine Peptides: Bioactivities and Applications

Cheung, R., Ng, T., & Wong, J. (2015) · Marine Drugs · doi:10.3390/md13074006 · Cited by 391

Microcins, gene-encoded antibacterial peptides from enterobacteria

Duquesne, S., Destoumieux-Garzón, D., Peduzzi, J., & Rebuffat, S. (2007) · Natural Product Reports · doi:10.1039/b516237h · Cited by 390

The therapeutic applications of antimicrobial peptides (AMPs): a patent review

Kang, H.-K., Kim, C., Seo, C. H., & Park, Y. (2017) · Journal of Microbiology · doi:10.1007/s12275-017-6452-1 · Cited by 386

Benefits and risks of antimicrobial use in food-producing animals

Hao, H., Cheng, G., Iqbal, Z., Ai, X., Hussain, H. I., Huang, L., Dai, M., Wang, Y., Liu, Z., & Yuan, Z. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00288 · Cited by 383

Progress in biophysics and molecular biology

ScienceDirect (1963) · Cited by 383

Antimicrobial peptides and plant disease control

Montesinos, E. (2007) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2007.00683.x · Cited by 376

Antimicrobial peptides under clinical investigation

Koo, H. B., & Seo, J. (2019) · Peptide Science · doi:10.1002/pep2.24122 · Cited by 376

Innate Immunity

Charlet, M., Chernysh, S., Philippe, H., Hetru, C., Hoffmann, J. A., & Bulet, P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.36.21808 · Cited by 371

Interaction between Heat Shock Proteins and Antimicrobial Peptides

Otvos, O, I., Rogers, M. E., Consolvo, P. J., Condie, B. A., Lovas, S., Bulet, P., & Blaszczyk-Thurin, M. (2000) · Biochemistry · doi:10.1021/bi0012843 · Cited by 370

Refined Structure of Charybdotoxin: Common Motifs in Scorpion Toxins and Insect Defensins

Bontems, F., Roumestand, C., Gilquin, B., Ménez, A., & Toma, F. (1991) · Science · doi:10.1126/science.1720574 · Cited by 365

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

Daptomycin: Another Novel Agent for Treating Infections Due to Drug‐Resistant Gram‐Positive Pathogens

Carpenter, C. F., & Chambers, H. F. (2004) · Clinical Infectious Diseases · doi:10.1086/383472 · Cited by 358

Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action

Nissen-Meyer, J., & Nes, I. F. (1997) · Archives of Microbiology · doi:10.1007/s002030050418 · Cited by 356

Pediocins: The bacteriocins of Pediococci. Sources, production, properties and applications

Papagianni, M., & Anastasiadou, S. (2009) · Microbial Cell Factories · doi:10.1186/1475-2859-8-3 · Cited by 342

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

Protein Expression and Purification

Růčková, E., Müller, P., & Vojtěšek, B. (2014) · Klinicka onkologie · doi:10.14735/amko20141s92 · Cited by 328

Strategies employed in the design and optimization of synthetic antimicrobial peptide amphiphiles with enhanced therapeutic potentials

Ong, Z. Y., Wiradharma, N., & Yang, Y. Y. (2014) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2014.10.013 · Cited by 313

A sub-nanometre view of how membrane curvature and composition modulate lipid packing and protein recruitment

Vanni, S., Hirose, H., Barelli, H., Antonny, B., & Gautier, R. (2014) · Nature Communications · doi:10.1038/ncomms5916 · Cited by 308

Susceptibility of Phytopathogenic Bacteria to Wheat Purothionins In Vitro

Caleya, R. F. D., Gonzalez-Pascual, B., García‐Olmedo, F., & Carbonero, P. (1972) · Applied Microbiology · doi:10.1128/aem.23.5.998-1000.1972 · Cited by 305

Probiotics and Antimicrobial Proteins

(2013) · Probiotics and Antimicrobial Proteins · doi:10.1007/12602.1867-1314 · Cited by 292

Selective Killing of Vaccinia Virus by LL-37: Implications for Eczema Vaccinatum

Howell, M. D., Jones, J. F., Kisich, K. O., Streib, J. E., Gallo, R. L., & Leung, D. Y. M. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.3.1763 · Cited by 291

The importance of plant health to food security

Flood, J. (2010) · Food Security · doi:10.1007/s12571-010-0072-5 · Cited by 283

Contribution of Amphipathicity and Hydrophobicity to the Antimicrobial Activity and Cytotoxicity of β-Hairpin Peptides

Edwards, I. A., Elliott, A. G., Kavanagh, A. M., Zuegg, J., Blaskovich, M. A. T., & Cooper, M. A. (2016) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.6b00045 · Cited by 277

Advances in plant molecular farming

Obembe, O. O., Popoola, J. O., Leelavathi, S., & Reddy, S. V. (2011) · Biotechnology Advances · doi:10.1016/j.biotechadv.2010.11.004 · Cited by 276

The association of posttraumatic stress disorder and metabolic syndrome: a study of increased health risk in veterans

Heppner, P. S., Crawford, E. F., Haji, U. A., Afari, N., Hauger, R. L., Dashevsky, B. A., Horn, P. S., Nunnink, S. E., & Baker, D. G. (2009) · BMC Medicine · doi:10.1186/1741-7015-7-1 · Cited by 274

Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution

Gesell, J., Zasloff, M., & Opella, S. J. (1997) · Journal of Biomolecular NMR · doi:10.1023/a:1018698002314 · Cited by 274

Application of Antimicrobial Peptides of the Innate Immune System in Combination With Conventional Antibiotics—A Novel Way to Combat Antibiotic Resistance?

Zharkova, M. S., Orlov, D. S., Golubeva, O. Y., Chakchir, O. B., Eliseev, I. E., Grinchuk, T. M., & Shamova, O. V. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00128 · Cited by 272

DBAASP v.2: an enhanced database of structure and antimicrobial/cytotoxic activity of natural and synthetic peptides

Pirtskhalava, M., Gabrielian, A., Cruz, P., Griggs, H. L., Squires, R. B., Hurt, D. E., Grigolava, M., Chubinidze, M., Gogoladze, G., Vishnepolsky, B., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1174 · Cited by 244

Prokaryotic lifestyles in deep sea habitats

Lauro, F. M., & Bartlett, D. H. (2008) · Extremophiles · doi:10.1007/s00792-006-0059-5 · Cited by 222

Combination Effects of Antimicrobial Peptides

Yu, G., Baeder, D. Y., Regoes, R. R., & Rolff, J. (2016) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02434-15 · Cited by 220

Pharmacokinetics/pharmacodynamics of colistin and polymyxin B: are we there yet?

Tran, T. B., Velkov, T., Nation, R. L., Forrest, A., Tsuji, B. T., Bergen, P. J., & Li, J. (2016) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2016.09.010 · 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

Retrocyclin, an Antiretroviral θ-Defensin, Is a Lectin

Wang, W., Cole, A. M., Hong, T., Waring, A. J., & Lehrer, R. I. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.9.4708 · Cited by 194

The next generation of antimicrobial peptides (AMPs) as molecular therapeutic tools for the treatment of diseases with social and economic impacts

da Cunha, N. B., Cobacho, N. B., Viana, J. F. C., Lima, L. A., Sampaio, K. B. O., Dohms, S. S. M., Ferreira, A. C. R., de la Fuente-Núñez, C., Costa, F. F., Franco, O. L., et al. (2017) · Drug Discovery Today · doi:10.1016/j.drudis.2016.10.017 · Cited by 192

An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome

Florin, T., Maracci, C., Graf, M., Karki, P., Klepacki, D., Berninghausen, O., Beckmann, R., Vázquez-Laslop, N., Wilson, D. N., Rodnina, M. V., et al. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3439 · Cited by 190

Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition

Gagnon, M. G., Roy, R. N., Lomakin, I. B., Florin, T., Mankin, A. S., & Steitz, T. A. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw018 · Cited by 186

Anti-biofilm peptides as a new weapon in antimicrobial warfare

Pletzer, D., Coleman, S. R., & Hancock, R. E. (2016) · Current Opinion in Microbiology · doi:10.1016/j.mib.2016.05.016 · Cited by 184

Copsin, a Novel Peptide-based Fungal Antibiotic Interfering with the Peptidoglycan Synthesis

Essig, A., Hofmann, D., Münch, D., Gayathri, S., Künzler, M., Kallio, P. T., Sahl, H.-G., Wider, G., Schneider, T., & Aebi, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.599878 · Cited by 179

Plant storage proteins with antimicrobial activity: novel insights into plant defense mechanisms

de Souza Cândido, E., Pinto, M. F. S., Pelegrini, P. B., Lima, T. B., Silva, O. N., Pogue, R., Grossi‐de‐Sá, M. F., & Franco, O. L. (2011) · The FASEB Journal · doi:10.1096/fj.11-184291 · Cited by 177

Recombinant production of antimicrobial peptides in heterologous microbial systems

Ingham, A. B., & Moore, R. J. (2007) · Biotechnology and Applied Biochemistry · doi:10.1042/ba20060207 · Cited by 175

MSI-99, a magainin analogue, imparts enhanced disease resistance in transgenic tobacco and banana

Chakrabarti, A., Ganapathi, T. R., Mukherjee, P. K., & Bapat, V. A. (2003) · Planta · doi:10.1007/s00425-002-0918-y · Cited by 172

Effects of dietary supplementation with an expressed fusion peptide bovine lactoferricin–lactoferrampin on performance, immune function and intestinal mucosal morphology in piglets weaned at age 21 d

Tang, Z., Yin, Y., Zhang, Y., Huang, R., Sun, Z., Li, T., Chu, W., Kong, X., Li, L., Geng, M., et al. (2008) · British Journal of Nutrition · doi:10.1017/s0007114508055633 · Cited by 171

Advances in Protein Chemistry and Structural Biology

(2021) · Advances in Protein Chemistry and Structural Biology · doi:10.1016/s1876-1623(21)00003-1 · Cited by 169

Solution NMR studies of amphibian antimicrobial peptides: Linking structure to function?

Haney, E. F., Hunter, H. N., Matsuzaki, K., & Vogel, H. J. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.01.002 · Cited by 169

Effects of the antimicrobial peptide cecropin AD on performance and intestinal health in weaned piglets challenged with Escherichia coli

Wu, S., Zhang, F., Huang, Z., Liu, H., Xie, C., Zhang, J., Thacker, P. A., & Qiao, S. (2012) · Peptides · doi:10.1016/j.peptides.2012.03.030 · Cited by 169

Biomedical Science, Engineering and Technology

(2012) · InTech eBooks · doi:10.5772/1020 · Cited by 168

Antimicrobial peptides from different plant sources: Isolation, characterisation, and purification

Tang, S.-S., Prodhan, Z. H., Biswas, S. K., Le, C.-F., & Sekaran, S. D. (2018) · Phytochemistry · doi:10.1016/j.phytochem.2018.07.002 · Cited by 168

Recombinant DNA procedures for producing small antimicrobial cationic peptides in bacteria

Piers, K. L., Brown, M. H., & Hancock, R. E. W. (1993) · Gene · doi:10.1016/0378-1119(93)90168-3 · Cited by 167

Marine Antimicrobial Peptides: Nature Provides Templates for the Design of Novel Compounds against Pathogenic Bacteria

Falanga, A., Lombardi, L., Franci, G., Vitiello, M., Iovene, M., Morelli, G., Galdiero, M., & Galdiero, S. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17050785 · Cited by 164

Application of antimicrobial peptides in agriculture and food industry

Keymanesh, K., Soltani, S., & Sardari, S. (2009) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-009-9984-7 · Cited by 162

Purification and characterization of three isoforms of chrysophsin, a novel antimicrobial peptide in the gills of the red sea bream, Chrysophrys major

Iijima, N., Tanimoto, N., Emoto, Y., Morita, Y., Uematsu, K., Murakami, T., & Nakai, T. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03419.x · Cited by 157

The Journal of General and Applied Microbiology

SAKAGUCHI, K. (1956) · Soil Science · doi:10.1097/00010694-195611000-00013 · Cited by 155

Antiviral Peptides: Identification and Validation

Agarwal, G., & Gabrani, R. (2020) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-020-10072-0 · Cited by 154

The Dolphin Proline-Rich Antimicrobial Peptide Tur1A Inhibits Protein Synthesis by Targeting the Bacterial Ribosome

Mardirossian, M., Pérébaskine, N., Benincasa, M., Gambato, S., Hofmann, S., Huter, P., Müller, C., Hilpert, K., Innis, C. A., Tossi, A., et al. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.02.004 · Cited by 148

Antimicrobial peptide production and plant-based expression systems for medical and agricultural biotechnology

Holásková, E., Galuszka, P., Frébort, I., & Öz, M. T. (2015) · Biotechnology Advances · doi:10.1016/j.biotechadv.2015.03.007 · Cited by 146

Discovery of six families of fungal defensin-like peptides provides insights into origin and evolution of the CSαβ defensins

Zhu, S. (2007) · Molecular Immunology · doi:10.1016/j.molimm.2007.06.354 · Cited by 146

A peptidomics study reveals the impressive antimicrobial peptide arsenal of the wax moth Galleria mellonella

Brown, S. E., Howard, A., Kasprzak, A. B., Gordon, K. H. J., & East, P. D. (2009) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2009.09.004 · Cited by 146

Omiganan Pentahydrochloride (MBI 226), a Topical 12-Amino-Acid Cationic Peptide: Spectrum of Antimicrobial Activity and Measurements of Bactericidal Activity

Sader, H. S., Fedler, K. A., Rennie, R. P., Stevens, S., & Jones, R. N. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.8.3112-3118.2004 · Cited by 144

Incorporation of a Hydrophobic Antibacterial Peptide into Amphiphilic Polyelectrolyte Multilayers: A Bioinspired Approach to Prepare Biocidal Thin Coatings

Guyomard-Lack, A., Dé, E., Jouenne, T., Malandain, J., Müller, G., & Glinel, K. (2008) · Advanced Functional Materials · doi:10.1002/adfm.200700793 · Cited by 139

Phylogenetic distribution, functional epitopes and evolution of the CSαβ superfamily

Zhu, S., Gao, B., & Tytgat, J. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5200-6 · Cited by 137

Physicochemical Features and Peculiarities of Interaction of AMP with the Membrane

Pirtskhalava, M., Vishnepolsky, B., Grigolava, M., & Managadze, G. (2021) · Pharmaceuticals · doi:10.3390/ph14050471 · Cited by 134

Molecular engineering of antimicrobial peptides: microbial targets, peptide motifs and translation opportunities

Cardoso, P. A., Glossop, H. D., Meikle, T. G., Aburto‐Medina, A., Conn, C. E., Sarojini, V., & Valéry, C. (2021) · Biophysical Reviews · doi:10.1007/s12551-021-00784-y · Cited by 128

Comparison of Biophysical and Biologic Properties of α‐Helical Enantiomeric Antimicrobial Peptides

Chen, Y., Vasil, A. I., Rehaume, L. M., Mant, C. T., Burns, J. L., Vasil, M. L., Hancock, R. E. W., & Hodges, R. S. (2006) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2006.00349.x · Cited by 125

Safety and tolerability of the antimicrobial peptide human lactoferrin 1-11 (hLF1-11)

van der Velden, W. J. F. M., van Iersel, T. M., Blijlevens, N. M. A., & Donnelly, J. P. (2009) · BMC Medicine · doi:10.1186/1741-7015-7-44 · Cited by 119

Collagencin, an antibacterial peptide from fish collagen: Activity, structure and interaction dynamics with membrane

Ennaas, N., Hammami, R., Gomaa, A. I., et al. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.03.121 · Cited by 117

Characterization of antimicrobial activity and mechanisms of low amphipathic peptides with different α-helical propensity

Zhu, X., Zhang, L., Wang, J., Ma, Z., Xu, W., Li, J., & Shan, A. (2015) · Acta Biomaterialia · doi:10.1016/j.actbio.2015.02.023 · Cited by 116

Suppression of SARS-CoV entry by peptides corresponding to heptad regions on spike glycoprotein

Yuan, K., Yi, L., Chen, J., Qu, X., Qing, T., Rao, X., Jiang, P., Hu, J., Xiong, Z., Nie, Y., et al. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.05.046 · Cited by 114

Inhibition of Plant-Pathogenic Bacteria by Short Synthetic Cecropin A-Melittin Hybrid Peptides

Ferré, R., Badosa, E., Feliu, L., Planas, M., Montesinos, E., & Bardají, E. (2006) · Applied and Environmental Microbiology · doi:10.1128/aem.72.5.3302-3308.2006 · Cited by 113

Oyster hemocytes express a proline-rich peptide displaying synergistic antimicrobial activity with a defensin

Gueguen, Y., Romestand, B., Julie, F., Schmitt, P., Destoumieux‐Garzón, D., Vandenbulcke, F., Bulet, P., & Bachère, E. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.07.021 · Cited by 112

Molecular mechanism of synergy between the antimicrobial peptides PGLa and magainin 2

Zerweck, J., Strandberg, E., Kukharenko, O. E., Reichert, J. C., Bürck, J., Wadhwani, P., & Ulrich, A. S. (2017) · Scientific Reports · doi:10.1038/s41598-017-12599-7 · Cited by 112

Lipid shape is a key factor for membrane interactions of amphipathic helical peptides

Strandberg, E., Tiltak, D., Ehni, S., Wadhwani, P., & Ulrich, A. S. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.02.027 · Cited by 108

Cathelicidin-Derived Antimicrobial Peptides Inhibit Zika Virus Through Direct Inactivation and Interferon Pathway

He, M., Zhang, H., Li, Y., Wang, G., Tang, B., Zhao, J., Huang, Y., & Zheng, J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00722 · Cited by 108

Treatment of microbial biofilms in the post-antibiotic era: prophylactic and therapeutic use of antimicrobial peptides and their design by bioinformatics tools

Luca, M. D., Maccari, G., & Nifosì, R. (2014) · Pathogens and Disease · doi:10.1111/2049-632x.12151 · Cited by 107

Synergistic Transmembrane Alignment of the Antimicrobial Heterodimer PGLa/Magainin

Tremouilhac, P., Strandberg, E., Wadhwani, P., & Ulrich, A. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604759200 · Cited by 107

International Journal of Peptide Research and Therapeutics

(2013) · International Journal of Peptide Research and Therapeutics · doi:10.1007/10989.1573-3904 · Cited by 107

Novel Synthetic, Salt-Resistant Analogs of Human Beta-Defensins 1 and 3 Endowed with Enhanced Antimicrobial Activity

Scudiero, O., Galdiero, S., Cantisani, M., Noto, R. D., Vitiello, M., Galdiero, M., Naclerio, G., Cassiman, J., Pedone, C., Castaldo, G., et al. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01550-09 · Cited by 105

Ohmyungsamycins A and B: Cytotoxic and Antimicrobial Cyclic Peptides Produced by Streptomyces sp. from a Volcanic Island

Um, S., Choi, T. J., Kim, H., Kim, B., Kim, S.-H., Lee, S. K., Oh, K., Shin, J., & Oh, D. (2013) · The Journal of Organic Chemistry · doi:10.1021/jo401974g · Cited by 104

Bioactive Marine Metabolites, IV. Isolation and the Amino Acid Composition of Discodermin A, an Antimicrobial Peptide, from the Marine Sponge Discodermia kiiensis

Matsunaga, S., Fusetani, N., & KÔNOSU, S. (1985) · Journal of Natural Products · doi:10.1021/np50038a006 · Cited by 103

Identification and characterization of a primary antibacterial domain in CAP18, a lipopolysaccharide binding protein from rabbit leukocytes

Tossi, A., Scocchi, M., Skerlavaj, B., et al. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80395-1 · Cited by 103

Effects of dietary supplementation of antimicrobial peptide-A3 on growth performance, nutrient digestibility, intestinal and fecal microflora and intestinal morphology in weanling pigs

Yoon, J. H., Ingale, S. L., Kim, J., Kim, K. H., Lee, S., Park, Y. K., Kwon, I. K., & Chae, B. J. (2012) · Animal Feed Science and Technology · doi:10.1016/j.anifeedsci.2012.06.009 · Cited by 102

The Potential of Antimicrobial Peptides as an Antiviral Therapy against COVID-19

Elnagdy, S. M., & AlKhazindar, M. (2020) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.0c00059 · Cited by 98

Cyclic Peptides as Novel Therapeutic Microbicides: Engineering of Human Defensin Mimetics

Falanga, A., Nigro, E., Biasi, M.-G. D., Daniele, A., Morelli, G., Galdiero, S., & Scudiero, O. (2017) · Molecules · doi:10.3390/molecules22071217 · Cited by 96

Peptides from Royal Jelly: studies on the antimicrobial activity of jelleins, jelleins analogs and synergy with temporins

Romanelli, A., Moggio, L., Montella, R. C., Campiglia, P., Iannaccone, M., Capuano, F., Pedone, C., & Capparelli, R. (2011) · Journal of Peptide Science · doi:10.1002/psc.1316 · Cited by 94

Plant defensins and virally encoded fungal toxin KP4 inhibit plant root growth

Allen, A., Snyder, A. K., Preuss, M. L., Nielsen, E., Shah, D. M., & Smith, T. J. (2007) · Planta · doi:10.1007/s00425-007-0620-1 · Cited by 93

Dietary Nisin Modulates the Gastrointestinal Microbial Ecology and Enhances Growth Performance of the Broiler Chickens

Józefiak, D., Kierończyk, B., Juśkiewicz, J., Zduńczyk, Z., Rawski, M., Długosz, J., Sip, A., & Højberg, O. (2013) · PLoS ONE · doi:10.1371/journal.pone.0085347 · Cited by 91

Potential novel therapeutic strategies in cystic fibrosis: antimicrobial and anti-biofilm activity of natural and designed α-helical peptides against Staphylococcus aureus, Pseudomonas aeruginosa, and Stenotrophomonas maltophilia

Pompilio, A., Crocetta, V., Scocchi, M., Pomponio, S., Vincenzo, V. D., Mardirossian, M., Gherardi, G., Fiscarelli, E. V., Dicuonzo, G., Gennaro, R., et al. (2012) · BMC Microbiology · doi:10.1186/1471-2180-12-145 · Cited by 91

Rationally Designed α‐Helical Broad‐Spectrum Antimicrobial Peptides with Idealized Facial Amphiphilicity

Wiradharma, N., Sng, M. Y. S., Khan, M., Ong, Z. Y., & Yang, Y. Y. (2012) · Macromolecular Rapid Communications · doi:10.1002/marc.201200534 · Cited by 90

Lipoglycopeptide Antibacterial Agents in Gram-Positive Infections: A Comparative Review

Françoise Van Bambeke, A. (2015) · Drugs · doi:10.1007/s40265-015-0505-8 · Cited by 90

A novel antifungal hevein‐type peptide from Triticum kiharae seeds with a unique 10‐cysteine motif

Odintsova, T. I., Vassilevski, A. A., Slavokhotova, A. A., Musolyamov, A. K., Finkina, E. I., Khadeeva, N. V., Rogozhin, E. A., Korostyleva, T. V., Pukhalsky, V. A., Grishin, E. V., et al. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07135.x · Cited by 89

Cysteine-stabilized αβ defensins: From a common fold to antibacterial activity

Dias, R. O., & Franco, O. L. (2015) · Peptides · doi:10.1016/j.peptides.2015.04.017 · Cited by 89

Joker: An algorithm to insert patterns into sequences for designing antimicrobial peptides

Porto, W. F., Fensterseifer, I. C. M., Ribeiro, S. M., & Franco, O. L. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.06.011 · Cited by 89

Combining genetic algorithm with machine learning strategies for designing potent antimicrobial peptides

Boone, K., Wisdom, C., Camarda, K., Spencer, P., & Tamerler, C. (2021) · BMC Bioinformatics · doi:10.1186/s12859-021-04156-x · Cited by 89

The Role of Antimicrobial Peptides in Influenza Virus Infection and Their Potential as Antiviral and Immunomodulatory Therapy

Hsieh, I.-N., & Hartshorn, K. L. (2016) · Pharmaceuticals · doi:10.3390/ph9030053 · Cited by 88

Inhibition of Coronavirus Entry In Vitro and Ex Vivo by a Lipid-Conjugated Peptide Derived from the SARS-CoV-2 Spike Glycoprotein HRC Domain

Outlaw, V. K., Bovier, F. T., Mears, M. C., Cajimat, M. N. B., Zhu, Y., Lin, M. J., Addetia, A., Lieberman, N. A. P., Peddu, V., Xie, X., et al. (2020) · mBio · doi:10.1128/mbio.01935-20 · Cited by 86

Antimicrobial Peptides: Insights into Membrane Permeabilization, Lipopolysaccharide Fragmentation and Application in Plant Disease Control

Datta, A., Ghosh, A., Airoldi, C., Sperandeo, P., Mroué, K. H., Jiménez‐Barbero, J., Kundu, P., Ramamoorthy, A., & Bhunia, A. (2015) · Scientific Reports · doi:10.1038/srep11951 · Cited by 84

Expression of active recombinant human lactoferrin in the milk of transgenic goats

Zhang, J., Li, L., Cai, Y.-F., Xu, X., Chen, J., Wu, Y., Yu, H., Yu, G., Liu, S., Zhang, A., et al. (2007) · Protein Expression and Purification · doi:10.1016/j.pep.2007.10.015 · Cited by 83

Evaluation of Transgenic ‘Chardonnay’ (Vitis vinifera) Containing Magainin Genes for Resistance to Crown Gall and Powdery Mildew

Vidal, J. R., Kikkert, J. R., Malnoy, M., Wallace, P. G., Barnard, J. A., & Reisch, B. I. (2006) · Transgenic Research · doi:10.1007/s11248-005-4423-5 · Cited by 82

The Cyclic Cystine Ladder in θ-Defensins Is Important for Structure and Stability, but Not Antibacterial Activity

Conibear, A. C., Rosengren, K. J., Daly, N. L., Henriques, S. T., & Craik, D. J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.451047 · Cited by 81

Review article: Commercialization of whole-plant systems for biomanufacturing of protein products: evolution and prospects

Davies, H. M. (2010) · Plant Biotechnology Journal · doi:10.1111/j.1467-7652.2010.00550.x · Cited by 80

The antifungal Dm‐AMP1 protein from Dahlia merckii expressed in Solanum melongena is released in root exudates and differentially affects pathogenic fungi and mycorrhizal symbiosis

Turrini, A., Sbrana, C., Pitto, L., et al. (2004) · New Phytologist · doi:10.1111/j.1469-8137.2004.01107.x · Cited by 80

Spheniscins, Avian β-Defensins in Preserved Stomach Contents of the King Penguin, Aptenodytes patagonicus

Thouzeau, C., Maho, Y. L., Froget, G., Ehret‐Sabatier, L., Bohec, C. L., Hoffmann, J. A., & Bulet, P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306839200 · Cited by 80

Genetic modification of potato against microbial diseases: in vitro and in planta activity of a dermaseptin B1 derivative, MsrA2

Osusky, M., Osuska, L., Kay, W. W., & Misra, S. (2005) · Theoretical and Applied Genetics · doi:10.1007/s00122-005-2056-y · Cited by 76

Isolation and Characterization of a Defensin-Like Peptide (Coprisin) from the Dung Beetle,Copris tripartitus

Hwang, J., Lee, J., Kim, Y.-J., Bang, H., Yun, E., Kim, S., Suh, H., Kang, B.-R., Nam, S., Jeon, J., et al. (2009) · International Journal of Peptides · doi:10.1155/2009/136284 · Cited by 75

Structural remodeling and oligomerization of human cathelicidin on membranes suggest fibril-like structures as active species

Sancho‐Vaello, E., François, P., Bonetti, E.-J., Lilie, H., Finger, S., Gil-Ortiz, F., Gil‐Carton, D., & Zeth, K. (2017) · Scientific Reports · doi:10.1038/s41598-017-14206-1 · Cited by 75

Antimicrobial packaging based on ɛ-polylysine bioactive film for the control of mycotoxigenic fungi in vitro and in bread

Luz, C., Calpe, J., Saladino, F., Luciano, F. B., Fernández-Franzón, M., Mañes, J., & Meca, G. (2017) · Journal of Food Processing and Preservation · doi:10.1111/jfpp.13370 · Cited by 72

Enhanced resistance to early blight in transgenic tomato lines expressing heterologous plant defense genes

Schaefer, S. C., Gašić, K., Cammue, B. P. A., et al. (2005) · Planta · doi:10.1007/s00425-005-0026-x · Cited by 70

Peptide based antimicrobials: Design strategies and therapeutic potential

Hazam, P. K., Goyal, R., & Ramakrishnan, V. (2018) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2018.08.006 · Cited by 69

Structural Characterization of the Cyclic Cystine Ladder Motif of θ-Defensins

Conibear, A. C., Rosengren, K. J., Harvey, P. J., & Craik, D. J. (2012) · Biochemistry · doi:10.1021/bi301363a · Cited by 68

NP213 (Novexatin®): A unique therapy candidate for onychomycosis with a differentiated safety and efficacy profile

Mercer, D. K., Robertson, J., Miller, L., Stewart, C. S., & O′Neil, D. A. (2020) · Medical Mycology · doi:10.1093/mmy/myaa015 · Cited by 67

Natural antimicrobial agents to improve foods shelf life

Delgado, L. H. V., Nevárez‐Moorillón, G. V., Caro, I., Quinto, E. J., & Mateo, J. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-817190-5.00004-5 · Cited by 66

Broad Antiviral Activity and Crystal Structure of HIV-1 Fusion Inhibitor Sifuvirtide

Yao, X. Q., Chong, H., Zhang, C., Waltersperger, S., Wang, M., Cui, S., & He, Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.317883 · Cited by 65

Bacterial resistance to antimicrobial peptides

Abdi, M., Mirkalantari, S., & Amirmozafari, N. (2019) · Journal of Peptide Science · doi:10.1002/psc.3210 · Cited by 65

De Novo Designed Amphipathic α-Helical Antimicrobial Peptides Incorporating Dab and Dap Residues on the Polar Face To Treat the Gram-Negative Pathogen, Acinetobacter baumannii

Mant, C. T., Jiang, Z., Gera, L., Davis, T., Nelson, K. L., Bevers, S. G., & Hodges, R. S. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01785 · Cited by 64

Expression of a magainin-type antimicrobial peptide gene (MSI-99) in tomato enhances resistance to bacterial speck disease

Alan, A. R., Blowers, A. D., & Earle, E. D. (2004) · Plant Cell Reports · doi:10.1007/s00299-003-0702-x · Cited by 60

Defensins: The Case for Their Use against Mycobacterial Infections

Dong, H., Lv, Y., Zhao, D., Barrow, P., & Zhou, X. (2016) · Journal of Immunology Research · doi:10.1155/2016/7515687 · Cited by 54

International Journal of Peptide and Protein Research

(2010) · International journal of peptide & protein research · doi:10.1111/(issn)1399-3011a · Cited by 54

Membrane Interaction of Chrysophsin-1, a Histidine-Rich Antimicrobial Peptide from Red Sea Bream

Mason, A. J., Bertani, P., Moulay, G., Marquette, A., Perrone, B., Drake, A. F., Kichler, A., & Bechinger, B. (2007) · Biochemistry · doi:10.1021/bi701344m · Cited by 51

Erwinia soft rot resistance of potato cultivars expressing antimicrobial peptide tachyplesin I

Allefs, S. J. H. M., de Jong, E. R., Florack, D. E. A., Hoogendoorn, C., & Stiekema, W. J. (1996) · Molecular Breeding · doi:10.1007/bf00441425 · Cited by 50

Synthetic and structural studies on Pyrularia pubera thionin: a single‐residue mutation enhances activity against Gram‐negative bacteria

Vila‐Perelló, M., Sánchez‐Vallet, A., García‐Olmedo, F., Molina, A., & Andreu, D. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00053-x · Cited by 49

Role of Aromatic Amino Acids in Lipopolysaccharide and Membrane Interactions of Antimicrobial Peptides for Use in Plant Disease Control

Datta, A., Bhattacharyya, D., Singh, S., Ghosh, A., Schmidtchen, A., Malmsten, M., & Bhunia, A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.719575 · Cited by 49

Heptad Repeat-Derived Peptides Block Protease-Mediated Direct Entry from the Cell Surface of Severe Acute Respiratory Syndrome Coronavirus but Not Entry via the Endosomal Pathway

Ujike, M., Nishikawa, H., Otaka, A., Yamamoto, N., Yamamoto, N., Matsuoka, M., Kodama, E. N., Fujii, N., & Taguchi, F. (2007) · Journal of Virology · doi:10.1128/jvi.01697-07 · Cited by 47

Innate Immunity in Plants: The Role of Antimicrobial Peptides

Stotz, H. U., Waller, F., & Wang, K. (2012) · Springer eBooks · doi:10.1007/978-3-0348-0541-4_2 · Cited by 46

Retro analog concept: comparative study on physico-chemical and biological properties of selected antimicrobial peptides

Neubauer, D., Jaśkiewicz, M., Migoń, D., Bauer, M., Sikora, K., Sikorska, E., Kamysz, E., & Kamysz, W. (2017) · Amino Acids · doi:10.1007/s00726-017-2473-7 · Cited by 46

Chemical synthesis and biological evaluation of an antimicrobial peptide gonococcal growth inhibitor

Wade, J. D., Lin, F. W., Hossain, M. A., & Dawson, R. M. (2012) · Amino Acids · doi:10.1007/s00726-012-1305-z · Cited by 44

Virocidal activity of Egyptian scorpion venoms against hepatitis C virus

El-Bitar, A. M. H., Sarhan, M. M. H., Aoki, C., Takahara, Y., Komoto, M., Deng, L., Moustafa, M. A., & Hotta, H. (2015) · Virology Journal · doi:10.1186/s12985-015-0276-6 · Cited by 43

Pichia pastoris: A notable heterologous expression system for the production of foreign proteins—Vaccines

Balamurugan, B., Reddy, G. R., & Suryanarayana, V. V. S. (2007) · Cited by 39

Chimeric Beta-Defensin Analogs, Including the Novel 3NI Analog, Display Salt-Resistant Antimicrobial Activity and Lack Toxicity in Human Epithelial Cell Lines

Scudiero, O., Galdiero, S., Nigro, E., Vecchio, L. D., Noto, R. D., Cantisani, M., Colavita, I., Galdiero, M., Cassiman, J., Daniele, A., et al. (2013) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00934-12 · Cited by 36

Primary structure and cellular localization of callinectin, an antimicrobial peptide from the blue crab

Noga, E. J., Stone, K. L., Wood, A., Gordon, W. L., & Robinette, D. W. (2010) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2010.11.015 · Cited by 34

Antimicrobial Peptide Precursor Structures Suggest Effective Production Strategies

Kozlov, S. A., Vassilevski, A. A., & Grishin, E. V. (2008) · Recent Patents on Inflammation & Allergy Drug Discovery · doi:10.2174/187221308783399261 · Cited by 34

Potency evaluation of a dermaseptin S4 derivative for antimicrobial food packaging applications

Miltz, J. W., Rydlo, T., Mor, A., & Polyakov, V. (2006) · Packaging Technology and Science · doi:10.1002/pts.738 · Cited by 34

Mammary Gland Expression of Antibacterial Peptide Genes to Inhibit Bacterial Pathogens Causing Mastitis

Zhang, J. X., Zhang, S. F., Wang, T. D., Guo, X., & Hu, R. (2007) · Journal of Dairy Science · doi:10.3168/jds.2007-0301 · Cited by 33

Structure and antibacterial activities of new cyclic peptide antibiotics, pargamicins B, C and D, from Amycolatopsis sp. ML1-hF4

Hashizume, H., Sawa, R., Yamashita, K., Nishimura, Y., & Igarashi, M. (2017) · The Journal of Antibiotics · doi:10.1038/ja.2017.34 · Cited by 33

Defense peptides: recent developments

Cytryńska, M., & Zdybicka‐Barabas, A. (2015) · BioMolecular Concepts · doi:10.1515/bmc-2015-0014 · Cited by 31

The Structure/Function Relationship in Antimicrobial Peptides: What Can we Obtain From Structural Data?

Cardoso, M. H. E. S., Oshiro, K. G. N., de Rezende, S. B., Cândido, E. D. S., & Franco, O. L. (2018) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2018.01.008 · Cited by 31

Functional structure and antimicrobial activity of persulcatusin, an antimicrobial peptide from the hard tick Ixodes persulcatus

Miyoshi, N., Saito, T., Ohmura, T., Kuroda, K., Kazumasa, S., Ihara, K., & Isogai, E. (2016) · Parasites & Vectors · doi:10.1186/s13071-016-1360-5 · Cited by 30

1.1.3.4 Paramagnetic anisotropy

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