Anti-microbial peptides: from invertebrates to vertebrates
Abstract
Gene-encoded anti-microbial peptides (AMPs) are widespread in nature, as they are synthesized by microorganisms as well as by multicellular organisms from both the vegetal and the animal kingdoms. These naturally occurring AMPs form a first line of host defense against pathogens and are involved in innate immunity. Depending on their tissue distribution, AMPs ensure either a systemic or a local protection of the organism against environmental pathogens. They are classified into three major groups: (i) peptides with an alpha-helical conformation (insect cecropins, magainins, etc.), (ii) cyclic and open-ended cyclic peptides with pairs of cysteine residues (defensins, protegrin, etc.), and (iii) peptides with an over-representation of some amino acids (proline rich, histidine rich, etc.). Most AMPs display hydrophobic and cationic properties, have a molecular mass below 25-30 kDa, and adopt an amphipathic structure (alpha-helix, beta-hairpin-like beta-sheet, beta-sheet, or alpha-helix/beta-sheet mixed structures) that is believed to be essential to their anti-microbial action. Interestingly, in recent years, a series of novel AMPs have been discovered as processed forms of large proteins. Despite the extreme diversity in their primary and secondary structures, all natural AMPs have the in vitro particularity to affect a large number of microorganisms (bacteria, fungi, yeast, virus, etc.) with identical or complementary activity spectra. This review focuses on AMPs forming alpha-helices, beta-hairpin-like beta-sheets, beta-sheets, or alpha-helix/beta-sheet mixed structures from invertebrate and vertebrate origins. These molecules show some promise for therapeutic use.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
AMPs can be secreted in the outer parts of the body and play functions in the control/establishment of ectosymbiosis, as described for the hydrothermal worm Alvinella pompejana.
“AMPs are chemical components that take part in both the internal and external immune defenses (i.e., they can be secreted in the outer parts of the body), thus playing functions in the control/establishment of ectosymbiosis as described for the hydrothermal worm Alvinella pompejana (19–21).”
From Antimicrobial Peptides and Ectosymbiotic Relationships: Involvement of a Novel Type IIa Crustin in the Life Cycle of a Deep-Sea Vent Shrimp (2020) · cites this paper as [20]
Cites
Phylogenetic Perspectives in Innate Immunity
Hoffmann, J. A., Kafatos, F. C., Janeway, C. A., & Ezekowitz, R. A. B. (1999) · Science · doi:10.1126/science.284.5418.1313 · Cited by 2,474 · see citing works
Zasloff, M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5449 · Cited by 2,305 · see citing works
Hepcidin, a urinary antimicrobial peptide synthesized in the liver
Park, C. H., Valore, E. V., Waring, A. J., & Ganz, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008922200 · Cited by 2,168 · see citing works
Shai, Y. (1999) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(99)00200-x · Cited by 1,872 · see citing works
Sequence and specificity of two antibacterial proteins involved in insect immunity
Steiner, H., Hultmark, D., Engström, Å., Bennich, H., & Boman, H. G. (1981) · Nature · doi:10.1038/292246a0 · Cited by 1,429 · see citing works
Cationic peptides: a new source of antibiotics
Hancock, R. E. W., & Lehrer, R. I. (1998) · Trends in biotechnology · doi:10.1016/s0167-7799(97)01156-6 · Cited by 1,348 · see citing works
Amphipathic, α-helical antimicrobial peptides
Tossi, A., Sandri, L., & Giangaspero, A. (2000) · Biopolymers · doi:10.1002/1097-0282(2000)55:1 · Cited by 1,245 · see citing works
The role of cationic antimicrobial peptides in innate host defences
Hancock, R. E. W., & Diamond, G. (2000) · Trends in Microbiology · doi:10.1016/s0966-842x(00)01823-0 · Cited by 1,233 · see citing works
Nicolas, G., Chauvet, C., Viatte, L., Danan, J. L., Bigard, X., Devaux, I., Beaumont, C., Kahn, A., & Vaulont, S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215686 · Cited by 1,214 · see citing works
Antimicrobial peptides in insects; structure and function
Bulet, P., Hétru, C., Dimarcq, J., & Hoffmann, D. (1999) · Developmental & Comparative Immunology · doi:10.1016/s0145-305x(99)00015-4 · Cited by 1,042 · see citing works
Self-citationIdentification of the bactericidal domain of lactoferrin
Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., Kawase, K., & TOMITA, M. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90346-f · Cited by 890 · see citing works
Frohm, M., Agerberth, B., Ahangari, G., Ståhle‐Bäckdahl, M., Lidén, S., Wigzell, H., & Gudmundsson, G. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.24.15258 · Cited by 803 · see citing works
Bals, R., Wang, X., ZASLOFF, M. A., & Wilson, J. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9541 · Cited by 745 · see citing works
Tang, Y., Yuan, J. J., Ösapay, G., Ősapay, K., Tran, D., Miller, C. J., Ouellette, A. J., & Selsted, M. E. (1999) · Science · doi:10.1126/science.286.5439.498 · Cited by 698 · see citing works
Tissue-Specific Inducible Expression of Antimicrobial Peptide Genes in Drosophila Surface Epithelia
Tzou, P., Ohresser, S., Ferrandon, D., Capovilla, M., Reichhart, J., Lemaître, B., Hoffmann, J. A., & Imler, J. (2000) · Immunity · doi:10.1016/s1074-7613(00)00072-8 · Cited by 613 · see citing works
Cole, A. M., Weis, P., & Diamond, G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.18.12008 · Cited by 541 · see citing works
García‐Olmedo, F., Molina, A., Alamillo, J. M., & Rodríguez‐Palenzuela, P. (1998) · Biopolymers · doi:10.1002/(sici)1097-0282(1998)47:6 · Cited by 521 · see citing works
Kragol, G., Lovas, S., Váradi, G., Condie, B. A., Hoffmann, R., & Otvos, L. J. (2001) · Biochemistry · doi:10.1021/bi002656a · Cited by 492 · see citing works
Structure–activity studies on magainins and other host defense peptides
Maloy, W. L., & Kari, U. P. (1995) · Biopolymers · doi:10.1002/bip.360370206 · Cited by 491 · see citing works
Destoumieux‐Garzón, D., Bulet, P., Loew, D., DORSSELAER, A. V., Rodríguez, J. A., & Evelyne Bachère, B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28398 · Cited by 442 · see citing works
Self-citationHunter, H. N., Fulton, D. B., Ganz, T., & Vogel, H. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205305200 · Cited by 400 · see citing works
Charlet, M., Chernysh, S., Philippe, H., Hétru, C., Hoffmann, J. A., & Bulet, P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.36.21808 · Cited by 374 · see citing works
Self-citationAntimicrobial peptides of vertebrates
Ganz, T., & Lehrer, R. I. (1998) · Current Opinion in Immunology · doi:10.1016/s0952-7915(98)80029-0 · Cited by 374 · see citing works
Bass hepcidin is a novel antimicrobial peptide induced by bacterial challenge
Shike, H., Lauth, X., Westerman, M. E., Ostland, V. E., Carlberg, J. M., Olst, J. C. V., Shimizu, C., Bulet, P., & Burns, J. C. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02881.x · Cited by 336 · see citing works
Self-citationFehlbaum, P., Bulet, P., Chernysh, S. I., Briand, J., Roussel, J., Letellìer, L., Hétru, C., & Hoffmann, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.3.1221 · Cited by 330 · see citing works
Self-citationMor, A., Huong, N. V., Delfour, A., Migliore-Samour, D., & Nicolas, P. (1991) · Biochemistry · doi:10.1021/bi00100a014 · Cited by 314 · see citing works
Cole, A. M., Hong, T., Boo, L. M., Nguyen, T. X., Zhao, C., Bristol, G., Zack, J. A., Waring, A. J., Yang, O. O., & Lehrer, R. I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052706399 · Cited by 298 · see citing works
Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus
Park, I. Y., Park, C. B., Kim, M. S., et al. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01238-1 · Cited by 286 · see citing works
Antimicrobial Peptides as Mediators of Epithelial Host Defense
Huttner, K. M., & Bevins, C. L. (1999) · Pediatric Research · doi:10.1203/00006450-199906000-00001 · Cited by 280 · see citing works
Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils.
Romeo, D., Skerlavaj, B., Bolognesi, M., & Gennaro, R. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81553-3 · Cited by 277 · see citing works
Lauth, X., Shike, H., Burns, J. C., Westerman, M. E., Ostland, V. E., Carlberg, J. M., Olst, J. C. V., Nizet, V., Taylor, S. W., Shimizu, C., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109173200 · Cited by 277 · see citing works
Self-citationSilva, P. I., Daffre, S., & Bulet, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001491200 · Cited by 272 · see citing works
Self-citationOriginal involvement of antimicrobial peptides in mussel innate immunity
Mitta, G., Vandenbulcke, F., & Roch, P. G. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02192-x · Cited by 266 · see citing works
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 257 · see citing works
Oren, Z., & Shai, Y. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0303n.x · Cited by 251 · see citing works
Lee, S. Y., Lee, B. L., & Söderhäll, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209239200 · Cited by 250 · see citing works
Orivel, J., Redeker, V., Caër, J. L., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100216200 · Cited by 241 · see citing works
Characterization of Novel Cysteine-rich Antimicrobial Peptides from Scorpion Blood
Ehret‐Sabatier, L., Loew, D., Goyffon, M., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.47.29537 · Cited by 230 · see citing works
Lamberty, M., Zachary, D., Lanot, R., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m002998200 · Cited by 227 · see citing works
Malm, J., Sørensen, O. E., Persson, T., Frohm‐Nilsson, M., Johansson, B., Bjartell, A. S., Lilja, H. G., Ståhle‐Bäckdahl, M., Borregaard, N., & Egesten, A. (2000) · Infection and Immunity · doi:10.1128/iai.68.7.4297-4302.2000 · Cited by 223 · see citing works
Hadrurin, a new antimicrobial peptide from the venom of the scorpion Hadrurus aztecus
Torres‐Larios, A., Gurrola, G. B., Zamudio, F. Z., et al. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01556.x · Cited by 206 · see citing works
Homodimeric θ-Defensins from Rhesus macaqueLeukocytes
Tran, D., Tran, P. A., Tang, Y., Yuan, J. J., Cole, T., & Selsted, M. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109117200 · Cited by 198 · see citing works
Innate immune response of Aedes aegypti
Lowenberger, C. A. (2001) · Insect Biochemistry and Molecular Biology · doi:10.1016/s0965-1748(00)00141-7 · Cited by 182 · see citing works
A novel antimicrobial peptide from the loach, Misgurnus anguillicaudatus
Park, C. B., Lee, J. H., Park, I. Y., Kim, M. S., & Kim, S. C. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00684-4 · Cited by 181 · see citing works
Fernandes, J. M. O. (2003) · Developmental & Comparative Immunology · doi:10.1016/s0145-305x(03)00120-4 · Cited by 181 · see citing works
Moerman, L., Bosteels, S., Noppe, W., Willems, J., Clynen, E., Schoofs, L., Thevissen, K., Tytgat, J., Eldere, J. V., van der Walt, J., et al. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03177.x · Cited by 180 · see citing works
Clavanins, α‐helical antimicrobial peptides from tunicate hemocytes
Lee, I. H., Zhao, C., Cho, Y., et al. (1997) · FEBS Letters · doi:10.1016/s0014-5793(96)01374-9 · Cited by 177 · see citing works
Antimicrobial Peptides from the Skin of a Korean Frog, Rana rugosa
Park, J. M., Jung, J.-E., & Lee, B. J. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.2757 · Cited by 168 · see citing works
Goraya, J., Wang, Y., Li, Z., et al. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01074.x · Cited by 165 · see citing works
Cole, A. M., Darouiche, R. O., Legarda, D., Connell, N. D., & Diamond, G. (2000) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.44.8.2039-2045.2000 · Cited by 161 · see citing works
Schuhmann, B., Seitz, V., Vilcinskas, A., et al. (2003) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.10091 · Cited by 158 · see citing works
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 · see citing works
Panyutich, A. V., Shi, J. N., Boutz, P. L., Zhao, C., & Ganz, T. (1997) · Infection and Immunity · doi:10.1128/iai.65.3.978-985.1997 · Cited by 153 · see citing works
Mignogna, G., Simmaco, M., Kreil, G., et al. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06172.x · Cited by 152 · see citing works
Lazarovici, P., Primor, N., & Loew, L. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66622-0 · Cited by 152 · see citing works
Castle, M., Nazarian, A., Yi, S. S., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.46.32555 · Cited by 141 · see citing works
Corzo, G. A., Villegas, E., Gómez‐Lagunas, F., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200511200 · Cited by 133 · see citing works
Zanetti, M., Sal, G. D., Storici, P., Schneider, C., & Romeo, D. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54182-x · Cited by 128 · see citing works
Pepsin-Mediated Processing of the Cytoplasmic Histone H2A to Strong Antimicrobial Peptide Buforin I
Kim, H. S., Yoon, H. S., Minn, I., Park, C. B., Lee, W. T., ZASLOFF, M. A., & Kim, S. C. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.6.3268 · Cited by 123 · see citing works
The solution structure of gomesin, an antimicrobial cysteine‐rich peptide from the spider
Mandard, N., Bulet, P., Caille, A., Daffre, S., & Vovelle, F. (2002) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2002.02760.x · Cited by 123 · see citing works
Self-citationTigerinins: Novel Antimicrobial Peptides from the Indian FrogRana tigerina
Sai, K. P., Jagannadham, M. V., Vairamani, M., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006615200 · Cited by 117 · see citing works
Mandard, N., Sodano, P., Labbe, H., Bonmatin, J., Bulet, P., Hétru, C., Ptak, M., & Vovelle, F. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2560404.x · Cited by 116 · see citing works
Self-citationJang, W. S., Kim, K. N., Lee, Y. S., et al. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02827-2 · Cited by 113 · see citing works
Lemaı̂tre, C., Orange, N., Saglio, P., et al. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0143h.x · Cited by 113 · see citing works
Kuhn‐Nentwig, L., Müller, J., Schaller, J., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111099200 · Cited by 111 · see citing works
Douglas, S. E., Gallant, J. W., Gong, Z., & Hew, C. S. (2001) · Developmental & Comparative Immunology · doi:10.1016/s0145-305x(00)00052-5 · Cited by 110 · see citing works
Styelin D, an Extensively Modified Antimicrobial Peptide from Ascidian Hemocytes
Taylor, S. W., Craig, A. G., Fischer, W. H., Park, M., & Lehrer, R. I. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006762200 · Cited by 109 · see citing works
Boulanger, N., Munks, R. J. L., Hamilton, J. V., Vovelle, F., Brun, R., Lehane, M. J., & Bulet, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206296200 · Cited by 105 · see citing works
Self-citationLeippe, M. (1999) · Developmental & Comparative Immunology · doi:10.1016/s0145-305x(99)00010-5 · Cited by 103 · see citing works
Tossi, A., Scocchi, M., Zanetti, M., Storici, P., & Gennaro, R. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20344.x · Cited by 100 · see citing works
Epithelia: Not just physical barriers
Ganz, T. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072073199 · Cited by 98 · see citing works
Boulanger, N., Brun, R., Ehret‐Sabatier, L., et al. (2002) · Insect Biochemistry and Molecular Biology · doi:10.1016/s0965-1748(02)00029-2 · Cited by 95 · see citing works
Antibacterial proteins in rainbow trout, Oncorhynchus mykiss
Smith, V. J., Fernandes, J. M. O., Jones, S., et al. (2000) · Fish & Shellfish Immunology · doi:10.1006/fsim.1999.0254 · Cited by 94 · see citing works
Ali, M. F., Soto, A., Knoop, F. C., et al. (2001) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(01)00272-2 · Cited by 92 · see citing works
The antimicrobial host defense of Drosophila.
Meister, M., Hétru, C., & Hoffmann, J. A. (2000) · Current Topics in Microbiology and Immunology · doi:10.1007/978-3-642-59674-2_2 · Cited by 86 · see citing works
Fernandes, J. M. O., Saint, N., Kemp, G. D., et al. (2003) · Biochemical Journal · doi:10.1042/bj20030259 · Cited by 86 · see citing works
Kim, H. S., Park, C. B., Kim, M. S., & Kim, S. C. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1814 · Cited by 81 · see citing works
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 · see citing works
Self-citationLamberty, M., Caille, A., Landon, C., Tassin-Moindrot, S., Hétru, C., Bulet, P., & Vovelle, F. (2001) · Biochemistry · doi:10.1021/bi0103563 · Cited by 79 · see citing works
Self-citationASABF, a Novel Cysteine-rich Antibacterial Peptide Isolated from the Nematode Ascaris suum
Kato, Y., & Komatsu, S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.48.30493 · Cited by 77 · see citing works
Insect peptides with improved protease‐resistance protect mice against bacterial infection
Otvos, L. J., Bokonyi, K., Varga, I., Ertl, H. C. J., Hoffmann, R., Bulet, P., Otvos, B., Wade, J. D., McManus, A. M., & Craik, D. J. (2000) · Protein Science · doi:10.1110/ps.9.4.742 · Cited by 77 · see citing works
Self-citationZhao, C., Liaw, L., Lee, I. H., et al. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00769-2 · Cited by 71 · see citing works
Steinborner, S. T., Currie, G., Bowie, J. H., et al. (1998) · Journal of Peptide Research · doi:10.1111/j.1399-3011.1998.tb00629.x · Cited by 71 · see citing works
Krishnakumari, V., & Nagaraj, R. (1997) · Journal of Peptide Research · doi:10.1111/j.1399-3011.1997.tb01173.x · Cited by 65 · see citing works
Interaction of hagfish cathelicidin antimicrobial peptides with model lipid membranes
Basáñez, G., Shinnar, A. E., & Zimmerberg, J. J. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03651-7 · Cited by 54 · see citing works
Membrane Activity of the Peptide Antibiotic Clavanin and the Importance of Its Glycine Residues
van Kan, E. J. M., van der Bent, A., Demel, R. A., & de Kruijff, B. (2001) · Biochemistry · doi:10.1021/bi0028136 · Cited by 52 · see citing works
Pierre, T. N., Séon, A. A., Amiche, M., et al. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01012.x · Cited by 49 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
The phagosome: compartment with a license to kill
Haas, A. (2007) · Traffic · doi:10.1111/j.1600-0854.2006.00531.x · Cited by 450 · see citing works
Antimicrobial peptides and plant disease control
Montesinos, E. (2007) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2007.00683.x · Cited by 376 · see citing works
Roudi, R., Syn, N. L., & Roudbary, M. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01320 · Cited by 139 · see citing works
Le Bloa, S., Boidin-Wichlacz, C., Cueff-Gauchard, V., Rosa, R. D., Cuvillier-Hot, V., Durand, L., Methou, P., Pradillon, F., Cambon-Bonavita, M.-A., & Tasiemski, A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01511 · Cited by 30 · see citing works
Lee, J., Lee, D., Choi, H., Kim, H. H., Kim, H., Hwang, J. S., Lee, D. G., & Kim, J. I. (2014) · BMB Reports · doi:10.5483/bmbrep.2014.47.11.262 · Cited by 25 · see citing works
- Authors
- Bulet, P., Stöcklin, R., & Menin, L.
- Affiliations
- Atheris Laboratories (Switzerland) (CH)
- Corresponding author
- Bulet, Philippe
- Venue
- Immunological Reviews
- Publisher
- Wiley
- Published
- 2004-03-05
- Volume
- 198
- Issue
- 1
- Pages
- 169-184
- ISSN
- 0105-2896 (ISSN-L)
- 1600-065X
- OpenAlex
- W2089175291
- Cited by
- 1,107
- References
- 87
- Citations by year
- 2026: 17 · 2025: 33 · 2024: 47 · 2023: 35 · 2022: 46 · 2021: 41 · 2020: 43 · 2019: 34 · 2018: 50 · 2017: 50 · 2016: 50 · 2015: 60 · 2014: 57 · 2013: 56 · 2012: 67
- FWCI
- 7.41
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Immunological Reviews (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Immunology and Microbiology › Immunology › Invertebrate Immune Response Mechanisms
- Physical Sciences › Chemistry › Organic Chemistry › Antimicrobial agents and applications
- Keywords
- antimicrobial peptides, innate immunity, host defense against infection, alpha-helical peptides, β-sheet peptides, cecropin, magainin, defensins, protegrins, proline-rich peptides, histidine-rich peptides
- MeSH terms
- Amino Acid Sequence, Animals, Anti-Bacterial Agents, Invertebrates, Models, Molecular, Molecular Sequence Data, Peptides, Cyclic, Vertebrates, Protein Structure, Secondary, Protein Structure, Tertiary, Antimicrobial Cationic Peptides
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 ›
Are you an author, or do you see a problem with this page? Request a review