Cathelicidins - a family of multifunctional antimicrobial peptides

Antimicrobial peptides of multicellular organisms

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Defensins. Natural peptide antibiotics of human neutrophils.

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Innate antimicrobial peptide protects the skin from invasive bacterial infection

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Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3

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The Expression of the Gene Coding for the Antibacterial Peptide LL-37 Is Induced in Human Keratinocytes during Inflammatory Disorders

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Activities of LL-37, a Cathelin-Associated Antimicrobial Peptide of Human Neutrophils

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Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells

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The human antimicrobial and chemotactic peptides LL-37 and α-defensins are expressed by specific lymphocyte and monocyte populations

Agerberth, B., Charo, J., Werr, J., Olsson, B., Idali, F., Lindbom, L., Kiessling, R., Jörnvall, H., Wigzell, H., & Gudmundsson, G. H. (2000) · Blood · doi:10.1182/blood.v96.9.3086 · Cited by 758 · see citing works

The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface

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Mechanism of Interaction of Different Classes of Cationic Antimicrobial Peptides with Planar Bilayers and with the Cytoplasmic Membrane of Escherichia coli

Wu, M., Maier, E., Benz, R., & Hancock, R. E. W. (1999) · Biochemistry · doi:10.1021/bi9826299 · Cited by 737 · see citing works

Cathelicidins: a novel protein family with a common proregion and a variable C‐terminal antimicrobial domain

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Amphipathic alpha 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 650 · see citing works

Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity

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The Human Gene FALL39 and Processing of the Cathelin Precursor to the Antibacterial Peptide LL‐37 in Granulocytes

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Human CAP18: a novel antimicrobial lipopolysaccharide-binding protein

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Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine

Boman, H. G., Agerberth, B., & Boman, A. (1993) · Infection and Immunity · doi:10.1128/iai.61.7.2978-2984.1993 · Cited by 554 · see citing works

Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins

Kokryakov, V. N., Harwig, S. S. L., Panyutich, E. A., Shevchenko, A. A., Gm, A., Валерьевна, Ш. О., Korneva, E. A., & Lehrer, R. I. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80175-t · Cited by 517 · see citing works

FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis.

Agerberth, B., Gunne, H., Odeberg, J., Kogner, P., Boman, H. G., & Gudmundsson, G. H. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.1.195 · Cited by 502 · see citing works

Epithelial antimicrobial peptides in host defense against infection

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Specific Lipopolysaccharide Found in Cystic Fibrosis Airway Pseudomonas aeruginosa

Ernst, R. K., Yi, E. C., Guo, L., Lim, K. B., Burns, J. L., Hackett, M., & Miller, S. I. (1999) · Science · doi:10.1126/science.286.5444.1561 · Cited by 484 · see citing works

How do bacteria resist human antimicrobial peptides?

Peschel, A. (2002) · Trends in Microbiology · doi:10.1016/s0966-842x(02)02333-8 · Cited by 462 · see citing works

Downregulation of bactericidal peptides in enteric infections: A novel immune escape mechanism with bacterial DNA as a potential regulator

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Identification of CRAMP, a Cathelin-related Antimicrobial Peptide Expressed in the Embryonic and Adult Mouse

Gallo, R. L., Kim, K. J., Bernfield, M. R., Kozak, C. A., Zanetti, M., Merluzzi, L., & Gennaro, R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13088 · Cited by 419 · see citing works

Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides

Dathe, M., Wieprecht, T., Nikolenko, H., et al. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00055-0 · Cited by 411 · see citing works

Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family

Shafer, W. M., Qu, X. D., Waring, A. J., & Lehrer, R. I. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1829 · Cited by 391 · see citing works

PR39, a peptide regulator of angiogenesis

Li, J., Post, M. J., Volk, R., Gao, Y., Li, M., Métais, C., Sato, K., Tsai, J. C., Aird, W. C., ROSENBERG, R. D., et al. (2000) · Nature Medicine · doi:10.1038/71527 · Cited by 387 · see citing works

The Human Antibacterial Cathelicidin, hCAP-18, Is Synthesized in Myelocytes and Metamyelocytes and Localized to Specific Granules in Neutrophils

Sørensen, O. E., Arnljots, K., Cowland, J. B., Bainton, D. F., & Borregaard, N. (1997) · Blood · doi:10.1182/blood.v90.7.2796 · Cited by 364 · see citing works

Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds.

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Antimicrobial Peptides: Properties and Applicability

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Statistical analysis of alamethicin channels in black lipid membranes

Boheim, G. (1974) · The Journal of Membrane Biology · doi:10.1007/bf01869983 · Cited by 356 · see citing works

The Human Cationic Antimicrobial Protein (hCAP18), a Peptide Antibiotic, Is Widely Expressed in Human Squamous Epithelia and Colocalizes with Interleukin-6

Nilsson, M. F., Sandstedt, B., Sørensen, O. E., Weber, G., Borregaard, N., & Ståhle‐Bäckdahl, M. (1999) · Infection and Immunity · doi:10.1128/iai.67.5.2561-2566.1999 · Cited by 351 · see citing works

Amino acid sequence of PR‐39

Agerberth, B., Jong‐Youn, L. E. E., Bergman, T., Carlquist, M., Boman, H. G., Mutt, V., & Jörnvall, H. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16442.x · Cited by 348 · see citing works

hCAP‐18, a cathelin/pro‐bactenecin‐like protein of human neutrophil specific granules

Cowland, J. B., Johnsen, A. H., & Borregaard, N. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00634-l · Cited by 347 · see citing works

Structure of the Bovine Antimicrobial Peptide Indolicidin bound to Dodecylphosphocholine and Sodium Dodecyl Sulfate Micelles

Rozek, A., Friedrich, C. L., & Hancock, R. E. W. (2000) · PubMed · doi:10.13018/bmr4552 · Cited by 330 · see citing works

Cathelicidins: a family of endogenous antimicrobial peptides

Lehrer, R. I., & Ganz, T. (2002) · Current Opinion in Hematology · doi:10.1097/00062752-200201000-00004 · Cited by 324 · see citing works

Augmentation of Innate Host Defense by Expression of a Cathelicidin Antimicrobial Peptide

Bals, R., Weiner, D. J., Moscioni, A. D., Meegalla, R. L., & Wilson, J. M. (1999) · Infection and Immunity · doi:10.1128/iai.67.11.6084-6089.1999 · Cited by 302 · see citing works

Cell Differentiation Is a Key Determinant of Cathelicidin LL-37/Human Cationic Antimicrobial Protein 18 Expression by Human Colon Epithelium

Hase, K., Eckmann, L., Leopard, J. D., Varki, N. M., & Kagnoff, M. F. (2002) · Infection and Immunity · doi:10.1128/iai.70.2.953-963.2002 · Cited by 294 · see citing works

Cathelicidin Family of Antibacterial Peptides CAP18 and CAP11 Inhibit the Expression of TNF-α by Blocking the Binding of LPS to CD14+ Cells

Nagaoka, I., Hirota, S., Niyonsaba, F., Hirata, M., Adachi, Y., Tamura, H., & Heumann, D. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.6.3329 · Cited by 258 · see citing works

Biological Characterization of Two Novel Cathelicidin-derived Peptides and Identification of Structural Requirements for Their Antimicrobial and Cell Lytic Activities

Skerlavaj, B., Gennaro, R., Bagella, L., Merluzzi, L., Risso, A., & Zanetti, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.45.28375 · Cited by 252 · see citing works

Increased Levels of Antimicrobial Peptides in Tracheal Aspirates of Newborn Infants during Infection

Schaller-Bals, S., Schulze, A., & Bals, R. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.165.7.200110-020 · Cited by 245 · see citing works

Mechanism of alamethicin insertion into lipid bilayers

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Biochemical and Antibacterial Analysis of Human Wound and Blister Fluid

Frohm, M., Gunne, H., Bergman, A., Agerberth, B., Bergman, T., Boman, A., Lidén, S., Jörnvall, H., & Boman, H. G. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0086n.x · Cited by 212 · see citing works

Rapid membrane permeabilization and inhibition of vital functions of gram-negative bacteria by bactenecins

Skerlavaj, B., Romeo, D., & Gennaro, R. (1990) · Infection and Immunity · doi:10.1128/iai.58.11.3724-3730.1990 · Cited by 202 · see citing works

Pleiotropic roles of formyl peptide receptors

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Transfer of a cathelicidin peptide antibiotic gene restores bacterial killing in a cystic fibrosis xenograft model

Bals, R., Weiner, D. J., Meegalla, R. L., & Wilson, J. M. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6570 · Cited by 190 · see citing works

Membrane Thinning Effect of the β-Sheet Antimicrobial Protegrin

Heller, W. T., Waring, A. J., Lehrer, R. I., et al. (1999) · Biochemistry · doi:10.1021/bi991892m · Cited by 190 · see citing works

Bacterial Phosphorylcholine Decreases Susceptibility to the Antimicrobial Peptide LL-37/hCAP18 Expressed in the Upper Respiratory Tract

Lysenko, E. S., Gould, J. M., Bals, R., et al. (2000) · Infection and Immunity · doi:10.1128/iai.68.3.1664-1671.2000 · Cited by 181 · see citing works

Antibacterial Components in Bronchoalveolar Lavage Fluid from Healthy Individuals and Sarcoidosis Patients

Agerberth, B., Grünewald, J., Castaños‐Vélez, E., OLSSON, B., Jörnvall, H., Wigzell, H., Eklúnd, A., & Gudmundsson, G. H. (1999) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.160.1.9807041 · Cited by 165 · see citing works

Augmentation of the Lipopolysaccharide-Neutralizing Activities of Human Cathelicidin CAP18/LL-37-Derived Antimicrobial Peptides by Replacement with Hydrophobic and Cationic Amino Acid Residues

Nagaoka, I., Hirota, S., Niyonsaba, F., et al. (2002) · Clinical and Vaccine Immunology · doi:10.1128/cdli.9.5.972-982.2002 · Cited by 163 · see citing works

Inhibition of ubiquitin-proteasome pathway–mediated IκBα degradation by a naturally occurring antibacterial peptide

Gao, Y., Lecker, S. H., Post, M. J., Hietaranta, A. J., Li, J., Volk, R., Li, M., Sato, K., Saluja, A. K., Steer, M. L., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9826 · Cited by 156 · see citing works

Bilayer Interactions of Indolicidin, a Small Antimicrobial Peptide Rich in Tryptophan, Proline, and Basic Amino Acids

Ladokhin, A. S., Selsted, M. E., & White, S. H. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78713-7 · Cited by 155 · see citing works

Porcine polymorphonuclear leukocytes generate extracellular microbicidal activity by elastase-mediated activation of secreted proprotegrins

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

Interactions of an antimicrobial peptide, magainin 2, with lipopolysaccharide‐containing liposomes as a model for outer membranes of Gram‐negative bacteria

Matsuzaki, K., Sugishita, K.-I., & Miyajima, K. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00443-3 · Cited by 152 · see citing works

Proteolytic cleavage by neutrophil elastase converts inactive storage proforms to antibacterial bactenecins

Scocchi, M., Skerlavaj, B., Romeo, D., & Gennaro, R. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17324.x · Cited by 149 · see citing works

Primary structure of a new cysteine proteinase inhibitor from pig leucocytes

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Influence of the Angle Subtended by the Positively Charged Helix Face on the Membrane Activity of Amphipathic, Antibacterial Peptides

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Induction of oral tolerance to cellular immune responses in the absence of Peyer's patches

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Chemoattractant properties of PR-39, a neutrophil antibacterial peptide

Huang, H.-J., Ross, C. R., & Blecha, F. (1997) · Journal of Leukocyte Biology · doi:10.1002/jlb.61.5.624 · Cited by 133 · see citing works

Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39.

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Complementary DNA sequence of rabbit CAP18—A unique lipopolysaccharide binding protein

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PR-39, a Syndecan-inducing Antimicrobial Peptide, Binds and Affects p130Cas

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Protective Effects of a Human 18-Kilodalton Cationic Antimicrobial Protein (CAP18)-Derived Peptide against Murine Endotoxemia

Kirikae, T., Hirata, M., Yamasu, H., Kirikae, F., Tamura, H., Kayama, F., Nakatsuka, K., Yokochi, T., & Nakano, M. (1998) · Infection and Immunity · doi:10.1128/iai.66.5.1861-1868.1998 · Cited by 112 · see citing works

Secondary Structure and Membrane Interaction of PR‐39, a Pro+Arg‐rich Antibacterial Peptide

Cabiaux, V., Agerberths, B., Johansson, J., Homblé, F., Goormaghtigh, E., & Ruysschaert, J. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.01019.x · Cited by 111 · see citing works

Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA

Storici, P., Scocchi, M., Tossi, A., Gennaro, R., & Zanetti, M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80214-9 · Cited by 109 · see citing works

Cathelicidin peptides as candidates for a novel class of antimicrobials

Zanetti, M., Gennaro, R., Skerlavaj, B., Tomasinsig, L., & Circo, R. (2002) · Current Pharmaceutical Design · doi:10.2174/1381612023395457 · Cited by 105 · see citing works

PMAP-37, a Novel Antibacterial Peptide from Pig Myeloid Cells. cDNA Cloning, Chemical Synthesis and Activity

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

Identification of a new member of the protegrin family by cDNA cloning

Zhao, C., Liu, L., & Lehrer, R. I. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00493-5 · Cited by 100 · see citing works

The structure of porcine protegrin genes

Zhao, C., Ganz, T., & Lehrer, R. I. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00633-k · Cited by 85 · see citing works

Structures of genes for two cathelin‐associated antimicrobial peptides: prophenin‐2 and PR‐39

Zhao, C., Ganz, T., & Lehrer, R. I. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)01237-3 · Cited by 78 · see citing works

Processing site and gene structure for the murine antimicrobial peptide CRAMP

Pestonjamasp, V. K., Huttner, K. H., & Gallo, R. L. (2001) · Peptides · doi:10.1016/s0196-9781(01)00499-5 · Cited by 77 · see citing works

Salt-Independent Abnormality of Antimicrobial Activity in Cystic Fibrosis Airway Surface Fluid

Bals, R., Weiner, D. J., Meegalla, R. L., et al. (2001) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.25.1.4436 · Cited by 76 · see citing works

PR-39, a potent neutrophil inhibitor, attenuates myocardial ischemia-reperfusion injury in mice

Hoffmeyer, M. R., Scalia, R. G., Ross, C. R., et al. (2000) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2000.279.6.h2824 · Cited by 73 · see citing works

Novel cathelicidins in horse leukocytes

Scocchi, M., Bontempo, D., Boscolo, S., Tomasinsig, L., Giulotto, E., & Zanetti, M. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01097-2 · Cited by 70 · see citing works

The Role of Protegrins and Other Elastase-Activated Polypeptides in the Bactericidal Properties of Porcine Inflammatory Fluids

Shi, J. N., & Ganz, T. (1998) · Infection and Immunity · doi:10.1128/iai.66.8.3611-3617.1998 · Cited by 69 · see citing works

Identification of a proline-arginine-rich antibacterial peptide from neutrophils that is analogous to PR-39, an antibacterial peptide from the small intestine

Shi, J. N., Ross, C. R., Chengappa, M. M., & Blecha, F. (1994) · Journal of Leukocyte Biology · doi:10.1002/jlb.56.6.807 · Cited by 69 · see citing works

RL-37, an Alpha-Helical Antimicrobial Peptide of the Rhesus Monkey

Zhao, C., Nguyen, T. X., Boo, L. M., Hong, T., Espiritu, C., Orlov, D. S., Wang, W., Waring, A. J., & Lehrer, R. I. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.10.2695-2702.2001 · Cited by 62 · see citing works

The antimicrobial peptide trichogin and its interaction with phospholipid membranes

Epand, R. F., Epand, R. M., Monaco, V., et al. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00945.x · Cited by 60 · see citing works

Structure–Activity Analysis of SMAP-29, a Sheep Leukocytes-Derived Antimicrobial Peptide

Shin, S. Y., Park, E. J., Yang, S., et al. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5280 · Cited by 58 · see citing works

Rhesus Monkey ( Macaca mulatta ) Mucosal Antimicrobial Peptides Are Close Homologues of Human Molecules

Bals, R., Lang, C., Weiner, D. J., Vogelmeier, C. F., WELSCH, U. N., & Wilson, J. M. (2001) · Clinical and Diagnostic Laboratory Immunology · doi:10.1128/cdli.8.2.370-375.2001 · Cited by 54 · see citing works

CRAMP Analogues Having Potent Antibiotic Activity against Bacterial, Fungal, and Tumor Cells without Hemolytic Activity

Shin, S. Y., Kang, S.-W., Lee, D. G., et al. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3269 · Cited by 46 · see citing works

PR-39, a proline/arginine-rich antimicrobial peptide, exerts cardioprotective effects in myocardial ischemia–reperfusion

Ikeda, Y. (2001) · Cardiovascular Research · doi:10.1016/s0008-6363(00)00226-1 · Cited by 44 · see citing works

Solution structure of a cathelicidin‐derived antimicrobial peptide, CRAMP as determined by NMR spectroscopy

Yu, K., Park, K., Kim, Y., Kang, S. ‐., Shin, S. Y., & Hahm, K. S. (2002) · Journal of Peptide Research · doi:10.1034/j.1399-3011.2002.01968.x · Cited by 43 · see citing works

A novel murine cathelin‐like protein expressed in bone marrow

Popsueva, A. E., Zinovjeva, M. V., Visser, J. W. M., Zijlmans, J. M. J. M., Fibbe, W. E., & Belyavsky, A. V. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00692-8 · Cited by 36 · see citing works

Host Defense Functions of Proteolytically Processed and Parent (Unprocessed) Cathelicidins of Rabbit Granulocytes

Zarember, K. A., Katz, S. S., Tack, B. F., et al. (2002) · Infection and Immunity · doi:10.1128/iai.70.2.569-576.2002 · Cited by 35 · see citing works

Molecular Mechanisms of Interaction of Rabbit CAP18 with Outer Membranes of Gram-Negative Bacteria

Gutsmann, T., Larrick, J. W., Seydel, U., et al. (1999) · Biochemistry · doi:10.1021/bi990643v · Cited by 31 · see citing works

Erratum to: Mechanisms of Action of Rabbit CAP18 on Monolayers and Liposomes Made from Endotoxins of Phospholipids

Gutsmann, T., Fix, M., Larrick, J. W., et al. (2000) · The Journal of Membrane Biology · doi:10.1007/s002320010023 · Cited by 20 · see citing works

Sorting of neutrophil-specific granule protein human cathelicidin, hCAP-18, when constitutively expressed in myeloid cells

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LL-37, the only human member of the cathelicidin family of antimicrobial peptides

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