The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Innate antimicrobial peptide protects the skin from invasive bacterial infection
Abstract
In mammals, several gene families encode peptides with antibacterial activity, such as the beta-defensins and cathelicidins. These peptides are expressed on epithelial surfaces and in neutrophils, and have been proposed to provide a first line of defence against infection by acting as 'natural antibiotics'. The protective effect of antimicrobial peptides is brought into question by observations that several of these peptides are easily inactivated and have diverse cellular effects that are distinct from antimicrobial activity demonstrated in vitro. To investigate the function of a specific antimicrobial peptide in a mouse model of cutaneous infection, we applied a combined mammalian and bacterial genetic approach to the cathelicidin antimicrobial gene family. The mature human (LL-37) and mouse (CRAMP) peptides are encoded by similar genes (CAMP and Cnlp, respectively), and have similar alpha-helical structures, spectra of antimicrobial activity and tissue distribution. Here we show that cathelicidins are an important native component of innate host defence in mice and provide protection against necrotic skin infection caused by Group A Streptococcus (GAS).
Overview
Integrity signals
Registry
Cites
Statistics
Verification
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?
In the citing paper
“This is aided by the skin—the epidermis in particular—up-regulating and secreting antimicrobial peptides early in response to barrier damage and exposure to microbes (Fig. 2) (36, 37).”
From Wound repair and regeneration: Mechanisms, signaling, and translation (2014) · cites this paper as [37]
Citations
Cites
Zasloff, M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5449 · Cited by 2,305
β-Defensins: Linking Innate and Adaptive Immunity Through Dendritic and T Cell CCR6
Yang, D., Chertov, O., Bykovskaia, S. N., Chen, Q., Buffo, M. J., Shogan, J., Anderson, M., Schröder, J. M., Wang, J. M., Howard, O. M. Z., et al. (1999) · Science · doi:10.1126/science.286.5439.525 · Cited by 1,809
Defensins. Natural peptide antibiotics of human neutrophils.
Ganz, T., Selsted, M. E., Szklarek, D., Harwig, S. S. L., Daher, K. A., Bainton, D. F., & Lehrer, R. I. (1985) · Journal of Clinical Investigation · doi:10.1172/jci112120 · Cited by 1,416
Yang, D., Chen, Q., Schmidt, A. P., Anderson, G. M., Wang, J., Wooters, J., Oppenheim, J. J., & Chertov, O. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.7.1069 · Cited by 1,238
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. A., & Wilson, J. M. (1997) · Cell · doi:10.1016/s0092-8674(00)81895-4 · Cited by 1,077
Complete genome sequence of an M1 strain of Streptococcus pyogenes
Ferretti, J. J., McShan, W. M., Ajdić, D., Savić, D. J., Savić, G., Lyon, K., Primeaux, C., Sezate, S. A., Suvorov, A. N., Kenton, S., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.071559398 · Cited by 936
Gudmundsson, G. H., Agerberth, B., Odeberg, J., Bergman, T., Olsson, B., & Salcedo, R. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0325z.x · Cited by 579
Dorschner, R. A., Pestonjamasp, V. K., Tamakuwala, S., Ohtake, T., Rudisill, J., Nizet, V., Agerberth, B., Gudmundsson, G. H., & Gallo, R. L. (2001) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2001.01340.x · Cited by 567
Self-citationChertov, O., Michiel, D. F., Xu, L., Wang, J., Tani, K., Murphy, W. J., Longo, D. L., Taub, D. D., & Oppenheim, J. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.6.2935 · Cited by 548
Islam, D., Bandholtz, L., Nilsson, J., Wigzell, H., Christensson, B., Agerberth, B., & Gudmundsson, G. H. (2001) · Nature Medicine · doi:10.1038/84627 · Cited by 429
Flagged first, then by citations
Cited by
Sorted by citations
Items 801–900 of 999
LL-37: An Immunomodulatory Antimicrobial Host Defence Peptide
Beaumont, P. E., Li, H., & Davidson, D. J. (2012) · Springer eBooks · doi:10.1007/978-3-0348-0541-4_4 · Cited by 18
Efficacy of Histatin5 in a murine model of vulvovaginal candidiasis caused by Candida albicans
Liao, H., Liu, S., Wang, H., Su, H., & Liu, Z. (2017) · Pathogens and Disease · doi:10.1093/femspd/ftx072 · Cited by 18
Antimicrobial RNases of Human Skin
ZASLOFF, M. A. (2009) · Journal of Investigative Dermatology · doi:10.1038/jid.2009.216 · Cited by 18
Sharma, P., Guha, S., Garg, P., & Roy, S. (2018) · Pathogens and Disease · doi:10.1093/femspd/fty001 · Cited by 18
Aidoukovitch, A., Anders, E., Dahl, S., Nebel, D., Svensson, D., & Nilsson, B. (2019) · Journal of Periodontal Research · doi:10.1111/jre.12667 · Cited by 18
Titeux, M., Mejía, J. E., Mejlumian, L., Bourthoumieu, S., Mirval, S., Tonasso‐Calvière, L., Heller, M., Prost‐Squarcioni, C., & Hovnanian, A. (2006) · Human Mutation · doi:10.1002/humu.9406 · Cited by 19
The role of the antimicrobial peptide cathelicidin in renal diseases
Chromek, M. (2014) · Pediatric Nephrology · doi:10.1007/s00467-014-2895-3 · Cited by 18
Wang, J., Gao, M., Cui, Z., Jia, Y., Liu, S., Chen, K.-F., Chen, X., Zhang, Y., Fang, Z., Chen, Y., et al. (2020) · Materials Chemistry Frontiers · doi:10.1039/d0qm00014k · Cited by 17
Dammann, A. N., Chamby, A. B., Catomeris, A. J., Davidson, K. M., Tettelin, H., van Pijkeren, J., Gopalakrishna, K. P., Keith, M. F., Elder, J. L., Ratner, A. J., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009116 · Cited by 18
Surfactant protein D in atopic dermatitis and psoriasis
Hohwy, T., Otkjær, K., Madsen, J., Søerensen, G., Nielsen, O., Vestergaard, C., Steiniche, T., Holmskov, U., & Lomholt, H. B. (2006) · Experimental Dermatology · doi:10.1111/j.1600-0625.2006.00406.x · Cited by 17
Gela, A., Bhongir, R. K. V., Mori, M., Keenan, P., Mörgelin, M., Erjefalt, J. S., Herwald, H., Egesten, A., & Kasetty, G. (2016) · PLoS ONE · doi:10.1371/journal.pone.0146192 · Cited by 17
Vitamin D in critically ill patients
Matysiak-Luśnia, K. (2016) · Anaesthesiology Intensive Therapy · doi:10.5603/ait.a2016.0034 · Cited by 17
Asthma and Allergy “Epidemic” and the Role of Vitamin D Deficiency
Douros, K., Boutopoulou, B., Fouzas, S., & Loukou, I. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-56017-5_14 · Cited by 16
Chronic features of allergic asthma are enhanced in the absence of resistin-like molecule-beta
LeMessurier, K. S., Palipane, M., Tiwary, M., Gavin, B. P., & Samarasinghe, A. E. (2018) · Scientific Reports · doi:10.1038/s41598-018-25321-y · Cited by 17
Site specific microbiome of Leishmania parasite and its cross-talk with immune milieu
Misra, P., & Singh, S. (2019) · Immunology Letters · doi:10.1016/j.imlet.2019.10.004 · Cited by 17
Wertenbruch, S., Drescher, H. K., Grossarth, V., Kroy, D. C., Giebeler, A., Erschfeld, S., Heinrichs, D., Soehnlein, O., Trautwein, C., Brandenburg, L., et al. (2015) · Digestion · doi:10.1159/000368304 · Cited by 17
Meyer‐Hoffert, U., Hornef, M. W., Henriques‐Normark, B., Normark, S. J., Andersson, M., & Pütsep, K. (2008) · The FASEB Journal · doi:10.1096/fj.07-103440 · Cited by 16
Membrane Bound Hydraphiles Facilitate Cation Translocation
Srinivas, G., Lopez, C. F., & Klein, M. L. (2004) · The Journal of Physical Chemistry B · doi:10.1021/jp036953b · Cited by 17
Kindrachuk, J., Paur, N., Reiman, C., Scruten, E., & Napper, S. (2007) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00854-07 · Cited by 16
Silva‐Santana, G., Sales, F., Aguiar, A. P., & Brandão, M. L. L. (2025) · Processes · doi:10.3390/pr13051270 · Cited by 16
Ma, L., Zhang, Z., Li, L., Zhang, L., Lin, Z., & Qin, H. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.1016592 · Cited by 16
Defensins and Other Antimicrobial Peptides: Innate Defense of Mucosal Surfaces
Cole, A. M., & Ganz, T. (2014) · ASM Press eBooks · doi:10.1128/9781555817619.ch2 · Cited by 16
Neutrophils LL-37 migrate to the nucleus during overwhelming infection
da Silva, F. P., Medeiros, M. C. R., Santos, A. B. G., Ferreira, M. A., Garippo, A. L., Chammas, R. J., Caldini, E. T. E. G., Velasco, I. T., de Souza, H. P., & Machado, M. C. C. (2013) · Tissue and Cell · doi:10.1016/j.tice.2013.04.003 · Cited by 16
Probiotic Bacteria in Wound Healing; An In-Vivo Study.
Sinha, A., Sagar, S. S., Madhumathy, M., & Osborne, W. J. (2019) · PubMed Central · doi:10.30498/ijb.2019.85188 · Cited by 16
Efficacy of Antigonococcal CMP-Nonulosonate Therapeutics Require Cathelicidins
Gulati, S., Schoenhofen, I. C., Lindhout, T., Lewis, L. A., Moustafa, I. Y., Saha, S., Zheng, B., Nowak, N., Rice, P. A., Varki, A. P., et al. (2020) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiaa438 · Cited by 16
d'Aldebert, E., Mve, M.-J. B. B., Mergey, M., Wendum, D., Coilly, A., Fouassier, L., Corpechot, C., Poupon, R. Y., Housset, C., & Chignard, N. (2009) · Springer eBooks · doi:10.1007/978-1-4020-9644-0_13 · Cited by 17
Káradóttir, H., Kulkarni, N. N., Guðjónsson, Þ., Kárason, S., & Gudmundsson, G. H. (2015) · PeerJ · doi:10.7717/peerj.1483 · Cited by 16
McDermott, A. M. (2009) · CRC Press eBooks · doi:10.1201/9781420061161-c16 · Cited by 16
Identification of 2 Hypothetical Genes Involved inNeisseria meningitidisCathelicidin Resistance
Frigimelica, E., Bartolini, E., Galli, G., Grandi, G., & Grifantini, R. (2008) · The Journal of Infectious Diseases · doi:10.1086/533456 · Cited by 16
Bacterial Evasion of Innate Defense at Epithelial Linings
Hornef, M. W., Normark, S. J., Henriques‐Normark, B., & Rhen, M. (2005) · KARGER eBooks · doi:10.1159/000086652 · Cited by 16
Srinivas, G., & Klein, M. L. (2004) · Nanotechnology · doi:10.1088/0957-4484/15/9/030 · Cited by 16
Secretion, blood levels and cutaneous expression of TL 1A in psoriasis patients
Pedersen, A. E., Schmidt, E. G. W., Sørensen, J. F., Faber, C., Nielsen, B. S., Holmstrøm, K., Omland, S. H., Tougaard, P., Skov, S., & Bang, B. K. (2015) · Apmis · doi:10.1111/apm.12385 · Cited by 15
Dinkela, A., Ferié, J., Mbata, M., Schmid‐Grendelmeier, M., & Hatz, C. (2007) · International Journal of Dermatology · doi:10.1111/j.1365-4632.2007.03208.x · Cited by 15
Therapeutic potential of adenovirus-mediated delivery of β-defensin 2 for experimental otitis media
Woo, J.-I., Kil, S., Brough, D. E., Lee, Y. J., LIM, D. J., & Moon, S. K. (2014) · Innate Immunity · doi:10.1177/1753425914534002 · Cited by 15
Watts, K. M., Lahiri, P., Arrazuria, R., Buck, J. D., Knight, C. G., Orsel, K., Barkema, H. W., & Cobo, E. R. (2019) · Cell and Tissue Research · doi:10.1007/s00441-019-03082-y · Cited by 15
Pathogenic Mechanisms of Streptococcal Necrotizing Soft Tissue Infections
Siemens, N., Snäll, J., Svensson, M., & Norrby‐Teglund, A. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-57616-5_9 · Cited by 15
Jiang, R., Zhang, P., Wu, X., Wang, Y., Rehman, T., Yao, X., Luo, Y., & Yang, Z. (2020) · Electronic Journal of Biotechnology · doi:10.1016/j.ejbt.2020.12.006 · Cited by 15
Lucky Number Seven: RNase 7 Can Prevent Staphylococcus aureus Skin Colonization
Cho, J. S., Xuan, C., & Miller, L. S. (2010) · Journal of Investigative Dermatology · doi:10.1038/jid.2010.294 · Cited by 15
Immunomodulation and effects on microbiota after in ovo administration of chicken cathelicidin-2
Cuperus, T., Kraaij, M. D., Zomer, A., van Dijk, A. I. J. M., & Haagsman, H. P. (2018) · PLoS ONE · doi:10.1371/journal.pone.0198188 · Cited by 15
The host defense peptide LL-37 triggers release of nucleic acids from human mast cells
Dahl, S., Anders, E., Gidlöf, O., Svensson, D., & Nilsson, B. (2018) · Peptides · doi:10.1016/j.peptides.2018.10.001 · Cited by 15
The Role of Antimicrobial Peptides in Preterm Birth
Son, G., Lee, J., Kim, Y., & Lee, K.-Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168905 · Cited by 16
Pereira, H. A., Tsyshevskaya-Hoover, I., Hinsley, H., Logan, S., Nguyen, M. L., Nguyen, T.-T., Pohl, J., Wozniak, K. L., & Fidel, P. L. (2010) · Medical Mycology · doi:10.3109/13693780903081976 · Cited by 15
Prosystemin-antimicrobial-peptide fusion reduces tomato late blight lesion expansion
Jones, R. W., Ospina-Giraldo, M. D., & Clemente, T. E. (2004) · Molecular Breeding · doi:10.1023/b:molb.0000038001.22029.07 · Cited by 15
Antimicrobial peptides: Resistant‐proof antibiotics of the new millennium
Ding, J. L., & Ho, B. (2004) · Drug Development Research · doi:10.1002/ddr.10394 · Cited by 15
Dahl, S., Cerps, S., Rippe, C., Swärd, K., Uller, L., Svensson, D., & Nilsson, B. (2020) · Inflammation Research · doi:10.1007/s00011-020-01340-2 · Cited by 14
Multifunctional Properties of BMAP-18 and Its Aliphatic Analog against Drug-Resistant Bacteria
Jahan, I., Kumar, S. D., Shin, S. Y., Lee, C. W., Shin, S., & Yang, S. (2023) · Pharmaceuticals · doi:10.3390/ph16101356 · Cited by 13
Wang, X., Xu, Z., Xia, Y., Chen, Z., Zong, R., Meng, Q., Wang, W., Zhuang, W., Meng, X., & Chen, G. (2024) · Virology · doi:10.1016/j.virol.2024.110155 · Cited by 14
Regulation of antimicrobial peptides in Hermetia illucens in response to fungal exposure
Herman, N., Vitenberg, T., Hayouka, Z., & Opatovsky, I. (2024) · Scientific Reports · doi:10.1038/s41598-024-80133-7 · Cited by 14
D’Amico, F., Granata, M., Skarmoutsou, E., Trovato, C., Lovero, G., Gangemi, P., Longo, V., Pettinato, M., & Mazzarino, M. C. (2018) · Inflammation Research · doi:10.1007/s00011-018-1147-6 · Cited by 14
Aidoukovitch, A., Dahl, S., Fält, F., Nebel, D., Svensson, D., Tufvesson, E., & Nilsson, B. (2019) · European Journal Of Oral Sciences · doi:10.1111/eos.12664 · Cited by 14
Host Defense Peptides as Templates for Antifungal Drug Development
Basso, V., Tran, D. Q., Ouellette, A. J., & Selsted, M. E. (2020) · Journal of Fungi · doi:10.3390/jof6040241 · Cited by 14
Bankell, E., Liu, X., Lundqvist, M., Svensson, D., Swärd, K., Sparr, E., & Nilsson, B. (2021) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2021.101192 · Cited by 14
Smith, K. J., Minns, D., McHugh, B. J., Holloway, R. K., O’Connor, R. A., Williams, A., Melrose, L. A., McPherson, R. C., Miron, V. E., Davidson, D. J., et al. (2022) · PLoS Biology · doi:10.1371/journal.pbio.3001554 · Cited by 20
Dudis, R. S., Wong, T. Y., Escatte, M. G., Alamneh, Y. A., Abu-Taleb, R., Su, W., Czintos, C., Fitzgerald, T. A., Breton, Y. S. L., & Zurawski, D. V. (2023) · Virulence · doi:10.1080/21505594.2023.2186331 · Cited by 14
Histochemical analysis of glycoconjugates in the eccrine glands of the raccoon digital pads.
Yasui, T., Tsukise, A., & Meyer, W. (2004) · PubMed · doi:10.4081/913 · Cited by 14
Pereira, H. A., Tsyshevskaya-Hoover, I., Hinsley, H., Logan, S., Nguyen, M. L., Nguyen, T.-T., Pohl, J., Wozniak, K. L., & Fidel, P. L. (2009) · Medical Mycology · doi:10.1080/13693780903081976 · Cited by 14
Paoletti, I., Buommino, E., Fusco, A., Baudouin, C., Msika, P., Tufano, M. A., Baroni, A., & Donnarumma, G. (2012) · Archives of Dermatological Research · doi:10.1007/s00403-012-1237-1 · Cited by 14
Wang, T., Lim, J., Bok, J., Kim, J., Kang, S., Lee, S.-B., Hwang, J. H., Lee, K., Kang, H.-S., Choi, Y., et al. (2013) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.6502 · Cited by 14
Gela, A., Jovic, S., Nordin, S. L., & Egesten, A. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12402 · Cited by 14
Bankell, E., Dahl, S., Gidlöf, O., Svensson, D., & Nilsson, B. (2020) · Peptides · doi:10.1016/j.peptides.2020.170432 · Cited by 14
Influence of alemtuzumab on the intestinal Paneth cells and microflora in macaques
Li, Q., Zhang, Q., Wang, C., Tang, C. X., Zhang, Y., Jiang, S., Li, N., & Li, J. (2010) · Clinical Immunology · doi:10.1016/j.clim.2010.05.004 · Cited by 14
Wang, G. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.07.028 · Cited by 14
Group A streptococcal invasion of host cells
Courtney, H. S., & Podbielski, A. (2004) · Cambridge University Press eBooks · doi:10.1017/cbo9780511546273.010 · Cited by 14
Protective effects of human milk antimicrobial peptides against bacterial infection
Håkansson, A. (2014) · Jornal de Pediatria · doi:10.1016/j.jped.2014.10.001 · Cited by 14
Choi, M., Jo, J., Lee, M., Park, J., Yao, T., & Park, Y. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13065 · Cited by 13
Sankar, S., & Muthukaliannan, G. K. (2024) · Saudi Journal of Biological Sciences · doi:10.1016/j.sjbs.2024.103963 · Cited by 14
Host-induced cell wall remodeling impairs opsonophagocytosis of Staphylococcus aureus by neutrophils
Ledger, E. V. K., & Edwards, A. M. (2024) · mBio · doi:10.1128/mbio.01643-24 · Cited by 13
Morgenthau, A., Partha, S. K., Adamiak, P. J., & Schryvers, A. B. (2014) · BioMetals · doi:10.1007/s10534-014-9767-y · Cited by 13
Gelalcha, B. D., Agga, G. E., & Dego, O. K. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.101533 · Cited by 13
Hanafusa, T., Yamaguchi, Y., & Katayama, I. (2007) · Journal of the American Academy of Dermatology · doi:10.1016/j.jaad.2007.04.011 · Cited by 13
Akoh, C. C., Pressman, E. K., Whisner, C. M., Thomas, C. E., Cao, C. Q., Kent, T. R., Cooper, E., & O'Brien, K. O. (2017) · Journal of Reproductive Immunology · doi:10.1016/j.jri.2017.06.001 · Cited by 13
The Microbiome and Graft Versus Host Disease
Mathewson, N. D., & Reddy, P. (2015) · Current Stem Cell Reports · doi:10.1007/s40778-014-0002-0 · Cited by 13
Vitamin D Therapy for Chronic Kidney Disease
Bhan, I., & Thadhani, R. (2009) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2008.10.010 · Cited by 13
Sarkar, A., Tilly, K., Stewart, P. E., Bestor, A. C., Battisti, J. M., & Rosa, P. A. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00558-09 · Cited by 13
Zahid, A., Despres, J., Bénard, M., Nguema‐Ona, E., Leprince, J., Vaudry, D., Rihouey, C., Vicré‐Gibouin, M., Driouich, A., & Follet‐Gueye, M. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25646 · Cited by 13
Antimicrobial peptides in skin disease
Schröder, J., & Harder, J. (2006) · Drug Discovery Today Therapeutic Strategies · doi:10.1016/j.ddstr.2006.02.007 · Cited by 13
Smith, K. J., & Findlay, E. G. (2022) · Discovery Immunology · doi:10.1093/discim/kyac003 · Cited by 16
Chan, H., Li, F., Dokoshi, T., Cavagnero, K. J., Li, Q., Chen, Y., Aguilera, C., Nakatsuji, T., Liu, E., Indra, A., et al. (2025) · Science Immunology · doi:10.1126/sciimmunol.ads0519 · Cited by 13
Self-citationDietary Vitamin D Intake in Advanced CKD/ESRD
Bhan, I., Hewison, M., & Thadhani, R. (2010) · Seminars in Dialysis · doi:10.1111/j.1525-139x.2010.00751.x · Cited by 12
Burn wounds infected with Pseudomonas aeruginosa triggers weight loss in rats
Steinstraesser, L., Burkhard, O., Fan, M. H., Jacobsen, F., Lehnhardt, M., Su, G. L., Daigeler, A., Steinau, H. U., Remick, D. G., & Wang, S. C. (2005) · BMC Surgery · doi:10.1186/1471-2482-5-19 · Cited by 12
Tani, K., Shimizu, T., Kida, Y., & Kuwano, K. (2011) · Microbiology and Immunology · doi:10.1111/j.1348-0421.2011.00353.x · Cited by 12
Biological roles of host defense peptides: lessons from transgenic animals and bioengineered tissues
Dybvig, T., Facci, M. R., Gerdts, V., & Wilson, H. L. (2010) · Cell and Tissue Research · doi:10.1007/s00441-010-1075-4 · Cited by 12
Svensson, D., Aidoukovitch, A., Anders, E., Agerberth, B., Andersson, F., Ekblad, E., Ericson, D., Nebel, D., Voss, U., & Nilsson, B. (2018) · European Journal Of Oral Sciences · doi:10.1111/eos.12407 · Cited by 12
The Development of Peptide-based Antimicrobial Agents against Dengue Virus
Huang, Y.-W., Lee, C., Wang, T.-C., Kao, Y.-C., Yang, C.-H., Lin, Y., & Huang, K. (2018) · Current Protein and Peptide Science · doi:10.2174/1389203719666180531122724 · Cited by 14
Shahid, M. S., Cavalcante, P. A., Knight, C. G., Barkema, H. W., Han, B., Gao, J., & Cobo, E. R. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.00031 · Cited by 12
Immunopathogenesis of Streptococcal Deep Tissue Infections
Johansson, L., & Norrby‐Teglund, A. (2012) · Current topics in microbiology and immunology · doi:10.1007/82_2012_282 · Cited by 12
Li, Y., Li, X., & Wang, G. (2007) · Protein Expression and Purification · doi:10.1016/j.pep.2007.04.023 · Cited by 12
Gonzalez, D. J., Vuong, L., Gonzalez, I. S., Keller, N., McGrosso, D., Hwang, J. H., Hung, J., Zinkernagel, A. S., Dixon, J. E., Dorrestein, P. C., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.031336 · Cited by 12
Self-citationLekbua, A., Thiruppathy, D., Coker, J. K. C., Weng, Y., Askarian, F., Kousha, A., Marotz, C. A., Hauw, A., Nizet, V., & Zengler, K. (2024) · Cell Reports Methods · doi:10.1016/j.crmeth.2024.100832 · Cited by 12
Self-citationTa, A., Thakur, B. K., Dutta, P., Sinha, R., Koley, H., & Das, S. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.03.016 · Cited by 11
Ito, T., Tanabe, H., Ayabe, T., Ishikawa, C., Inaba, Y., Maemoto, A., Kono, T., Ashida, T., Fujiya, M., & Kohgo, Y. (2012) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.227.39 · Cited by 11
Kanchongkittiphon, W., Gaffin, J. M., & Phipatanakul, W. (2014) · Annals of Allergy Asthma & Immunology · doi:10.1016/j.anai.2014.08.016 · Cited by 11
Hydrocarbon‐stapled lipopeptides exhibit selective antimicrobial activity
Jenner, Z. B., Crittenden, C. M., Gonzalez, M., Brodbelt, J. S., & Bruns, K. A. (2017) · Biopolymers · doi:10.1002/bip.23006 · Cited by 11
Role of Vitamin D in Reducing the Risk of Preterm Labour
Singh, A., Hariharan, D., & Bhaumik, D. (2015) · International Journal of Reproduction Contraception Obstetrics and Gynecology · doi:10.5455/2320-1770.ijrcog20150217 · Cited by 11
Epithelial cells as sentinels in mucosal immune barrier
Hase, K., & Ohno, H. (2006) · Japanese Journal of Clinical Immunology · doi:10.2177/jsci.29.16 · Cited by 11
Antimicrobial Peptidesas an Alternative Approach to Treat Bacterial Infections
Thomassin, H. L. M. J.-L. (2013) · Journal of Clinical & Cellular Immunology · doi:10.4172/2155-9899.s13-004 · Cited by 11
Antimicrobial Activity of the Antibacterial Peptide PMAP-GI24 and Its Analogs
Liu, Y., Yan, Z., Chai, J., Zhou, J., & Wang, C. (2020) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-020-10026-6 · Cited by 10
Tu, Y., Hou, A., Zhou, Z., Cheng, L., Luo, J., Deng, Y., Li, J., Li, J., Yang, J., & Liang, K. (2024) · Nano Today · doi:10.1016/j.nantod.2024.102390 · Cited by 11
Physiological role of bicarbonate in microbes: A double-edged sword?
Aspatwar, A., Parkkinen, J., & Parkkila, S. (2025) · Virulence · doi:10.1080/21505594.2025.2474865 · Cited by 10
Perez‐Perez, D. A., Villanueva-Ramirez, T. D. J., Hernandez-Pedraza, A. E., Casillas-Vega, N. G., González-Barranco, P., & Zárate, X. (2021) · Antibiotics · doi:10.3390/antibiotics10101271 · Cited by 10
Metadata
- Authors
- Nizet, V., Ohtake, T., Lauth, X., Trowbridge, J., Rudisill, J., Dorschner, R. A., Pestonjamasp, V., Piraino, J., Huttner, K., & Gallo, R. L.
- Affiliations
- University of California San Diego (US)
- Massachusetts General Hospital (US)
- Corresponding author
- Gallo, Richard L.
- Venue
- Nature
- Published
- 2001-11
- Volume
- 414
- Issue
- 6862
- Pages
- 454-457
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1964758221
- Cited by
- 1,198
- References
- 30
- Citations by year
- 2026: 12 · 2025: 16 · 2024: 29 · 2023: 21 · 2022: 25 · 2021: 26 · 2020: 51 · 2019: 37 · 2018: 45 · 2017: 42 · 2016: 46 · 2015: 58 · 2014: 74 · 2013: 61 · 2012: 57
- FWCI
- 36.82
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Antimicrobial agents and applications
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- antimicrobial peptides, cathelicidin, LL-37, cramps, innate immunity, skin infections, Streptococcus pyogenes, host defense, beta-defensins
- MeSH terms
- Animals, Female, Immunity, Innate, Male, Mice, Inbred C57BL, Mutation, Proteins, Recombinant Fusion Proteins, Streptococcal Infections, Streptococcus pyogenes, Skin Diseases, Bacterial, Mice, Knockout, Antimicrobial Cationic Peptides, Drug Resistance, Bacterial, Mice, Cathelicidins
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