The DOI matches its Crossref record; 53 of the 56 references it cites were found in a registry or an index.
Cutaneous Injury Induces the Release of Cathelicidin Anti-Microbial Peptides Active Against Group A Streptococcus
Open accessAbstract
Cathelicidins are a family of peptides thought to provide an innate defensive barrier against a variety of potential microbial pathogens. The human and mouse cathelicidins (LL-37 and CRAMP, respectively) are expressed at select epithelial interfaces where they have been proposed to kill a number of gram-negative and gram-positive bacteria. To determine if these peptides play a part in the protection of skin against wound infections, the anti-microbial activity of LL-37 and CRAMP was determined against the common wound pathogen group A Streptococcus, and their expression was examined after cutaneous injury. We observed a large increase in the expression of cathelicidins in human and murine skin after sterile incision, or in mouse following infection by group A Streptococcus. The appearance of cathelicidins in skin was due to both synthesis within epidermal keratinocytes and deposition from granulocyctes that migrate to the site of injury. Synthesis and deposition in the wound was accompanied by processing from the inactive prostorage form to the mature C-terminal peptide. Analysis of anti-microbial activity of this C-terminal peptide against group A Streptococcus revealed that both LL-37 and CRAMP potently inhibited bacterial growth. Action against group A Streptococcus occurred in conditions that typically abolish the activity of anti-microbial peptides against other organisms. Thus, cathelicidins are well suited to provide defense against infections due to group A Streptococcus, and represent an important element of cutaneous innate immunity.
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
“Early events in the innate immune response to skin injury include the recruitment of neutrophils and the induction of antimicrobial peptides, particularly, in humans, the cathelicidin LL-37.17”
From The Innate Immune System in Acute and Chronic Wounds (2016) · cites this paper as [17]
In the citing paper
“Interestingly, suction blister wounds, where the blister roof is still intact, do not show substantial inflammation,9 whereas excisional wounds, ultraviolet (UV)-induced skin damage, superficial tape stripping or chemical skin irritants, and contact sensitizers cause inflammatory infiltrates,17,23–26”
From The Innate Immune System in Acute and Chronic Wounds (2016) · cites this paper as [17]
Citations
Cites
Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction
Chomczynski, P., & Sacchi, N. (1987) · Analytical Biochemistry · doi:10.1006/abio.1987.9999 · Cited by 65,515
Manual of Clinical Microbiology
Klainer, A. (1970) · Postgraduate Medical Journal · doi:10.1136/pgmj.46.542.733-c · Cited by 5,344
Zasloff, M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5449 · Cited by 2,305
Manual of Clinical Microbiology, 7th ed.
Balows, A. (2000) · Diagnostic Microbiology and Infectious Disease · doi:10.1016/s0732-8893(99)00102-9 · Cited by 1,613
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
A peptide antibiotic from human skin
Harder, J., Bartels, J., Christophers, E., & Schröder, J. ‐. (1997) · Nature · doi:10.1038/43088 · Cited by 1,365
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
Defensins: Antimicrobial and Cytotoxic Peptides of Mammalian Cells
Lehrer, R. I., Lichtenstein, A. K., & Ganz, T. (1993) · Annual Review of Immunology · doi:10.1146/annurev.iy.11.040193.000541 · Cited by 1,000
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
Self-citationActivities of LL-37, a Cathelin-Associated Antimicrobial Peptide of Human Neutrophils
Turner, J., Cho, Y., Dinh, N.-N., Waring, A. J., & Lehrer, R. I. (1998) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.42.9.2206 · Cited by 800
Cited by
Sorted by citations
Items 301–400 of 567
Boccardo, E., Baldi, C. V. M., de Carvalho, A. F., Rabachini, T., Torres, C., Barreta, L. A. N., Brentani, H., & Villa, L. L. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp333 · Cited by 39
Plichta, J. K., Droho, S., Curtis, B. J., Patel, P., Gamelli, R. L., & Radek, K. A. (2014) · Critical Care Medicine · doi:10.1097/ccm.0000000000000309 · Cited by 37
Tomasinsig, L., Scocchi, M., Loreto, C. D., Artico, D., & Zanetti, M. (2002) · Journal of Leukocyte Biology · doi:10.1189/jlb.72.5.1003 · Cited by 37
Wang, Y., Cong, H., Shen, Y., & Yu, B. (2024) · Chemical Engineering Journal · doi:10.1016/j.cej.2024.158962 · Cited by 37
Trémezaygues, L., Sticherling, M., Pföhler, C., Friedrich, M., Meineke, V., Seifert, M., Tilgen, W., & Reichrath, J. (2006) · PubMed · Cited by 36
Variation, Indispensability, and Masking in the M protein
Ghosh, P. (2017) · Trends in Microbiology · doi:10.1016/j.tim.2017.08.002 · Cited by 36
Zhang, R., Wang, Z., Tian, Y., Yin, Q., Cheng, X., Lian, M., Zhou, B., Zhang, X., & Yang, L. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01175 · Cited by 36
Host defense peptides: An alternative as antiinfective and immunomodulatory therapeutics
Alba, A., López‐Abarrategui, C., & Otero‐González, A. J. (2012) · Biopolymers · doi:10.1002/bip.22076 · Cited by 35
Zhang, M., Liang, W., Gong, W., Yoshimura, T., Chen, K., & Wang, J. (2019) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.2019030225 · Cited by 35
Liggins, M. C., Li, F., Zhang, L., Dokoshi, T., & Gallo, R. L. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1900520 · Cited by 36
Self-citationAnti-infective efficacy of the lactoferrin-derived antimicrobial peptide HLR1r
Björn, C., Mahlapuu, M., Mattsby‐Baltzer, I., & Håkansson, J. (2016) · Peptides · doi:10.1016/j.peptides.2016.04.005 · Cited by 35
Han, F.-F., Liu, Y., Xie, Y., Gao, Y., Luan, C., & Wang, Y. (2011) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-010-0643-9 · Cited by 34
Love, J. F., Tran-Winkler, H. J., & Wessels, M. R. (2012) · mBio · doi:10.1128/mbio.00394-12 · Cited by 34
Plichta, J. K., Holmes, C. J., Gamelli, R. L., & Radek, K. A. (2016) · Journal of Burn Care & Research · doi:10.1097/bcr.0000000000000357 · Cited by 34
Human Catestatin Alters Gut Microbiota Composition in Mice
Rabbi, M. F., Munyaka, P. M., Eissa, N., Metz‐Boutigue, M., Khafipour, E., & Ghia, J. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.02151 · Cited by 35
Adrenomedullin Expression by Gastric Epithelial Cells in Response to Infection
Allaker, R. P., & Kapas, S. (2003) · Clinical and Vaccine Immunology · doi:10.1128/cdli.10.4.546-551.2003 · Cited by 34
Biswas, D., Ambalavanan, P., Ravins, M., Anand, A., Sharma, A., Lim, K. X. Z., Tan, R. Y. M., Lim, H. Y., Sol, A., Bachrach, G., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108766 · Cited by 32
Uhlmann, J., Rohde, M., Siemens, N., Kreikemeyer, B., Bergman, P., Johansson, L., & Norrby‐Teglund, A. (2015) · Journal of Innate Immunity · doi:10.1159/000441896 · Cited by 33
Cathelicidin a potential therapeutic peptide for gastrointestinal inflammation and cancer
Chow, J. Y. C. (2013) · World Journal of Gastroenterology · doi:10.3748/wjg.v19.i18.2731 · Cited by 32
Exploring the mechanisms of action of human secretory RN ase 3 and RN ase 7 against Candida albicans
Salazar, V. A., Arranz‐Trullén, J., Navarro, S., Blanco, J. A., Sánchez, D., Moussaoui, M., & Boix, E. (2016) · MicrobiologyOpen · doi:10.1002/mbo3.373 · Cited by 32
Agha, N. H., Baker, F. L., Kunz, H., Spielmann, G., Mylabathula, P. L., Rooney, B. V., Mehta, S. K., Pierson, D. L., Laughlin, M. S., Markofski, M. M., et al. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00560.2019 · Cited by 32
Susceptibility of Treponema pallidum to host-derived antimicrobial peptides
Cox, D. L., Sun, Y., Liu, H., Lehrer, R. I., & Shafer, W. M. (2003) · Peptides · doi:10.1016/j.peptides.2003.07.026 · Cited by 32
Yang, X., Niu, L. N., Pan, Y., Feng, X., Liu, J., Guo, Y., Pan, C., Geng, F., & Tang, X. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.561761 · Cited by 30
Vaccinia virus–specific molecular signature in atopic dermatitis skin
Grigoryev, D. N., Howell, M. D., Watkins, T. N., Chen, Y.-C., Cheadle, C., Boguniewicz, M., Barnes, K. C., & Leung, D. Y. M. (2010) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2009.10.024 · Cited by 31
Innate barriers against skin infection and associated disorders
Gallo, R. L., & Nizet, V. (2008) · Drug Discovery Today Disease Mechanisms · doi:10.1016/j.ddmec.2008.04.009 · Cited by 33
Self-citationHost Cathelicidin Exacerbates Group B Streptococcus Urinary Tract Infection
Patras, K. A., Coady, A. M., Babu, P., Shing, S. R., Ha, A., Rooholfada, E., Brandt, S. L., Geriak, M., Gallo, R. L., & Nizet, V. (2020) · mSphere · doi:10.1128/msphere.00932-19 · Cited by 31
Self-citationAntimicrobial Peptides as Effector Molecules of Mammalian Host Defense
Bevins, C. L. (2002) · KARGER eBooks · doi:10.1159/000068134 · Cited by 31
Antimicrobial peptide killing of African trypanosomes
HARRINGTON, J. M. (2011) · Parasite Immunology · doi:10.1111/j.1365-3024.2011.01294.x · Cited by 30
Wanmakok, M., Orrapin, S., Intorasoot, A., & Intorasoot, S. (2018) · Gene · doi:10.1016/j.gene.2018.05.106 · Cited by 30
Golla, R. M., Mishra, B., Dang, X., Narayana, J. L., Li, A., Xu, L., & Wang, G. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00112 · Cited by 29
Strömstedt, A. A., Felth, J., & Bohlin, L. (2013) · Phytochemical Analysis · doi:10.1002/pca.2468 · Cited by 30
Partidos, C. D., & Muller, S. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-4529-1 · Cited by 30
Minidefensins and other antimicrobial peptides: candidate anti-HIV microbicides
Cole, A. M. (2003) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.7.3.329 · Cited by 29
Localization of human beta-defensin-2 and human neutrophil peptides in superficial folliculitis
Oono, T., Huh, W.-K., Shirafuji, Y., Akiyama, H., & Iwatsuki, K. (2003) · British Journal of Dermatology · doi:10.1046/j.1365-2133.2003.509915.x · Cited by 30
Muehleisen, B., Jiang, S. B., Gladsjo, J. A., Gerber, M., Hata, T. R., & Gallo, R. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040754 · Cited by 29
Self-citationJiang, H., Liang, L., Qin, J., Lu, Y., Li, B., Wang, Y., Lin, C., Zhou, Q., Feng, S., Yip, S. H., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9033 · Cited by 29
Miura, S., Garcet, S., Li, X., Cueto, I., Salud-Gnilo, C., Kunjravia, N., Yamamura, K., Gonzalez, J., Murai‐Yamamura, M., Rambhia, D., et al. (2022) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2022.10.017 · Cited by 29
Marini, A., Farwick, M., Grether‐Beck, S., Brenden, H., Felsner, I., Jaenicke, T., Weber, M., Schild, J., Maczkiewitz, U., Köhler, T., et al. (2011) · Experimental Dermatology · doi:10.1111/j.1600-0625.2011.01415.x · Cited by 28
Ooi, E. H., Wormald, P., Carney, A. S., James, C. L., & Tan, L. W. (2007) · American Journal of Rhinology · doi:10.2500/ajr.2007.21.3048 · Cited by 28
Cathelicidin Contributes to the Restriction of Leishmania in Human Host Macrophages
Crauwels, P., Bank, E., Walber, B., Wenzel, U. A., Agerberth, B., Chanyalew, M., Abebe, M., König, R., Ritter, U., Reiling, N., et al. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02697 · Cited by 27
Self-citationAdase, C. A., Borkowski, A. W., Zhang, L., Williams, M. R., Sato, E., Sanford, J. A., & Gallo, R. L. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.725317 · Cited by 28
Self-citationThe contribution of IL-17 to the development of autoimmunity in psoriasis
Furue, M., & Kadono, T. (2019) · Innate Immunity · doi:10.1177/1753425919852156 · Cited by 27
Keratinocytes in skin inflammation
Pastore, S., Mascia, F., Mariani, V., & Girolomoni, G. (2006) · Expert Review of Dermatology · doi:10.1586/17469872.1.2.279 · Cited by 27
Pulmonary defense and the human cathelicidin hCAP-18/LL-37
Fahy, R. J., & Wewers, M. D. (2005) · Immunologic Research · doi:10.1385/ir:31:2:075 · Cited by 27
LL-37 suppresses sodium nitroprusside-induced apoptosis of systemic sclerosis dermal fibroblasts
Kim, H. J., Cho, D. H., Lee, K. J., Cho, C. S., Bang, S. I., Cho, B. K., & Park, H. J. (2011) · Experimental Dermatology · doi:10.1111/j.1600-0625.2011.01327.x · Cited by 26
Bernard, Q., Gallo, R. L., Jaulhac, B., Nakatsuji, T., Luft, B. J., Yang, X., & Boulanger, N. (2015) · Experimental Dermatology · doi:10.1111/exd.12853 · Cited by 25
Self-citationSharma, P., Sharma, N., Mishra, P., Joseph, J., Mishra, D. K., Garg, P., & Roy, S. (2019) · Pathogens · doi:10.3390/pathogens8010031 · Cited by 25
Park, A. J., Okhovat, J., & Kim, J. J. (2017) · Springer eBooks · doi:10.1007/978-3-319-29785-9_6 · Cited by 27
Wu, P., Yu, Y., McGhee, C. E., Tan, L. H., & Lu, Y. (2014) · Advanced Materials · doi:10.1002/adma.201304891 · Cited by 25
Santos, J. C., Silva‐Gomes, S., Silva, J. P., Gama, M., Rosa, G. M., Gallo, R. L., & Appelberg, R. (2013) · Immunity Inflammation and Disease · doi:10.1002/iid3.7 · Cited by 24
Self-citationAlarmins and antimicrobial immunity
Yang, D., & Oppenheim, J. J. (2009) · Medical Mycology · doi:10.1080/13693780902721416 · Cited by 24
Design and characterization of a new hybrid peptide from LL-37 and BMAP-27
Tall, Y. R. A., Abualhaijaa, A., Alsaggar, M., Almaaytah, A. M., Masadeh, M. M., & Alzoubi, K. H. (2019) · Infection and Drug Resistance · doi:10.2147/idr.s199473 · Cited by 24
Sensory neuronal control of skin barrier immunity
Feng, X., Zhan, H., & Sokol, C. L. (2024) · Trends in Immunology · doi:10.1016/j.it.2024.03.008 · Cited by 22
Chéneau, C., & Kremer, E. J. (2020) · Viruses · doi:10.3390/v12121351 · Cited by 23
Lu, J., & Lü, Y. (2023) · Journal of Translational Autoimmunity · doi:10.1016/j.jtauto.2023.100211 · Cited by 23
Gaudio, G. D., Lombardi, L., Maisetta, G., Esin, S., Batoni, G., Sanguinetti, M., Senesi, S., & Tavanti, A. (2013) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00904-13 · Cited by 23
Augmentation of Epithelial Resistance to Invading Bacteria by Using mRNA Transfections
Zou, X., Sorenson, B. S., Ross, K. F., & Herzberg, M. C. (2013) · Infection and Immunity · doi:10.1128/iai.00539-13 · Cited by 23
Lee, E. Y., Lee, C. K., Schmidt, N. W., Jin, F., Lande, R., Curk, T., Frenkel, D., Dobnikar, J., Gilliet, M. F., & Wong, G. C. L. (2016) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2016.02.003 · Cited by 23
Boink, M. A., Roffel, S., Nazmi, K., Bolscher, J. G. M., Veerman, E. C. I., & Gibbs, S. (2017) · Journal of Immunology Research · doi:10.1155/2017/3078194 · Cited by 23
Zhang, H., Zhang, B., Zhang, X., Wang, X., Wu, K., & Guan, Q. (2017) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2017.09.005 · Cited by 23
Al-Farsi, H. M., Adwani, S. A., Ahmed, S., Vogt, C., Ambikan, A. T., Leber, A. T., Al‐Jardani, A., Al-Azri, S., Muharrmi, Z. A., Toprak, M. S., et al. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02632 · Cited by 23
Goo, J., Ji, J. H., Jeon, H., Kim, M. J., Jeon, S.-Y., Cho, M.-Y., Lee, S. H., & Choi, E. H. (2010) · Pediatric Dermatology · doi:10.1111/j.1525-1470.2010.01122.x · Cited by 23
The Corneal Expression of Antimicrobial Peptides during Experimental Fungal Keratitis
Yuan, X., Hua, X., & Wilhelmus, K. R. (2010) · Current Eye Research · doi:10.3109/02713683.2010.495812 · Cited by 23
Type I IFNs at the Interface between Cutaneous Immunity and Epidermal Remodeling
Conrad, C., & Gilliet, M. F. (2012) · Journal of Investigative Dermatology · doi:10.1038/jid.2012.149 · Cited by 25
The Antibiotic Effects of Vitamin D
Guo, C., & Gombart, A. F. (2014) · Endocrine Metabolic & Immune Disorders - Drug Targets · doi:10.2174/1871530314666140709085159 · Cited by 22
A novel protocol for the production of recombinant LL-37 expressed as a thioredoxin fusion protein
Li, Y. (2011) · Protein Expression and Purification · doi:10.1016/j.pep.2011.10.011 · Cited by 22
Antimicrobial Peptides for Skin Wound Healing
Wu, Y., Liu, T., Jin, L., Wang, C., & Zhang, D. (2025) · Biomolecules · doi:10.3390/biom15111613 · Cited by 21
Knappe, D., Kabankov, N., Herth, N., & Hoffmann, R. (2016) · Future Medicinal Chemistry · doi:10.4155/fmc-2016-0083 · Cited by 21
Das, S., Sardar, A. H., Abhishek, K., Kumar, A., Rabidas, V. N., & Das, P. K. (2017) · International Immunopharmacology · doi:10.1016/j.intimp.2017.06.010 · Cited by 21
Immuno-Stimulatory Peptides as a Potential Adjunct Therapy against Intra-Macrophagic Pathogens
Silva, T., & Gomes, M. S. (2017) · Molecules · doi:10.3390/molecules22081297 · Cited by 21
Nanofiber-based Sutures Induce Endogenous Antimicrobial Peptide
Chen, S., Ge, L., Gombart, A. F., Shuler, F. D., Carlson, M. A., Reilly, D. A., & Xie, J. (2017) · Nanomedicine · doi:10.2217/nnm-2017-0161 · Cited by 21
Jiang, J., Zhang, Y., Indra, A. K., Ganguli‐Indra, G., Le, M., Wang, H., Hollins, R. R., Reilly, D. A., Carlson, M. A., Gallo, R. L., et al. (2018) · Nanomedicine · doi:10.2217/nnm-2018-0011 · Cited by 21
Self-citationHuang, Y., Wang, P., Tiao, M., Chou, M.-H., Du, Y.-Y., Huang, C., & Chuang, J. (2011) · Journal of Surgical Research · doi:10.1016/j.jss.2011.05.033 · Cited by 21
Li, H., Zhang, S., Nie, B., Long, T., Qu, X., & Yue, B. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00639 · Cited by 20
Yi, J., Deng, Q., Liu, Z., Wang, H., Liu, X., Ren, J., & Qu, X. (2023) · Small · doi:10.1002/smll.202301096 · Cited by 20
The role of cathelicidins in neutrophil biology
Yoon, G., Puentes, R., Tran, J., Multani, A., & Cobo, E. R. (2024) · Journal of Leukocyte Biology · doi:10.1093/jleuko/qiae112 · Cited by 22
Zhang, J., Movahedi, A., Wang, X., Wu, X., Yin, T., & Zhuge, Q. (2014) · Peptides · doi:10.1016/j.peptides.2014.09.011 · Cited by 20
Weistroffer, P. L., Joly, S., Srikantha, R., Tack, B. F., Brogden, K. A., & Guthmiller, J. M. (2008) · Oral Microbiology and Immunology · doi:10.1111/j.1399-302x.2007.00389.x · Cited by 20
Wei, J., Cao, X., Qian, J., Liu, Z., Wang, X., Su, Q., Wang, Y., Xie, R., & Li, X. (2021) · Medicine · doi:10.1097/md.0000000000027426 · Cited by 19
Neutrophil-derived cathelicidin promotes cerebral angiogenesis after ischemic stroke
Xie, W., Huang, T., Guo, Y., Zhang, Y., Chen, W., Li, Y., Chen, C., & Li, P. (2023) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x231175190 · Cited by 19
Alan, E., & Liman, N. (2012) · Veterinary Research Communications · doi:10.1007/s11259-012-9529-7 · Cited by 19
Zhang, J., Movahedi, A., Wei, Z., Sang, M., Wu, X., Wang, M., Wei, H., Pan, H., Yin, T., & Zhuge, Q. (2016) · Analytical Biochemistry · doi:10.1016/j.ab.2016.06.031 · Cited by 19
Novel phospholipase A2 inhibitors from python serum are potent peptide antibiotics
Samy, R. P., Thwin, M. M., Stiles, B. G., Satyanarayanajois, S. D., Chinnathambi, A., Zayed, M., Alharbi, S. A., Siveen, K. S., Sikka, S., Kumar, A. P., et al. (2015) · Biochimie · doi:10.1016/j.biochi.2015.01.003 · Cited by 18
Mammalian Antimicrobial Peptides; Defensins and Cathelicidins
Dorin, J. R., McHugh, B. J., Cox, S. L., & Davidson, D. J. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397169-2.00030-5 · Cited by 19
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
Kapitány, A., Medgyesi, B., Jenei, A., Somogyi, O., Szabó, L., Gáspár, K., Méhes, G., Hendrik, Z., Dócs, K., Szűcs, P., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910428 · Cited by 19
McGonagle, D., & Georgouli, T. (2008) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.2008.02114.x · Cited by 18
Xiao, Q., Luo, Y., Shi, W., Lü, Y., Xiong, R., Wu, X., Huang, H., Zhao, C., Zeng, J., & Cha, C. (2022) · Annals of Translational Medicine · doi:10.21037/atm-22-617 · Cited by 17
Antimicrobial Peptide Loss, Except for LL-37, is not Characteristic of Atopic Dermatitis
Szabó, L., Kapitány, A., Somogyi, O., Alhafez, I., Gáspár, K., Palatka, R., Soltész, L., Törőcsik, D., Hendrik, Z., Dajnoki, Z., et al. (2023) · Acta Dermato Venereologica · doi:10.2340/actadv.v103.9413 · 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
The antibacterial peptide ABP-CM4: the current state of its production and applications
Li, J. F., Zhang, J., Xu, X. Z., Han, Y., Cui, X., Chen, Y. Q., & Zhang, S. Q. (2011) · Amino Acids · doi:10.1007/s00726-011-0982-3 · Cited by 17
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
Bickers, D. R., & Modlin, R. L. (2012) · Journal of Investigative Dermatology · doi:10.1038/jid.2011.391 · 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
Antimicrobial Peptides for Diabetic Wound Healing: Preclinical and Clinical Studies
Herman, A., & Herman, A. P. (2023) · Advances in Wound Care · doi:10.1089/wound.2023.0011 · Cited by 15
Salem, S. A. M., Abu-Zeid, R. M., & Nada, O. H. (2012) · Archives of Dermatological Research · doi:10.1007/s00403-012-1267-8 · Cited by 15
Group A Streptococcus Prevents Mast Cell Degranulation to Promote Extracellular Trap Formation
Clark, M. C., Kim, J., Etesami, N. S., Shimamoto, J., Whalen, R. V., Martin, G. G., & Okumura, C. Y. M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00327 · Cited by 15
Heimroth, R. D., Casadei, E., & Salinas, I. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01259 · Cited by 19
Wei, R., Dhawan, P., Baiocchi, R. A., Kim, K., & Christakos, S. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27702 · Cited by 15
Murine cathelicidin: as a host defensive response against Leishmania major infection
Asadi, A., Kareshk, A. T., Sharifi, I., & Firouzeh, N. (2020) · Journal of Parasitic Diseases · doi:10.1007/s12639-020-01238-0 · Cited by 15
Metadata
- Authors
- Dorschner, R. A., Pestonjamasp, V. K., Tamakuwala, S., Ohtake, T., Rudisill, J., Nizet, V., Agerberth, B., Gudmundsson, G. H., & Gallo, R. L.
- Affiliations
- University of California San Diego (US)
- Karolinska Institutet (SE)
- Corresponding author
- Gallo, Richard L.
- Venue
- Journal of Investigative Dermatology
- Publisher
- Elsevier BV
- Published
- 2001-07
- Volume
- 117
- Issue
- 1
- Pages
- 91-97
- ISSN
- 0022-202X (ISSN-L)
- OpenAlex
- W2085793178
- Cited by
- 567
- References
- 56
- Citations by year
- 2026: 8 · 2025: 10 · 2024: 13 · 2023: 17 · 2022: 11 · 2021: 12 · 2020: 16 · 2019: 25 · 2018: 23 · 2017: 24 · 2016: 20 · 2015: 26 · 2014: 25 · 2013: 23 · 2012: 33
- FWCI
- 14.20
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Journal of Investigative Dermatology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (AI48176, R21AI048176)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR-44379)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Health Sciences › Medicine › Infectious Diseases › Streptococcal Infections and Treatments
- Health Sciences › Medicine › Surgery › Wound Healing and Treatments
- Keywords
- cathelicidin, LL-37, cramps, Streptococcus pyogenes, skin wounds, wound infection, antimicrobial peptides, innate immunity, keratinocytes, granulocytes, skin
- MeSH terms
- Amino Acid Sequence, Animals, Female, Humans, Male, Mice, Inbred C57BL, Molecular Sequence Data, Proteins, RNA, Messenger, Skin, Streptococcal Infections, Streptococcus pyogenes, Wound Healing, Keratinocytes, Gene Expression, Antimicrobial Cationic Peptides, 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