about
The vitamin D-antimicrobial peptide pathway and its role in protection against infectionStructural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37Antimicrobial peptides in reptilesLL37 and cationic peptides enhance TLR3 signaling by viral double-stranded RNAsNovel cathelicidin-derived antimicrobial peptides from Equus asinus.Gene cloning, expression and characterization of avian cathelicidin orthologs, Cc-CATHs, from Coturnix coturnix.Paneth cell trypsin is the processing enzyme for human defensin-5.Endogenous cathelicidin production limits inflammation and protective immunity to Mycobacterium avium in mice.The front line of enteric host defense against unwelcome intrusion of harmful microorganisms: mucins, antimicrobial peptides, and microbiotaAntimicrobial peptides in the oral environment: expression and function in health and disease.Cathelicidins from the bullfrog Rana catesbeiana provides novel template for peptide antibiotic design.What is the real role of antimicrobial polypeptides that can mediate several other inflammatory responses?Cathelicidins and innate defense against invasive bacterial infection.Bactericidal activities of cathelicidin LL-37 and select cationic lipids against the hypervirulent Pseudomonas aeruginosa strain LESB58.Novel Cathelicidins from Pigeon Highlights Evolutionary Convergence in Avain Cathelicidins and Functions in Modulation of Innate Immunity.Proline-rich antimicrobial peptides: converging to a non-lytic mechanism of action.Epithelial antimicrobial peptides: guardian of the oral cavity.Expression and secretion of cathelicidin LL-37 in human epithelial cells after infection by Mycobacterium bovis Bacillus Calmette-GuérinResistance of the antibacterial agent ceragenin CSA-13 to inactivation by DNA or F-actin and its activity in cystic fibrosis sputum.Induction of cathelicidin in normal and CF bronchial epithelial cells by 1,25-dihydroxyvitamin D(3).Differential effects on human immunodeficiency virus type 1 replication by alpha-defensins with comparable bactericidal activities.The Mechanism of Killing by the Proline-Rich Peptide Bac7(1-35) against Clinical Strains of Pseudomonas aeruginosa Differs from That against Other Gram-Negative BacteriaInteraction and cellular localization of the human host defense peptide LL-37 with lung epithelial cells.In vitro and in vivo evaluation of BMAP-derived peptides for the treatment of cystic fibrosis-related pulmonary infections.Antibacterial activities of rhodamine B-conjugated gelsolin-derived peptides compared to those of the antimicrobial peptides cathelicidin LL37, magainin II, and melittin.Cathelicidin-trypsin inhibitor loop conjugate represents a promising antibiotic candidate with protease stabilityInteraction of the gelsolin-derived antibacterial PBP 10 peptide with lipid bilayers and cell membranes.A novel organotypic dento-epithelial culture model: effect of Fusobacterium nucleatum biofilm on B-defensin-2, -3, and LL-37 expression.Sinonasal epithelial cells synthesize active vitamin D, augmenting host innate immune function.Identification and polymorphism discovery of the cathelicidins, Lf-CATHs in ranid amphibian (Limnonectes fragilis).Gingival crevicular fluid levels of human beta-defensin-2 and cathelicidin in smoker and non-smoker patients: a cross-sectional study.Suppressive effect of an analog of the antimicrobial peptide of LL‑37 on colon cancer cells via exosome‑encapsulated miRNAs
P2860
Q24647840-B9E79356-1503-4597-B78A-9D22F7EDB715Q27676356-56FA88B2-8670-4B28-AA03-E285E5C32182Q28656399-19DD06A0-FE90-4E45-90FE-750843F127BEQ28743558-189D6F73-537D-44B2-B8C8-DC87C3B8AB1DQ33566187-D9D171CE-0C91-4E3F-B0EC-BCE01AF8A2ECQ33837370-5BC7B729-E034-4F37-8B83-5EBD1DDF10B5Q34129474-4D9798D9-EF77-497E-BEAB-40ACD598D902Q34454677-6FF04ACB-DAC6-44D9-ACA4-E0A0EEB3E93BQ34647328-376BEEB6-0E8E-405A-97DC-85AB52B1D829Q34684398-0AFF5350-8844-4813-942B-F4FE1B543814Q35133502-D6FFFADA-6D01-4132-BCEE-D785C40F5277Q35143463-5F52872D-8D02-450A-ABB1-D8D83B415AD0Q35585098-4F75D1FA-8180-4ED3-BBEA-BF59EBA68055Q35746038-8515EE41-A905-4EF0-9809-130B5CBAB7FAQ35868929-746C196C-E9D9-4FF3-95BA-630C87A5FDEFQ37877177-0035BF1C-49F4-43C6-BC2A-56B32691A07BQ38272974-9891D96C-E94B-4D1B-A9C8-71D281C1BE36Q39968181-6C607F68-D0BE-4860-A959-28E9E90D151BQ40116758-A123D857-84F8-4432-81FF-70C904BDD259Q40139526-D8BB652E-9FFE-4D7D-9EB8-1B8005560940Q40214947-FEDC8705-34C6-445F-897D-060FF538EFCFQ40352859-2CC2B2F2-1B8F-4C0D-8876-1198CA0F3EBBQ40477356-5BC83FEA-7FA9-4239-A552-1C4A45E7157FQ40642439-AC669D07-AB2A-4A5B-9114-8D456A869E90Q40815963-EE53BAA8-D736-44F9-9C69-5909382F12DFQ41807091-6879C296-9C79-45C3-A25C-E9D9DA3EE5D7Q42144931-871BA203-4BF5-4578-BA67-34411419B8BCQ42490311-58DFBC69-9CD9-4C00-800E-FFEA15E8DE8EQ43939229-76ABDB0D-844D-47EF-860F-16022201B17CQ44668643-E44CFE5C-8A45-417F-83D4-F894229A1BE4Q50950571-BEC64DEA-F5E4-4159-B54E-4AC57BBA4895Q58742009-26BC6281-BDF7-4D97-AD0D-7B2C31BC72C3
P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Structure and biology of cathelicidins.
@ast
Structure and biology of cathelicidins.
@en
type
label
Structure and biology of cathelicidins.
@ast
Structure and biology of cathelicidins.
@en
prefLabel
Structure and biology of cathelicidins.
@ast
Structure and biology of cathelicidins.
@en
P2093
P356
P1476
Structure and biology of cathelicidins.
@en
P2093
P304
P356
10.1007/0-306-46831-X_17
P407
P577
2000-01-01T00:00:00Z