Susceptibility of Chlamydia trachomatis to protegrins and defensins
about
Susceptibility of Neisseria gonorrhoeae to protegrinsGene expression, immunolocalization, and secretion of human defensin-5 in human female reproductive tractBinding of protegrin-1 to Pseudomonas aeruginosa and Burkholderia cepacia.Cathelicidins: family of antimicrobial peptides. A reviewNatural Products for the Treatment of Chlamydiaceae InfectionsRole for inducible nitric oxide synthase in protection from chronic Chlamydia trachomatis urogenital disease in mice and its regulation by oxygen free radicalsAntiviral activity and increased host defense against influenza infection elicited by the human cathelicidin LL-37Distinct defensin profiles in Neisseria gonorrhoeae and Chlamydia trachomatis urethritis reveal novel epithelial cell-neutrophil interactions.Comparison of interactions between beta-hairpin decapeptides and SDS/DPC micelles from experimental and simulation data.Susceptibility of Chlamydia trachomatis to chlorhexidine gluconate gel.Killing of Chlamydia trachomatis by novel antimicrobial lipids adapted from compounds in human breast milk.Haemophilus ducreyi is susceptible to protegrin.The role of protegrins and other elastase-activated polypeptides in the bactericidal properties of porcine inflammatory fluids.Biosynthesized tea polyphenols inactivate Chlamydia trachomatis in vitroPeptide-based Antifungal Therapies against Emerging Infections.Chlamydia trachomatis persistence in the female mouse genital tract: inducible nitric oxide synthase and infection outcomeIn vitro microbicidal activities of cecropin peptides D2A21 and D4E1 and gel formulations containing 0.1 to 2% D2A21 against Chlamydia trachomatis.Human alpha-defensins block papillomavirus infectionAntibacterial activity of human neutrophil defensin HNP-1 analogs without cysteinesModulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family.Protegrin-1: a broad-spectrum, rapidly microbicidal peptide with in vivo activity.Bactericidal activity of a synthetic peptide (CG 117-136) of human lysosomal cathepsin G is dependent on arginine content.Protegrins: structural requirements for inactivating elementary bodies of Chlamydia trachomatis.Broad-spectrum antimicrobial activity of human intestinal defensin 5.Targeting bacterial membrane function: an underexploited mechanism for treating persistent infectionsCorrelation between simulated physicochemical properties and hemolycity of protegrin-like antimicrobial peptides: predicting experimental toxicity.Susceptibility of Chlamydia trachomatis to the excipient hydroxyethyl cellulose: pH and concentration dependence of antimicrobial activityProtegrin interaction with lipid monolayers: Grazing incidence X-ray diffraction and X-ray reflectivity study.Innate immunity in the human female reproductive tract: endocrine regulation of endogenous antimicrobial protection against HIV and other sexually transmitted infections.IL-23 induces IL-22 and IL-17 production in response to Chlamydia muridarum genital tract infection, but the absence of these cytokines does not influence disease pathogenesis.Dermaseptins and magainins: antimicrobial peptides from frogs' skin-new sources for a promising spermicides microbicides-a mini review.Specific polymorphisms in the vitamin D metabolism pathway are not associated with susceptibility to Chlamydia trachomatis infection in humans.Activity of Cathelicidin Peptides against Simkania negevensis.The cell-penetrating peptide, Pep-1, has activity against intracellular chlamydial growth but not extracellular forms of Chlamydia trachomatisRole of matrix metalloproteinase-7 in the modulation of a Chlamydia trachomatis infection.Activity of cathelicidin peptides against Chlamydia spp.Activation of human mast cells by retrocyclin and protegrin highlight their immunomodulatory and antimicrobial properties.Protegrin structure and activity against Neisseria gonorrhoeae.In vitro spectrum of pexiganan activity when tested against pathogens from diabetic foot infections and with selected resistance mechanisms.Expression and characterization of antimicrobial peptides Retrocyclin-101 and Protegrin-1 in chloroplasts to control viral and bacterial infections.
P2860
Q24671037-745D19BB-7CEF-4A7F-A908-89552144FB2CQ24678044-F1142DCF-D256-479B-A127-4A7DFF3FA7CEQ24807172-1E75998C-24D6-46BA-9223-11E72690E1B1Q27027603-4993353E-D7DD-4DC6-9E70-4B784FC4D8A0Q28066312-8DA1A351-D3E9-415B-9DF0-46C6EE3E85E0Q28363828-B9DAF6CD-7699-4AE0-9ED0-2C276A7643E7Q28477585-FD6B03FF-6D59-4916-A129-785CC5AEC36DQ30794373-199F2F6F-FACB-481D-91D6-FF54951499CBQ31119012-3EE73250-29FC-4A3E-986C-F87B41F5003FQ33694203-4CECE754-DCB1-4180-98E6-C354CDC11F24Q33695909-3FF52FDD-871D-4BCE-8C8C-2B9417127137Q33699859-0401C738-3889-4FBE-B7E2-976151B8D876Q33757436-FB85A7BA-B810-4C46-8486-A44BA0B1CBDBQ33836572-EFFFF3DE-03BC-4D82-8ABF-607A7BAF6C24Q33862289-49DFD273-911F-41C5-A4D0-C942DD659F6AQ34008708-B4699091-25E4-4EE2-A5C5-8FF9E3F1F268Q34104390-1734F272-6EEB-47E6-971D-3CBBFE944176Q34334899-8BD9C161-F62B-41BC-98AE-91C3A2861616Q34463066-88565586-2BC4-411B-A4AF-83389A46C11FQ34745204-BE1CCB66-2B16-4FD4-BBEA-48AD5B056536Q35137651-040D0EBD-F719-4CD7-A651-A4C47C677D07Q35530266-7B3C7323-0790-414D-A2BE-967B73BF33B3Q35530362-87969CE9-59A3-4798-BC7A-F84247C7BAB4Q35549706-DD08E499-E002-4FA1-84A9-92888875CCFCQ36393640-64C88A08-0D95-4D28-A470-F0F1FA3D4520Q36713864-862C1B68-D13E-4B9A-867E-CA7158C6E53EQ36744864-0E053960-1E52-4879-8627-2DF0EA6F8C3CQ37297389-7388066D-591D-4B5F-927F-C9A52A2B9BC4Q37334286-E889AB9E-FAE6-4BE4-BF2F-1859E969CC2CQ37366047-DBB61AB6-3213-45D1-B4A2-0F3B50C9B7FAQ37412040-225338CA-9F58-45C0-B5A8-FEFBBC152FD3Q37837499-F9E770E6-6814-437C-94E1-381B39F71317Q37850584-0FAFE8A4-45B4-44FD-AA6C-9400BFBE072CQ37856351-B7104F85-4351-4038-A55E-84047C375A52Q37863103-CB9422B7-7E31-4C72-86DD-135FE5B6F33DQ37865416-36C8A3FF-EB8A-454B-BA0B-887A16256BC6Q38285790-850309AB-6A19-45E6-A354-9A7C0F84B9A7Q39833250-326AEE50-B60B-4E80-AF62-8B5D62AC2267Q41547513-B8F7D71A-FD4B-4F2E-9FD9-A773711716CEQ42429984-9AE507DF-81A9-4B41-A0D0-9FD1817C51C5
P2860
Susceptibility of Chlamydia trachomatis to protegrins and defensins
description
1996 nî lūn-bûn
@nan
1996 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի մարտին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Susceptibility of Chlamydia trachomatis to protegrins and defensins
@ast
Susceptibility of Chlamydia trachomatis to protegrins and defensins
@en
Susceptibility of Chlamydia trachomatis to protegrins and defensins
@nl
type
label
Susceptibility of Chlamydia trachomatis to protegrins and defensins
@ast
Susceptibility of Chlamydia trachomatis to protegrins and defensins
@en
Susceptibility of Chlamydia trachomatis to protegrins and defensins
@nl
prefLabel
Susceptibility of Chlamydia trachomatis to protegrins and defensins
@ast
Susceptibility of Chlamydia trachomatis to protegrins and defensins
@en
Susceptibility of Chlamydia trachomatis to protegrins and defensins
@nl
P2093
P2860
P1476
Susceptibility of Chlamydia trachomatis to protegrins and defensins
@en
P2093
P2860
P304
P407
P577
1996-03-01T00:00:00Z