Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure-function correlations and membrane-perturbing abilities.
about
The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spiderThe solution structure of the active domain of CAP18--a lipopolysaccharide binding protein from rabbit leukocytesNatural Products for the Treatment of Chlamydiaceae InfectionsOn the Functional Overlap between Complement and Anti-Microbial PeptidesComparison of the membrane association of two antimicrobial peptides, magainin 2 and indolicidin.Amphipathic α-helices in proteins: Results from analysis of protein structuresTigerinins: novel antimicrobial peptides from the Indian frog Rana tigerina.Biological activities of retro and diastereo analogs of a 13-residue peptide with antimicrobial and hemolytic activities.Heterologous expression of abaecin peptide from Apis mellifera in Pichia pastoris.Novel bifunctional inhibitor of xylanase and aspartic protease: implications for inhibition of fungal growthIn vitro microbicidal activities of cecropin peptides D2A21 and D4E1 and gel formulations containing 0.1 to 2% D2A21 against Chlamydia trachomatis.Cupiennin 1d*: the cytolytic activity depends on the hydrophobic N-terminus and is modulated by the polar C-terminus.Membrane lysis by the antibacterial peptides cecropins B1 and B3: A spin-label electron spin resonance study on phospholipid bilayersA class of highly potent antibacterial peptides derived from pardaxin, a pore-forming peptide isolated from Moses sole fish Pardachirus marmoratus.Antibacterial activity of human neutrophil defensin HNP-1 analogs without cysteinesMembrane disruptive antimicrobial activities of human β-defensin-3 analogs.Susceptibilities of Bordetella pertussis strains to antimicrobial peptidesHuman β-defensin 4 with non-native disulfide bridges exhibit antimicrobial activity.Peptides from American alligator plasma are antimicrobial against multi-drug resistant bacterial pathogens including Acinetobacter baumannii.Melittin: a membrane-active peptide with diverse functions.Rapid identification of compounds with enhanced antimicrobial activity by using conformationally defined combinatorial libraries.Peptides: isolation, production, and use in India.Natural products for the treatment of trachoma and Chlamydia trachomatis.The potential of antimicrobial peptides as biocides.Bioactive substances from marine fishes, shrimps, and algae and their functions: present and future.Identification and characterization of the antimicrobial peptide corresponding to C-terminal beta-sheet domain of tenecin 1, an antibacterial protein of larvae of Tenebrio molitorAntifungal indole and pyrrolidine-2,4-Dione derivative peptidomimetic lead design based on in silico study of bioactive Peptide families.Structure-function relationship studies on the frog skin antimicrobial peptide tigerinin 1: design of analogs with improved activity and their action on clinical bacterial isolates.Synthetic combinatorial libraries: novel discovery strategy for identification of antimicrobial agents.Morphological behavior of acidic and neutral liposomes induced by basic amphiphilic alpha-helical peptides with systematically varied hydrophobic-hydrophilic balance.Interaction of melittin with membrane cholesterol: a fluorescence approach.Perforin and lymphocyte-mediated cytolysis.Seminal plasmin.Snake venom cardiotoxins-structure, dynamics, function and folding.The use of antimicrobial peptides in ophthalmology: an experimental study in corneal preservation and the management of bacterial keratitisOrientation and dynamics of melittin in membranes of varying composition utilizing NBD fluorescenceImmune mediators of sea-cucumber Holothuria tubulosa (Echinodermata) as source of novel antimicrobial and anti-staphylococcal biofilm agents.Interactions between the plasma membrane and the antimicrobial peptide HP (2-20) and its analogues derived from Helicobacter pylori.Pore formation and translocation of melittin.Synthetic histatin analogues with broad-spectrum antimicrobial activity.
P2860
Q27637943-D74CE525-C8DA-4AB4-978B-666CDC8BDF2BQ27729827-2DDD1DC3-CCE4-4AFE-8C9E-5E28AA2D172BQ28066312-14B4E257-0FF5-4B22-87DF-713DBCE3F833Q28082379-14280C48-2906-41F8-9F77-38DE9672DFE4Q28362033-0E176175-A80C-4127-929A-3702C488A88AQ29543244-6E9DF008-9EF0-46AE-812F-59DA9B40FE5AQ31459025-31E5331B-E1D7-4767-A3ED-FD3603411AFAQ31902860-099B22EF-7791-48D4-9A18-A1DD9BD0C676Q33630088-5DBA7175-1214-4A25-85FB-46484671FC59Q33982498-F0DCF07A-FB5D-498D-B3E6-8E2027497F74Q34104390-AF7DFA56-BF7C-4069-AAD9-3758C8DB5CFEQ34148704-4106AE1C-E7F2-4659-A77E-3AEFE9E2C4D8Q34171949-45558718-1A20-472A-A8D7-4ECDD917A6C5Q34377886-A5FB9B09-6CDE-4404-99C1-F771CA7D8566Q34463066-132206AD-17E3-4235-8089-7C30C67C276CQ35027911-81EA0666-D39D-47B1-9E38-43DCA62F7CAEQ35123992-190DE9B1-88B4-4245-B64F-DAD95E47108BQ35580348-960A3454-021B-4E65-ACF9-6F37B88FB862Q36108116-B8A35691-BA9C-4A73-BD69-1E89938FAB6FQ36670624-9C12228B-F069-4ACE-8301-310CFCB9144FQ36789434-14E7E7FF-17AC-4D8B-A44B-83C6511B672DQ37373511-A7CBF0B4-9B22-4FBE-99B6-1F90F0D9B525Q37841577-80F35BEA-0393-42FE-BABD-0C021769B7A8Q37954604-82CB5F7B-0409-4250-AE5A-2B5DEA626483Q38219133-4EAE9E0A-3520-4BCC-A7B6-D33A90E30555Q38528833-E0B0408D-5DA7-4EEA-8174-C6B46E9C2F14Q39428443-D99497D0-BD7C-406A-91D2-9BF8574C966AQ39652252-268343B9-C921-485F-AF21-8A867F4C623DQ39781961-B8D0528B-A86E-4105-9EE5-07AA0894B1F5Q40139002-9A4CB3A5-7FB1-470C-839D-36D2D463678EQ40299186-E31CB788-3212-4FCF-841E-A93D6625F705Q40378876-320C78D1-40FC-4DD5-85F5-088CF93BA730Q40547902-E80760F0-A940-49D6-BCC5-BBC22134DEF2Q40872119-742608A2-9DC9-4A43-97DB-0A178F8A6F3DQ41770407-512F5A17-0D10-4922-9916-58BDA92EB745Q41847726-B5EEE95A-F417-4F6E-AE79-54E59E9F5521Q41898618-7F09E975-2D60-4A53-B075-08D854D98EEAQ41917395-3225A546-2651-4213-BA6C-3B140AD85F9BQ42029147-44A40D17-5396-4319-9307-12A07670AA63Q42113164-AE9C0BBA-28A4-4982-8EC6-6C3FED7C28C8
P2860
Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure-function correlations and membrane-perturbing abilities.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Cell-lytic and antibacterial p ...... membrane-perturbing abilities.
@en
type
label
Cell-lytic and antibacterial p ...... membrane-perturbing abilities.
@en
prefLabel
Cell-lytic and antibacterial p ...... membrane-perturbing abilities.
@en
P1476
Cell-lytic and antibacterial p ...... membrane-perturbing abilities.
@en
P2093
P304
P356
10.1016/0304-4157(94)90002-7
P577
1994-06-01T00:00:00Z