The membrane-bound structure and topology of a human α-defensin indicate a dimer pore mechanism for membrane disruption.
about
Sometimes it takes two to tango: contributions of dimerization to functions of human α-defensin HNP1 peptideCationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMRAn intrinsically disordered region of the adenovirus capsid is implicated in neutralization by human alpha defensin 5NMR Solution Structure and Condition-Dependent Oligomerization of the Antimicrobial Peptide Human Defensin 5Dimerization of Plant Defensin NaD1 Enhances Its Antifungal ActivityAntibacterial membrane attack by a pore-forming intestinal C-type lectinThermodynamic instability of viral proteins is a pathogen-associated molecular pattern targeted by human defensinsHuman defensin 5 disulfide array mutants: disulfide bond deletion attenuates antibacterial activity against Staphylococcus aureusMolecular evolution of the primate α-/θ-defensin multigene family.Variations in the interaction of human defensins with Escherichia coli: Possible implications in bacterial killingStructure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR.Structures of β-hairpin antimicrobial protegrin peptides in lipopolysaccharide membranes: mechanism of gram selectivity obtained from solid-state nuclear magnetic resonance.Human defensins facilitate local unfolding of thermodynamically unstable regions of bacterial protein toxins.Human β-defensin 4 with non-native disulfide bridges exhibit antimicrobial activity.High fidelity processing and activation of the human α-defensin HNP1 precursor by neutrophil elastase and proteinase 3Molecular basis for membrane pore formation by Bax protein carboxyl terminusStructural perspectives on antimicrobial chemokines.Cellular response to Trypanosoma cruzi infection induces secretion of defensin α-1, which damages the flagellum, neutralizes trypanosome motility, and inhibits infection.A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes.The Interplay between Defensins and Microbiota in Crohn's Disease.ProHNPs are specific markers of normal myelopoiesis.α-Defensins in human innate immunity.Defensins: antifungal lessons from eukaryotesGuardians of the Gut: Enteric Defensins.Probing Oligomerized Conformations of Defensin in the Membrane.In situ production of human β defensin-3 in lager yeasts provides bactericidal activity against beer-spoiling bacteria under fermentation conditions.Oral Administration of Probiotics Increases Paneth Cells and Intestinal Antimicrobial Activity.Analysis of the antimicrobial mechanism of porcine beta defensin 2 against E. coli by electron microscopy and differentially expressed genes
P2860
Q24613395-9E1B270F-B3CE-4005-B8AF-2BD7D9E877ABQ26830018-93CE9F65-581D-4E4E-B29D-0E15F6254CFDQ27324472-82FDC99B-6AF7-426D-8708-4319F4C5E66AQ27675169-1AF8A15C-7E35-40C2-91F3-74BCA1A4A7A4Q27678587-7893C483-BB54-4C3F-B68F-6085E3E6FA1BQ27680655-C917B593-C937-4CB3-AE47-E40F405210ACQ28828268-EE893103-D3D9-4C24-AB57-218657512781Q30032656-27EBE369-E6C5-45D2-A635-C8F103065E0EQ31161057-4C627DDD-2491-4E91-816F-059E799A2C6AQ33579842-74E713B6-C521-40AF-8951-4F64299F1ACDQ33827462-E46AD4F3-AED9-46DB-BD85-CD8A45E511AFQ34709011-3D4913AF-4C6A-45F2-8DE2-5ABF1A674A7AQ34727874-009F04FC-1219-41FA-9EBC-6AA43690901BQ35580348-DAA3D026-07C5-4FFE-B090-5DA1F090946FQ35842408-07E4B6F5-78BB-4E1B-AD4C-9F61A9FE1AAFQ35955513-A1566FBC-679E-40D7-AB2C-496CC20FD15CQ36492362-D67788AC-87D9-469F-A06E-6F529CEDF21DQ37264811-AE65EB83-0958-464A-9E77-725E6AFFBF4CQ37337990-5F2A1745-DFCE-4165-B8BB-069A7255EB24Q37633135-0CBA004C-C404-439E-A570-E1A1655DFE78Q37679269-4FC4B262-B9A0-4CE2-98E1-AA909AB7D5B2Q37968296-E766EE56-B0C8-4598-973A-8B4B6E22AD3AQ38201011-39E118E3-1D74-4091-A0C2-88D8621F9D32Q39281980-FCA1298E-62A6-4457-8E5F-1BA368348B39Q46643064-6B0A12EB-7DC6-4877-A605-53A09190FFC3Q46976807-B83C42A0-7C8E-4940-9428-557410AA3EBAQ55038841-D5485EFF-A2F1-4685-A9DB-35498568D8B1Q57050221-025A0336-2709-4DF1-9067-92720286CBBC
P2860
The membrane-bound structure and topology of a human α-defensin indicate a dimer pore mechanism for membrane disruption.
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The membrane-bound structure a ...... anism for membrane disruption.
@ast
The membrane-bound structure a ...... anism for membrane disruption.
@en
type
label
The membrane-bound structure a ...... anism for membrane disruption.
@ast
The membrane-bound structure a ...... anism for membrane disruption.
@en
prefLabel
The membrane-bound structure a ...... anism for membrane disruption.
@ast
The membrane-bound structure a ...... anism for membrane disruption.
@en
P2093
P2860
P356
P1433
P1476
The membrane-bound structure a ...... anism for membrane disruption.
@en
P2093
P2860
P304
P356
10.1021/BI101512J
P407
P577
2010-10-26T00:00:00Z