The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins
about
Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxinsCrystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components2-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal α-hemolysin into heptameric pore structureStructural and Functional Analysis of the Pore-Forming Toxin NetB from Clostridium perfringensStructural Insights into Clostridium perfringens Delta Toxin Pore FormationResidues Essential for Panton-Valentine Leukocidin S Component Binding to Its Cell Receptor Suggest Both Plasticity and Adaptability in Its Interaction SurfaceMolecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxinsCrystal structure of leucotoxin S component: new insight into the Staphylococcal beta-barrel pore-forming toxinsStaphylococcus aureus Pore-Forming Toxins.Identification of a crucial residue required for Staphylococcus aureus LukAB cytotoxicity and receptor recognition.Staphylococcal Panton-Valentine leucocidin as a major virulence factor associated to furuncles.Distinction between pore assembly by staphylococcal alpha-toxin versus leukotoxins.Assembly of the Bi-component leukocidin pore examined by truncation mutagenesis.Homologous versus heterologous interactions in the bicomponent staphylococcal gamma-haemolysin pore.Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217.The leukocidin pore: evidence for an octamer with four LukF subunits and four LukS subunits alternating around a central axis.Ion channels and bacterial infection: the case of beta-barrel pore-forming protein toxins of Staphylococcus aureus.Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore.Membrane insertion of the heptameric staphylococcal alpha-toxin pore. A domino-like structural transition that is allosterically modulated by the target cell membrane.Novel characteristics of community-acquired methicillin-resistant Staphylococcus aureus strains belonging to multilocus sequence type 59 in Taiwan.The Relationship between Glycan Binding and Direct Membrane Interactions in Vibrio cholerae Cytolysin, a Channel-forming Toxin.Stochastic assembly of two-component staphylococcal gamma-hemolysin into heteroheptameric transmembrane pores with alternate subunit arrangements in ratios of 3:4 and 4:3.Structural model of the pre-pore ring-like structure of Panton-Valentine leukocidin: providing dimensionality to biophysical and mutational data.The bicomponent pore-forming leucocidins of Staphylococcus aureusStaphylococcus aureus Panton-Valentine leukocidin directly targets mitochondria and induces Bax-independent apoptosis of human neutrophils.Structure and hydration of the DNA-human topoisomerase I covalent complex.Molecular modeling reveals the novel inhibition mechanism and binding mode of three natural compounds to staphylococcal α-hemolysin.Five birds, one stone: neutralization of α-hemolysin and 4 bi-component leukocidins of Staphylococcus aureus with a single human monoclonal antibody.Crystallization and preliminary crystallographic studies of both components of the staphylococcal LukE-LukD leukotoxin.Context matters: The importance of dimerization-induced conformation of the LukGH leukocidin of Staphylococcus aureus for the generation of neutralizing antibodies.Staphylococcus aureus hemolysins, bi-component leukocidins, and cytolytic peptides: a redundant arsenal of membrane-damaging virulence factors?High resolution crystallographic studies of alpha-hemolysin-phospholipid complexes define heptamer-lipid head group interactions: implication for understanding protein-lipid interactions.Vibrio cholerae cytolysin is composed of an alpha-hemolysin-like core.Crystal structures of the components of the Staphylococcus aureus leukotoxin ED.Role of pore-forming toxins in neonatal sepsisStaphylococcus aureus leukotoxin ED targets the chemokine receptors CXCR1 and CXCR2 to kill leukocytes and promote infection.Inflammasome Activation Can Mediate Tissue-Specific Pathogenesis or Protection in Staphylococcus aureus Infection.Protein conducting channels-mechanisms, structures and applications.Staphylococcal bicomponent pore-forming toxins: targets for prophylaxis and immunotherapy.Properties of Bacillus cereus hemolysin II: a heptameric transmembrane pore.
P2860
Q24598975-FC4F842D-B097-46DB-A790-E85DA23EA811Q24634854-CF9B54BB-59C4-434C-8186-282F3C7DE6BBQ27666788-96A11793-AF74-4735-8465-6155DE027626Q27676177-7F667E6D-7EBD-4566-BBA7-816843783EEEQ27678825-E5AC2F41-790D-431C-B536-3882D06AD378Q27682292-2E1F28E7-32A4-408F-A770-1D227BC7C854Q27695660-BADA2C7F-BB92-4A6D-A6A2-37B71193B524Q28272895-D5670D44-7B8D-4F40-B26B-D328C8B0DE15Q30152755-F4F917E0-D9F6-469D-931E-86D126D722F5Q30153456-5A259491-5211-43B7-9310-94142CC0EFBBQ30155449-02D71AC9-D128-4FA7-8400-A19B5F8A32AAQ30157977-FF1D83B6-0E9D-4AC9-9CAE-BA8A172DBF43Q30160079-FB8B914F-3992-40C8-B3FB-FF74BB33A326Q30160102-CAEC6CFB-8F42-4A47-A93A-9DB1B5113828Q30160110-8B6E26AA-9F4D-4F0C-8A28-782639458C1AQ30160120-91AE7E2C-33BE-4D77-A85F-726C03B8E50BQ30164517-6E4995E2-F8B8-4D8D-BC6B-9C889C577AE7Q30167424-91FEEC9C-23FF-46A2-8F30-A4F70D9C00CFQ30168331-CE2444CB-8E15-4848-973C-DC9865100339Q30366587-3C7FB9BD-EF55-4F0E-B97A-19A61BFE9D1AQ30379698-E1586C7E-A5F2-4F22-A726-374B57ED3073Q30712777-52B20C96-3F19-49B8-8A00-F9DA2F548BEEQ33579346-03C699E2-8AA6-45C4-AA86-3A66D681DEA8Q33743499-A7DC97E3-F4F3-407F-8ED8-147CD53C23AAQ34097530-48022DFF-5AC5-4BCD-8530-6420A9B1B13EQ34175951-33969245-F9AB-4545-B4FA-96E6551BF7BEQ35060252-D17D8BC6-EC76-4FB4-9C5E-DF1C0B2E7907Q35530119-EC20B1D6-7FA6-4625-BB9F-5E2350EEB131Q36019218-F906CACE-843C-4642-92CC-5E4C6449D28BQ36088381-7AE3A547-D3D9-4011-834C-959D09B555CBQ36159649-FCF62360-91BF-457D-99FC-1191C7FB6420Q36519414-3D7F7354-2531-4B57-9B1D-A8F485317DBDQ36559789-87794985-B875-46FF-81DF-30828B724AD0Q36588360-680D5874-6863-4203-8280-9ABBE8E0F7F2Q36848321-61DEA1FA-D71D-473E-830B-91D81A248DD4Q37422943-33CF6159-463A-4863-ABE6-3C709CDF7193Q37486275-877555DD-C5B8-4E4A-9E5B-1F71C3D90469Q37976983-ED8C8802-A0DA-4FD4-B187-3E81F7E9BA50Q38193690-42B07097-2B5A-4261-BE5C-438139E589E8Q38270075-BEF89EFC-EBEC-4309-9980-A5BEC7803CB3
P2860
The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins
description
1999 nî lūn-bûn
@nan
1999 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մարտին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The structure of a Staphylococ ...... nsmembrane pore-forming toxins
@ast
The structure of a Staphylococ ...... nsmembrane pore-forming toxins
@en
The structure of a Staphylococ ...... nsmembrane pore-forming toxins
@nl
type
label
The structure of a Staphylococ ...... nsmembrane pore-forming toxins
@ast
The structure of a Staphylococ ...... nsmembrane pore-forming toxins
@en
The structure of a Staphylococ ...... nsmembrane pore-forming toxins
@nl
prefLabel
The structure of a Staphylococ ...... nsmembrane pore-forming toxins
@ast
The structure of a Staphylococ ...... nsmembrane pore-forming toxins
@en
The structure of a Staphylococ ...... nsmembrane pore-forming toxins
@nl
P2093
P3181
P1433
P1476
The structure of a Staphylococ ...... nsmembrane pore-forming toxins
@en
P2093
A González
E Courcelle
J D Pédelacq
J P Samama
L Baba-Moussa
P304
P3181
P356
10.1016/S0969-2126(99)80038-0
P577
1999-03-15T00:00:00Z