about
RTX proteins: a highly diverse family secreted by a common mechanismCharacterization of binding of adenylate cyclase toxin to target cells by flow cytometry.Virulence potential and genomic mapping of the worldwide clone Escherichia coli ST131.Shiga toxin binds human platelets via globotriaosylceramide (Pk antigen) and a novel platelet glycosphingolipidUse of zebrafish to probe the divergent virulence potentials and toxin requirements of extraintestinal pathogenic Escherichia coli.Cloning and characterization of two bistructural S-layer-RTX proteins from Campylobacter rectus.Correlation of Pasteurella haemolytica leukotoxin binding with susceptibility to intoxication of lymphoid cells from various species.Characterization of hemolysin of Moraxella bovis using a hemolysis-neutralizing monoclonal antibodyRegulation of Aggregatibacter (Actinobacillus) actinomycetemcomitans leukotoxin secretion by ironThe deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.Binding of Pasteurella haemolytica leukotoxin to bovine leukocytesPore forming activity of the potent RTX-toxin produced by pediatric pathogen Kingella kingae: Characterization and comparison to other RTX-family members.The UPEC pore-forming toxin α-hemolysin triggers proteolysis of host proteins to disrupt cell adhesion, inflammatory, and survival pathways.Aggregatibacter actinomycetemcomitans leukotoxin utilizes a cholesterol recognition/amino acid consensus site for membrane association.Membrane interaction of Escherichia coli hemolysin: flotation and insertion-dependent labeling by phospholipid vesicles.Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function.Prelytic and lytic conformations of erythrocyte-associated Escherichia coli hemolysin.Identification and characterization of hemolysin-like proteins similar to RTX toxin in Pasteurella pneumotropica.Effects of Moraxella (Branhamella) ovis culture filtrates on bovine erythrocytes, peripheral mononuclear cells, and corneal epithelial cells.Cytotoxic activity of Kingella kingae RtxA toxin depends on post-translational acylation of lysine residues and cholesterol bindingMembrane localization of the Repeats-in-Toxin (RTX) Leukotoxin (LtxA) produced by Aggregatibacter actinomycetemcomitans
P2860
Q24630254-EEEA9835-F2C2-4A5E-B80E-095767FC03DEQ30304238-579A53CF-CD19-48D8-8AA9-879E2D4800DFQ30414720-43857FE9-A459-400F-863E-42258B137B61Q33503400-9EC3FC77-0260-4934-AA52-33B8709B0720Q33519502-46FB7CA8-5A52-4972-9B3A-82A6522E910FQ33991777-90176F90-3935-496F-ABE7-0DBB9C6FE772Q34002667-290EF83D-FF24-4627-8879-17B4EFC6C4F6Q34004767-A3AFCEDA-F52B-4087-BC34-4B882577DFFBQ35220707-74B3A05A-702E-4F33-A36B-2C454CB6F14EQ35478487-7DF5D852-CE55-434C-BC92-8C88540224C3Q35555032-DF0B0E04-63B8-4C1C-82DE-3B2B2CADED9DQ35602763-684EB81A-0E98-4DFA-93D8-2E5AA4AE65E2Q35697535-4BBFB2A6-8A33-441F-9EE2-C47E9EF5F7C3Q37629800-B3BF4BBA-A602-4B6B-A006-68F2775A67DCQ39504781-D1BA7D46-0E40-4387-BD79-F29F86A8A8F6Q39523324-4F13AB02-D009-45C6-8973-A68C80C8B71FQ39830076-F0092157-FC6B-45FC-9ED1-686436ECC8F9Q43127705-52967CF3-487E-440A-B716-B93A4E755FBAQ43234701-9A873D36-C89B-448E-9FFA-19F7D483A0EFQ58594613-1A158B42-E600-4237-ACA8-AF4249EE47C9Q58602040-1A16BF35-5BC5-4DAA-A54B-DA729B235ABB
P2860
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Association of RTX toxins with erythrocytes.
@en
Association of RTX toxins with erythrocytes.
@nl
type
label
Association of RTX toxins with erythrocytes.
@en
Association of RTX toxins with erythrocytes.
@nl
prefLabel
Association of RTX toxins with erythrocytes.
@en
Association of RTX toxins with erythrocytes.
@nl
P2860
P1476
Association of RTX toxins with erythrocytes.
@en
P2093
P2860
P304
P407
P577
1996-11-01T00:00:00Z