Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins - Wikidata - wikimedia - TriplyDB

Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins

Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins

http://www.wikidata.org/entity/Q28743234

about

LRP1 is a receptor for Clostridium perfringens TpeL toxin indicating a two-receptor model of clostridial glycosylating toxins Bacterial factors exploit eukaryotic Rho GTPase signaling cascades to promote invasion and proliferation within their host.Characterization of Clostridium perfringens TpeL toxin gene carriage, production, cytotoxic contributions, and trypsin sensitivity.Toward a structural understanding of Clostridium difficile toxins A and B.The Tip of the Four N-Terminal α-Helices of Clostridium sordellii Lethal Toxin Contains the Interaction Site with Membrane Phosphatidylserine Facilitating Small GTPases Glucosylation Toxin plasmids of Clostridium perfringens.How Bacteria Subvert Animal Cell Structure and Function.Bacterial glycosyltransferase toxins.Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.Adhesion and invasion of Clostridium perfringens type A into epithelial cells.TcdB or not TcdB: a tale of two Clostridium difficile toxins.Haemorrhagic toxin and lethal toxin from Clostridium sordellii strain vpi9048: molecular characterization and comparative analysis of substrate specificity of the large clostridial glucosylating toxins.The role of toxins in Clostridium difficile infection.The catalytic domains of Clostridium sordellii lethal toxin and related large clostridial glucosylating toxins specifically recognize the negatively charged phospholipids phosphatidylserine and phosphatidic acid.Quantification of small GTPase glucosylation by clostridial glucosylating toxins using multiplexed MRM analysis.Targeting oncogenic Ras by the Clostridium perfringens toxin TpeL.

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P2860

Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins

http://www.wikidata.org/entity/Q28743234

description

2011 nî lūn-bûn

@nan

2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins

@ast

Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins

@en

Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins

@nl

type

label

Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins

@ast

Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins

@en

Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins

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prefLabel

Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins

@ast

Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins

@en

Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins

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Infection and Immunity

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Clostridium perfringens TpeL glycosylates the Rac and Ras subfamily proteins

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Akiko Ohkubo

http://www.w3.org/2001/XMLSchema#string

Jun Sakurai

http://www.w3.org/2001/XMLSchema#string

Katsuhiko Amimoto

http://www.w3.org/2001/XMLSchema#string

Kazuaki Miyamoto

http://www.w3.org/2001/XMLSchema#string

Keiko Kobayashi

http://www.w3.org/2001/XMLSchema#string

Masahiro Nagahama

http://www.w3.org/2001/XMLSchema#string

Masataka Oda

http://www.w3.org/2001/XMLSchema#string

P2860

Clostridium difficile toxins: mechanism of action and role in disease.

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Identification of toxin A-negative, toxin B-positive Clostridium difficile by PCR.

Biological activities and pore formation of Clostridium perfringens beta toxin in HL 60 cells.

Clostridium perfringens beta toxin and Clostridium septicum alpha toxin: their mechanisms and possible role in pathogenesis.

Clostridium novyi alpha-toxin-catalyzed incorporation of GlcNAc into Rho subfamily proteins.

Structural basis for the function of Clostridium difficile toxin B.

Rho-glucosylating Clostridium difficile toxins A and B: new insights into structure and function.

Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O

The enteric toxins of Clostridium perfringens.

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905-10

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scholarly article

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5048382

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10.1128/IAI.01019-10

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2

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79

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2011-02-01T00:00:00Z

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21098103

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infectious disease

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3028844

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