Monoglucosylation of low-molecular-mass GTP-binding Rho proteins by clostridial cytotoxins (Q34290942)

1 August 2017

title

Monoglucosylation of low-molecular-mass GTP-binding Rho proteins by clostridial cytotoxins (English)

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1 August 2017

Aktories K

1

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1 August 2017

Just I

series ordinal

2

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1 August 2017

publication date

1 December 1995

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1 August 2017

published in

Trends in Cell Biology

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1 August 2017

volume

5

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1 August 2017

issue

12

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1 August 2017

page(s)

441-443

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Small GTP-binding proteins and the regulation of the actin cytoskeleton

1 August 2017

cites work

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The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF

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Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1

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Rac mediates growth factor-induced arachidonic acid release.

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A GTP-binding protein (Era) has an essential role in growth rate and cell cycle control in Escherichia coli

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Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia

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Role of toxins A and B in the pathogenesis of Clostridium difficile disease

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Comparative sequence analysis of the Clostridium difficile toxins A and B.

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Clostridium difficile toxin B is more potent than toxin A in damaging human colonic epithelium in vitro

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Clostridium difficile toxin B induces reorganization of actin, vinculin, and talin in cultured cells.

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Glucosylation of Rho proteins by Clostridium difficile toxin B.

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7 January 2021

The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins

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7 January 2021

Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation

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Identifiers

DOI

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1 August 2017

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