Glucosylation of Rho proteins by Clostridium difficile toxin B.
about
Clostridial glucosylating toxins enter cells via clathrin-mediated endocytosisEvidence for a novel Cdc42GAP domain at the carboxyl terminus of BNIP-2Universal phosphatase-coupled glycosyltransferase assayActivation of a bacterial virulence protein by the GTPase RhoAClostridium difficile toxin B induces apoptosis in intestinal cultured cellsClostridium difficile toxins: mechanism of action and role in disease.Characterization of the catalytic domain of Clostridium novyi alpha-toxinToxins A and B from Clostridium difficile differ with respect to enzymatic potencies, cellular substrate specificities, and surface binding to cultured cellsThe acetyltransferase activity of the bacterial toxin YopJ of Yersinia is activated by eukaryotic host cell inositol hexakisphosphateToxin B is essential for virulence of Clostridium difficileErbB2 directly activates the exchange factor Dock7 to promote Schwann cell migration.The Regulatory Networks That Control Clostridium difficile Toxin SynthesisClostridium difficile Toxins A and B: Insights into Pathogenic Properties and Extraintestinal EffectsReactive Oxygen Species as Additional Determinants for Cytotoxicity of Clostridium difficile Toxins A and BThe Role of Rho GTPases in Toxicity of Clostridium difficile ToxinsClostridium difficile infection: molecular pathogenesis and novel therapeuticsClostridium difficile toxin CDT induces formation of microtubule-based protrusions and increases adherence of bacteriaConformational analysis of Clostridium difficile toxin B and its implications for substrate recognitionClostridium difficile Toxin B causes epithelial cell necrosis through an autoprocessing-independent mechanismStructure-Function Analysis of Inositol Hexakisphosphate-induced Autoprocessing in Clostridium difficile Toxin AInhibition of the glucosyltransferase activity of clostridial Rho/Ras-glucosylating toxins by castanospermineStructural Basis for Substrate Recognition in the Enzymatic Component of ADP-ribosyltransferase Toxin CDTa from Clostridium difficileMolecular mechanism of elongation factor 1A inhibition by a Legionella pneumophila glycosyltransferaseRational Design of Inhibitors and Activity-Based Probes Targeting Clostridium difficile Virulence Factor TcdBStructural Determinants of Clostridium difficile Toxin A Glucosyltransferase ActivityThe structure of Clostridium difficile toxin A glucosyltransferase domain bound to Mn2+ and UDP provides insights into glucosyltransferase activity and product releaseA bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteinsCrystal structure of human RhoA in a dominantly active form complexed with a GTP analogueActivity of the yeast MNN1 alpha-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferasesCdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity.Stimulation of M3 muscarinic receptors induces phosphorylation of the Cdc42 effector activated Cdc42Hs-associated kinase-1 via a Fyn tyrosine kinase signaling pathwayThe cytotoxin YopT of Yersinia enterocolitica induces modification and cellular redistribution of the small GTP-binding protein RhoAOsmotic stress-induced remodeling of the cortical cytoskeletonPhospholipase DVariations in TcdB activity and the hypervirulence of emerging strains of Clostridium difficileIdentification of a conserved membrane localization domain within numerous large bacterial protein toxinsInvasion activity of a Mycobacterium tuberculosis peptide presented by the Escherichia coli AIDA autotransporterLate activation of stress kinases (SAPK/JNK) by genotoxins requires the DNA repair proteins DNA-PKcs and CSBRegulation of RhoA signaling by the cAMP-dependent phosphorylation of RhoGDIαIntegration of metabolism and virulence by Clostridium difficile CodY
P2860
Q21136368-061D3495-A4C2-4A97-98DF-E91DBC1E88E5Q22254035-746DA682-28BE-474B-99B1-2518820CB9DBQ24307519-E466EFC3-B77D-4113-8BFC-9C1A696E7DA0Q24314319-B4A975F4-667B-4DAF-B43C-B92F2A6FDC25Q24522411-19718615-973D-4045-A915-D669FA150778Q24522454-15A142D0-751B-41F9-9F1D-2340F5BDD456Q24548756-CC605538-1CAB-4080-8C9D-D44A1D80E235Q24561508-2E09222C-F86D-4146-87D8-AB53FFE42196Q24632913-015A6171-659F-4094-BDAE-6AF8E6184408Q24647539-7FFB2ADD-850A-4789-A9DE-486AD21A0C13Q24648256-1907AD2A-C78A-4128-81C1-94B171441FCCQ26748946-6E4EF9DE-5DD8-4547-8127-6B07B9BE480AQ26751477-EB00B807-CB3D-4A82-9B31-C25B22D9C69CQ26770068-12B4313E-47CD-4A79-9E28-0D8EC3EC3DCDQ26775010-6638E412-E8B8-4CDD-A389-F225690E3E6FQ26864237-472C3491-CABF-4114-ABC9-09EF4ED4E67FQ27316166-3CA77BCA-ADDB-4AB0-BF48-EA06276E8196Q27331744-15D68E79-2311-4C26-B1D9-FEEA6DE47341Q27339318-729195C4-769B-434C-8A21-7B4A68C4434CQ27646280-DB974656-B912-4291-BA92-1129BD2906C3Q27650694-8E1EFEBF-9919-4352-89B6-065F89D0665EQ27657077-6435CE26-1DCF-4741-8E17-4DAA9C33927AQ27658750-960B986F-DE77-4D6F-A751-9743A63B3A55Q27666020-5603F302-B5D7-4258-A06A-49A151EA7AB4Q27676848-41801A11-DE4F-4F91-8C5B-31E67FC3F670Q27681638-6EDF4032-E0D1-4C6D-9184-78DFE4DAE943Q27687313-9EC506FC-FDB7-4FEA-8B61-3364F502AD3BQ27749065-E9A6A8FA-537D-4956-8E21-CFEF8B25F125Q27935328-738BC6D3-3B67-454F-B490-AD3E4FA798D9Q27939243-8C3AEB32-C68D-47DB-9724-AA1353DA1194Q28138302-03FA7826-6845-4A28-9DB9-1E7100DD6CF8Q28145375-F25452B8-5AFF-4A0A-8F28-33A9F057788CQ28217767-9443D3FA-BFF3-478D-A78F-3CB1A61BF968Q28253553-B46691E8-CC65-4F3C-9B51-BAE72AB57E71Q28475218-429D1473-BDAB-4060-860D-EF260088E68BQ28485722-6FC6FE02-7886-40DE-BEF2-B56CDC76EBCFQ28486635-84616435-2B83-4CC6-91AD-C746B7CA9B15Q28509902-D654DB99-6749-4AD6-98D1-F26D8E0A8146Q28577831-9003EE4F-E6C6-4672-BB91-991D4BD95AEBQ29346637-1795ED3A-ECFE-4909-90F3-0C2D1FD8B428
P2860
Glucosylation of Rho proteins by Clostridium difficile toxin B.
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Glucosylation of Rho proteins by Clostridium difficile toxin B.
@ast
Glucosylation of Rho proteins by Clostridium difficile toxin B.
@en
Glucosylation of Rho proteins by Clostridium difficile toxin B.
@nl
type
label
Glucosylation of Rho proteins by Clostridium difficile toxin B.
@ast
Glucosylation of Rho proteins by Clostridium difficile toxin B.
@en
Glucosylation of Rho proteins by Clostridium difficile toxin B.
@nl
prefLabel
Glucosylation of Rho proteins by Clostridium difficile toxin B.
@ast
Glucosylation of Rho proteins by Clostridium difficile toxin B.
@en
Glucosylation of Rho proteins by Clostridium difficile toxin B.
@nl
P2093
P356
P1433
P1476
Glucosylation of Rho proteins by Clostridium difficile toxin B
@en
P2093
Aktories K
von Eichel-Streiber C
P2888
P304
P356
10.1038/375500A0
P407
P577
1995-06-01T00:00:00Z
P6179
1018579057