Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin - Wikidata - wikimedia - TriplyDB

Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

http://www.wikidata.org/entity/Q24318594

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Cytotoxicity of the Vibrio vulnificus MARTX toxin effector DUF5 is linked to the C2A subdomain.Vibrio vulnificus rtxA1 gene recombination generates toxin variants with altered potency during intestinal infection A novel phosphatidylinositol 4,5-bisphosphate binding domain mediates plasma membrane localization of ExoU and other patatin-like phospholipases.Cellular and molecular action of the mitogenic protein-deamidating toxin from Pasteurella multocida.Plasma membrane association of three classes of bacterial toxins is mediated by a basic-hydrophobic motif Substrate specificity of Pasteurella multocida toxin for α subunits of heterotrimeric G proteins 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 Pasteurella multocida toxin (PMT) upregulates CTGF which leads to mTORC1 activation in Swiss 3T3 cells What a difference a Dalton makes: bacterial virulence factors modulate eukaryotic host cell signaling systems via deamidation Recent insights into Pasteurella multocida toxin and other G-protein-modulating bacterial toxins.Effector glycosyltransferases in legionella.Bacterial toxin effector-membrane targeting: outside in, then back again.Membrane interaction of Pasteurella multocida toxin involves sphingomyelin.Backbone and side-chain assignments of an effector membrane localization domain from Vibrio vulnificus MARTX toxin.Pasteurella multocida toxin as a transporter of non-cell-permeating proteins.Enzymatic actions of Pasteurella multocida toxin detected by monoclonal antibodies recognizing the deamidated α subunit of the heterotrimeric GTPase Gq.Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurella multocida toxin The catalytic domains of Clostridium sordellii lethal toxin and related large clostridial glucosylating toxins specifically recognize the negatively charged phospholipids phosphatidylserine and phosphatidic acid.The membrane localization domains of two distinct bacterial toxins form a 4-helix-bundle in solution.

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Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

http://www.wikidata.org/entity/Q24318594

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年学术文章

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2010年学术文章

@zh-cn

2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

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2010年學術文章

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name

Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

@ast

Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

@en

Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

@en-gb

Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

@nl

type

label

Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

@ast

Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

@en

Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

@en-gb

Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

@nl

prefLabel

Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

@ast

Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

@en

Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

@en-gb

Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

@nl

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JBC.M110.102285

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Journal of Biological Chemistry

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Characterization of the membrane-targeting C1 domain in Pasteurella multocida toxin

@en

P2093

Aya Fukui

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

Hirono Toshima

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

Hiroyuki Abe

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

Masami Miyake

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

Masayuki Miyazawa

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

Yasuhiko Horiguchi

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

P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Crystal structures reveal a thiol protease-like catalytic triad in the C-terminal region of Pasteurella multocida toxin

Protein structure comparison by alignment of distance matrices

Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease domain

Identification of a conserved membrane localization domain within numerous large bacterial protein toxins

Two mammalian helix-loop-helix factors structurally related to Drosophila hairy and Enhancer of split

Isolation and nucleotide sequence of the gene encoding cytotoxic necrotizing factor 1 of Escherichia coli.

Structural basis for the function of Clostridium difficile toxin B.

Cytotoxic necrotizing factor type 2 produced by virulent Escherichia coli modifies the small GTP-binding proteins Rho involved in assembly of actin stress fibers.

Pasteurella multocida toxin is a mitogen for bone cells in primary culture.

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33

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Shigeki Kamitani

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