Clostridium difficile toxin A decreases acetylation of tubulin, leading to microtubule depolymerization through activation of histone deacetylase 6, and this mediates acute inflammation.
about
Mice lacking α-tubulin acetyltransferase 1 are viable but display α-tubulin acetylation deficiency and dentate gyrus distortionIn vivo physiological and transcriptional profiling reveals host responses to Clostridium difficile toxin A and toxin BGlutamine and alanyl-glutamine increase RhoA expression and reduce Clostridium difficile toxin-a-induced intestinal epithelial cell damageCrosstalk between HDAC6 and Nox2-based NADPH oxidase mediates HIV-1 Tat-induced pro-inflammatory responses in astrocytes.Role of NADH: quinone oxidoreductase-1 in the tight junctions of colonic epithelial cells.Tubulin acetylation: responsible enzymes, biological functions and human diseases.Persistence and toxin production by Clostridium difficile within human intestinal organoids result in disruption of epithelial paracellular barrier function.Critical roles of Clostridium difficile toxin B enzymatic activities in pathogenesis.Identification of a novel virulence factor in Clostridium difficile that modulates toxin sensitivity of cultured epithelial cells.Host-Microbiota Interactions in the Pathogenesis of Antibiotic-Associated Diseases.Clostridium difficile toxins: mediators of inflammation.Nitrotyrosine impairs mitochondrial function in fetal lamb pulmonary artery endothelial cells.The antimicrobial peptide cathelicidin modulates Clostridium difficile-associated colitis and toxin A-mediated enteritis in mice.Natural indoles, indole-3-carbinol and 3,3'-diindolymethane, inhibit T cell activation by staphylococcal enterotoxin B through epigenetic regulation involving HDAC expression.Multifaceted interactions of bacterial toxins with the gastrointestinal mucosa.Photorhabdus luminescens PirAB-fusion protein exhibits both cytotoxicity and insecticidal activity.Development and evaluation of an ovine antibody-based platform for treatment of Clostridium difficile infection
P2860
Q24294186-4A659B2C-EBF5-40CA-9F88-691C0608E5F1Q30414030-93DB2218-4AF2-4154-8F5A-286BA8BD25A0Q30421944-5EC3A345-BE6F-4B11-A8B1-1C163BE009CDQ33676138-513AA636-BC2C-441F-A151-5BDD174E3E90Q34389757-F53CDD88-6CFC-442F-AF8B-EEB1CCFBE147Q34487624-9001C29A-1D48-4B51-9837-5D7C3CF22AE4Q34889659-D616F440-433E-4CD9-8B6D-133219401E6CQ34955649-D7B21D45-9961-4386-AEE4-B1ACE41AD4C3Q35191951-B2857D4F-CE87-4138-8E08-A0080353C4CCQ35910975-84233CCB-7CF8-47BC-AB63-A20E9483EB15Q36072072-9F46ACF1-13E7-423C-94B6-731735A6095EQ36422698-6B59F84E-DFEA-496C-942D-28D6208ED39EQ37079669-CEA7F564-9B32-4961-BC99-0453F2EDF5BBQ37417983-A300BB44-3D52-4FFC-BCA9-E3A23DBCFF36Q37907307-B80B1EB7-282D-4E4C-AF42-687D3A33E1A9Q38993854-1F5B110A-DBFA-42F0-8BA8-A7DE7ACF002CQ40603225-CECB4770-E34A-4993-B70F-E50AF520CBBB
P2860
Clostridium difficile toxin A decreases acetylation of tubulin, leading to microtubule depolymerization through activation of histone deacetylase 6, and this mediates acute inflammation.
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
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Clostridium difficile toxin A ...... s mediates acute inflammation.
@ast
Clostridium difficile toxin A ...... s mediates acute inflammation.
@en
Clostridium difficile toxin A ...... s mediates acute inflammation.
@nl
type
label
Clostridium difficile toxin A ...... s mediates acute inflammation.
@ast
Clostridium difficile toxin A ...... s mediates acute inflammation.
@en
Clostridium difficile toxin A ...... s mediates acute inflammation.
@nl
prefLabel
Clostridium difficile toxin A ...... s mediates acute inflammation.
@ast
Clostridium difficile toxin A ...... s mediates acute inflammation.
@en
Clostridium difficile toxin A ...... s mediates acute inflammation.
@nl
P2093
P2860
P356
P1476
Clostridium difficile toxin A ...... s mediates acute inflammation.
@en
P2093
Charalabos Pothoulakis
Hyo Jung Nam
Jin Ku Kang
John Thomas Lamont
Jong Soo Chang
Keun Jae Ahn
Sang Joon Park
Sung-Kuk Kim
P2860
P304
32888-32896
P356
10.1074/JBC.M110.162743
P407
P577
2010-08-09T00:00:00Z