The Helicobacter pylori GroES cochaperonin HspA functions as a specialized nickel chaperone and sequestration protein through its unique C-terminal extension

The Helicobacter pylori GroES cochaperonin HspA functions as a specialized nickel chaperone and sequestration protein through its unique C-terminal extension

Item
http://www.wikidata.org/entity/Q33648641
Helicobacter pylori genotyping from American indigenous groups shows novel Amerindian vacA and cagA alleles and Asian, African and European admixture.Hierarchical regulation of the NikR-mediated nickel response in Helicobacter pyloriEvolution of Helicobacter: Acquisition by Gastric Species of Two Histidine-Rich Proteins Essential for Colonization.Characterization in Helicobacter pylori of a Nickel Transporter Essential for Colonization That Was Acquired during Evolution by Gastric Helicobacter Species.Helicobacter hepaticus NikR controls urease and hydrogenase activities via the NikABDE and HH0418 putative nickel import proteins.Helicobacter pylori stores nickel to aid its host colonization.Hydrogen Metabolism in Helicobacter pylori Plays a Role in Gastric Carcinogenesis through Facilitating CagA Translocation.Common themes and unique proteins for the uptake and trafficking of nickel, a metal essential for the virulence of Helicobacter pyloriNickel trafficking system responsible for urease maturation in Helicobacter pylori.Importance of the C-terminal histidine residues of Helicobacter pylori GroES for Toll-like receptor 4 binding and interleukin-8 cytokine productionNickel-responsive regulation of two novel Helicobacter pylori NikR-targeted genes.The Hsp60 protein of helicobacter pylori displays chaperone activity under acidic conditions.Genome characterization of two bile-isolated Vibrio fluvialis strains: an insight into pathogenicity and bile salt adaption.On-line coupling of continuous-flow gel electrophoresis with inductively coupled plasma-mass spectrometry to quantitatively evaluate intracellular metal binding properties of metallochaperones HpHypA and HpHspA in E. coli cells.Nickel translocation between metallochaperones HypA and UreE in Helicobacter pylori.The Escherichia coli metal-binding chaperone SlyD interacts with the large subunit of [NiFe]-hydrogenase 3.The –Cys–Cys– motif in Helicobacter pylori's Hpn and HspA proteins is an essential anchoring site for metal ions
P2860

The Helicobacter pylori GroES cochaperonin HspA functions as a specialized nickel chaperone and sequestration protein through its unique C-terminal extension

Item
http://www.wikidata.org/entity/Q33648641
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունվարին 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
The Helicobacter pylori GroES ...... ts unique C-terminal extension
@ast
The Helicobacter pylori GroES ...... ts unique C-terminal extension
@en
type
label
The Helicobacter pylori GroES ...... ts unique C-terminal extension
@ast
The Helicobacter pylori GroES ...... ts unique C-terminal extension
@en
prefLabel
The Helicobacter pylori GroES ...... ts unique C-terminal extension
@ast
The Helicobacter pylori GroES ...... ts unique C-terminal extension
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
P932
P356
P1433
P1476
The Helicobacter pylori GroES ...... ts unique C-terminal extension
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
P932