In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure.
about
Redox-dependent disulfide bond formation in SAP30L corepressor protein: Implications for structure and functionThe Helicobacter pylori GroES cochaperonin HspA functions as a specialized nickel chaperone and sequestration protein through its unique C-terminal extensionImmunization with Heat Shock Protein A and γ-Glutamyl Transpeptidase Induces Reduction on the Helicobacter pylori Colonization in Mice.Importance of the C-terminal histidine residues of Helicobacter pylori GroES for Toll-like receptor 4 binding and interleukin-8 cytokine production
P2860
In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure.
description
2008 nî lūn-bûn
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2008年の論文
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2008年学术文章
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2008年学术文章
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2008年学术文章
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name
In HspA from Helicobacter pylo ...... rminant of domain B structure.
@en
In HspA from Helicobacter pylo ...... rminant of domain B structure.
@nl
type
label
In HspA from Helicobacter pylo ...... rminant of domain B structure.
@en
In HspA from Helicobacter pylo ...... rminant of domain B structure.
@nl
prefLabel
In HspA from Helicobacter pylo ...... rminant of domain B structure.
@en
In HspA from Helicobacter pylo ...... rminant of domain B structure.
@nl
P2093
P2860
P1433
P1476
In HspA from Helicobacter pylo ...... rminant of domain B structure.
@en
P2093
Adriana Zagari
Alessandra Scannella
Angela Flagiello
Cyril Dian
Laurent Terradot
Piero Pucci
Salvatore Loguercio
P2860
P304
P356
10.1016/J.FEBSLET.2008.09.025
P407
P577
2008-09-19T00:00:00Z