Asp3 mediates multiple protein-protein interactions within the accessory Sec system of Streptococcus gordonii.
about
Bacterial Secretion Systems: An OverviewA role for glycosylated serine-rich repeat proteins in gram-positive bacterial pathogenesis.Asp2 and Asp3 interact directly with GspB, the export substrate of the Streptococcus gordonii accessory Sec SystemA molecular chaperone mediates a two-protein enzyme complex and glycosylation of serine-rich streptococcal adhesins.Canonical SecA associates with an accessory secretory protein complex involved in biogenesis of a streptococcal serine-rich repeat glycoprotein.Gap1 functions as a molecular chaperone to stabilize its interactive partner Gap3 during biogenesis of serine-rich repeat bacterial adhesinProtein secretion and surface display in Gram-positive bacteria.Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly.A Specific interaction between SecA2 and a region of the preprotein adjacent to the signal peptide occurs during transport via the accessory Sec system.Secretion genes as determinants of Bacillus anthracis chain length.Emerging themes in SecA2-mediated protein export.The accessory Sec protein Asp2 modulates GlcNAc deposition onto the serine-rich repeat glycoprotein GspBDifferential localization of the streptococcal accessory sec components and implications for substrate export.Gap2 promotes the formation of a stable protein complex required for mature Fap1 biogenesis.Recent advances in platelet proteomics.Selective transport by SecA2: an expanding family of customized motor proteins.The Canonical and Accessory Sec System of Gram-positive Bacteria.O-acetylation of the serine-rich repeat glycoprotein GspB is coordinated with accessory Sec transport.Composition and Activity of the Non-canonical Gram-positive SecY2 Complex.Unraveling the sequence of cytosolic reactions in the export of GspB adhesin from Streptococcus gordonii.
P2860
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P2860
Asp3 mediates multiple protein-protein interactions within the accessory Sec system of Streptococcus gordonii.
description
2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին 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
Asp3 mediates multiple protein ...... tem of Streptococcus gordonii.
@ast
Asp3 mediates multiple protein ...... tem of Streptococcus gordonii.
@en
Asp3 mediates multiple protein ...... tem of Streptococcus gordonii.
@nl
type
label
Asp3 mediates multiple protein ...... tem of Streptococcus gordonii.
@ast
Asp3 mediates multiple protein ...... tem of Streptococcus gordonii.
@en
Asp3 mediates multiple protein ...... tem of Streptococcus gordonii.
@nl
prefLabel
Asp3 mediates multiple protein ...... tem of Streptococcus gordonii.
@ast
Asp3 mediates multiple protein ...... tem of Streptococcus gordonii.
@en
Asp3 mediates multiple protein ...... tem of Streptococcus gordonii.
@nl
P2093
P2860
P1476
Asp3 mediates multiple protein ...... tem of Streptococcus gordonii.
@en
P2093
Barbara A Bensing
Paul M Sullam
Ravin Seepersaud
Yihfen T Yen
P2860
P304
P356
10.1111/J.1365-2958.2010.07346.X
P407
P577
2010-09-02T00:00:00Z