The SPI2-encoded SseA chaperone has discrete domains required for SseB stabilization and export, and binds within the C-terminus of SseB and SseD
about
Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Functional dissection of translocon proteins of the Salmonella pathogenicity island 2-encoded type III secretion systemHpaB-Dependent Secretion of Type III Effectors in the Plant Pathogens Ralstonia solanacearum and Xanthomonas campestris pv. vesicatoria.Salmonella enterica serovar Typhimurium skills to succeed in the host: virulence and regulation.Identification of novel type III secretion chaperone-substrate complexes of Chlamydia trachomatis.Novel pegylated silver coated carbon nanotubes kill Salmonella but they are non-toxic to eukaryotic cells.A molecular chaperone mediates a two-protein enzyme complex and glycosylation of serine-rich streptococcal adhesins.Gap1 functions as a molecular chaperone to stabilize its interactive partner Gap3 during biogenesis of serine-rich repeat bacterial adhesinLeptospiral outer membrane protein LipL41 is not essential for acute leptospirosis but requires a small chaperone protein, lep, for stable expression.Functional characterization of SsaE, a novel chaperone protein of the type III secretion system encoded by Salmonella pathogenicity island 2.A screen for over-secretion of proteins by yeast based on a dual component cellular phosphatase and immuno-chromogenic stain for exported bacterial alkaline phosphatase reporter.
P2860
Q30318075-192B398B-B773-4F6F-8F11-A47B2E82B2DAQ33551035-9F924965-A48B-4D6F-8868-57FE3A525BE2Q33884910-63D0CC4D-65DE-4B50-B554-0704B0830FCAQ34336985-FCA21200-FFAF-4359-83F3-391910878ECCQ34595020-5263150F-991E-4267-BA48-67A3EA1C7E5EQ35226168-C9F59585-1F20-44A7-8344-6B826BE47294Q35266929-779B0BFC-20A4-4742-82F0-5578F7BAAB0DQ35774545-23DA9E3D-2DAB-490C-8220-71A99E2A1787Q37036077-1C9A2CF2-BB64-4854-BF86-613804220C58Q37410187-EEC2FDDE-D1F5-4A88-B124-395745FA3C6EQ40738327-E9ABCBC3-BBF2-45DB-9FEC-3C5C69C3A42E
P2860
The SPI2-encoded SseA chaperone has discrete domains required for SseB stabilization and export, and binds within the C-terminus of SseB and SseD
description
2004 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2004
@ast
im Juli 2004 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2004/07/01)
@sk
vědecký článek publikovaný v roce 2004
@cs
wetenschappelijk artikel (gepubliceerd op 2004/07/01)
@nl
наукова стаття, опублікована в липні 2004
@uk
مقالة علمية (نشرت في يوليو 2004)
@ar
name
The SPI2-encoded SseA chaperon ...... he C-terminus of SseB and SseD
@ast
The SPI2-encoded SseA chaperon ...... he C-terminus of SseB and SseD
@en
The SPI2-encoded SseA chaperon ...... he C-terminus of SseB and SseD
@nl
type
label
The SPI2-encoded SseA chaperon ...... he C-terminus of SseB and SseD
@ast
The SPI2-encoded SseA chaperon ...... he C-terminus of SseB and SseD
@en
The SPI2-encoded SseA chaperon ...... he C-terminus of SseB and SseD
@nl
prefLabel
The SPI2-encoded SseA chaperon ...... he C-terminus of SseB and SseD
@ast
The SPI2-encoded SseA chaperon ...... he C-terminus of SseB and SseD
@en
The SPI2-encoded SseA chaperon ...... he C-terminus of SseB and SseD
@nl
P356
P1433
P1476
The SPI2-encoded SseA chaperon ...... he C-terminus of SseB and SseD
@en
P2093
Daniel V. Zurawski
Murry A. Stein
P304
P356
10.1099/MIC.0.26997-0
P577
2004-07-01T00:00:00Z