Stability and assembly of pilus subunits of Streptococcus pneumoniae.
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A Model for Group B Streptococcus Pilus Type 1: The Structure of a 35-kDa C-Terminal Fragment of the Major Pilin GBS80Structure of the Full-Length Major Pilin from Streptococcus pneumoniae: Implications for Isopeptide Bond Formation in Gram-Positive Bacterial PiliThe full-length Streptococcus pneumoniae major pilin RrgB crystallizes in a fibre-like structure, which presents the D1 isopeptide bond and provides details on the mechanism of pilus polymerizationStructural Basis of Pilus Anchoring by the Ancillary Pilin RrgC of Streptococcus pneumoniaeThe Streptococcus pneumoniae pilus-1 displays a biphasic expression patternNMR spectroscopic and theoretical analysis of a spontaneously formed Lys-Asp isopeptide bondThe two variants of the Streptococcus pneumoniae pilus 1 RrgA adhesin retain the same function and elicit cross-protection in vivo.Structural and functional characterization of the Streptococcus pneumoniae RrgB pilus backbone D1 domain.Protective activity of the CnaBE3 domain conserved among Staphylococcus aureus Sdr proteins.Isopeptide ligation catalyzed by quintessential sortase A: mechanistic cues from cyclic and branched oligomers of indolicidin.New cell surface protein involved in biofilm formation by Streptococcus parasanguinisStructure and assembly of group B streptococcus pilus 2b backbone protein.Protein secretion and surface display in Gram-positive bacteria.The metal ion-dependent adhesion site motif of the Enterococcus faecalis EbpA pilin mediates pilus function in catheter-associated urinary tract infection.A distinct sortase SrtB anchors and processes a streptococcal adhesin AbpA with a novel structural property.Yet more intramolecular cross-links in Gram-positive surface proteins.Cellular interactions by LPxTG-anchored pneumococcal adhesins and their streptococcal homologues.Autocatalytic association of proteins by covalent bond formation: a Bio Molecular Welding toolbox derived from a bacterial adhesinPilus backbone protein PitB of Streptococcus pneumoniae contains stabilizing intramolecular isopeptide bonds.
P2860
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P2860
Stability and assembly of pilus subunits of Streptococcus pneumoniae.
description
2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
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2010年學術文章
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2010年學術文章
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2010年學術文章
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name
Stability and assembly of pilus subunits of Streptococcus pneumoniae.
@en
Stability and assembly of pilus subunits of Streptococcus pneumoniae.
@nl
type
label
Stability and assembly of pilus subunits of Streptococcus pneumoniae.
@en
Stability and assembly of pilus subunits of Streptococcus pneumoniae.
@nl
prefLabel
Stability and assembly of pilus subunits of Streptococcus pneumoniae.
@en
Stability and assembly of pilus subunits of Streptococcus pneumoniae.
@nl
P2093
P2860
P356
P1476
Stability and assembly of pilus subunits of Streptococcus pneumoniae.
@en
P2093
Anne Marie Di Guilmi
Lamya El Mortaji
Remi Terrasse
Thierry Vernet
P2860
P304
12405-12415
P356
10.1074/JBC.M109.082776
P407
P577
2010-02-10T00:00:00Z