Investigating the role of secA2 in secretion and glycosylation of a fimbrial adhesin in Streptococcus parasanguis FW213.
about
Identification of critical residues in Gap3 of Streptococcus parasanguinis involved in Fap1 glycosylation, fimbrial formation and in vitro adhesionGenome of the opportunistic pathogen Streptococcus sanguinisA unique Mycobacterium ESX-1 protein co-secretes with CFP-10/ESAT-6 and is necessary for inhibiting phagosome maturationATPase activity of Mycobacterium tuberculosis SecA1 and SecA2 proteins and its importance for SecA2 function in macrophagesInteraction between two putative glycosyltransferases is required for glycosylation of a serine-rich streptococcal adhesin.A conserved domain of previously unknown function in Gap1 mediates protein-protein interaction and is required for biogenesis of a serine-rich streptococcal adhesin.A novel glucosyltransferase is required for glycosylation of a serine-rich adhesin and biofilm formation by Streptococcus parasanguinisTransport of preproteins by the accessory Sec system requires a specific domain adjacent to the signal peptideThe sweet tooth of bacteria: common themes in bacterial glycoconjugates.A role for glycosylated serine-rich repeat proteins in gram-positive bacterial pathogenesis.Pili with strong attachments: Gram-positive bacteria do it differently.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.Two gene determinants are differentially involved in the biogenesis of Fap1 precursors in Streptococcus parasanguis.Label-free Quantitative Proteomics Reveals a Role for the Mycobacterium tuberculosis SecA2 Pathway in Exporting Solute Binding Proteins and Mce Transporters to the Cell WallGap1 functions as a molecular chaperone to stabilize its interactive partner Gap3 during biogenesis of serine-rich repeat bacterial adhesinSecA: a potential antimicrobial target.A Specific interaction between SecA2 and a region of the preprotein adjacent to the signal peptide occurs during transport via the accessory Sec system.Emerging themes in SecA2-mediated protein export.Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain.Gap2 promotes the formation of a stable protein complex required for mature Fap1 biogenesis.Role of the serine-rich surface glycoprotein GspB of Streptococcus gordonii in the pathogenesis of infective endocarditis.A conserved C-terminal 13-amino-acid motif of Gap1 is required for Gap1 function and necessary for the biogenesis of a serine-rich glycoprotein of Streptococcus parasanguinis.A new twist on an old pathway--accessory Sec [corrected] systemsMolecular dissection of the secA2 locus of group B Streptococcus reveals that glycosylation of the Srr1 LPXTG protein is required for full virulence.New Helical Binding Domain Mediates a Glycosyltransferase Activity of a Bifunctional ProteinThe Streptococcus pneumoniae adhesin PsrP binds to Keratin 10 on lung cells.Engineering and Dissecting the Glycosylation Pathway of a Streptococcal Serine-rich Repeat AdhesinProtein export systems of Mycobacterium tuberculosis: novel targets for drug development?The ins and outs of Mycobacterium tuberculosis protein export.Interactions in bacterial biofilm development: a structural perspective.Pour some sugar on it: the expanding world of bacterial protein O-linked glycosylation.Selective transport by SecA2: an expanding family of customized motor proteins.Breaking the bacterial protein targeting and translocation model: oral organisms as a case in point.The Canonical and Accessory Sec System of Gram-positive Bacteria.Clostridium difficile cell wall protein CwpV undergoes enzyme-independent intramolecular autoproteolysis.The group B streptococcal serine-rich repeat 1 glycoprotein mediates penetration of the blood-brain barrierClostridium difficile has two parallel and essential Sec secretion systemsIdentification of two Mycobacterium smegmatis lipoproteins exported by a SecA2-dependent pathway
P2860
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P2860
Investigating the role of secA2 in secretion and glycosylation of a fimbrial adhesin in Streptococcus parasanguis FW213.
description
2004 nî lūn-bûn
@nan
2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
name
Investigating the role of secA ...... reptococcus parasanguis FW213.
@ast
Investigating the role of secA ...... reptococcus parasanguis FW213.
@en
type
label
Investigating the role of secA ...... reptococcus parasanguis FW213.
@ast
Investigating the role of secA ...... reptococcus parasanguis FW213.
@en
prefLabel
Investigating the role of secA ...... reptococcus parasanguis FW213.
@ast
Investigating the role of secA ...... reptococcus parasanguis FW213.
@en
P2093
P2860
P1476
Investigating the role of secA ...... reptococcus parasanguis FW213.
@en
P2093
Paula M Fives-Taylor
Qiang Chen
P2860
P304
P356
10.1111/J.1365-2958.2004.04116.X
P407
P577
2004-08-01T00:00:00Z