The Neisseria lipooligosaccharide-specific alpha-2,3-sialyltransferase is a surface-exposed outer membrane protein.
about
Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surfaceDiversity of microbial sialic acid metabolismStructure and Mechanism of the Lipooligosaccharide Sialyltransferase from Neisseria meningitidisThe lipooligosaccharide-modifying enzyme LptA enhances gonococcal defence against human neutrophils.Phase-Variable Heptose I Glycan Extensions Modulate Efficacy of 2C7 Vaccine Antibody Directed against Neisseria gonorrhoeae Lipooligosaccharide.Sialic acid, periodontal pathogens and Tannerella forsythia: stick around and enjoy the feast!Enhanced factor H binding to sialylated Gonococci is restricted to the sialylated lacto-N-neotetraose lipooligosaccharide species: implications for serum resistance and evidence for a bifunctional lipooligosaccharide sialyltransferase in GonococciVaccines against gonorrhea: current status and future challenges.Differential expression and transcriptional analysis of the alpha-2,3-sialyltransferase gene in pathogenic Neisseria sppAlpha-2,3-sialyltransferase enhances Neisseria gonorrhoeae survival during experimental murine genital tract infectionDistinct binding and immunogenic properties of the gonococcal homologue of meningococcal factor h binding proteinIdentification of a novel bacterial outer membrane interleukin-1Β-binding protein from Aggregatibacter actinomycetemcomitans.The Omp85 protein of Neisseria meningitidis is required for lipid export to the outer membraneα-2,3-sialyltransferase expression level impacts the kinetics of lipooligosaccharide sialylation, complement resistance, and the ability of Neisseria gonorrhoeae to colonize the murine genital tractThe Pathobiology of Neisseria gonorrhoeae Lower Female Genital Tract Infection.Utilizing CMP-Sialic Acid Analogs to Unravel Neisseria gonorrhoeae Lipooligosaccharide-Mediated Complement Resistance and Design Novel Therapeutics.The molecular mechanisms used by Neisseria gonorrhoeae to initiate infection differ between men and women.Is gonococcal disease preventable? The importance of understanding immunity and pathogenesis in vaccine development.Vaccine research for gonococcal infections: where are we?Control of pili and sialyltransferase expression in Neisseria gonorrhoeae is mediated by the transcriptional regulator CrgA.Gonococcal lipooligosaccharide sialylation: virulence factor and target for novel immunotherapeutics.The phosphocarrier protein HPr of Neisseria meningitidis interacts with the transcription regulator CrgA and its deletion affects capsule production, cell adhesion, and virulence.
P2860
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P2860
The Neisseria lipooligosaccharide-specific alpha-2,3-sialyltransferase is a surface-exposed outer membrane protein.
description
2002 nî lūn-bûn
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2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2002年の論文
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2002年学术文章
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2002年学术文章
@zh-cn
2002年学术文章
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2002年学术文章
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2002年学术文章
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2002年學術文章
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name
The Neisseria lipooligosacchar ...... xposed outer membrane protein.
@ast
The Neisseria lipooligosacchar ...... xposed outer membrane protein.
@en
The Neisseria lipooligosacchar ...... xposed outer membrane protein.
@nl
type
label
The Neisseria lipooligosacchar ...... xposed outer membrane protein.
@ast
The Neisseria lipooligosacchar ...... xposed outer membrane protein.
@en
The Neisseria lipooligosacchar ...... xposed outer membrane protein.
@nl
prefLabel
The Neisseria lipooligosacchar ...... xposed outer membrane protein.
@ast
The Neisseria lipooligosacchar ...... xposed outer membrane protein.
@en
The Neisseria lipooligosacchar ...... xposed outer membrane protein.
@nl
P2093
P2860
P1476
The Neisseria lipooligosacchar ...... xposed outer membrane protein.
@en
P2093
Dawn M Shell
Lisa Chiles
Ralph C Judd
Richard F Rest
Samar Seal
P2860
P304
P356
10.1128/IAI.70.7.3744-3751.2002
P407
P577
2002-07-01T00:00:00Z