Stealth proteins: in silico identification of a novel protein family rendering bacterial pathogens invisible to host immune defense.
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Comparative genome analysis of Streptococcus infantarius subsp. infantarius CJ18, an African fermented camel milk isolate with adaptations to dairy environmentThe DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase is a substrate recognition moduleAnalysis of mucolipidosis II/III GNPTAB missense mutations identifies domains of UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase involved in catalytic function and lysosomal enzyme recognitionMucolipidosis II-related mutations inhibit the exit from the endoplasmic reticulum and proteolytic cleavage of GlcNAc-1-phosphotransferase precursor protein (GNPTAB)Comparative genomic characterization of Actinobacillus pleuropneumoniaeEngineering of GlcNAc-1-Phosphotransferase for Production of Highly Phosphorylated Lysosomal Enzymes for Enzyme Replacement Therapy.Mutations That Alter the Bacterial Cell Envelope Increase Lipid Production.UDP-GlcNAc:Glycoprotein N-acetylglucosamine-1-phosphotransferase mediates the initial step in the formation of the methylphosphomannosyl residues on the high mannose oligosaccharides of Dictyostelium discoideum glycoproteins.A novel xylosylphosphotransferase activity discovered in Cryptococcus neoformans.Multiple Domains of GlcNAc-1-phosphotransferase Mediate Recognition of Lysosomal Enzymes.Capsular Polysaccharide Expression in Commensal Streptococcus Species: Genetic and Antigenic Similarities to Streptococcus pneumoniae.Haemophilus parainfluenzae expresses diverse lipopolysaccharide O-antigens using ABC transporter and Wzy polymerase-dependent mechanisms.Transcriptional response to vancomycin in a highly vancomycin-resistant Streptomyces coelicolor mutant.The capsule polymerase CslB of Neisseria meningitidis serogroup L catalyzes the synthesis of a complex trimeric repeating unit comprising glycosidic and phosphodiester linkages.Molecular cloning and functional characterization of components of the capsule biosynthesis complex of Neisseria meningitidis serogroup A: toward in vitro vaccine production.Characterization of the meningococcal serogroup X capsule N-acetylglucosamine-1-phosphotransferase.Role of spacer-1 in the maturation and function of GlcNAc-1-phosphotransferase.Efficient solid-phase synthesis of meningococcal capsular oligosaccharides enables simple and fast chemoenzymatic vaccine production.A New Family of Capsule Polymerases Generates Teichoic Acid-Like Capsule Polymers in Gram-Negative Pathogens.
P2860
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P2860
Stealth proteins: in silico identification of a novel protein family rendering bacterial pathogens invisible to host immune defense.
description
2005 nî lūn-bûn
@nan
2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Stealth proteins: in silico id ...... visible to host immune defense
@nl
Stealth proteins: in silico id ...... isible to host immune defense.
@ast
Stealth proteins: in silico id ...... isible to host immune defense.
@en
type
label
Stealth proteins: in silico id ...... visible to host immune defense
@nl
Stealth proteins: in silico id ...... isible to host immune defense.
@ast
Stealth proteins: in silico id ...... isible to host immune defense.
@en
prefLabel
Stealth proteins: in silico id ...... visible to host immune defense
@nl
Stealth proteins: in silico id ...... isible to host immune defense.
@ast
Stealth proteins: in silico id ...... isible to host immune defense.
@en
P2093
P2860
P1476
Stealth proteins: in silico id ...... isible to host immune defense.
@en
P2093
Christoph D Schmid
Olav Zilian
Peter Sperisen
Philipp Bucher
P2860
P356
10.1371/JOURNAL.PCBI.0010063
P407
P577
2005-11-18T00:00:00Z