N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli. - Test2 - elhamkhani - TriplyDB

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

http://www.wikidata.org/entity/Q34161971

about

Similarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotes Complete genome sequence and analysis of Wolinella succinogenes Secretion and N-linked glycosylation are required for prostatic acid phosphatase catalytic and antinociceptive activity In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer.Diversity of microbial sialic acid metabolism Production of glycoprotein vaccines in Escherichia coli Structure, function, and evolution of bacterial ATP-binding cassette systems Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions Ribophorin I regulates substrate delivery to the oligosaccharyltransferase core Photocross-linking of nascent chains to the STT3 subunit of the oligosaccharyltransferase complex An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli Polyisoprenol specificity in the Campylobacter jejuni N-linked glycosylation pathway Identification and quantification of glycoproteins using ion-pairing normal-phase liquid chromatography and mass spectrometry Hib Vaccines: Past, Present, and Future Perspectives Cell factories for insulin production Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency Structural context for proteinN-glycosylation in bacteria: The structure of PEB3, an adhesin fromCampylobacter jejuni Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases Structure-guided identification of a new catalytic motif of oligosaccharyltransferase X-ray structure of a bacterial oligosaccharyltransferase Structure and mechanism of an active lipid-linked oligosaccharide flippase Subunits of the translocon interact with components of the oligosaccharyl transferase complex.Insight into functional aspects of Stt3p, a subunit of the oligosaccharyl transferase. Evidence for interaction of the N-terminal domain of Stt3p with the protein kinase C cascade.Dimeric organization of the yeast oligosaccharyl transferase complex.Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit.Membrane topology of the Alg14 endoplasmic reticulum UDP-GlcNAc transferase subunit.High-throughput recombinant protein expression in Escherichia coli: current status and future perspectives Ribophorin I associates with a subset of membrane proteins after their integration at the sec61 translocon Lipid somersaults: Uncovering the mechanisms of protein-mediated lipid flipping The Haemophilus influenzae HMW1C protein is a glycosyltransferase that transfers hexose residues to asparagine sites in the HMW1 adhesin Galactosaminogalactan, a new immunosuppressive polysaccharide of Aspergillus fumigatus Two distinct but interchangeable mechanisms for flipping of lipid-linked oligosaccharides Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz Bibliometric analysis of publications on Campylobacter: (2000-2015)A catalytically essential motif in external loop 5 of the bacterial oligosaccharyltransferase PglB Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli.Exploitation of bacterial N-linked glycosylation to develop a novel recombinant glycoconjugate vaccine against Francisella tularensis.

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P2860

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

http://www.wikidata.org/entity/Q34161971

description

2002 nî lūn-bûn

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2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2002 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

@ast

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

@en

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

@nl

type

label

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

@ast

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

@en

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

@nl

prefLabel

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

@ast

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

@en

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

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SCIENCE.298.5599.1790

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N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.

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Anne Dell

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Dennis Linton

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Howard R Morris

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Maria Panico

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Markus Aebi

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Stuart M Haslam

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Escherichia coli