Functional analysis of the Helicobacter pullorum N-linked protein glycosylation system.

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A recombinant conjugated pneumococcal vaccine that protects against murine infections with a similar efficacy to Prevnar-13

P2860

Q58587115-101F904B-618C-4992-B298-EAA309F87C5C

P2860

Functional analysis of the Helicobacter pullorum N-linked protein glycosylation system.

Item

http://www.wikidata.org/entity/Q50014995

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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name

Functional analysis of the Helicobacter pullorum N-linked protein glycosylation system.

@en

Functional analysis of the Helicobacter pullorum N-linked protein glycosylation system.

@nl

type

Item

label

Functional analysis of the Helicobacter pullorum N-linked protein glycosylation system.

@en

Functional analysis of the Helicobacter pullorum N-linked protein glycosylation system.

@nl

prefLabel

Functional analysis of the Helicobacter pullorum N-linked protein glycosylation system.

@en

Functional analysis of the Helicobacter pullorum N-linked protein glycosylation system.

@nl

P1476

Functional analysis of the Helicobacter pullorum N-linked protein glycosylation system.

@en

P2093

Adrian J Jervis

http://www.w3.org/2001/XMLSchema#string

Alison G Wood

http://www.w3.org/2001/XMLSchema#string

Dennis Linton

http://www.w3.org/2001/XMLSchema#string

Elizabeth Lord

http://www.w3.org/2001/XMLSchema#string

Helen Frost

http://www.w3.org/2001/XMLSchema#string

Joel A Cain

http://www.w3.org/2001/XMLSchema#string

Rebecca Langdon

http://www.w3.org/2001/XMLSchema#string

P2860

In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation

X-ray structure of a bacterial oligosaccharyltransferase

Structural Insights into the Glycosyltransferase Activity of the Actinobacillus pleuropneumoniae HMW1C-like Protein

The Haemophilus influenzae HMW1C protein is a glycosyltransferase that transfers hexose residues to asparagine sites in the HMW1 adhesin

Two distinct but interchangeable mechanisms for flipping of lipid-linked oligosaccharides

Chemoenzymatic synthesis of glycopeptides with PglB, a bacterial oligosaccharyl transferase from Campylobacter jejuni

Direct biochemical evidence for the utilization of UDP-bacillosamine by PglC, an essential glycosyl-1-phosphate transferase in the Campylobacter jejuni N-linked glycosylation pathway

In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system

Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli.

From peptide to protein: comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni.

P304

233-244

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P31

scholarly article

P356

10.1093/GLYCOB/CWX110

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Stuart J. Cordwell

Jonathan A Butler

Brendan W Wren

P577

2018-04-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

29340583

http://www.w3.org/2001/XMLSchema#string

P921

glycosylation

P932

6025236

http://www.w3.org/2001/XMLSchema#string

Functional analysis of the Helicobacter pullorum N-linked protein glycosylation system.

about

P2860

P2860

Functional analysis of the Helicobacter pullorum N-linked protein glycosylation system.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P921

P932