(Q33786797)

English

The Actinobacillus pleuropneumoniae HMW1C-like glycosyltransferase mediates N-linked glycosylation of the Haemophilus influenzae HMW1 adhesin

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

The Actinobacillus pleuropneumoniae HMW1C-like glycosyltransferase mediates N-linked glycosylation of the Haemophilus influenzae HMW1 adhesin (English)

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

1 reference

based on heuristic

inferred from title

Haemophilus influenzae

object named as

Haemophilus influenzae

1 reference

based on heuristic

inferred from title

Actinobacillus pleuropneumoniae

object named as

Actinobacillus pleuropneumoniae

1 reference

based on heuristic

inferred from title

Joseph W St Geme

4

object named as

Joseph W St Geme

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

author name string

Kyoung-Jae Choi

1

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

Susan Grass

2

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

Seonghee Paek

3

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

Hye-Jeong Yeo

5

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

language of work or name

0 references

publication date

30 December 2010

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

5

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

12

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

e15888

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

copyright license

Creative Commons Attribution 4.0 International

30 December 2010

1 reference

April 2022 Public Data File from Crossref

copyright status

0 references

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

1 reference

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A prototype two-partner secretion pathway: the Haemophilus influenzae HMW1 and HMW2 adhesin systems

1 reference

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1 reference

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Glycosylation and biogenesis of a family of serine-rich bacterial adhesins

1 reference

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1 reference

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1 reference

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1 reference

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Cross-talk between GlcNAcylation and phosphorylation: site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc

1 reference

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Campylobacter sugars sticking out.

1 reference

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4 July 2018

The Haemophilus influenzae HMW1 adhesin is a glycoprotein with an unusual N-linked carbohydrate modification

1 reference

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1 reference

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1 reference

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1 reference

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O-linked glycosylation ensures the normal conformation of the autotransporter adhesin involved in diffuse adherence

1 reference

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Protein glycosylation in bacterial mucosal pathogens

1 reference

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Evolutionary and functional relationships among the nontypeable Haemophilus influenzae HMW family of adhesins

1 reference

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Roles of N-linked glycans in the endoplasmic reticulum

1 reference

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Sweet new world: glycoproteins in bacterial pathogens

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Roles of the Tetratricopeptide Repeat Domain in O-GlcNAc Transferase Targeting and Protein Substrate Specificity

1 reference

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4 July 2018

The Haemophilus influenzae HMW1 adhesin is glycosylated in a process that requires HMW1C and phosphoglucomutase, an enzyme involved in lipooligosaccharide biosynthesis.

1 reference

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An evolving hierarchical family classification for glycosyltransferases

1 reference

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Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases

1 reference

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Structure of the UDP-glucosyltransferase GtfB that modifies the heptapeptide aglycone in the biosynthesis of vancomycin group antibiotics

1 reference

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Glycosylation and the immune system

1 reference

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Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity

1 reference

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1 reference

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1 reference

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inferred from PubMed ID database lookup

Identifiers

10.1371/JOURNAL.PONE.0015888

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

2010PLoSO...515888C

0 references

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

ResearchGate publication ID

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