Neisseria gonorrhoeae O-linked pilin glycosylation: functional analyses define both the biosynthetic pathway and glycan structure. (Q35990764)

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1 January 2020

title

Neisseria gonorrhoeae O-linked pilin glycosylation: functional analyses define both the biosynthetic pathway and glycan structure (English)

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1 January 2020

main subject

Neisseria gonorrhoeae

0 references

1 reference

4

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1 January 2020

author name string

Finn Erik Aas

1

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1 January 2020

Ashild Vik

2

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1 January 2020

John Vedde

3

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1 January 2020

Wolfgang Egge-Jacobsen

5

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language of work or name

English

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publication date

29 June 2007

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1 January 2020

published in

Molecular Microbiology

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1 January 2020

volume

65

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issue

3

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1 January 2020

page(s)

607-624

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A critical role for peptidoglycan N-deacetylation in Listeria evasion from the host innate immune system

1 January 2020

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2 October 2017

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2 October 2017

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2 October 2017

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23 September 2018

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23 September 2018

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Glycosylation with heptose residues mediated by the aah gene product is essential for adherence of the AIDA-I adhesin

23 September 2018

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23 September 2018

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23 September 2018

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Use of a non-selective transformation technique to construct a multiply restriction/modification-deficient mutant of Neisseria gonorrhoeae

23 September 2018

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Meningococcal pilin: a glycoprotein substituted with digalactosyl 2,4-diacetamido-2,4,6-trideoxyhexose

23 September 2018

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23 September 2018

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The Role of Common and Type-specific Pilus Antigenic Domains in Adhesion and Virulence of Gonococci for Human Epithelial Cells

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1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/17608667

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Consequences of the loss of O-linked glycosylation of meningococcal type IV pilin on piliation and pilus-mediated adhesion

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/17608667

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Neisseria gonorrhoeae type IV pili undergo multisite, hierarchical modifications with phosphoethanolamine and phosphocholine requiring an enzyme structurally related to lipopolysaccharide phosphoethanolamine transferases

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/17608667

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1111/J.1365-2958.2007.05806.X

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17608667%20AND%20SRC:MED&resulttype=core&format=json

1 January 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17608667%20AND%20SRC:MED&resulttype=core&format=json

1 January 2020

PubMed publication ID

17608667

1 reference