Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family. (Q36617733)

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scientific article published on 26 November 2015

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English	Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family.	scientific article published on 26 November 2015

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1 March 2020

Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family (English)

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1 March 2020

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Eric P. Bennett

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1 March 2020

Donald L Jarvis

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1 March 2020

Lawrence A. Tabak

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Lawrence A Tabak

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1 March 2020

Kelley W Moremen

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Kelley W Moremen

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1 March 2020

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Leslie Revoredo

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Shengjun Wang

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1 March 2020

Henrik Clausen

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Kelly G Ten Hagen

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Thomas A Gerken

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26 November 2015

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1 March 2020

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26

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4

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1 March 2020

360-376

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1 March 2020

Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation.

1 reference

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The lectin domain of the polypeptide GalNAc transferase family of glycosyltransferases (ppGalNAc Ts) acts as a switch directing glycopeptide substrate glycosylation in an N- or C-terminal direction, further controlling mucin type O-glycosylation

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Mucin-type O-glycosylation during development

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O-glycosylation modulates integrin and FGF signalling by influencing the secretion of basement membrane components

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Lectin domains of polypeptide GalNAc transferases exhibit glycopeptide binding specificity

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30 September 2017

O-glycosylation modulates proprotein convertase activation of angiopoietin-like protein 3: possible role of polypeptide GalNAc-transferase-2 in regulation of concentrations of plasma lipids

1 reference

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30 September 2017

Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2

1 reference

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Processing of pro-brain natriuretic peptide is suppressed by O-glycosylation in the region close to the cleavage site

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Structural basis for sugar recognition, including the Tn carcinoma antigen, by the lectin SNA-II from Sambucus nigra

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The catalytic and lectin domains of UDP-GalNAc:polypeptide alpha-N-Acetylgalactosaminyltransferase function in concert to direct glycosylation site selection

1 reference

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Prediction of mucin-type O-glycosylation sites in mammalian proteins using the composition of k-spaced amino acid pairs

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Newly identified loci that influence lipid concentrations and risk of coronary artery disease

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The genomic landscapes of human breast and colorectal cancers

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30 September 2017

The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4767052

30 September 2017

Identification of common and unique peptide substrate preferences for the UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases T1 and T2 derived from oriented random peptide substrates

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Mucin-type O-glycans in human colon and breast cancer: glycodynamics and functions

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Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation

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Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2

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1 reference

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The specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase as inferred from a database of in vivo substrates and from the in vitro glycosylation of proteins and peptides

1 reference

https://pubmed.ncbi.nlm.nih.gov/26610890

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Fold recognition and molecular modeling of a lectin-like domain in UDP- GalNac:polypeptide N-acetylgalactosaminyltransferases

1 reference

https://pubmed.ncbi.nlm.nih.gov/26610890

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10)

1 reference

https://pubmed.ncbi.nlm.nih.gov/26610890

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Galnt3 deficiency disrupts acrosome formation and leads to oligoasthenoteratozoospermia

1 reference

https://pubmed.ncbi.nlm.nih.gov/26610890

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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10.1093/GLYCOB/CWV108

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Europe PubMed Central

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1 March 2020

release_yqgpqao2ubdnhlnbo7td7l4dge

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24 November 2022

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1 March 2020

PubMed publication ID

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1 March 2020

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