The structure of the colorectal cancer-associated enzyme GalNAc-T12 reveals how nonconserved residue...
The structure of the colorectal cancer-associated enzyme GalNAc-T12 reveals how nonconserved residues dictate its function
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Publisher
United States: National Academy of Sciences
Journal title
Language
English
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Publisher
United States: National Academy of Sciences
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Scope and Contents
Contents
Polypeptide N-acetylgalactosaminyl transferases (GalNAc-Ts) initiate mucin type O-glycosylation by catalyzing the transfer of N-acetylgalactosamine (GalNAc) to Ser or Thr on a protein substrate. Inactive and partially active variants of the isoenzyme GalNAc-T12 are present in subsets of patients with colorectal cancer, and several of these variants...
Alternative Titles
Full title
The structure of the colorectal cancer-associated enzyme GalNAc-T12 reveals how nonconserved residues dictate its function
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Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6789641
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6789641
Other Identifiers
ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.1902211116
