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Thomas A. Gerken
Researcher at Case Western Reserve University
Publications - 81
Citations - 4031
Thomas A. Gerken is an academic researcher from Case Western Reserve University. The author has contributed to research in topics: Glycosylation & Mucin. The author has an hindex of 35, co-authored 80 publications receiving 3647 citations. Previous affiliations of Thomas A. Gerken include University Hospitals of Cleveland & University of Akron.
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Journal ArticleDOI
Control of mucin-type O-glycosylation: A classification of the polypeptide GalNAc-transferase gene family
Eric P. Bennett,Ulla Mandel,Henrik Clausen,Thomas A. Gerken,Timothy A. Fritz,Lawrence A. Tabak +5 more
TL;DR: An overview of the GalNAc-T gene family in animals is presented and a classification of the genes into subfamilies, which appear to be conserved in evolution structurally as well as functionally are proposed.
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Role of glycosylation on the conformation and chain dimensions of O-linked glycoproteins: light-scattering studies of ovine submaxillary mucin
TL;DR: Results indicate that steric interactions of the O-linked GalNAc residue with the peptide core are primarily responsible for the expanded mucin structure and that these perturbations extend to the nonglycosylated amino acid residues.
Journal ArticleDOI
Emerging Paradigms for the Initiation of Mucin-type Protein O-Glycosylation by the Polypeptide GalNAc Transferase Family of Glycosyltransferases *
Thomas A. Gerken,Oliver Jamison,Cynthia L. Perrine,Jeremy C. Collette,Helen Moinova,Lakshmeswari Ravi,Sanford D. Markowitz,Wei Shen,Himatkumar V Patel,Lawrence A. Tabak +9 more
TL;DR: It is concluded that each ppGalNAc T isoform may be uniquely sensitive to peptide sequence and overall charge, which together dictates the substrate sites that will be glycosylated.
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Effects of glycosylation on the conformation and dynamics of O-linked glycoproteins: carbon-13 NMR studies of ovine submaxillary mucin
TL;DR: The absence of chemical shift heterogeneity in apo mucin is taken to indicate a loss in the peptide-carbohydrate steric interactions, consistent with a more relaxed random coiled structure.
Journal ArticleDOI
Inactivating germ-line and somatic mutations in polypeptide N-acetylgalactosaminyltransferase 12 in human colon cancers
Kishore Guda,Helen Moinova,Jian He,Oliver Jamison,Lakshmeswari Ravi,Leanna Natale,James Lutterbaugh,Earl Lawrence,Susan Lewis,James K V Willson,John B. Lowe,Georgia L. Wiesner,Giovanni Parmigiani,Jill S. Barnholtz-Sloan,Dawn M. Dawson,Victor E. Velculescu,Kenneth W. Kinzler,Nikolas Papadopoulos,Bert Vogelstein,Joseph Willis,Thomas A. Gerken,Sanford D. Markowitz +21 more
TL;DR: Finding somatic and germ-line mutations in the gene encoding for polypeptide N-acetylgalactosaminyltransferase 12 in individuals with colon cancer suggest genetic defects in the O-glycosylation pathway in part underlie aberrant glycosylations in colon cancers, and they contribute to the development of a subset of these malignancies.