Lawrence A. Tabak
Affiliations: | University of Rochester, Rochester, NY |
Area:
Biochemistry, Molecular BiologyGoogle:
"Lawrence Tabak"Mean distance: (not calculated yet)
BETA: Related publications
See more...
Publications
|
You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect. |
| May C, Ji S, Syed ZA, et al. (2020) Differential splicing of the lectin domain of an O-glycosyltransferase modulates both peptide and glycopeptide preferences. The Journal of Biological Chemistry |
| Fernandez AJ, Daniel EJP, Mahajan SP, et al. (2019) The structure of the colorectal cancer-associated enzyme GalNAc-T12 reveals how nonconserved residues dictate its function. Proceedings of the National Academy of Sciences of the United States of America |
| Ji S, Samara NL, Revoredo L, et al. (2018) A molecular switch orchestrates enzyme specificity and secretory granule morphology. Nature Communications. 9: 3508 |
| Becker JL, Tran DT, Tabak LA. (2018) Members of the GalNAc-T family of enzymes utilize distinct Golgi localization mechanisms. Glycobiology |
| Herbomel GG, Rojas RE, Tran DT, et al. (2017) The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation. Plos One. 12: e0179241 |
| Famiglietti AL, Wei Z, Beres TM, et al. (2017) Characterization and expression analysis of Galnts in developing Strongylocentrotus purpuratus embryos. Plos One. 12: e0176479 |
| Revoredo L, Wang S, Bennett EP, et al. (2015) Mucin Type O-Glycosylation is Controlled by Short and Long Range Glycopeptide Substrate Recognition that Varies Among Members of the Polypeptide GalNAc Transferase (ppGalNAc-T) Family. Glycobiology |
| Gómez H, Rojas R, Patel D, et al. (2014) A computational and experimental study of O-glycosylation. Catalysis by human UDP-GalNAc polypeptide:GalNAc transferase-T2. Organic & Biomolecular Chemistry. 12: 2645-55 |
| Gerken TA, Revoredo L, Thome JJ, et al. (2013) 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. The Journal of Biological Chemistry. 288: 19900-14 |
| Raman J, Guan Y, Perrine CL, et al. (2012) UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases: completion of the family tree. Glycobiology. 22: 768-77 |