Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

A Gerken

Showing results (101-110 of 119) with videos related to

Pageof 12
Sort By:
The Journal of Biological Chemistry|May 23, 2009
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 T2Cynthia L Perrine, Anjali Ganguli, Peng Wu, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 25, 2019
The structure of the colorectal cancer-associated enzyme GalNAc-T12 reveals how nonconserved residues dictate its functionAmy J Fernandez, Earnest James Paul Daniel, Sai Pooja Mahajan, et al.
Psychoneuroendocrinology|January 1, 1984
ACTH and multisteroid responses to corticotropin-releasing factor in depressive illness: relationship to multisteroid responses after ACTH stimulation and dexamethasone suppressionF Holsboer, O A Müller, H G Doerr, et al.
Scientific Reports|March 24, 2016
Biochemical and functional characterization of glycosylation-associated mutational landscapes in colon cancerSrividya Venkitachalam, Leslie Revoredo, Vinay Varadan, et al.
The Journal of Biological Chemistry|February 26, 2011
Emerging paradigms for the initiation of mucin-type protein O-glycosylation by the polypeptide GalNAc transferase family of glycosyltransferasesThomas A Gerken, Oliver Jamison, Cynthia L Perrine, et al.
Glycobiology|November 28, 2015
Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase familyLeslie Revoredo, Shengjun Wang, Eric Paul Bennett, et al.
The Journal of Biological Chemistry|July 17, 2020
Differential splicing of the lectin domain of an <i>O</i>-glycosyltransferase modulates both peptide and glycopeptide preferencesCarolyn May, Suena Ji, Zulfeqhar A Syed, et al.
Glycobiology|March 10, 2025
Charge matters: how flanking substrate charge modulates O-glycan Core elongationCollin J Ballard, Matthew R Smutny, Lam D Chau, et al.
The Journal of Biological Chemistry|May 22, 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-glycosylationThomas A Gerken, Leslie Revoredo, Joseph J C Thome, et al.
Human Mutation|May 12, 2018
Evidence for GALNT12 as a moderate penetrance gene for colorectal cancerDaniel R Evans, Srividya Venkitachalam, Leslie Revoredo, et al.
Pageof 12

Showing results (101-110 of 119) with videos related to

Sort By:
Pageof 12
The Journal of Biological Chemistry|May 23, 2009
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 T2Cynthia L Perrine, Anjali Ganguli, Peng Wu, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 25, 2019
The structure of the colorectal cancer-associated enzyme GalNAc-T12 reveals how nonconserved residues dictate its functionAmy J Fernandez, Earnest James Paul Daniel, Sai Pooja Mahajan, et al.
Psychoneuroendocrinology|January 1, 1984
ACTH and multisteroid responses to corticotropin-releasing factor in depressive illness: relationship to multisteroid responses after ACTH stimulation and dexamethasone suppressionF Holsboer, O A Müller, H G Doerr, et al.
Scientific Reports|March 24, 2016
Biochemical and functional characterization of glycosylation-associated mutational landscapes in colon cancerSrividya Venkitachalam, Leslie Revoredo, Vinay Varadan, et al.
The Journal of Biological Chemistry|February 26, 2011
Emerging paradigms for the initiation of mucin-type protein O-glycosylation by the polypeptide GalNAc transferase family of glycosyltransferasesThomas A Gerken, Oliver Jamison, Cynthia L Perrine, et al.
Glycobiology|November 28, 2015
Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase familyLeslie Revoredo, Shengjun Wang, Eric Paul Bennett, et al.
The Journal of Biological Chemistry|July 17, 2020
Differential splicing of the lectin domain of an <i>O</i>-glycosyltransferase modulates both peptide and glycopeptide preferencesCarolyn May, Suena Ji, Zulfeqhar A Syed, et al.
Glycobiology|March 10, 2025
Charge matters: how flanking substrate charge modulates O-glycan Core elongationCollin J Ballard, Matthew R Smutny, Lam D Chau, et al.
The Journal of Biological Chemistry|May 22, 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-glycosylationThomas A Gerken, Leslie Revoredo, Joseph J C Thome, et al.
Human Mutation|May 12, 2018
Evidence for GALNT12 as a moderate penetrance gene for colorectal cancerDaniel R Evans, Srividya Venkitachalam, Leslie Revoredo, et al.
Pageof 12