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
about
Characterization and expression analysis of Galnts in developing Strongylocentrotus purpuratus embryos.The genetics and immunobiology of IgA nephropathy.Development of isoform-specific sensors of polypeptide GalNAc-transferase activity.Probing polypeptide GalNAc-transferase isoform substrate specificities by in vitro analysisO-linked glycosylation of the mucin domain of the herpes simplex virus type 1-specific glycoprotein gC-1 is temporally regulated in a seed-and-spread mannerMucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family.Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiaeMaking Home Sweet and Sturdy: Toxoplasma gondii ppGalNAc-Ts Glycosylate in Hierarchical Order and Confer Cyst Wall Rigidity.N-acetylgalactosaminyltransferases in cancer.The Distribution of Lectins across the Phylum Nematoda: A Genome-Wide Search.Eukaryotic protein glycosylation: a primer for histochemists and cell biologistsNanotechnologies in glycoproteomics.Convergent and divergent mechanisms of sugar recognition across kingdoms.Insights into the Evolution of Hydroxyproline-Rich Glycoproteins from 1000 Plant Transcriptomes.Differential protein modulation by ketoprofen and ibuprofen underlines different cellular response by gastric epithelium.Loss of N-Acetylgalactosaminyltransferase-4 Orchestrates Oncogenic MicroRNA-9 in Hepatocellular Carcinoma.Polypeptide N-Acetylgalactosaminyltransferase 13 Contributes to Neurogenesis via Stabilizing the Mucin-type O-Glycoprotein Podoplanin.Galectin-9 binds to O-glycans on protein disulfide isomerase.Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation.The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation.Biological and biochemical properties of two Xenopus laevis N-acetylgalactosaminyltransferases with contrasting roles in embryogenesis.UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyl-transferase from the snail Biomphalaria glabrata - substrate specificity and preference of glycosylation sites.The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences.Revisiting the human polypeptide GalNAc-T1 and T13 paralogs.Expression system for structural and functional studies of human glycosylation enzymes.Hydrazide-functionalized affinity on conventional support materials for glycopeptide enrichment.Structural and Mechanistic Insights into the Catalytic-Domain-Mediated Short-Range Glycosylation Preferences of GalNAc-T4A molecular switch orchestrates enzyme specificity and secretory granule morphologyThe Interaction of the Gut Microbiota with the Mucus Barrier in Health and Disease in Human
P2860
Q33610666-6F08E200-062D-4C5A-A459-556B75FA16C1Q33872517-C6F98228-95A0-426B-8A37-01D91DD759A4Q34431015-3C061570-FE6E-4BA9-82A1-2269EA494C09Q34579581-06F4D3B8-5EE6-40BA-822A-3040FA564B08Q35104007-FCE7448C-1148-4D50-A437-405F791F9E61Q36617733-6504E9A2-6BB2-4797-9E13-E33A429DD0E9Q36778284-20CDCCA8-9D96-4C11-B48B-4B8D15D492F0Q37578540-505FD7A3-7D42-40D5-8CB7-7C5B6B30F07CQ37619873-7DFC6AA3-5990-415E-8878-A8F98BB47CCEQ37631520-97A680D6-E19B-4582-9E0B-F9E5C5130B7CQ37639440-18375B05-AD06-4FC7-ACFB-D5106B89C5A0Q38221130-EEC1F47D-F0BD-4C87-9FFF-671E4957554DQ38237844-FA14867E-469A-487A-A76C-134BAECD4E02Q38370602-7A72030E-480C-40DD-BAC4-0F60A9974CA7Q38677846-F0DB195C-E6AD-4457-9645-B62FE486C178Q38722581-8CB95C15-887F-4458-B12A-6F261DBA222CQ38746279-86B66E2D-E73D-474D-AF97-4639E3CE4980Q40082362-4838C2D2-D13B-4BD2-83BB-3A1A982FB028Q40692511-EE8120C0-92A7-4F31-A0BA-F82078B27B88Q41047615-2DCF48B6-2461-48CE-8668-0CCFFD95E8A5Q41758636-F83DB9D9-C1E1-4263-8C74-DFB9F321E5BAQ42001083-68735FF8-1B32-45E7-94B0-B1518A895A61Q47116819-CFFBDCE4-1C3B-469B-B8FD-C72521780C78Q47131748-3387AABB-FCD3-4ACA-90BF-F7151026B545Q47281956-B54263CC-F16B-45BF-983F-0F880677C362Q52786842-99149E9B-0C29-45E9-AB84-A0413B7BDE0BQ57068905-975800AF-7695-4700-ADE2-AE7A5B1FDDD2Q58695574-91DCAE6F-26BD-4703-B5AE-C7A6D6ABE644Q58802621-C28305B0-31FA-4C03-82A1-CDEA273D5A57
P2860
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
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 20 May 2013
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The lectin domain of the polyp ...... ing mucin type O-glycosylation
@en
The lectin domain of the polyp ...... ng mucin type O-glycosylation.
@nl
type
label
The lectin domain of the polyp ...... ing mucin type O-glycosylation
@en
The lectin domain of the polyp ...... ng mucin type O-glycosylation.
@nl
prefLabel
The lectin domain of the polyp ...... ing mucin type O-glycosylation
@en
The lectin domain of the polyp ...... ng mucin type O-glycosylation.
@nl
P2093
P2860
P356
P1476
The lectin domain of the polyp ...... ing mucin type O-glycosylation
@en
P2093
Donald L Jarvis
Gagandeep K Gahlay
Heather A Moniz
Henrik Clausen
Joseph J C Thome
Kelley Moremen
Lawrence A Tabak
Leslie Revoredo
Malene Bech Vester-Christensen
Roy W Johnson
P2860
P304
19900-19914
P356
10.1074/JBC.M113.477877
P407
P577
2013-05-20T00:00:00Z