Lectin domains of polypeptide GalNAc transferases exhibit glycopeptide binding specificity - sprookjes - yvandenbroek - TriplyDB

Lectin domains of polypeptide GalNAc transferases exhibit glycopeptide binding specificity

Lectin domains of polypeptide GalNAc transferases exhibit glycopeptide binding specificity

http://www.wikidata.org/entity/Q28740409

about

The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia type and laterality.Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family Deciphering Structural Elements of Mucin Glycoprotein Recognition Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update for 2011-2012.Probing polypeptide GalNAc-transferase isoform substrate specificities by in vitro analysis A glycogene mutation map for discovery of diseases of glycosylation.The origin and function of platelet glycosyltransferases.Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family.Functional identification of a hydroxyproline-o-galactosyltransferase specific for arabinogalactan protein biosynthesis in Arabidopsis 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 Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus.Initiation of GalNAc-type O-glycosylation in the endoplasmic reticulum promotes cancer cell invasiveness.Novel regulation of Skp1 by the Dictyostelium AgtA α-galactosyltransferase involves the Skp1-binding activity of its WD40 repeat domain Enzymatic glycosylation of multivalent scaffolds.A sensor of protein O-glycosylation based on sequential processing in the Golgi apparatus.Engineering mammalian mucin-type O-glycosylation in plants.Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation.Structure and functional impact of seed region variant in MIR-499 gene family in bronchial asthma Carbohydrate microarrays.The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences.Revisiting the human polypeptide GalNAc-T1 and T13 paralogs.Structural and Mechanistic Insights into the Catalytic-Domain-Mediated Short-Range Glycosylation Preferences of GalNAc-T4

P2860

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P2860

Lectin domains of polypeptide GalNAc transferases exhibit glycopeptide binding specificity

http://www.wikidata.org/entity/Q28740409

description

2011 nî lūn-bûn

@nan

2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Lectin domains of polypeptide ...... ycopeptide binding specificity

@ast

Lectin domains of polypeptide ...... ycopeptide binding specificity

@en

Lectin domains of polypeptide ...... ycopeptide binding specificity

@nl

type

label

Lectin domains of polypeptide ...... ycopeptide binding specificity

@ast

Lectin domains of polypeptide ...... ycopeptide binding specificity

@en

Lectin domains of polypeptide ...... ycopeptide binding specificity

@nl

prefLabel

Lectin domains of polypeptide ...... ycopeptide binding specificity

@ast

Lectin domains of polypeptide ...... ycopeptide binding specificity

@en

Lectin domains of polypeptide ...... ycopeptide binding specificity

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P356

JBC.M111.273722

P1433

Journal of Biological Chemistry

P1476

Lectin domains of polypeptide ...... ycopeptide binding specificity

@en

P2093

Andreas P Holmér

http://www.w3.org/2001/XMLSchema#string

Emiliano Cló

http://www.w3.org/2001/XMLSchema#string

Eric P Bennett

http://www.w3.org/2001/XMLSchema#string

Hans H Wandall

http://www.w3.org/2001/XMLSchema#string

Henrik Clausen

http://www.w3.org/2001/XMLSchema#string

Johannes W Pedersen

http://www.w3.org/2001/XMLSchema#string

Katrine T-B G Schjoldager

http://www.w3.org/2001/XMLSchema#string

Morten Meldal

http://www.w3.org/2001/XMLSchema#string

Ola Blixt

http://www.w3.org/2001/XMLSchema#string

Steven B Levery

http://www.w3.org/2001/XMLSchema#string

P2860

Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2

Identification of molecular intermediates in the assembly pathway of the MUC5AC mucin

Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3

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 T2

Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2

Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation

The catalytic and lectin domains of UDP-GalNAc:polypeptide alpha-N-Acetylgalactosaminyltransferase function in concert to direct glycosylation site selection

Biological, clinical and population relevance of 95 loci for blood lipids

Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding module

Evidence of reciprocal reorientation of the catalytic and hemopexin-like domains of full-length MMP-12

P304

32684-96

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M111.273722

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P407

P433

37

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P478

286

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2011-09-16T00:00:00Z

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21768105

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3173194

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