Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases. - Wikidata - awgldk - TriplyDB

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.

http://www.wikidata.org/entity/Q27967635

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Abnormal type I collagen post-translational modification and crosslinking in a cyclophilin B KO mouse model of recessive osteogenesis imperfecta The human collagen beta(1-O)galactosyltransferase, GLT25D1, is a soluble endoplasmic reticulum localized protein Collagen beta (1-O) galactosyltransferase 1 (GLT25D1) is required for the secretion of high molecular weight adiponectin and affects lipid accumulation Multifunctional materials for bone cancer treatment.Glycosylation modulates melanoma cell α2β1 and α3β1 integrin interactions with type IV collagen Identification of domains and amino acids essential to the collagen galactosyltransferase activity of GLT25D1.Exposure to mimivirus collagen promotes arthritis.Rab GTPase mediated procollagen trafficking in ascorbic acid stimulated osteoblasts.The activities of lysyl hydroxylase 3 (LH3) regulate the amount and oligomerization status of adiponectin.Molecular Characterization of Collagen Hydroxylysine O-Glycosylation by Mass Spectrometry: Current Status.Lysyl hydroxylase 3 modifies lysine residues to facilitate oligomerization of mannan-binding lectin.Mechano-regulation of collagen biosynthesis in periodontal ligament.Lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture.Protein glycosylation in cancer.Glycosylated synaptomatrix regulation of trans-synaptic signaling.Mimivirus collagen is modified by bifunctional lysyl hydroxylase and glycosyltransferase enzyme.Cyclophilin-B Modulates Collagen Cross-linking by Differentially Affecting Lysine Hydroxylation in the Helical and Telopeptidyl Domains of Tendon Type I Collagen.Lysyl hydroxylase 3-mediated glucosylation in type I collagen: molecular loci and biological significance.Genome-wide association screens for Achilles tendon and ACL tears and tendinopathy.Lysine post-translational modifications of collagen Unusual fragmentation pathways in collagen glycopeptides Vertebrate protein glycosylation: diversity, synthesis and function.Eukaryotic protein glycosylation: a primer for histochemists and cell biologists Matrix metalloproteinase collagenolysis in health and disease.Comprehensive Characterization of Glycosylation and Hydroxylation of Basement Membrane Collagen IV by High-Resolution Mass Spectrometry.Collagen Accumulation in Osteosarcoma Cells lacking GLT25D1 Collagen Galactosyltransferase.Glycosylation Quality Control by the Golgi Structure The lh3 Glycosyltransferase Directs Target-Selective Peripheral Nerve Regeneration.Recombinant expression of hydroxylated human collagen in Escherichia coli.Development of a novel method for analyzing collagen O-glycosylations by hydrazide chemistry.Effects of fish collagen peptides on collagen post-translational modifications and mineralization in an osteoblastic cell culture system.The fibrotic tumor stroma.Optimizing Genomic Methods for Mapping and Identification of Candidate Variants in ENU Mutagenesis Screens Using Inbred Mice.COLGALT1;COLGALT2 bind Lysyl hydroxylated collagen propeptides Galactosylation of collagen propeptide hydroxylysines by procollagen galactosyltransferases 1; 2.COLGALT1;COLGALT2:Galactosyl-hydroxylysyl collagen propeptides dissociates Downregulation of Glt25d1 aggravates carbon tetrachloride‑induced acute hepatic injury through activation of the TGF‑β1/Smad2 signaling pathway

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P2860

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.

http://www.wikidata.org/entity/Q27967635

description

2009 nî lūn-bûn

@nan

2009 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2009年の論文

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2009年論文

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2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.

@ast

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.

@en

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.

@nl

type

label

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.

@ast

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.

@en

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.

@nl

altLabel

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases

@en

prefLabel

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.

@ast

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.

@en

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.

@nl

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Molecular and Cellular Biology

P1476

Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases.

@en

P2093

Andreas J Hülsmeier

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

Belinda Schegg

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

Charlotte Maag

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

Christoph Rutschmann

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

Thierry Hennet

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

P2860

Variants in a novel epidermal collagen gene (COL29A1) are associated with atopic dermatitis

Cerebral cell adhesion molecule: a novel leukocyte adhesion determinant on blood-brain barrier capillary endothelium

Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta

Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes

Human RFT1 deficiency leads to a disorder of N-linked glycosylation

Genome-wide RNAi of C. elegans using the hypersensitive rrf-3 strain reveals novel gene functions

Systematic functional analysis of the Caenorhabditis elegans genome using RNAi

Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity.

The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro.

Cloning of a human UDP-N-acetyl-alpha-D-Galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat

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943-52

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scholarly article

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10.1128/MCB.02085-07

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4

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29

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2009-02-01T00:00:00Z

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19075007

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P932

2643808

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