Initiation of GalNAc-type O-glycosylation in the endoplasmic reticulum promotes cancer cell invasiveness. - Wikidata - awgldk - TriplyDB

Initiation of GalNAc-type O-glycosylation in the endoplasmic reticulum promotes cancer cell invasiveness.

Initiation of GalNAc-type O-glycosylation in the endoplasmic reticulum promotes cancer cell invasiveness.

http://www.wikidata.org/entity/Q37117895

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ERK8 is a negative regulator of O-GalNAc glycosylation and cell migration Enzymes for N-Glycan Branching and Their Genetic and Nongenetic Regulation in Cancer A Bitter Sweet Symphony: Immune Responses to Altered O-glycan Epitopes in Cancer MGL Receptor and Immunity: When the Ligand Can Make the Difference Challenges in Antibody Development against Tn and Sialyl-Tn Antigens C1GALT1 overexpression promotes the invasive behavior of colon cancer cells through modifying O-glycosylation of FGFR2.Salivary glycopatterns as potential biomarkers for diagnosis of gastric cancer Mammalian O-mannosylation of cadherins and plexins is independent of protein O-mannosyltransferases 1 and 2.Human Eosinophil Leukocytes Express Protein Disulfide Isomerase in Secretory Granules and Vesicles: Ultrastructural Studies Human germline and pan-cancer variomes and their distinct functional profiles Immature truncated O-glycophenotype of cancer directly induces oncogenic features Development of isoform-specific sensors of polypeptide GalNAc-transferase activity.Global mass spectrometry and transcriptomics array based drug profiling provides novel insight into glucosamine induced endoplasmic reticulum stress Single molecule study of heterotypic interactions between mucins possessing the Tn cancer antigen.The Breast Cancer-Associated Glycoforms of MUC1, MUC1-Tn and sialyl-Tn, Are Expressed in COSMC Wild-Type Cells and Bind the C-Type Lectin MGL.Probing the O-glycoproteome of gastric cancer cell lines for biomarker discovery.Up-regulation of C1GALT1 promotes breast cancer cell growth through MUC1-C signaling pathway The Ubiquitin Ligase CBLC Maintains the Network Organization of the Golgi Apparatus Defective Intestinal Mucin-Type O-Glycosylation Causes Spontaneous Colitis-Associated Cancer in Mice Interactions between the breast cancer-associated MUC1 mucins and C-type lectin characterized by optical tweezers.MGL ligand expression is correlated to BRAF mutation and associated with poor survival of stage III colon cancer patients.Association of the variants and haplotypes in the DOCK7, PCSK9 and GALNT2 genes and the risk of hyperlipidaemia.GalNAc-T14 promotes metastasis through Wnt dependent HOXB9 expression in lung adenocarcinoma GALNT14 promotes lung-specific breast cancer metastasis by modulating self-renewal and interaction with the lung microenvironment Dissecting the molecular basis of the role of the O-mannosylation pathway in disease: α-dystroglycan and forms of muscular dystrophy.N-acetylgalactosaminyltransferases in cancer.O-glycan sialylation alters galectin-3 subcellular localization and decreases chemotherapy sensitivity in gastric cancer.Engineered CAR T Cells Targeting the Cancer-Associated Tn-Glycoform of the Membrane Mucin MUC1 Control Adenocarcinoma Mucin-Type O-Glycosylation in Invertebrates.Inhibition of HIF-1α Affects Autophagy Mediated Glycosylation in Oral Squamous Cell Carcinoma Cells.GalNAc-T4 putatively modulates the estrogen regulatory network through FOXA1 glycosylation in human breast cancer cells.A Synthetic MUC1 Glycopeptide Bearing βGalNAc-Thr as a Tn Antigen Isomer Induces the Production of Antibodies against Tumor Cells.Interactions of mucins with the Tn or Sialyl Tn cancer antigens including MUC1 are due to GalNAc-GalNAc interactions.On-chip lectin microarray for glycoprofiling of different gastritis types and gastric cancer.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.Comment on "The GalNAc-T Activation Pathway (GALA) is not a general mechanism for regulating mucin-type O-glycosylation".Activity Detection of GalNAc Transferases by Protein-Based Fluorescence Sensors In Vivo.Digging deep into Golgi phenotypic diversity with unsupervised machine learning.Over forty years of bladder cancer glycobiology: Where do glycans stand facing precision oncology?

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Initiation of GalNAc-type O-glycosylation in the endoplasmic reticulum promotes cancer cell invasiveness.

http://www.wikidata.org/entity/Q37117895

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 02 August 2013

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Initiation of GalNAc-type O-gl ...... otes cancer cell invasiveness.

@en

Initiation of GalNAc-type O-gl ...... otes cancer cell invasiveness.

@nl

type

label

Initiation of GalNAc-type O-gl ...... otes cancer cell invasiveness.

@en

Initiation of GalNAc-type O-gl ...... otes cancer cell invasiveness.

@nl

prefLabel

Initiation of GalNAc-type O-gl ...... otes cancer cell invasiveness.

@en

Initiation of GalNAc-type O-gl ...... otes cancer cell invasiveness.

@nl

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PNAS.1305269110

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Proceedings of the National Academy of Sciences of the United States of America

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Initiation of GalNAc-type O-gl ...... motes cancer cell invasiveness

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David J Gill

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

Emilie A Bard-Chapeau

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

Frederic A Bard

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

Henrik Clausen

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

Joanne Chia

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

Keit Min Tham

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

Shyi Chyi Wang

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

P2860

Hallmarks of Cancer: The Next Generation

Cloning and expression of human core 1 beta1,3-galactosyltransferase

A unique molecular chaperone Cosmc required for activity of the mammalian core 1 beta 3-galactosyltransferase

Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family

Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus

Lectin domains of polypeptide GalNAc transferases exhibit glycopeptide binding specificity

Role of platelet-derived growth factors in physiology and medicine

Tumor metastasis: molecular insights and evolving paradigms

High density O-glycosylation of the MUC2 tandem repeat unit by N-acetylgalactosaminyltransferase-3 in colonic adenocarcinoma extracts.

The lectin domains of polypeptide GalNAc-transferases exhibit carbohydrate-binding specificity for GalNAc: lectin binding to GalNAc-glycopeptide substrates is required for high density GalNAc-O-glycosylation.

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E3152-61

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scholarly article

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10.1073/PNAS.1305269110

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34

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110

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Catharina Steentoft

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2013-08-02T00:00:00Z

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255177202

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23912186

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endoplasmic reticulum

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3752262

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