GPR56 inhibits melanoma growth by internalizing and degrading its ligand TG2. - Wikidata - wikimedia - TriplyDB

GPR56 inhibits melanoma growth by internalizing and degrading its ligand TG2.

GPR56 inhibits melanoma growth by internalizing and degrading its ligand TG2.

http://www.wikidata.org/entity/Q42004258

about

Transglutaminase is a tumor cell and cancer stem cell survival factor International Union of Basic and Clinical Pharmacology. XCIV. Adhesion G protein-coupled receptors Physiological, pathological, and structural implications of non-enzymatic protein-protein interactions of the multifunctional human transglutaminase 2 Adhesion GPCRs in Tumorigenesis.New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors.Hunting for the function of orphan GPCRs - beyond the search for the endogenous ligand.FRIZZLED7 Is Required for Tumor Inititation and Metastatic Growth of Melanoma Cells.Indomethacin induced gene regulation in the rat hippocampus Genome-wide mutation profiles of colorectal tumors and associated liver metastases at the exome and transcriptome levels.Tethered Agonism: A Common Activation Mechanism of Adhesion GPCRs.Contribution of collagen adhesion receptors to tissue fibrosis.7TM Domain Structure of Adhesion GPCRs.Versatile Signaling Activity of Adhesion GPCRs.Structural Basis for Regulation of GPR56/ADGRG1 by Its Alternatively Spliced Extracellular Domains.Stachel-independent modulation of GPR56/ADGRG1 signaling by synthetic ligands directed to its extracellular region.Effect of p53 on pancreatic cancer-glucose tolerance abnormalities by regulating transglutaminase 2 in resistance to glucose metabolic stress.The Adhesion G-Protein-Coupled Receptor, GPR56/ADGRG1, Inhibits Cell-Extracellular Matrix Signaling to Prevent Metastatic Melanoma Growth.The Activation and Signaling Mechanisms of GPR56/ADGRG1 in Melanoma Cell

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GPR56 inhibits melanoma growth by internalizing and degrading its ligand TG2.

http://www.wikidata.org/entity/Q42004258

description

2013 nî lūn-bûn

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2013年の論文

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2013年論文

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2013年論文

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2013年论文

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2013年论文

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2013年论文

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name

GPR56 inhibits melanoma growth by internalizing and degrading its ligand TG2.

@en

GPR56 inhibits melanoma growth by internalizing and degrading its ligand TG2.

@nl

type

label

GPR56 inhibits melanoma growth by internalizing and degrading its ligand TG2.

@en

GPR56 inhibits melanoma growth by internalizing and degrading its ligand TG2.

@nl

prefLabel

GPR56 inhibits melanoma growth by internalizing and degrading its ligand TG2.

@en

GPR56 inhibits melanoma growth by internalizing and degrading its ligand TG2.

@nl

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0008-5472.CAN-13-1268

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Cancer Research

P1476

GPR56 inhibits melanoma growth by internalizing and degrading its ligand TG2.

@en

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Lei Xu

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Liquan Yang

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Nancy Corson

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Scott Friedland

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P2860

GPR56, an atypical G protein-coupled receptor, binds tissue transglutaminase, TG2, and inhibits melanoma tumor growth and metastasis

Disease-associated GPR56 mutations cause bilateral frontoparietal polymicrogyria via multiple mechanisms

GPR56 Regulates VEGF production and angiogenesis during melanoma progression

G protein-coupled receptor-dependent development of human frontal cortex

Matrix crosslinking forces tumor progression by enhancing integrin signaling

Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin

Tensional homeostasis and the malignant phenotype

alpha-Latrotoxin stimulates exocytosis by the interaction with a neuronal G-protein-coupled receptor

Autocatalytic cleavage of the EMR2 receptor occurs at a conserved G protein-coupled receptor proteolytic site motif

A combinatorial extracellular matrix platform identifies cell-extracellular matrix interactions that correlate with metastasis

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1022-1031

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scholarly article

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10.1158/0008-5472.CAN-13-1268

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4

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74

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2013-12-19T00:00:00Z

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