The face of TSR revealed: an extracellular signaling domain is exposed - Wikidata - awgldk - TriplyDB

The face of TSR revealed: an extracellular signaling domain is exposed

The face of TSR revealed: an extracellular signaling domain is exposed

http://www.wikidata.org/entity/Q34982166

about

A thrombospondin structural repeat containing rhoptry protein from Plasmodium falciparum mediates erythrocyte invasion Thrombospondin-1-N-terminal domain induces a phagocytic state and thrombospondin-1-C-terminal domain induces a tolerizing phenotype in dendritic cells A diverse host thrombospondin-type-1 repeat protein repertoire promotes symbiont colonization during establishment of cnidarian-dinoflagellate symbiosis.Effects of ADAMTS14 genetic polymorphism and cigarette smoking on the clinicopathologic development of hepatocellular carcinoma.Thrombospondin 1 is an autocrine negative regulator of human dendritic cell activation The thrombospondin-1 receptor CD36 is an important mediator of ovarian angiogenesis and folliculogenesis.A binding site for highly sulfated heparan sulfate is identified in the N terminus of the circumsporozoite protein: significance for malarial sporozoite attachment to hepatocytes.Thrombospondin-1-deficient mice are not protected from bleomycin-induced pulmonary fibrosis Chemical synthesis and biotinylation of the thrombospondin domain TSR2.Localization of thrombospondin-1 and its receptor CD36 in the ovary of the ostrich (Struthio camelus).

P2860

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P2860

The face of TSR revealed: an extracellular signaling domain is exposed

http://www.wikidata.org/entity/Q34982166

description

2002 nî lūn-bûn

@nan

2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

The face of TSR revealed: an extracellular signaling domain is exposed

@ast

The face of TSR revealed: an extracellular signaling domain is exposed

@en

The face of TSR revealed: an extracellular signaling domain is exposed

@nl

type

label

The face of TSR revealed: an extracellular signaling domain is exposed

@ast

The face of TSR revealed: an extracellular signaling domain is exposed

@en

The face of TSR revealed: an extracellular signaling domain is exposed

@nl

prefLabel

The face of TSR revealed: an extracellular signaling domain is exposed

@ast

The face of TSR revealed: an extracellular signaling domain is exposed

@en

The face of TSR revealed: an extracellular signaling domain is exposed

@nl

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P1433

Journal of Cell Biology

P1476

The face of TSR revealed: an extracellular signaling domain is exposed

@en

P2093

Roy L Silverstein

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

P2860

Isolation of the thrombospondin membrane receptor

Diversity of function is inherent in matricellular proteins: an appraisal of thrombospondin 1

Peptides derived from two separate domains of the matrix protein thrombospondin-1 have anti-angiogenic activity

Crystal structure of the TSP-1 type 1 repeats

Lysosomal integral membrane protein II binds thrombospondin-1. Structure-function homology with the cell adhesion molecule CD36 defines a conserved recognition motif

The thrombospondin type 1 repeat (TSR) superfamily: diverse proteins with related roles in neuronal development.

The cell biology of thrombospondin-1.

The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins.

CD36 mediates the In vitro inhibitory effects of thrombospondin-1 on endothelial cells

Thrombospondin-1 is required for normal murine pulmonary homeostasis and its absence causes pneumonia.

P304

203-206

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scholarly article

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10.1083/JCB.200209138

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P433

2

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159

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2002-10-28T00:00:00Z

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11059870

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12403807

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P921

membrane proteins

P932

2173053

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