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Negative regulation of transforming growth factor-beta by the proteoglycan decorin

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Negative regulation of transforming growth factor-beta by the proteoglycan decorin (English)

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author name string

Y Yamaguchi

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1

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D M Mann

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E Ruoslahti

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3

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English

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publication date

19 July 1990

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published in

Nature

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volume

346

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page(s)

281-4

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issue

6281

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cites work

Expression of human proteoglycan in Chinese hamster ovary cells inhibits cell proliferation

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Structure and biology of proteoglycans

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Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA

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Detecting homology of distantly related proteins with consensus sequences.

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Complete amino acid sequence of human hemopexin, the heme-binding protein of serum

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The Toll gene of Drosophila, required for dorsal-ventral embryonic polarity, appears to encode a transmembrane protein

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Chaoptin, a cell surface glycoprotein required for Drosophila photoreceptor cell morphogenesis, contains a repeat motif found in yeast and human.

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Transforming growth factors and control of neoplastic cell growth

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Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta

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Immunocytochemical investigation on the distribution of small chondroitin sulfate-dermatan sulfate proteoglycan in the human.

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The transforming growth factor-beta system, a complex pattern of cross-reactive ligands and receptors

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HIV infection is blocked in vitro by recombinant soluble CD4.

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LIGAND: A versatile computerized approach for characterization of ligand-binding systems

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Structural analysis of chick-embryo cartilage proteoglycan by selective degradation with chondroitin lyases (chondroitinases) and endo-beta-D-galactosidase (keratanase)

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(Q28292224)

Negative regulation of transforming growth factor-beta by the proteoglycan decorin

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