Binding of the NG2 proteoglycan to kringle domains modulates the functional properties of angiostatin and plasmin(ogen). (Q41746287)

8 October 2017

Binding of the NG2 proteoglycan to kringle domains modulates the functional properties of angiostatin and plasmin(ogen). (English)

1 reference

8 October 2017

Goretzki L

1

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8 October 2017

Lombardo CR

series ordinal

2

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8 October 2017

Stallcup WB

series ordinal

3

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8 October 2017

language of work or name

English

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publication date

1 September 2000

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Journal of Biological Chemistry

8 October 2017

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8 October 2017

275

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8 October 2017

37

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8 October 2017

28625-28633

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Expression of NG2 proteoglycan causes retention of type VI collagen on the cell surface

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Binding of the NG2 proteoglycan to type VI collagen and other extracellular matrix molecules

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The membrane-spanning proteoglycan NG2 binds to collagens V and VI through the central nonglobular domain of its core protein

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Generation of truncated forms of the NG2 proteoglycan by cell surface proteolysis

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The tumor-suppressing activity of angiostatin protein resides within kringles 1 to 3

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Identifiers

DOI

10.1074/JBC.M002290200

1 reference

8 October 2017

1 reference