Identification of a novel heparin-binding site in the alternatively spliced IIICS region of fibronectin: roles of integrins and proteoglycans in cell adhesion to fibronectin splice variants (Q43540787)

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scientific article published in February 2001

Language	Label	Description	Also known as
English	Identification of a novel heparin-binding site in the alternatively spliced IIICS region of fibronectin: roles of integrins and proteoglycans in cell adhesion to fibronectin splice variants	scientific article published in February 2001

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

Identification of a novel heparin-binding site in the alternatively spliced IIICS region of fibronectin: roles of integrins and proteoglycans in cell adhesion to fibronectin splice variants (English)

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Europe PubMed Central

PubMed publication ID

24 November 2017

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based on heuristic

inferred from title

Martin J. Humphries

4

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Europe PubMed Central

PubMed publication ID

24 November 2017

author name string

Mostafavi-Pour Z

1

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Europe PubMed Central

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24 November 2017

Askari JA

2

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Europe PubMed Central

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24 November 2017

Whittard JD

3

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Europe PubMed Central

PubMed publication ID

24 November 2017

language of work or name

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inferred from title

publication date

1 February 2001

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Europe PubMed Central

PubMed publication ID

24 November 2017

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Europe PubMed Central

PubMed publication ID

24 November 2017

20

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Europe PubMed Central

PubMed publication ID

24 November 2017

1

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24 November 2017

63-73

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Europe PubMed Central

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24 November 2017

Evidence that binding to the carboxyl-terminal heparin-binding domain (Hep II) dominates the interaction between plasma fibronectin and heparin

1 reference

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Heparin Binding by Fibronectin Module III-13 Involves Six Discontinuous Basic Residues Brought Together to Form a Cationic Cradle

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Expression and functional significance of alternatively spliced CS1 fibronectin in rheumatoid arthritis microvasculature

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Rationale and methods for the use of nude mice to study the biology and therapy of human cancer metastasis

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The extended family of proteoglycans: social residents of the pericellular zone

1 reference

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Lymphoid cells recognize an alternatively spliced segment of fibronectin via the integrin receptor alpha 4 beta 1.

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Endothelial cell interactions with synthetic peptides from the carboxyl-terminal heparin-binding domains of fibronectin

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Identification of an alternatively spliced site in human plasma fibronectin that mediates cell type-specific adhesion

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Role of fibronectin in adhesion, migration, and metastasis

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Coordinate role for cell surface chondroitin sulfate proteoglycan and alpha 4 beta 1 integrin in mediating melanoma cell adhesion to fibronectin

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Interaction of heparin with fibronectin and isolated fibronectin domains

1 reference

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Binding of heparin by type III domains and peptides from the carboxy terminal hep-2 region of fibronectin

1 reference

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An unusual heparin-binding peptide from the carboxy-terminal hep-2 region of fibronectin

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Rapid and efficient site-specific mutagenesis without phenotypic selection

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Localization and chemical synthesis of fibronectin peptides with melanoma adhesion and heparin binding activities

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Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C

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Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule

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Syndecan-regulated receptor signaling

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Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis

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Isolation and chemical characterization of a melanoma-associated proteoglycan antigen

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Crystal structure of a heparin- and integrin-binding segment of human fibronectin.

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Identification and characterization of the T lymphocyte adhesion receptor for an alternative cell attachment domain (CS-1) in plasma fibronectin

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Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta

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Identifiers

10.1016/S0945-053X(00)00131-1

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

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