Journal ArticleDOI
Integrins: a family of cell surface receptors.
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TLDR
This brief review of sequence data from embryogenesis, thrombosis, and lymphocyte help and killing is summarized and attempts to clarify the relationships among the members of this family of cell surface receptors.About:
This article is published in Cell.The article was published on 1987-02-27. It has received 4229 citations till now. The article focuses on the topics: Integrin & Cell adhesion.read more
Citations
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Integrins: versatility, modulation, and signaling in cell adhesion.
Journal ArticleDOI
Integrins: Bidirectional, Allosteric Signaling Machines
TL;DR: Current structural and cell biological data suggest models for how integrins transmit signals between their extracellular ligand binding adhesion sites and their cytoplasmic domains, which link to the cytoskeleton and to signal transduction pathways.
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Adhesion receptors of the immune system.
TL;DR: Three families of cell-surface molecules regulate the migration of lymphocytes and the interactions of activated cells during immune responses.
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New perspectives in cell adhesion : RGD and integrins
TL;DR: Together, the adhesion proteins and their receptors constitute a versatile recognition system providing cells with anchorage, traction for migration, and signals for polarity, position, differentiation, and possibly growth.
Journal ArticleDOI
Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation.
TL;DR: General themes are emerging that yield new strategies for prognosis and therapy of hu- man metastatic cancer, and an imbalanced regulation of motility and proteoly- sis appears to be required for invasion and metastasis.
References
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Journal ArticleDOI
Structure of Integrin, a Glycoprotein Involved in the Transmembrane Linkage between Fibronectin and Actin
John W. Tamkun,Douglas W. DeSimone,Deborah Fonda,Ramila S. Patel,Clayton A. Buck,Alan F. Horwitz,Richard O. Hynes +6 more
TL;DR: The name integrin is proposed for this protein complex to denote its role as an integral membrane complex involved in the transmembrane association between the extracellular matrix and the cytoskeleton.
Journal ArticleDOI
Variants of the cell recognition site of fibronectin that retain attachment-promoting activity
TL;DR: The result presented here show that the arginine, glycine, and aspartic acid residues are absolutely required for the cell recognition, and that the surrounding amino acids may play a role in the expression of cell attachment activity in fibronectin and other proteins having this sequence.
Journal ArticleDOI
The effect of Arg-Gly-Asp-containing peptides on fibrinogen and von Willebrand factor binding to platelets.
Edward F. Plow,Michael D. Pierschbacher,Erkki I. Ruoslahti,Gérard Marguerie,Mark H. Ginsberg +4 more
TL;DR: In this paper, the effects of Arg-Gly-Asp-containing peptides on the interaction of these latter two adhesive proteins with platelets were examined, and it was shown that the peptide was 1/2 to 1/3rd as potent in inhibiting fibrinogen as fibronectin binding to platelets.
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The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins.
Jack Lawler,Richard O. Hynes +1 more
TL;DR: Two monoclonal antibodies are used to isolate cDNA clones of thrombospondin from a human endothelial cell cDNA library and the complete nucleotide sequence of the coding region is determined.
Journal ArticleDOI
Cloning of the beta subunit of the leukocyte adhesion proteins: homology to an extracellular matrix receptor defines a novel supergene family.
TL;DR: The deduced 769-amino-acid sequence defines a cysteine-rich polypeptide with the characteristic features of an integral membrane protein that defines a new supergene family of cellular adhesion proteins.