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Clayton A. Buck
Researcher at Wistar Institute
Publications - 89
Citations - 15388
Clayton A. Buck is an academic researcher from Wistar Institute. The author has contributed to research in topics: Integrin & Cell adhesion molecule. The author has an hindex of 52, co-authored 89 publications receiving 15213 citations. Previous affiliations of Clayton A. Buck include Indiana University & Thomas Jefferson University.
Papers
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Journal ArticleDOI
Integrins and other cell adhesion molecules.
TL;DR: Recent data describing the structure and function of some of these cell adhesion molecules are summarized and the possible role of these molecules in development, inflammation, wound healing, coagulation, and tumor metastasis is discussed.
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Interaction of plasma membrane fibronectin receptor with talin—a transmembrane linkage
TL;DR: The interaction of the purified CSAT antigen with these cytoskeletal components is investigated, and an interaction specifically between theCSAT antigen and talin is demonstrated.
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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 Article
Integrin distribution in malignant melanoma: association of the beta 3 subunit with tumor progression
Steven M. Albelda,Stephen A. Mette,David E. Elder,Rosemary Stewart,László Damjanovich,Meenhard Herlyn,Clayton A. Buck +6 more
TL;DR: The distribution of integrin adhesion receptors was examined in benign and malignant lesions of human melanocytes and in tissue sections from benign to increasingly malignant melanocytic lesions using a panel of monoclonal antibodies against specific integrin subunits to examine the presence of this integrin.
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Cell surface receptors for extracellular matrix molecules
Clayton A. Buck,Alan F. Horwitz +1 more
TL;DR: Avian integrin shows little specificity and appears to behave as a multifunctional, promiscuous receptor for extracellular matrix molecules, and post-translational modifications provide yet another mechanism for regulating integrin-ligand binding.