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David E. Birk

Researcher at University of South Florida

Publications -  203
Citations -  16972

David E. Birk is an academic researcher from University of South Florida. The author has contributed to research in topics: Fibrillogenesis & Extracellular matrix. The author has an hindex of 68, co-authored 198 publications receiving 15251 citations. Previous affiliations of David E. Birk include Thomas Jefferson University & University of Medicine and Dentistry of New Jersey.

Papers
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Journal ArticleDOI

Altered wound healing in mice lacking a functional osteopontin gene (spp1).

TL;DR: Data indicate a role for OPN in tissue remodeling in vivo, and suggest physiological functions during matrix reorganization after injury, which are suggested by ultrastructural analysis.
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Collagen fibrillogenesis in vitro: interaction of types I and V collagen regulates fibril diameter.

TL;DR: Electron microscopy using collagen type-specific monoclonal antibodies demonstrated that the fibrils formed were heterotypic, containing both collagen types I and V, indicating that the interaction of type V with type I collagen is at least partially responsible for the regulation of collagen fibril formation.
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Type V Collagen Controls the Initiation of Collagen Fibril Assembly

TL;DR: A central role for the evolutionary, ancient type V collagen in the regulation of fibrillogenesis and matrix assembly is defined, indicative of the critical role of the latter in early fibril initiation in mouse embryos completely deficient in pro-α1(V) chains.
Patent

Biodegradable matrix and methods for producing same

TL;DR: In this paper, a carrier compound is incorporated during processing to form a collagen-based matrix in sponge or sheet form impregnated with the carrier compound, which is selected from the group consisting of types IV and V collagen, fibronecting, laminin, hyaluronate, proteoglycan, epidermal growth factor, platelet derived growth factor and angiogenesis factor.
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The molecular basis of corneal transparency

TL;DR: The growth factor mediated synthesis ofSeveral different collagen types and the core proteins of several different leucine-rich type proteoglycans are required to produce collagen fibrils with the size and spacing needed for corneal stromal transparency.