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Daniel A. Lawrence

Researcher at University of Michigan

Publications -  201
Citations -  13506

Daniel A. Lawrence is an academic researcher from University of Michigan. The author has contributed to research in topics: Plasminogen activator & Plasminogen activator inhibitor-1. The author has an hindex of 63, co-authored 187 publications receiving 12696 citations. Previous affiliations of Daniel A. Lawrence include Scripps Health & University of Maryland, Baltimore.

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The serpin PAI-1 inhibits cell migration by blocking integrin alpha V beta 3 binding to vitronectin.

TL;DR: It is reported that vitronectin significantly enhances the migration of smooth muscle cells (SMCs), and that the specific VNR αvβ3 is required for cell motility, and that PAI-1 can control cell–matrix interactions by regulating the accessibility of specific cell-attachment sites.
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Tissue-type plasminogen activator induces opening of the blood-brain barrier via the LDL receptor-related protein.

TL;DR: It is demonstrated that tPA is both necessary and sufficient to directly increase vascular permeability in the early stages of BBB opening, and suggested that this occurs through a receptor-mediated cell signaling event and not through generalized degradation of the vascular basement membrane.
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Purification of an inhibitor of plasminogen activator (antiactivator) synthesized by endothelial cells.

TL;DR: Results indicate that cultured bovine aortic endothelial cells synthesize and secrete a protein which inhibits plasminogen activators and is distinct from protease nexin, a major endothelial cell product, and, as such, probably plays an important role in regulating the fibrinolytic system of these cells.
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Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor.

TL;DR: A lambda gt11 expression library containing cDNA inserts prepared from human placental mRNA was screened immunologically using an antibody probe developed against the beta-migrating plasminogen activator inhibitor (beta-PAI) purified from cultured bovine aortic endothelial cells, indicating that the beta -PAI is a member of the serine proteinase inhibitor (serpin) superfamily.