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William F. Bennett

Researcher at Genentech

Publications -  42
Citations -  2245

William F. Bennett is an academic researcher from Genentech. The author has contributed to research in topics: Tissue plasminogen activator & Plasminogen activator. The author has an hindex of 15, co-authored 42 publications receiving 2224 citations.

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Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli

TL;DR: Bacterial clones containing human tissue-type plasminogen activator cDNA sequences were identified in a cDNA library prepared using gel-fractionated mRNA from human melanoma cells and a polypeptide was produced having the fibrinolytic properties characteristic of authentic human t-PA.
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High resolution analysis of functional determinants on human tissue-type plasminogen activator

TL;DR: Variants of tPA were found that had reduced activity with respect to each tested property; in a few cases increased activity was observed, and a model of the tPA protease domain has been used to map some of the critical residues and regions.
Journal Article

Biological properties of human tissue-type plasminogen activator obtained by expression of recombinant DNA in mammalian cells.

TL;DR: It is concluded that the potentially more readily available rt-PA could constitute a specific, fibrin-selective thrombolytic agent.
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A long-half-life and fibrin-specific form of tissue plasminogen activator in rabbit models of embolic stroke and peripheral bleeding.

TL;DR: Findings show that by combining increased fibrin specificity with decreased plasma clearance, it is possible to produce a thrombolytic agent that is more convenient and more potent than wild-type TPA.
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Identification of carbohydrate structures in glycoprotein peptide maps by the use of LC/MS with selected ion extraction with special reference to tissue plasminogen activator and a glycosylation variant produced by site directed mutagenesis

TL;DR: Electrospray ionization mass spectrometry utilizing a single quadrupole on line with reversed-phase HPLC (LC/MS) enables the characterization of glycoproteins in a relatively short period of time.