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James E. Strickler

Researcher at Smith, Kline & French

Publications -  39
Citations -  6130

James E. Strickler is an academic researcher from Smith, Kline & French. The author has contributed to research in topics: Protease & Binding protein. The author has an hindex of 23, co-authored 39 publications receiving 6036 citations. Previous affiliations of James E. Strickler include Albert Einstein College of Medicine & Cetus Corporation.

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A protein kinase involved in the regulation of inflammatory cytokine biosynthesis.

TL;DR: Production of interleukin-1 and tumour necrosis factor from stimulated human monocytes is inhibited by a new series of pyridinyl-imidazole compounds, suggesting that the CSBPs are critical for cytokine production.
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Molecular cloning of the complementary dna for human tumor necrosis factor

TL;DR: Human TNF was purified to apparent homogeneity as a 17.3-kilodalton protein from HL-60 leukemia cells and showed cytotoxic and cytostatic activities against various human tumor cell lines.
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Human immunodeficiency virus protease expressed in Escherichia coli exhibits autoprocessing and specific maturation of the gag precursor

TL;DR: This system will allow detailed structure-function analysis of the HIV protease and provides a simple assay for the development of potential therapeutic agents directed against this critical viral enzyme.
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Inhibition of HIV-1 protease in infected T-lymphocytes by synthetic peptide analogues.

TL;DR: It is demonstrated that synthetic peptide analogues, which are potent inhibitors of purified HIV-1 protease, inhibit the processing of the viral polyproteins in cultures of HIV- 1-infected T lymphocytes and attenuate viral infectivity.
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Inhibition of human immunodeficiency virus 1 protease in vitro: rational design of substrate analogue inhibitors

TL;DR: Inhibitors of the protease from human immunodeficiency virus 1 (HIV-1) were designed, synthesized, and kinetically characterized and effectively blocked the proteolytic processing of a recombinant form of Pr55gag by HIV-1 protease in a cell-free assay.