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John H. Griffin

Researcher at Scripps Research Institute

Publications -  566
Citations -  31390

John H. Griffin is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Protein C & Thrombin. The author has an hindex of 90, co-authored 551 publications receiving 29967 citations. Previous affiliations of John H. Griffin include United States Department of Veterans Affairs & University of Maryland, Baltimore.

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Deficiency of protein C in congenital thrombotic disease.

TL;DR: It is suggested that the recurrent thrombotic disease in this family is due to an inherited deficiency in protein C, a potent in vitro anticoagulant enzyme and an in vivo profibrinolytic agent.
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The cytoprotective protein C pathway.

TL;DR: This review summarizes insights gleaned from recent in vitro and in vivo studies of the direct cytoprotective effects of APC that include beneficial alterations in gene expression profiles, anti-inflammatory actions, antiapoptotic activities, and stabilization of endothelial barriers that suggest the possibility of developing APC variants with an improved profile for the ratio of cy toprotective to anticoagulant actions.
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Protein synthesis by native chemical ligation: Expanded scope by using straightforward methodology

TL;DR: A straightforward methodology that has enabled us to rapidly analyze the compatibility of the native chemical ligation strategy for X-Cys ligation sites, where X is any of the 20 naturally occurring amino acids, and shows that all 20 amino acids are suitable for ligation.
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Endothelial and Antithrombotic Actions of HDL

TL;DR: There is evidence of a variety of mechanisms by which HDL is antithrombotic and thereby protective against arterial and venous thrombosis, including through the activation of prostacyclin synthesis.
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Activated protein C blocks p53-mediated apoptosis in ischemic human brain endothelium and is neuroprotective.

TL;DR: It is reported that APC directly prevents apoptosis in hypoxic human brain endothelium through transcriptionally dependent inhibition of tumor suppressor protein p53, normalization of the pro-apoptotic Bax/Bcl-2 ratio and reduction of caspase-3 signaling.