Zachary Herrera
Stanford University
5 Papers
Zachary Herrera is an academic researcher from Stanford University. The author has contributed to research in topics: Small molecule binding & Tissue transglutaminase. The author has an hindex of 5, co-authored 5 publications.
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Papers
Elevated Transglutaminase 2 Activity Is Associated with Hypoxia-Induced Experimental Pulmonary Hypertension in Mice
Thomas R. DiRaimondo,Cornelius Klöck,Rod R. Warburton,Zachary Herrera,Krishna Penumatsa,Deniz Toksoz,Nicholas S. Hill,Chaitan Khosla,Barry L. Fanburg +8 more
TL;DR: It is shown that pulmonary TG2 undergoes marked post-translational activation in a mouse model of hypoxia-induced PH, and irreversible fluorinated TG2 inhibitors are identified that may find use as non-invasive positron emission tomography probes for diagnosis and management of this debilitating, lifelong disorder.
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Specific Inhibition of the Bifunctional Farnesyl/Geranylgeranyl Diphosphate Synthase in Malaria Parasites via a New Small-Molecule Binding Site.
TL;DR: A new non-bisphosphonate compound is identified, MMV019313, which is highly selective for PfFPPS/GGPPS and showed no activity against human FPPS or GGPPS and sets the stage for the development of Plasmodium-specific FPPS/ GGPPS inhibitors.
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A Specific Non-Bisphosphonate Inhibitor Of The Bifunctional Farnesyl/Geranylgeranyl Diphosphate Synthase In Malaria Parasites
TL;DR: The findings uncover a new small molecule binding site in this important antimalarial drug target and provide a promising starting point for development of Plasmodium-specific FPPS/GGPPS inhibitors.
A chemical rescue screen identifies a Plasmodium falciparum apicoplast inhibitor targeting MEP isoprenoid precursor biosynthesis
TL;DR: MMV-08138, the first PfIspD inhibitor to be identified, provides the foundation for further development of this promising antimalarial drug candidate lead and validates the use of the apicoplast chemical rescue screen coupled with target elucidation as a discovery tool to identify specific apicOPlast-targeting compounds with new mechanisms of action.
Discovery of potent and specific dihydroisoxazole inhibitors of human transglutaminase 2.
TL;DR: This work profiled the selectivity of existing inhibitors against the most pertinent TG isoforms and identified modifications that improved potency and isoform selectivity, providing a clear basis for the rational selection of dihydroisoxazole inhibitors as tools for in vivo biological investigation.