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David E. Heppner

Researcher at Harvard University

Publications -  47
Citations -  2733

David E. Heppner is an academic researcher from Harvard University. The author has contributed to research in topics: Epidermal growth factor receptor & Allosteric regulation. The author has an hindex of 19, co-authored 38 publications receiving 2002 citations. Previous affiliations of David E. Heppner include Stanford University & State University of New York System.

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Copper Active Sites in Biology

TL;DR: This review presents in depth discussions of all these classes of Cu enzymes and the correlations within and among these classes, as well as the present understanding of the enzymology, kinetics, geometric structures, electronic structures and the reaction mechanisms these have elucidated.
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A Quantitative Tissue-Specific Landscape of Protein Redox Regulation during Aging

TL;DR: Oximouse is developed, a comprehensive and quantitative mapping of the mouse cysteine redox proteome in vivo that comprehensively identifies redox-modified disease networks that remodel in aged mice, establishing a systemic molecular basis for the long-standing proposed links between redox dysregulation and tissue aging.
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Single and Dual Targeting of Mutant EGFR with an Allosteric Inhibitor.

TL;DR: This study identifies a mutant-selective EGFR allosteric inhibitor that is effective as a single agent and in combination with the EGFR TKI osimertinib and suggests that the combination of a covalent mutant- selective ATP-competitive inhibitor and an allosterics EGFR inhibitor may be an effective therapeutic approach for patients with EGFR-mutant lung cancer.
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Copper dioxygen (bio)inorganic chemistry

TL;DR: This review considers how the respective intermediate electronic structures overcome the spin-forbidden nature of O2 binding, activate O2 for electrophilic aromatic attack and H-atom abstraction, catalyze the 4 e- reduction of O 2 to H2O, and discusses the role of exchange coupling between Cu ions in determining reactivity.
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Reaction coordinate of a functional model of tyrosinase: spectroscopic and computational characterization.

TL;DR: Parallels and contrasts are drawn between the spectroscopically and computationally supported mechanism of the DBED system, presented here, and the experimentally derived mechanism ofThe coupled binuclear copper protein tyrosinase.