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Che-Hong Chen

Researcher at Stanford University

Publications -  89
Citations -  6702

Che-Hong Chen is an academic researcher from Stanford University. The author has contributed to research in topics: Aldehyde dehydrogenase & ALDH2. The author has an hindex of 33, co-authored 86 publications receiving 6052 citations. Previous affiliations of Che-Hong Chen include Veterans Health Administration.

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An improved permeabilization protocol for the introduction of peptides into cardiac myocytes: Application to protein kinase C research

TL;DR: The results demonstrate a methodology for the introduction of peptides into neonatal cardiac myocytes that allows study of their actions without substantial compromises in cell integrity.
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Activation of aldehyde dehydrogenase 2 (ALDH2) confers cardioprotection in protein kinase C epsilon (PKCɛ) knockout mice

TL;DR: It is reported that ethanol preconditioning requires PKCvarepsilon, whereas direct activation of ALDH2 reduces infarct size in both wild type and PKCVarepsilus knockout hearts, suggesting that direct activated aldehyde dehydrogenase 2 may represent a method of harnessing the cardioprotective effect of ethanol without the side effects associated with alcohol consumption.
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Aldehyde dehydrogenase-2 regulates nociception in rodent models of acute inflammatory pain

TL;DR: The data in rodent models suggest that the mitochondrial enzyme ALDH2 regulates nociception and could serve as a molecular target for pain control, with AL DH2 activators, such as Alda-1, as potential non-narcotic, cardiac-safe analgesics.
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Neuroprotective effects of aldehyde dehydrogenase 2 activation in rotenone-induced cellular and animal models of parkinsonism

TL;DR: It is demonstrated that ALDH2 plays a crucial role in maintaining normal mitochondrial function to protect against neurotoxicity and that Alda-1 is effective in ameliorating mitochondrial dysfunction and inhibiting mitochondria-mediated apoptotic pathway.
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Discovery of a novel class of covalent inhibitor for aldehyde dehydrogenases.

TL;DR: The discovery of a general class of ALDH inhibitors with a common mechanism of action is reported, and it is demonstrated that these inhibitors undergo an enzyme-mediated β-elimination reaction generating a vinyl ketone intermediate that covalently modifies the active site cysteine residue present in these enzymes.