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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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Development of selective inhibitors for aldehyde dehydrogenases based on substituted indole-2,3-diones.

TL;DR: Aldehyde dehydrogenases (ALDHs) participate in multiple metabolic pathways and have been indicated to play a role in several cancerous disease states as mentioned in this paper, and the authors of this paper are interested in developing novel and selective ALDH inhibitors.
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Transcriptome analysis and prognosis of ALDH isoforms in human cancer

TL;DR: RNA sequencing data from The Cancer Genome Atlas (TCGA) was used to evaluate the differential expression of 19 ALDH isoforms in 5 common human cancers and showed that each AL DH isoform had a specific differential expression pattern, most of which were related to prognosis in human cancer.
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Aldehyde dehydrogenase 2 activity and aldehydic load contribute to neuroinflammation and Alzheimer’s disease related pathology

TL;DR: In this article, the authors showed that fibroblasts derived from AD patients harboring ApoE e4 allele exhibited increased aldehydic load, oxidative stress, and increased mitochondrial dysfunction relative to healthy subjects and exposure to ethanol exacerbated these dysfunctions.
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Targeting aldehyde dehydrogenase activity in head and neck squamous cell carcinoma with a novel small molecule inhibitor

TL;DR: Data indicate that ALDH3A1 contributes to cisplatin resistance in HNSCC and that the targeting of ALDH, specifically, ALDH 3A1, appears to be a promising strategy in this disease.

Development of Selective Inhibitors for Aldehyde Dehydrogenases Based on Substituted Indole-2,3-diones

TL;DR: A class of isoenzyme-selective inhibitors using similar indole-2,3-diones that exhibit differential inhibition of ALDH1A1, ALDH2, and ALDH3A1 are developed, suggesting that these inhibitors are competitive against aldehyde binding, forming direct interactions with active-site cysteine residues.