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Article

An aggregate-prone mutant of human glyceraldehyde-3-phosphate dehydrogenase augments oxidative stress-induced cell death in SH-SY5Y cells.

Biochemical and biophysical research communications - 18 Dec 2009

Nakajima Hidemitsu, Amano Wataru, Fukuhara Ayano, Kubo Takeya, Misaki Shouhei, Azuma Yasu-Taka, Inui Takashi, Takeuchi Tadayoshi

Abstract excerpt

Glycerladehyde-3-phosphate dehydrogenase (GAPDH), a classic glycolytic enzyme, also has a role in mediating cell death under oxidative stress. Our previous reports suggest that oxidative stress-induced GAPDH aggregate formation is, at least in part, a mechanism to account for the death signaling. Here we show that substitution of cysteine for serine-284 of human GAPDH (S284C-GAPDH) leads to aggregate-prone GAPDH,...

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Identifiers

PMID: 19874799
DOI: 10.1016/j.bbrc.2009.10.118

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GAPDH

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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