The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
GAPDH: A common enzyme with uncommon functions
Abstract
Summary: 1. Glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) has long been recognized as an important enzyme for energy metabolism and the production of ATP and pyruvate through anaerobic glycolysis in the cytoplasm. 2. Recent studies have shown that GAPDH has multiple functions independent of its role in energy metabolism. Although increased GAPDH gene expression and enzymatic function is associated with cell proliferation and tumourigenesis, conditions such as oxidative stress impair GAPDH catalytic activity and lead to cellular aging and apoptosis. 3. The mechanism(s) underlying the effects of GAPDH on cellular proliferation remains unclear, yet much evidence has been accrued that demonstrates a variety of interacting partners for GAPDH, including proteins, various RNA species and telomeric DNA. 4. The present mini review summarizes recent findings relating to the extraglycolytic functions of GAPDH and highlights the significant role this enzyme plays in regulating both cell survival and apoptotic death.
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Cites
Colony-Stimulating Factor 1 Promotes Progression of Mammary Tumors to Malignancy
Lin, E. Y., Nguyen, A. V., Russell, R. G., & Pollard, J. W. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.6.727 · Cited by 1,594
S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
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Enhanced expression of a glyceraldehyde-3-phosphate dehydrogenase gene in human lung cancers.
Tokunaga, K., Nakamura, Y., Sakata, K., Fujimori, K., Ohkubo, M., Sawada, K., & Sakiyama, S. (1987) · PubMed · Cited by 537
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Colell, A., Ricci, J.-E., Tait, S., Milasta, S., Maurer, U., Bouchier-Hayes, L., Fitzgerald, P., Guio-Carrion, A., Waterhouse, N. J., Li, C. W., et al. (2007) · Cell · doi:10.1016/j.cell.2007.03.045 · Cited by 516
Sequence-Specific Binding of Transfer RNA by Glyceraldehyde-3-Phosphate Dehydrogenase
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Nitric oxide-induced nuclear GAPDH activates p300/CBP and mediates apoptosis
Sen, N., Hara, M. R., Kornberg, M. D., Cascio, M. B., Bae, B.-I., Shahani, N., Thomas, B., Dawson, T. M., Dawson, V. L., Snyder, S. H., et al. (2008) · Nature Cell Biology · doi:10.1038/ncb1747 · Cited by 407
GAPDH mediates nitrosylation of nuclear proteins
Kornberg, M. D., Sen, N., Hara, M. R., Juluri, K. R., Nguyen, J. V. K., Snowman, A. M., Law, L., Hester, L. D., & Snyder, S. H. (2010) · Nature Cell Biology · doi:10.1038/ncb2114 · Cited by 394
Cited by
Targeting glycolysis in non-small cell lung cancer: Promises and challenges
Xu, J.-Q., Fu, Y.-L., Zhang, J., Zhang, K.-Y., Ma, J., Tang, J.-Y., Zhang, Z.-W., & Zhou, Z.-Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1037341 · Cited by 75
Bathelt, J., Barnes, J., Raymond, F. L., Baker, K., & Astle, D. (2017) · Cerebral Cortex · doi:10.1093/cercor/bhx027 · Cited by 15
Metadata
- Authors
- Nicholls, C., Li, H., & Liu, J.
- Venue
- Clinical and Experimental Pharmacology and Physiology
- Publisher
- Wiley
- Published
- 2012-07-25
- Volume
- 39
- Issue
- 8
- Pages
- 674-679
- ISSN
- 0305-1870 (ISSN-L)
- 1440-1681
- OpenAlex
- W1948183507
- Cited by
- 311
- References
- 61
- FWCI
- 2.65
- Type
- journal article
- Language
- en
- Open access
- closed
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- Nicholls, C., Li, H., & Liu, J. (2012). GAPDH: A common enzyme with uncommon functions. Clinical and Experimental Pharmacology and Physiology. https://doi.org/10.1111/j.1440-1681.2011.05599.x
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
