The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
New nuclear functions of the glycolytic protein, glyceraldehyde‐3‐phosphate dehydrogenase, in mammalian cells
Abstract
Recent studies establish that the glycolytic protein, glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH), is not simply a classical metabolic protein involved in energy production. Instead, it is a multifunctional protein with defined functions in numerous subcellular processes. New investigations establish a primary role for GAPDH in a variety of critical nuclear pathways apart from its already recognized role in apoptosis. These new roles include its requirement for transcriptional control of histone gene expression, its essential function in nuclear membrane fusion, its necessity for the recognition of fraudulently incorporated nucleotides in DNA, and its mandatory participation in the maintenance of telomere structure. Each of these new functions requires GAPDH association into a series of multienzyme complexes. Although other proteins in those complexes are variable, GAPDH remains the single constant protein in each structure. To undertake these new functions, GAPDH is recruited to the nucleus in S phase or its intracellular distribution is regulated as a function of drug exposure. Other investigations relate a substantial role for nuclear GAPDH in hyperglycemic stress and the development of metabolic syndrome. Considerations of future directions as well as the role of GAPDH post‐translational modification as a basis for its multifunctional activities is suggested. © 2005 Wiley‐Liss, Inc.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage
Nishikawa, T., Edelstein, D., Du, X. L., Yamagishi, S.-I., Matsumura, T., Kaneda, Y., Yorek, M. A., Beebe, D., Oates, P. J., Hammes, H.-P., et al. (2000) · Nature · doi:10.1038/35008121 · Cited by 4,277
Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome
Eriksson, M., Brown, W. T., Gordon, L. B., Glynn, M. W., Singer, J., Scott, L., Erdos, M. R., Robbins, C. M., Moses, T. Y., Berglund, P., et al. (2003) · Nature · doi:10.1038/nature01629 · Cited by 1,990
Lamin a truncation in Hutchinson-Gilford progeria
De Sandre-Giovannoli, A., Bernard, R., Cau, P., Navarro, C., Amiel, J., Boccaccio, I., Lyonnet, S., Stewart, C. L., Munnich, A., Le Merrer, M., et al. (2003) · Science · doi:10.1126/science.1084125 · Cited by 1,346
Pathophysiology of insulin resistance in human disease
Reaven, G. M. (1995) · Physiological Reviews · doi:10.1152/physrev.1995.75.3.473 · Cited by 1,226
Du, X.-L., Edelstein, D., Rossetti, L., Fantus, I. G., Goldberg, H., Ziyadeh, F., Wu, J., & Brownlee, M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.22.12222 · Cited by 1,152
Pot1, the Putative Telomere End-Binding Protein in Fission Yeast and Humans
Baumann, P., & Cech, T. R. (2001) · Science · doi:10.1126/science.1060036 · Cited by 1,028
Human telomeres contain two distinct Myb–related proteins, TRF1 and TRF2
Broccoli, D., Smogorzewska, A., Chong, L., & de Lange, T. (1997) · Nature Genetics · doi:10.1038/ng1097-231 · Cited by 926
Du, X., Matsumura, T., Edelstein, D., Rossetti, L., Zsengellér, Z., Szabó, C., & Brownlee, M. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18127 · Cited by 832
Sirover, M. A. (1999) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00119-3 · Cited by 808
Self-citationKhorasanizadeh, S. (2004) · Cell · doi:10.1016/s0092-8674(04)00044-3 · Cited by 674
Cited by
Huang, Q., Lan, F., Zheng, Z., Xie, F., Han, J., Dong, L., Xie, Y., & Zheng, F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.296905 · Cited by 97
Mamczur, P., Borsuk, B., Paszko, J., Sas, Z., Mozrzymas, J., Wiśniewski, J. R., Gizak, A., & Rakus, D. (2015) · Glia · doi:10.1002/glia.22753 · Cited by 71
Metadata
- Authors
- Sirover, M. A.
- Venue
- Journal of Cellular Biochemistry
- Publisher
- Wiley
- Published
- 2005-03-15
- Volume
- 95
- Issue
- 1
- Pages
- 45-52
- ISSN
- 0730-2312 (ISSN-L)
- 1097-4644
- OpenAlex
- W2033816859
- Cited by
- 320
- References
- 53
- FWCI
- 7.03
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: New nuclear functions of the glycolytic protein, glyceraldehyde‐3‐phosphate dehydrogenase, in mammalian cells. https://app.cochat.ai/papers/10.1002/jcb.20399
- The paper
- Sirover, M. A. (2005). New nuclear functions of the glycolytic protein, glyceraldehyde‐3‐phosphate dehydrogenase, in mammalian cells. Journal of Cellular Biochemistry. https://doi.org/10.1002/jcb.20399
Data sources
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.
