Cited by 361RNA Research and SplicingRNA and protein synthesis mechanismsBiochemical and Molecular Research

The DOI matches its Crossref record; 67 of the 67 references it cites were found in a registry or an index.

Glyceraldehyde-3-phosphate Dehydrogenase Selectively Binds AU-rich RNA in the NAD+-binding Region (Rossmann Fold)

Open access

Nagy, Eszter, Rigby, William F.C.·1995·Journal of Biological Chemistry

Open this paper in CoChat — free account Open PDF

Abstract

A 36-kDa protein that binds AU-rich RNA was purified from human spleen and identified as glyceraldehyde-3-phosphate dehydrogenase (GAPDH). GAPDH has been previously demonstrated to bind tRNA with high affinity. Competition studies suggested that cytoplasmic GAPDH binds the AU-rich elements (AREs) of lymphokine mRNA 3'-untranslated regions with higher affinity than tRNA. The AUUUA-specific RNA binding activity of GAPDH was inhibited by NAD+, NADH, and ATP in a concentration-dependent manner, suggesting that RNA binding of GAPDH might involve the NAD(+)-binding region, or dinucleotide-binding (Rossmann) fold. This hypothesis was supported by experiments that localized RNA binding to the predicted N-terminal 6.8-kDa peptide, known to be involved in the formation of the NAD(+)-binding domain. The direct demonstration of ARE-specific binding protein activity localized to the NAD(+)-binding region of GAPDH supports the general concept that enzymes containing this domain may exhibit specific RNA binding activity and play additional roles in nucleic acid metabolism. Finally, cytoplasmic GAPDH was found in the polysomal fraction of T lymphocytes. Thus, the RNA binding specificity of GAPDH as well as its localization within the cell merit its strong consideration as a protein important in the regulation of ARE-dependent mRNA turnover and translation in addition to its well described role in glycolysis.

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

Crossref · 10.1074/jbc.270.6.2755

Cites

67 of 67 references verified0 citation errors · 0 not checkable

Statistics

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.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.
Schägger, H., & von Jagow, G. (1987) · Analytical Biochemistry · doi:10.1016/0003-2697(87)90587-2 · Cited by 11,420
A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation
Shaw, G. D., & Kamen, R. (1986) · Cell · doi:10.1016/0092-8674(86)90341-7 · Cited by 3,946
hnRNP PROTEINS AND THE BIOGENESIS OF mRNA
Dreyfuss, G., Matunis, M. J., Piñol-Roma, S., & Burd, C. G. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.001445 · Cited by 1,558
Regulating the fate of mRNA: the control of cellular iron metabolism
Klausner, R. D., Rouault, T. A., & Harford, J. B. (1993) · Cell · doi:10.1016/0092-8674(93)90046-s · Cited by 1,210
Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
Wierenga, R. K., Terpstra, P., & Hol, W. G. J. (1986) · Journal of Molecular Biology · doi:10.1016/0022-2836(86)90409-2 · Cited by 1,159
Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm
Piñol-Roma, S., & Dreyfuss, G. (1992) · Nature · doi:10.1038/355730a0 · Cited by 842
Homogeneously staining chromosomal regions contain amplified copies of an abundantly expressed cellular oncogene (c-myc) in malignant neuroendocrine cells from a human colon carcinoma.
Alitalo, K., Schwab, M., Lin, C. C., Varmus, H. E., & Bishop, J. M. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.6.1707 · Cited by 761
Staphylococcal Protease: A Proteolytic Enzyme Specific for Glutamoyl Bonds
Houmard, J., & Drapeau, G. R. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.12.3506 · Cited by 702
Expression of human immune interferon cDNA in E. coli and monkey cells
Gray, P. W., Leung, D. W., Pennica, D., Yelverton, E., Najarian, R. C., Simonsen, C. C., Derynck, R., Sherwood, P. J., Wallace, D. M., Berger, S. L., et al. (1982) · Nature · doi:10.1038/295503a0 · Cited by 691

Flagged first, then by citations

Show all 67 references

Research works printed but not linked: 8

Jones, 1987, Mol. Cell. Biol., 7, 4513
Bohjanen, 1991, Mol. Cell. Biol., 11, 3288
Vakalopoulou, 1991, Mol. Cell. Biol., 11, 3355
Brewer, 1991, Mol. Cell. Biol., 11, 2460
Levine, 1993, Mol. Cell. Biol., 13, 3494
Zhang, 1993, Mol. Cell. Biol., 13, 7652
Aharon, 1993, Mol. Cell. Biol., 13, 1971
Grafi, 1993, Mol. Cell. Biol., 13, 3487

Sorted by citations

Posttranscriptional Control of T Cell Effector Function by Aerobic Glycolysis
Chang, C.-H., Curtis, J. D., Maggi, L. B., Faubert, B., Villarino, A. V., O’Sullivan, D., Huang, S. C.-C., van der Windt, G. J. W., Blagih, J., Qiu, J., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.016 · Cited by 2,204
Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins
Castello, A., Fischer, B., Eichelbaum, K., Horos, R., Beckmann, B. M., Strein, C., Davey, N. E., Humphreys, D. T., Preiss, T., Steinmetz, L. M., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.031 · Cited by 2,132
AU-rich elements: characterization and importance in mRNA degradation
Chen, C.-Y. A., & Shyu, A.-B. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89102-1 · Cited by 1,948
A brave new world of RNA-binding proteins
Hentze, M. W., Castello, A., Schwarzl, T., & Preiss, T. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.130 · Cited by 1,821
Fueling Immunity: Insights into Metabolism and Lymphocyte Function
Pearce, E. L., Poffenberger, M. C., Chang, C.-H., & Jones, R. G. (2013) · Science · doi:10.1126/science.1242454 · Cited by 1,363
mRNA stability in mammalian cells
Ross, J. (1995) · Microbiological Reviews · doi:10.1128/mr.59.3.423-450.1995 · Cited by 1,411
HuR and mRNA stability
Brennan, C. M., & Steitz*, J. A. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000854 · Cited by 1,095
AU-rich elements and associated factors: are there unifying principles?
Barreau, C. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki1012 · Cited by 907
Metabolic regulation of immune responses
Ganeshan, K., & Chawla, A. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032713-120236 · Cited by 926
Pyruvate kinase type M2 and its role in tumor growth and spreading
Mazurek, S., Boschek, C. B., Hugo, F., & Eigenbrodt, E. (2005) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2005.04.009 · Cited by 812
New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
Sirover, M. A. (1999) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00119-3 · Cited by 813
RNA stabilization by the AU‐rich element binding protein, HuR, an ELAV protein
Peng, S., Chen, C. A., Xu, N., & Shyu, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.12.3461 · Cited by 739
Regulation of mRNA stability in mammalian cells
Guhaniyogi, J., & Brewer, G. (2001) · Gene · doi:10.1016/s0378-1119(01)00350-x · Cited by 729
Pyruvate kinase type M2: A key regulator of the metabolic budget system in tumor cells
Mazurek, S. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.02.005 · Cited by 694
Dimethyl fumarate targets GAPDH and aerobic glycolysis to modulate immunity
Kornberg, M. D., Bhargava, P., Kim, P. M., Putluri, V., Snowman, A. M., Putluri, N., Calabresi, P. A., & Snyder, S. H. (2018) · Science · doi:10.1126/science.aan4665 · Cited by 687
Multifaceted roles of glycolytic enzymes
Kim, J., & Dang, C. V. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.01.005 · Cited by 692
Comprehensive Identification of RNA-Binding Domains in Human Cells
Castelló, A., Fischer, B., Frese, C. K., Horos, R., Alleaume, A.-M., Föehr, S., Curk, T., Krijgsveld, J., & Hentze, M. W. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.06.029 · Cited by 630
Immunometabolism: Cellular Metabolism Turns Immune Regulator
Loftus, R. M., & Finlay, D. K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.693903 · Cited by 460
Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH
Burke, J. R., Enghild, J. J., Martin, M. E., Jou, Y., Myers, R., Roses, A. D., Vance, J. M., & Strittmatter, W. J. (1996) · Nature Medicine · doi:10.1038/nm0396-347 · Cited by 430
The structure, function and evolution of proteins that bind DNA and RNA
Hudson, W. H., & Ortlund, E. A. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3884 · Cited by 418
Nucleolin and YB-1 are required for JNK-mediated interleukin-2 mRNA stabilization during T-cell activationPreprint
Chen, C., Gherzi, R., Andersen, J., Gaietta, G. M., Jürchott, K., Royer, H. D., Mann, M., & Karin, M. (2000) · Genes & Development · doi:10.1101/gad.14.10.1236 · Cited by 380
Modulation of the Fate of Cytoplasmic mRNA by AU-Rich Elements: Key Sequence Features Controlling mRNA Deadenylation and Decay
Xu, N., Chen, C. A., & Shyu, A. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.8.4611 · Cited by 350
Post-transcriptional Control of Cyclooxygenase-2 Gene Expression
Dixon, D. A., Kaplan, C. D., McIntyre, T. M., Zimmerman, G. A., & Prescott, S. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.11750 · Cited by 348
Metabolic signaling in T cells
Shyer, J. A., Flavell, R. A., & Bailis, W. (2020) · Cell Research · doi:10.1038/s41422-020-0379-5 · Cited by 346
On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: Biochemical mechanisms and regulatory control
Sirover, M. A. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.05.010 · Cited by 333
Metabolic regulation of inflammation
Gaber, T., Strehl, C., & Buttgereit, F. (2017) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2017.37 · Cited by 320
Post‐transcriptional regulation of gene expression by degradation of messenger RNAs
Bevilacqua, A., Ceriani, M. C., Capaccioli, S., & Nicolin, A. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10272 · Cited by 320
GAPDH: A common enzyme with uncommon functions
Nicholls, C., Li, H., & Liu, J. (2011) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2011.05599.x · Cited by 314
Pondering the Promyelocytic Leukemia Protein (PML) Puzzle: Possible Functions for PML Nuclear Bodies
Borden, K. L. B. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5259-5269.2002 · Cited by 314
The involvement of AU-rich element-binding proteins in p38 mitogen-activated protein kinase pathway-mediated mRNA stabilisation
Dean, J. L. E., Sully, G., Clark, A. R., & Saklatvala, J. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2004.04.006 · Cited by 312
The 3′ Untranslated Region of Tumor Necrosis Factor Alpha mRNA Is a Target of the mRNA-Stabilizing Factor HuR
Dean, J. L. E., Wait, R., Mahtani, K. R., Sully, G., Clark, A. R., & Saklatvala, J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.3.721-730.2001 · Cited by 294
Metabolic Modulation in Macrophage Effector Function
Diskin, C., & Pålsson‐McDermott, E. M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00270 · Cited by 310
Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU-rich element
Loflin, P., Chen, C.-Y. A., & Shyu, A.-B. (1999) · Genes & Development · doi:10.1101/gad.13.14.1884 · Cited by 246
Patterns of Protein Synthesis and Tolerance of Anoxia in Root Tips of Maize Seedlings Acclimated to a Low-Oxygen Environment, and Identification of Proteins by Mass Spectrometry
Chang, W. W. P., Huang, L., Shen, M., Webster, C., Burlingame, A. L., & Roberts, J. K. M. (2000) · PLANT PHYSIOLOGY · doi:10.1104/pp.122.2.295 · Cited by 292
Metabolic Enzymes Enjoying New Partnerships as RNA-Binding Proteins
Castelló, A., Hentze, M. W., & Preiß, T. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.09.012 · Cited by 274
Oxidatively Modified Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) and Alzheimer's Disease: Many Pathways to Neurodegeneration
Butterfield, D. A., Hardas, S. S., & Lange, M. L. B. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1375 · Cited by 266
H19 lncRNA alters DNA methylation genome wide by regulating S-adenosylhomocysteine hydrolase
Zhou, J., Yang, L., Zhong, T., Mueller, M., Men, Y., Zhang, N., Xie, J., Giang, K., Chung, H., Sun, X., et al. (2015) · Nature Communications · doi:10.1038/ncomms10221 · Cited by 254
Cellular metabolism regulates the differentiation and function of T-cell subsets
Ma, S., Ming, Y., Wu, J., & Cui, G. (2024) · Cellular and Molecular Immunology · doi:10.1038/s41423-024-01148-8 · Cited by 276
Role of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in normal cell function and in cell pathology
Sirover, M. A. (1997) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19970801)66:2 · Cited by 245
The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl‐ and glutamyl‐tRNA synthetases.
Simos, G., Segref, A., Fasiolo, F., Hellmuth, K., Shevchenko, A. A., Mann, M., & Hurt, E. C. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00927.x · Cited by 229
Potential role of nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase in apoptosis and oxidative stress
Dastoor, Z., & Dreyer, J. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.9.1643 · Cited by 217
Malonylation of GAPDH is an inflammatory signal in macrophages
Galván-Peña, S., Carroll, R. G., Newman, C. F., Hinchy, E. C., Pålsson‐McDermott, E. M., Robinson, E. K., Covarrubias, S., Nadin, A. J., James, A. M., Haneklaus, M., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-08187-6 · Cited by 220
Hypoxia-inducible Protein Binding to Vascular Endothelial Growth Factor mRNA and Its Modulation by the von Hippel-Lindau Protein
Levy, A. P., Levy, N. S., & Goldberg, M. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.41.25492 · Cited by 214
mRNA Stability and the Control of Gene Expression: Implications for Human Disease
Hollams, E. M., Giles, K. M., Thomson, A. M., & Leedman, P. J. (2002) · Neurochemical Research · doi:10.1023/a:1020992418511 · Cited by 212
Regulation of Human Vascular Endothelial Growth Factor mRNA Stability in Hypoxia by Heterogeneous Nuclear Ribonucleoprotein L
Shih, S., & Claffey, K. P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.3.1359 · Cited by 213
Glyceraldehyde-3-phosphate Dehydrogenase, the Putative Target of the Antiapoptotic Compounds CGP 3466 and R-(−)-Deprenyl
Kragten, E. A., Lalande, I., Zimmermann, K., Roggo, S. P., Schindler, P. A., Müller, D., van Oostrum, J., Waldmeier, P. C., & Fürst, P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5821 · Cited by 209
Macromolecular Compartmentation and Channeling
Ovádi, J., & Sreret, P. A. (1999) · International review of cytology · doi:10.1016/s0074-7696(08)60529-x · Cited by 205
Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting properties
Zaffagnini, M., Fermani, S., Costa, A., Lemaire, S. D., & Trost, P. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00450 · Cited by 205
RNA templating the epigenome
Spitale, R. C., Tsai, M.-C., & Chang, H. Y. (2011) · Epigenetics · doi:10.4161/epi.6.5.15221 · Cited by 203
Insulin-like growth factor-I-dependent stimulation of nuclear phospholipase C-?1 activity in Swiss 3T3 cells requires an intact cytoskeleton and is paralleled by increased phosphorylation of the phospholipase
Martelli, A. M., Cocco, L., Bareggi, R., Tabellini, G., Rizzoli, R., Ghibellini, M. D., & Narducci, P. (1999) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19990301)72:3 · Cited by 38
Protein Kinase Cα-dependent Phosphorylation of the mRNA-stabilizing Factor HuR: Implications for Posttranscriptional Regulation of Cyclooxygenase-2
Doller, A., Huwiler, A., Müller, R., Radeke, H. H., Pfeilschifter, J. M., & Eberhardt, W. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-09-0850 · Cited by 191
Subcellular dynamics of multifunctional protein regulation: Mechanisms of GAPDH intracellular translocation
Sirover, M. A. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24113 · Cited by 191
Glucose, glycolysis and lymphocyte responses
Donnelly, R. P., & Finlay, D. K. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.07.034 · Cited by 193
Identification of a Human VPF/VEGF 3′ Untranslated Region Mediating Hypoxia-induced mRNA Stability
Claffey, K. P., Shih, S., Mullen, A. R., Dziennis, S., Cusick, J. L., Abrams, K., Lee, S. W., & Detmar, M. J. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.2.469 · Cited by 181
Modulation of mRNA stability as a novel therapeutic approach
Eberhardt, W., Doller, A., Akool, E.-S., & Pfeilschifter, J. (2007) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2007.01.002 · Cited by 173
Transfection‐enforced Bcl‐2 overexpression and an anti‐Parkinson drug, rasagiline, prevent nuclear accumulation of glyceraldehyde‐3‐phosphate dehydrogenase induced by an endogenous dopaminergic neurotoxin, N‐methyl(R)salsolinol
Maruyama, W., Akao, Y., Youdim, M. B. H., Davis, B. A., & Naoi, M. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00448.x · Cited by 169
Tomato bushy stunt virus Co-Opts the RNA-Binding Function of a Host Metabolic Enzyme for Viral Genomic RNA Synthesis
Wang, R., & Nagy, P. D. (2008) · Cell Host & Microbe · doi:10.1016/j.chom.2008.02.005 · Cited by 167
Oxidative modifications of glyceraldehyde-3-phosphate dehydrogenase play a key role in its multiple cellular functions
Hwang, N. R., Yim, S.-H., Kim, Y., Jeong, J., Song, E. J., Lee, Y., Lee, J. H., Choi, S., & Lee, K. (2009) · Biochemical Journal · doi:10.1042/bj20090854 · Cited by 164
Reduced Apoptosis after Nerve Growth Factor and Serum Withdrawal: Conversion of Tetrameric Glyceraldehyde-3-Phosphate Dehydrogenase to a Dimer
Carlile, G. W., Chalmers-Redman, R. M. E., Tatton, N. A., Pong, A., Borden, K. L. B., & Tatton, W. G. (2000) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)26436-1 · Cited by 164
Proteome-Wide Search Reveals Unexpected RNA-Binding Proteins in Saccharomyces cerevisiae
Tsvetanova, N. G., Klass, D. M., Salzman, J., & Brown, P. O. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012671 · Cited by 156
Perspectives on the mechanism of transcriptional regulation by long non-coding RNAs
Roberts, T. C., Morris, K. V., & Weinberg, M. S. (2013) · Epigenetics · doi:10.4161/epi.26700 · Cited by 155
Suppression of FIP200 and autophagy by tumor-derived lactate promotes naïve T cell apoptosis and affects tumor immunity
Xia, H., Wang, W., Crespo, J., Kryczek, I., Li, W., Wei, S., Bian, Z., Maj, T., He, M., Liu, J. R., et al. (2017) · Science Immunology · doi:10.1126/sciimmunol.aan4631 · Cited by 160
Specific Interaction of Glyceraldehyde 3-Phosphate Dehydrogenase with the 5′-Nontranslated RNA of Hepatitis A Virus
Schultz, D. E., Hardin, C. C., & Lemon, S. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.24.14134 · Cited by 148
The immunologic Warburg effect: Evidence and therapeutic opportunities in autoimmunity
Kornberg, M. D. (2020) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1486 · Cited by 151
GAPDH Binding to TNF-α mRNA Contributes to Posttranscriptional Repression in Monocytes: A Novel Mechanism of Communication between Inflammation and Metabolism
Millet, P., Vachharajani, V., McPhail, L. C., Yoza, B. K., & McCall, C. E. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501345 · Cited by 141
Manganese Neurotoxicity: An Update of Pathophysiologic Mechanisms
Normandin, L., & Hazell, A. S. (2002) · Metabolic Brain Disease · doi:10.1023/a:1021970120965 · Cited by 138
Induction by Glucose of Genes Coding for Glycolytic Enzymes in a Pancreatic β-Cell Line (INS-1)
Roche, E., Assimacopoulos‐Jeannet, F., Witters, L. A., Perruchoud, B., Yaney, G. C., Corkey, B. E., Asfari, M., & Prentki, M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.5.3091 · Cited by 136
HuA and Tristetraprolin Are Induced following T Cell Activation and Display Distinct but Overlapping RNA Binding Specificities
Raghavan, A., Robison, R. L., McNabb, J., Miller, C. R., Williams, D. A., & Bohjanen, P. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m109511200 · Cited by 136
The Search for Trans-Acting Factors Controlling Messenger RNA Decay
Wilson, G. M., & Brewer, G. (1998) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60510-3 · Cited by 135
GOSPEL: A Neuroprotective Protein that Binds to GAPDH upon S-Nitrosylation
Sen, N., Hara, M. R., Ahmad, A. S., Cascio, M. B., Kamiya, A., Ehmsen, J. T., Aggrawal, N., Hester, L. D., Doré, S., Snyder, S. H., et al. (2009) · Neuron · doi:10.1016/j.neuron.2009.05.024 · Cited by 132
Glyceraldehyde-3-phosphate Dehydrogenase and Nm23-H1/Nucleoside Diphosphate Kinase A
Engel, M., Seifert, M., Theisinger, B., Seyfert, U. T., & Welter, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.20058 · Cited by 125
Actin-Binding Cellular Proteins inside Human Immunodeficiency Virus Type 1
Ott, D. E., Coren, L. V., Johnson, D. G., Kane, B., Sowder, R. C., Kim, Y. D., Fisher, R. J., Zhou, X. Z., Lu, K. P., & Henderson, L. E. (2000) · Virology · doi:10.1006/viro.1999.0075 · Cited by 127
The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short‐chain dehydrogenase/reductases
STAMMERS, D. K., Ren, J., Leslie, K., Nichols, C. E., Lamb, H. K., Cocklin, S., Dodds, A., & Hawkins, A. R. (2001) · The EMBO Journal · doi:10.1093/emboj/20.23.6619 · Cited by 119
Mammalian Hsp70 and Hsp110 Proteins Bind to RNA Motifs Involved in mRNA Stability
Henics, T., Nagy, E., Oh, H. J., Csermely, P., von Gabain, A., & Subjeck, J. R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.24.17318 · Cited by 119
Self-citation
Glyceraldehyde-3-Phosphate Dehydrogenase Regulates Endothelin-1 Expression by a Novel, Redox-Sensitive Mechanism Involving mRNA Stability
Rodríguez‐Pascual, F., Redondo‐Horcajo, M., Magán-Marchal, N., Lagares, D., Martı́nez-Ruiz, A., Kleinert, H., & Lamas, S. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01145-08 · Cited by 119
Structure, function and regulation of gonadotropin receptors – A perspective
Menon, K. M. J., & Menon, B. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.01.021 · Cited by 118
Root proteomic responses to heat stress in two Agrostis grass species contrasting in heat tolerance
Xu, C., & Huang, B. (2008) · Journal of Experimental Botany · doi:10.1093/jxb/ern258 · Cited by 118
Increased expression of mRNA encoding interleukin-1? and caspase-1, and the secreted isoform of interleukin-1 receptor antagonist in the rat brain following systemic kainic acid administration
Eriksson, C., Tehranian, R., Iverfeldt, K., Winblad, B. G., & Schultzberg, M. (2000) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(20000415)60:2 · Cited by 79
Glycolysis determines dichotomous regulation of T cell subsets in hypoxia
Xu, Y., Chaudhury, A., Zhang, M., Savoldo, B., Metelitsa, L. S., Rodgers, J. R., Yustein, J. T., Neilson, J. R., & Dotti, G. (2016) · Journal of Clinical Investigation · doi:10.1172/jci85834 · Cited by 117
Specific Interaction in Vitro and in Vivo of Glyceraldehyde-3-phosphate Dehydrogenase and LA Protein with Cis-acting RNAs of Human Parainfluenza Virus Type 3
De, B. P., Gupta, S., Zhao, H. L., Drazba, J. A., & Banerjee, A. K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.40.24728 · Cited by 116
The REM phase of gene regulation
Hentze, M. W., & Preiss, T. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.05.009 · Cited by 115
Astrocytes and manganese neurotoxicity
Hazell, A. S. (2002) · Neurochemistry International · doi:10.1016/s0197-0186(02)00013-x · Cited by 114
Structural analysis of glyceraldehyde-3-phosphate dehydrogenase functional diversity
Sirover, M. A. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.09.026 · Cited by 114
Biochemistry of proinflammatory macrophage activation
Nonnenmacher, Y., & Hiller, K. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2784-1 · Cited by 112
Post-Transcriptional Control of the Hypoxic Response by RNA-Binding Proteins and MicroRNAs
Gorospe, M., Tominaga, K., Wu, X., Fähling, M., & Ivan, M. (2011) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2011.00007 · Cited by 115
Glyceraldehyde-3-Phosphate Dehydrogenase Binds to the AU-Rich 3′ Untranslated Region of Colony-Stimulating Factor–1 (CSF-1) Messenger RNA in Human Ovarian Cancer Cells: Possible Role in CSF-1 Posttranscriptional Regulation and Tumor Phenotype
Bonafé, N., Gilmore-Hebert, M., Folk, N. L., Azodi, M., Zhou, Y., & Chambers, S. K. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3954 · Cited by 105
Modulation of AUUUA Response Element Binding by Heterogeneous Nuclear Ribonucleoprotein A1 in Human T Lymphocytes
Hamilton, B. J., Burns, C. M., Nichols, R. C., & Rigby, W. F. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28732 · Cited by 109
Self-citation
Metabolic cooperation between different oncogenes during cell transformation: interaction between activated ras and HPV-16 E7
Mazurek, S., Zwerschke, W., Jansen‐Dürr, P., & EIGENBRODT, E. (2001) · Oncogene · doi:10.1038/sj.onc.1204792 · Cited by 107
Metabolic enzymes that bind RNA: yet another level of cellular regulatory network?
Cieśla, J. (2006) · Acta Biochimica Polonica · doi:10.18388/abp.2006_3360 · Cited by 106
The Multifunctional Protein Glyceraldehyde-3-Phosphate Dehydrogenase Is Both Regulated and Controls Colony-Stimulating Factor-1 Messenger RNA Stability in Ovarian Cancer
Zhou, Y., Yi, X., Stoffer, J. B., Bonafé, N., Gilmore-Hebert, M., McAlpine, J. N., & Chambers, S. K. (2008) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-07-2170 · Cited by 106
Effect of Extracellular AMP on Cell Proliferation and Metabolism of Breast Cancer Cell Lines with High and Low Glycolytic Rates
Mazurek, S., Michel, A., & EIGENBRODT, E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.8.4941 · Cited by 105
Uracil DNA-glycosylase/glyceraldehyde-3-phosphate dehydrogenase is an Ap4A binding protein
Baxi, M. D., & Vishwanatha, J. K. (1995) · Biochemistry · doi:10.1021/bi00030a007 · Cited by 104
Functional Significance of the Interaction of Hepatitis A Virus RNA with Glyceraldehyde 3-Phosphate Dehydrogenase (GAPDH): Opposing Effects of GAPDH and Polypyrimidine Tract Binding Protein on Internal Ribosome Entry Site Function
Yi, M., Schultz, D. E., & Lemon, S. M. (2000) · Journal of Virology · doi:10.1128/jvi.74.14.6459-6468.2000 · Cited by 103
Glyceraldehyde-3-phosphate dehydrogenase in neurodegeneration and apoptosis signaling
Tatton, W. G., Chalmers-Redman, R. M. E., Elstner, M., Leesch, W., Jagodzinski, F. B., Stupak, D. P., Sugrue, M. M., & Tatton, N. A. (2000) · Springer eBooks · doi:10.1007/978-3-7091-6301-6_5 · Cited by 105
Inosine 5′-monophosphate dehydrogenase binds nucleic acids in vitro and in vivo
McLean, J. E., Hamaguchi, N., Belenky, P. A., MORTIMER, S. E., Stanton, M. J., & Hedstrom, L. (2004) · Biochemical Journal · doi:10.1042/bj20031585 · Cited by 102
Protein profile analysis of salt-responsive proteins in leaves and roots in two cultivars of creeping bentgrass differing in salinity tolerance
Xu, C., Sibicky, T., & Huang, B. (2010) · Plant Cell Reports · doi:10.1007/s00299-010-0847-3 · Cited by 100
Emerging Evidence of Translational Control by AU-Rich Element-Binding Proteins
Otsuka, H., Fukao, A., Funakami, Y., Duncan, K. E., & Fujiwara, T. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00332 · Cited by 101
Identification of the NAD+-Binding Fold of Glyceraldehyde-3-Phosphate Dehydrogenase as a Novel RNA-Binding Domain
Nagy, E., Henics, T., Eckert, M., Miseta, A., Lightowlers, R. N., & Kellermayer, M. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3246 · Cited by 99
Self-citation
Biological targets for isatin and its analogues: Implications for therapy.
Medvedev, A. E., Бунеева, О. А., & Glover, V. A. S. (2007) · PubMed Central · Cited by 99
Housekeeping Gene Selection Advisory: Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) and β-Actin Are Targets of miR-644a
Sikand, K., Singh, J., Ebron, J. S., & Shukla, G. C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047510 · Cited by 99

Authors: Nagy, E., & Rigby, W. F. C.
Affiliations: White River Junction VA Medical Center (US)
Corresponding author: Rigby, William F.C.
ORCID: Nagy, Eszter
Rigby, William F.C.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1995-02
Volume: 270
Issue: 6
Pages: 2755-2763
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.270.6.2755
OpenAlex: W2050843429
Cited by: 361
References: 67
Citations by year: 2026: 5 · 2025: 14 · 2024: 10 · 2023: 7 · 2022: 5 · 2021: 4 · 2020: 18 · 2019: 9 · 2018: 15 · 2017: 10 · 2016: 12 · 2015: 7 · 2014: 12 · 2013: 11 · 2012: 14
FWCI: 6.32
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 9402 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (5k04ai000910-02)
National Institute of Allergy and Infectious Diseases (KO4 AI00910, R0 1 AI2434)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Keywords: glyceraldehyde-3-phosphate dehydrogenase, NAD-binding domain, Rossmann fold, RNA-binding proteins, tRNA binding, 3' untranslated region, mRNA turnover, translational regulation, T cells, polysomes
MeSH terms: Adenine, Base Sequence, Cells, Cultured, Glyceraldehyde-3-Phosphate Dehydrogenases, Humans, Molecular Sequence Data, NAD, Protein Binding, RNA, Substrate Specificity, T-Lymphocytes, Uridine, Protein Folding

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

Glyceraldehyde-3-phosphate Dehydrogenase Selectively Binds AU-rich RNA in the NAD+-binding Region (Rossmann Fold)

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks