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
Hyaluronan‐binding proteins in development, tissue homeostasis, and disease
Knudson, C. B., & Knudson, W. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.13.7691670 · Cited by 653
Positive selection of antigen-specific T cells in thymus by restricting MHC molecules
Kisielow, P., Teh, H., Blüthmann, H., & von Boehmer, H. (1988) · Nature · doi:10.1038/335730a0 · Cited by 618
The c-fos transcript is targeted for rapid decay by two distinct mRNA degradation pathways.Preprint
Shyu, A. B., Greenberg, M. E., & Belasco, J. G. (1989) · Genes & Development · doi:10.1101/gad.3.1.60 · Cited by 575
Purification, Characterization, and cDNA Cloning of an AU-Rich Element RNA-Binding Protein, AUF1
Zhang, W., Wagner, B., Ehrenman, K., Schaefer, A., DeMaria, C. T., Crater, D. L., DeHaven, K., Long, L., & Brewer, G. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7652 · Cited by 540
Identification of an AUUUA-Specific Messenger RNA Binding Protein
Malter, J. S. (1989) · Science · doi:10.1126/science.2814487 · Cited by 497
An A + U-rich element RNA-binding factor regulates c-myc mRNA stability in vitro.
Brewer, G. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.5.2460 · Cited by 484
Sequence-Specific Binding of Transfer RNA by Glyceraldehyde-3-Phosphate Dehydrogenase
Singh, R., & Green, M. R. (1993) · Science · doi:10.1126/science.8420004 · Cited by 481
Control of Messenger RNA Stability
(1993) · Elsevier eBooks · doi:10.1016/c2009-0-03269-3 · Cited by 386
Oxidation-Reduction and the Molecular Mechanism of a Regulatory RNA-Protein Interaction
Hentze, M. W., Rouault, T. A., Harford, J. B., & Klausner, R. D. (1989) · Science · doi:10.1126/science.2711187 · Cited by 377
Hel-N1: an Autoimmune RNA-Binding Protein with Specificity for 3' Uridylate-Rich Untranslated Regions of Growth Factor mRNAs
Levine, T., Gao, F., King, P. H., Andrews, L. G., & Keene, J. D. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.6.3494 · Cited by 356
A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase.
Meyer‐Siegler, K. L., Mauro, D. J., Seal, G., Wurzer, J. C., deRiel, J. K., & Sirover, M. A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.19.8460 · Cited by 344
Translational Blockade Imposed by Cytokine-Derived UA-Rich Sequences
Kruys, V., Marinx, O., Shaw, G. D., Deschamps, J., & Huez, G. (1989) · Science · doi:10.1126/science.2672333 · Cited by 328
Rapid Cytoplasmic Turnover of c-myc mRNA: Requirement of the 3′ Untranslated Sequences
Jones, T. R., & Cole, M. D. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.12.4513-4521.1987 · Cited by 309
An Inducible Cytoplasmic Factor (AU-B) Binds Selectively to AUUUA Multimers in the 3′ Untranslated Region of Lymphokine mRNA
Bohjanen, P. R., Petryniak, B., June, C. H., Thompson, C. B., & Lindsten, T. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.6.3288 · Cited by 288
A 32-kilodalton protein binds to AU-rich domains in the 3' untranslated regions of rapidly degraded mRNAs.
Vakalopoulou, E., Schaack, J. B., & Shenk, T. E. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.6.3355 · Cited by 266
Translocation of a specific premessenger ribonucleoprotein particle through the nuclear pore studied with electron microscope tomography
Mehlin, H., Daneholt, B., & Skoglund, U. (1992) · Cell · doi:10.1016/0092-8674(92)90224-z · Cited by 260
RNA recognition: A family matter?
Mattaj, I. W. (1993) · Cell · doi:10.1016/0092-8674(93)90265-r · Cited by 252
Regulation of Cytokine Gene Expression
Taniguchi, T. (1988) · Annual Review of Immunology · doi:10.1146/annurev.iy.06.040188.002255 · Cited by 238
Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts.
Burd, C. G., Swanson, M. S., Görlach, M., & Dreyfuss, G. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.24.9788 · Cited by 237
Association of heterogeneous nuclear ribonucleoprotein A1 and C proteins with reiterated AUUUA sequences.
Hamilton, B. J., Nagy, E., Malter, J. S., Arrick, B. A., & Rigby, W. F. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52955-0 · Cited by 209
Self-citation
A regulated RNA binding protein also possesses aconitase activity.
Kaptain, S., Downey, W. E., Tang, C., Philpott, C. M., Haile, D. J., Orloff, D. G., Harford, J. B., Rouault, T. A., & Klausner, R. D. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.22.10109 · Cited by 201
The Acyl-enzyme Intermediate and the Kinetic Mechanism of the Glyceraldehyde 3-Phosphate Dehydrogenase Reaction
Furfine, C. S., & Velick, S. F. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45252-5 · Cited by 186
A redox switch and phosphorylation are involved in the post-translational up-regulation of the adenosine-uridine binding factor by phorbol ester and ionophore.
Malter, J. S., & Hong, Y. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)49969-3 · Cited by 181
Bundling of microtubules by glyceraldehyde‐3‐phosphate dehydrogenase and its modulation by ATP
Huitorel, P., & Pantaloni, D. (1985) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1985.tb09016.x · Cited by 181
Identification of an RNA binding site for human thymidylate synthase.
Chu, E., Voeller, D. M., Koeller, D. M., Drake, J. C., Takimoto, C. H. M., Maley, G. F., Maley, F., & Allegra, C. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.2.517 · Cited by 178
Evidence for instability of mRNAs containing AUUUA motifs mediated through translation-dependent assembly of a > 20S degradation complex.Preprint
Savant‐Bhonsale, S., & Cleveland, D. W. (1992) · Genes & Development · doi:10.1101/gad.6.10.1927 · Cited by 173
Renaturation of complementary DNA strands mediated by purified mammalian heterogeneous nuclear ribonucleoprotein A1 protein: implications for a mechanism for rapid molecular assembly.
Pontius, B. W., & Berg, P. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.21.8403 · Cited by 139
Specific binding of human dihydrofolate reductase protein to dihydrofolate reductase messenger RNA in vitro
Chu, E., Takimoto, C. H. M., Voeller, D. M., Grem, J. L., & Allegra, C. J. (1993) · Biochemistry · doi:10.1021/bi00069a009 · Cited by 138
Selective Destabilization of Short-Lived mRNAs with the Granulocyte-Macrophage Colony-Stimulating Factor AU-Rich 3' Noncoding Region Is Mediated by a Cotranslational Mechanism
Aharon, T., & Schneider, R. J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.3.1971-1980.1993 · Cited by 135
Enzymes as RNA-binding proteins: a role for (di)nucleotide-binding domains?
Hentze, M. W. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90198-8 · Cited by 127
Autophosphorylation of glyceraldehyde phosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes
Kawamoto, R. M., & Caswell, A. H. (1986) · Biochemistry · doi:10.1021/bi00351a022 · Cited by 120
Mechanisms regulating the level of IL-2 mRNA in T lymphocytes.
Shaw, J., Meerovitch, K., Bleackley, R. C., & Paetkau, V. H. (1988) · The Journal of Immunology · doi:10.4049/jimmunol.140.7.2243 · Cited by 114
Lactate dehydrogenase and glyceraldehyde‐phosphate dehydrogenase are single‐stranded DNA‐binding proteins that affect the DNA‐polymerase‐α–primase complex
Große, F., Nasheuer, H., Scholtissek, S., & SCHOMBURG, U. (1986) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1986.tb10062.x · Cited by 110
T-cell growth factor: complete nucleotide sequence and organization of the gene in normal and malignant cells.
Holbrook, N. J., Smith, K. A., Fornace, A. J., Comeau, C. M., Wiskocil, R. L., & Crabtree, G. R. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.6.1634 · Cited by 107
Glyceraldehyde‐3‐Phosphate Dehydrogenase Is a Nonhistone Protein and a Possible Activator of Transcription in Neurons
Morgenegg, G., Winkler, G. C., Hübscher, U., Heizmann, C. W., Mous, J., & Kuenzle, C. C. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb02830.x · Cited by 106
Messenger RNA turnover in cell-free extracts
Brewer, G., & Ross, J. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)81122-b · Cited by 100
Enhanced stability of interleukin-2 mRNA in MLA 144 cells. Possible role of cytoplasmic AU-rich sequence-binding proteins.
Henics, T., Sanfridson, A., Hamilton, B. J., Nagy, E., & Rigby, W. F. C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37697-4 · Cited by 94
Self-citation
Metabolic control and structure of glycolytic enzymes. VI. Competitive inhibition of yeast glyceraldehyde 3-phosphate dehydrogenase by cyclic adenosine monophosphate, adenosine triphosphate, and other adenine-containing compounds
Yang, S. T., & Deal, W. C. (1969) · Biochemistry · doi:10.1021/bi00835a017 · Cited by 92
Immunological lesions in human uracil DNA glycosylase: association with Bloom syndrome.
Seal, G., Brech, K., Karp, S. J., Cool, B. L., & Sirover, M. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.7.2339 · Cited by 85
AU-A, an RNA-binding activity distinct from hnRNP A1, is selective for AUUUA repeats and shuttles between the nucleus and the cytoplasm
Katz, D. A., Theodorakis, N. D., Cleveland, D. W., & Lindsten, T. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.2.238 · Cited by 78
Yeast mitochondrial NAD+-dependent isocitrate dehydrogenase is an RNA-binding protein
Elzinga, S. D. J., Bednarz, A. L., van Oosterum, K., Dekker, P., & Grivell, L. A. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.23.5328 · Cited by 78
Identification of the Mammalian DNA‐Binding Protein P8 as Glyceraldehyde‐3‐Phosphate Dehydrogenase
Perucho, M., Salas, J., & Salas, M. L. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11982.x · Cited by 77
Characterization of yeast mitochondrial RNase P: an intact RNA subunit is not essential for activityin vitro
Morales, M. J., Wise, C. A., Hollingsworth, M. J., & Martín, N. C. R. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.17.6865 · Cited by 74
Antigenic probes locate binding sites for the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase on the actin monomer in microfilaments
Méjean, C., Pons, F., Benyamin, Y., & Roustan, C. (1989) · Biochemical Journal · doi:10.1042/bj2640671 · Cited by 74
Post-transcriptional regulation of granulocyte-macrophage colony-stimulating factor synthesis in murine T cells.
Bickel, M., Cohen, R. B., & Pluznik, D. H. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.145.3.840 · Cited by 72
Structural similarities in glutaminyl- and methionyl-tRNA synthetases suggest a common overall orientation of tRNA binding.
Perona, J. J., Rould, M. A., Steitz, T. A., Risler, J., Zelwer, C., & Brunie, S. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.7.2903 · Cited by 67
The M(r) 35,000 beta-adrenergic receptor mRNA-binding protein induced by agonists requires both an AUUUA pentamer and U-rich domains for RNA recognition.
Huang, L., Tholanikunnel, B. G., Vakalopoulou, E., & Malbon, C. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74456-1 · Cited by 60
Glyceraldehyde‐3‐phosphate dehydrogenase is one of the three major RNA‐binding proteins of rabbit reticulocytes
Ryazanov, A. G. (1985) · FEBS Letters · doi:10.1016/0014-5793(85)80058-2 · Cited by 60
Identification of bovine glutamate dehydrogenase as an RNA-binding protein.
Preiß, T., Hall, A. G., & Lightowlers, R. N. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74494-9 · Cited by 53
Binding of sequence-specific proteins to the adenosine- plus uridine-rich sequences of the murine granulocyte/macrophage colony-stimulating factor mRNA.
Bickel, M., Iwai, Y., Pluznik, D. H., & Cohen, R. B. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.21.10001 · Cited by 51
Translational Regulation of Human Beta Interferon mRNA: Association of the 3' AU-rich Sequence with the Poly(A) Tail Reduces Translation Efficiency in Vitro
Grafi, G., Sela, I., & Galili, G. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.6.3487 · Cited by 48
Purification of an AU-Rich RNA Binding Protein from Sarcophaga peregrina (Flesh Fly) and Its Identification as a Thiolase1
Nanbu, R., Kubo, T., Hashimoto, T., & Natori, S. (1993) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a124193 · Cited by 38
A basic isozyme of yeast glyceraldehyde-3-phosphate dehydrogenase with nucleic acid helix-destabilizing activity
Karpel, R. L., & Burchard, A. C. (1981) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(81)90180-5 · Cited by 37
Evolutionary clustering and functional similarity of RNA‐binding proteins
Fukami-Kobayashi, K., Tomoda, S., & Gō, M. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80749-k · Cited by 36
Mammalian seryl-tRNA synthetase associates with mRNA in vivo and has homology to elongation factor 1 alpha.
Miseta, A., Woodley, C. L., Greenberg, J. R., & Slobin, L. I. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54975-9 · Cited by 31
Association of AUUUA-binding Protein with A + U-rich mRNA during nucleo-cytoplasmic transport
Müller, W. E. G., Slor, H., Pfeifer, K., Hühn, P., Bek, A., Oršulić, S., Ushijima, H., & Schröder, H. C. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90628-w · Cited by 31
Cancer predisposition in bloom's syndrome
Sullivan, N. F., & Willis, A. E. (1992) · BioEssays · doi:10.1002/bies.950140508 · Cited by 12

Flagged first, then by citations

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

See all 361

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