Uncharged tRNA Activates GCN2 by Displacing the Protein Kinase Moiety from a Bipartite tRNA-Binding Domain

Escherichia Coli and Salmonella: Typhimurium Cellular and Molecular Biology

Neidhardt, F. C., & Ingraham, J. L. (1987) · Medical Entomology and Zoology · Cited by 4,089 · see citing works

Escherichia coli and Salmonella typhimurium: Cellular and molecular biology

Lejeune, P. (1988) · Biochimie · doi:10.1016/0300-9084(88)90119-8 · Cited by 4,086 · see citing works

Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

Harding, H. P., Zhang, Y., & Ron, D. (1999) · Nature · doi:10.1038/16729 · Cited by 3,310 · see citing works

The stringent response

Cashel, M. (1996) · Medical Entomology and Zoology · Cited by 819 · see citing works

Identification and Characterization of Pancreatic Eukaryotic Initiation Factor 2 α-Subunit Kinase, PEK, Involved in Translational Control

Shi, Y., Vattem, K. M., Sood, R., An, J., Liang, J., Stramm, L. E., & Wek, R. C. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7499 · Cited by 776 · see citing works

Class II Aminoacyl Transfer Rna Synthetases: Crystal Structure of Yeast Aspartyl-trna Synthetase Complexed with tRNA Asp

Ruff, M., Krishnaswamy, S., Boeglin, M., Poterszman, A., Mitschler, A., PODJARNY, A. D., Rees, B., Thierry, J. C., & Moras, D. (1991) · Science · doi:10.1126/science.2047877 · Cited by 640 · see citing works

Aminoacyl-tRNA Synthetases: General Features and Recognition of Transfer RNAs

SCHIMMEL, P. R., & Söll, D. G. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.003125 · Cited by 633 · see citing works

The Histidyl-tRNA Synthetase-Related Sequence in the eIF-2α Protein Kinase GCN2 Interacts with tRNA and Is Required for Activation in Response to Starvation for Different Amino Acids

Wek, S. A., Zhu, S., & Wek, R. C. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.8.4497 · Cited by 487 · see citing works

Translational control

(1991) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240470805 · Cited by 433 · see citing works

Aminoacyl-tRNA synthetases

Cusack, S. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80161-3 · Cited by 381 · see citing works

A Mammalian Homologue of GCN2 Protein Kinase Important for Translational Control by Phosphorylation of Eukaryotic Initiation Factor-2α

Sood, R., Porter, A. C., Olsen, D. S., Cavener, D. R., & Wek, R. C. (2000) · Genetics · doi:10.1093/genetics/154.2.787 · Cited by 297 · see citing works

Juxtaposition of domains homologous to protein kinases and histidyl-tRNA synthetases in GCN2 protein suggests a mechanism for coupling GCN4 expression to amino acid availability.

Wek, R. C., Jackson, B. M., & Hinnebusch, A. G. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.12.4579 · Cited by 293 · see citing works

Autophosphorylation in the Activation Loop Is Required for Full Kinase Activity In Vivo of Human and Yeast Eukaryotic Initiation Factor 2α Kinases PKR and GCN2

Romano, P. R., Garcia-Barrio, M. T., Zhang, X., Wang, Q., Taylor, D. R., Zhang, F., Herring, C., Mathews, M. B., Qin, J., & Hinnebusch, A. G. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.4.2282 · Cited by 272 · see citing works

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 · see citing works

Ribosome association of GCN2 protein kinase, a translational activator of the GCN4 gene of Saccharomyces cerevisiae.

Ramírez, M., Wek, R. C., & Hinnebusch, A. G. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.6.3027 · Cited by 169 · see citing works

Translation initiation: adept at adapting

Dever, T. E. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01457-7 · Cited by 163 · see citing works

Association of GCN1–GCN20 regulatory complex with the N‐terminus of eIF2α kinase GCN2 is required for GCN2 activation

Garcia-Barrio, M. T., Dong, J., Ufano, S., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.8.1887 · Cited by 159 · see citing works

Crystal structure of histidyl‐tRNA synthetase from Escherichia coli complexed with histidyl‐adenylate.

Arnez, J. G., Harris, D. C., Mitschler, A., Rees, B., Francklyn, C. S., & Moras, D. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00088.x · Cited by 143 · see citing works

Escherichia coli formylmethionine tRNA: mutations in GGGCCC sequence conserved in anticodon stem of initiator tRNAs affect initiation of protein synthesis and conformation of anticodon loop.

Seong, B. L., & RajBhandary, U. L. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.2.334 · Cited by 142 · see citing works

7 Translational Control of GCN4: Gene-specific Regulation by Phosphorylation of elF2Preprint

Hinnebusch, A. G. (1996) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969458.30.199 · Cited by 141 · see citing works

Homologous Segments in Three Subunits of the Guanine Nucleotide Exchange Factor eIF2B Mediate Translational Regulation by Phosphorylation of eIF2

Pavitt, G. D., Yang, W., & Hinnebusch, A. G. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.3.1298 · Cited by 134 · see citing works

Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases.

Ramírez, M., Wek, R. C., de Aldana, C. R. V., et al. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5801 · Cited by 127 · see citing works

Plasmid Vectors Carrying the Replication Origin of Filamentous Single-Stranded Phages

Cesareni, G., & Murray, J. A. H. (1987) · Springer eBooks · doi:10.1007/978-1-4684-5377-5_9 · Cited by 126 · see citing works

Identification of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expression.

Wek, R. C., Ramírez, M., Jackson, B. M., et al. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.6.2820 · Cited by 119 · see citing works

Histidyl-tRNA Synthetase-related Sequences in GCN2 Protein Kinase Regulate in Vitro Phosphorylation of eIF-2

Zhu, S., Sobolev, A. Y., & Wek, R. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.40.24989 · Cited by 115 · see citing works

Functional Characterization of the RNA-binding Domain and Motif of the Double-stranded RNA-dependent Protein Kinase DAI (PKR)

Schmedt, C., Green, S. R., Manche, L., Taylor, D. R., Ma, Y., & Mathews, M. B. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0278 · Cited by 106 · see citing works

5 Protein Kinases That Phosphorylate eIF2 and eIF2B, and Their Role in Eukaryotic Cell Translational ControlPreprint

Clemens, M. J. (1996) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969458.30.139 · Cited by 100 · see citing works

Characterization of the Hemin-sensitive Eukaryotic Initiation Factor 2α Kinase from Mouse Nonerythroid Cells

Berlanga, J. J., Herrero, S., & de Haro, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.48.32340 · Cited by 90 · see citing works

Ribosome-binding Domain of Eukaryotic Initiation Factor-2 Kinase GCN2 Facilitates Translation Control

Zhu, S., & Wek, R. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.3.1808 · Cited by 76 · see citing works

Cloning and Characterization of a cDNA Encoding a Protein Synthesis Initiation Factor-2α (eIF-2α) Kinase fromDrosophila melanogaster

Santoyo‐López, J., Alcalde, J., Méndez, R., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.19.12544 · Cited by 76 · see citing works

Aminoacyl-transfer RNA populations in mammalian cells. Chromatographic profiles and patterns of codon recognition

Hatfield, D. L., Matthews, C. R., & Rice, M. (1979) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(79)90032-7 · Cited by 74 · see citing works

Dimerization by Translation Initiation Factor 2 Kinase GCN2 Is Mediated by Interactions in the C-Terminal Ribosome-Binding Region and the Protein Kinase Domain

Qiu, H., Garcia-Barrio, M. T., & Hinnebusch, A. G. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.5.2697 · Cited by 69 · see citing works

cpc-3, the Neurospora crassa Homologue of Yeast GCN2, Encodes a Polypeptide with Juxtaposed eIF2α Kinase and Histidyl-tRNA Synthetase-related Domains Required for General Amino Acid Control

Sattlegger, E., Hinnebusch, A. G., & Barthelmess, I. B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.20404 · Cited by 55 · see citing works

Isolation of the Gene Encoding the Drosophila melanogaster Homolog of the Saccharomyces cerevisiae GCN2 eIF-2α Kinase

Olsen, D. S., Jordan, B. M., Chen, D., et al. (1998) · Genetics · doi:10.1093/genetics/149.3.1495 · Cited by 52 · see citing works

tRNA Discrimination at the Binding Step by a Class II Aminoacyl-tRNA Synthetase

Bovée, M., Wen, Y., Sproat, B. S., et al. (1999) · Biochemistry · doi:10.1021/bi991182g · Cited by 36 · see citing works

Nutrient-sensing mechanisms and pathways

Efeyan, A., Comb, W. C., & Sabatini, D. M. (2015) · Nature · doi:10.1038/nature14190 · Cited by 1,110 · see citing works

Molecular mechanisms of dietary restriction promoting health and longevity

Green, C. L., Lamming, D. W., & Fontana, L. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00411-4 · Cited by 714 · see citing works

Placental Origins of Chronic Disease

Burton, G. J., Fowden, A. L., & Thornburg, K. L. (2016) · Physiological Reviews · doi:10.1152/physrev.00029.2015 · Cited by 717 · see citing works

Asparagine Plays a Critical Role in Regulating Cellular Adaptation to Glutamine Depletion

Zhang, J., Fan, J., Venneti, S., Cross, J. R., Takagi, T., Bhinder, B., Djaballah, H., Kanai, M., Cheng, E. H., Judkins, A. R., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.08.018 · Cited by 439 · see citing works

Amino acids and mTORC1: from lysosomes to disease

Efeyan, A., Zoncu, R., & Sabatini, D. M. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.05.007 · Cited by 436 · see citing works

New frontiers in translational control of the cancer genome

Truitt, M. L., & Ruggero, D. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.27 · Cited by 378 · see citing works

Glutamine synthetase is a genetic determinant of cell type-specific glutamine independence in breast epithelia

Kung, H.-N., Marks, J. R., & Chi, J.-T. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002229 · Cited by 277 · see citing works

Activation of GCN2 kinase by ribosome stalling links translation elongation with translation initiation

Ishimura, R., Nagy, G., Dotu, I., Chuang, J. H., & Ackerman, S. L. (2016) · eLife · doi:10.7554/elife.14295 · Cited by 221 · see citing works

Dual role of methionyl-tRNA synthetase in the regulation of translation and tumor suppressor activity of aminoacyl-tRNA synthetase-interacting multifunctional protein-3

Kwon, N. H., Kang, T., Lee, J. Y., Kim, H. H., Kim, H. R., Hong, J., Oh, Y. S., Han, J. M., Ku, M. J., Lee, S. Y., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103922108 · Cited by 120 · see citing works

p58IPK is an inhibitor of the eIF2α kinase GCN2 and its localization and expression underpin protein synthesis and ER processing capacity

Roobol, A., Roobol, J., Bastide, A., Knight, J. R. P., Willis, A. E., & Smales, C. M. (2015) · Biochemical Journal · doi:10.1042/bj20140852 · Cited by 50 · see citing works

Gut microbiota dysbiosis induced by brain tumors modulates the efficacy of immunotherapy

Kim, H. C., Kim, H.-J., La, J., Park, W. H., Park, S. H., Kang, B. H., Kim, Y., & Lee, H. K. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115825 · Cited by 23 · see citing works

In vivo aminoacylation of human and Xenopus suppressor tRNAs constructed by site-specific mutagenesis.

Ho, Y., & Kan, Y. W. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.8.2185 · Cited by 51 · see citing works

Determining the fidelity of tRNA aminoacylation via microarrays

Schwartz, M. H., & Pan, T. (2016) · Methods · doi:10.1016/j.ymeth.2016.09.004 · Cited by 11 · see citing works

The specificity of aminoacylation: a tRNA-tRNA interaction model

Lestienne, P. P. (1978) · Journal of Theoretical Biology · doi:10.1016/0022-5193(78)90184-4 · Cited by 13 · see citing works

Importance of structural features for tRNA(Met) identity.

Aphasizhev, R., Senger, B., & Fasiolo, F. (1997) · PubMed · Cited by 13 · see citing works

The C-Terminal Domain of the Archaeal Leucyl-tRNA Synthetase Prevents Misediting of Isoleucyl-tRNAIle

Fukunaga, R., & Yokoyama, S. (2007) · Biochemistry · doi:10.1021/bi6024935 · Cited by 15 · see citing works