Literature Help
GCD2 / YGR083C Literature
All manually curated literature for the specified gene, organized by relevance to the gene and by
association with specific annotations to the gene in SGD. SGD gathers references via a PubMed search for
papers whose titles or abstracts contain “yeast” or “cerevisiae;” these papers are reviewed manually and
linked to relevant genes and literature topics by SGD curators.
- Unique References
- 128
- Aliases
-
GCD12
9
13
Primary Literature
Literature that either focuses on the gene or contains information about function, biological role,
cellular location, phenotype, regulation, structure, or disease homologs in other species for the gene
or gene product.
No primary literature curated.
Download References (.nbib)
- Gordiyenko Y, et al. (2019) Structural basis for the inhibition of translation through eIF2α phosphorylation. Nat Commun 10(1):2640 PMID:31201334
- Moon SL and Parker R (2018) Analysis of eIF2B bodies and their relationships with stress granules and P-bodies. Sci Rep 8(1):12264 PMID:30115954
- Li H, et al. (2016) Data on dynamic study of cytoophidia in Saccharomyces cerevisiae. Data Brief 8:40-4 PMID:27274529
- Yofe I, et al. (2016) One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. Nat Methods 13(4):371-378 PMID:26928762
- Beilsten-Edmands V, et al. (2015) eIF2 interactions with initiator tRNA and eIF2B are regulated by post-translational modifications and conformational dynamics. Cell Discov 1:15020 PMID:27462419
- Gordiyenko Y, et al. (2014) eIF2B is a decameric guanine nucleotide exchange factor with a γ2ε2 tetrameric core. Nat Commun 5:3902 PMID:24852487
- Jennings MD, et al. (2013) eIF2B promotes eIF5 dissociation from eIF2*GDP to facilitate guanine nucleotide exchange for translation initiation. Genes Dev 27(24):2696-707 PMID:24352424
- Reid PJ, et al. (2012) Identification of intersubunit domain interactions within eukaryotic initiation factor (eIF) 2B, the nucleotide exchange factor for translation initiation. J Biol Chem 287(11):8275-85 PMID:22238343
- Dev K, et al. (2010) The beta/Gcd7 subunit of eukaryotic translation initiation factor 2B (eIF2B), a guanine nucleotide exchange factor, is crucial for binding eIF2 in vivo. Mol Cell Biol 30(21):5218-33 PMID:20805354
- Noree C, et al. (2010) Identification of novel filament-forming proteins in Saccharomyces cerevisiae and Drosophila melanogaster. J Cell Biol 190(4):541-51 PMID:20713603
- Taylor EJ, et al. (2010) Fusel alcohols regulate translation initiation by inhibiting eIF2B to reduce ternary complex in a mechanism that may involve altering the integrity and dynamics of the eIF2B body. Mol Biol Cell 21(13):2202-16 PMID:20444979
- Dev K, et al. (2009) Archaeal aIF2B interacts with eukaryotic translation initiation factors eIF2alpha and eIF2Balpha: Implications for aIF2B function and eIF2B regulation. J Mol Biol 392(3):701-22 PMID:19616556
- Hiyama TB, et al. (2009) Crystal structure of the alpha subunit of human translation initiation factor 2B. J Mol Biol 392(4):937-51 PMID:19631657
- Dey M, et al. (2005) PKR and GCN2 kinases and guanine nucleotide exchange factor eukaryotic translation initiation factor 2B (eIF2B) recognize overlapping surfaces on eIF2alpha. Mol Cell Biol 25(8):3063-75 PMID:15798194
- Hinnebusch AG, et al. (2004) Study of translational control of eukaryotic gene expression using yeast. Ann N Y Acad Sci 1038:60-74 PMID:15838098
- Cuesta R, et al. (1998) Identification of GCD14 and GCD15, novel genes required for translational repression of GCN4 mRNA in Saccharomyces cerevisiae. Genetics 148(3):1007-20 PMID:9539420
- Pavitt GD, et al. (1998) eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange. Genes Dev 12(4):514-26 PMID:9472020
- Pavitt GD, et al. (1997) Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2. Mol Cell Biol 17(3):1298-313 PMID:9032257
- Yang W and Hinnebusch AG (1996) Identification of a regulatory subcomplex in the guanine nucleotide exchange factor eIF2B that mediates inhibition by phosphorylated eIF2. Mol Cell Biol 16(11):6603-16 PMID:8887689
- Dever TE, et al. (1995) Modulation of tRNA(iMet), eIF-2, and eIF-2B expression shows that GCN4 translation is inversely coupled to the level of eIF-2.GTP.Met-tRNA(iMet) ternary complexes. Mol Cell Biol 15(11):6351-63 PMID:7565788
- Vazquez de Aldana CR and Hinnebusch AG (1994) Mutations in the GCD7 subunit of yeast guanine nucleotide exchange factor eIF-2B overcome the inhibitory effects of phosphorylated eIF-2 on translation initiation. Mol Cell Biol 14(5):3208-22 PMID:8164676
- Bushman JL, et al. (1993) Guanine nucleotide exchange factor for eukaryotic translation initiation factor 2 in Saccharomyces cerevisiae: interactions between the essential subunits GCD2, GCD6, and GCD7 and the regulatory subunit GCN3. Mol Cell Biol 13(8):4618-31 PMID:8336705
- Cigan AM, et al. (1993) A protein complex of translational regulators of GCN4 mRNA is the guanine nucleotide-exchange factor for translation initiation factor 2 in yeast. Proc Natl Acad Sci U S A 90(11):5350-4 PMID:8506384
- Cigan AM, et al. (1991) Complex formation by positive and negative translational regulators of GCN4. Mol Cell Biol 11(6):3217-28 PMID:2038327
- Foiani M, et al. (1991) GCD2, a translational repressor of the GCN4 gene, has a general function in the initiation of protein synthesis in Saccharomyces cerevisiae. Mol Cell Biol 11(6):3203-16 PMID:2038326
- Hannig EM, et al. (1990) The translational activator GCN3 functions downstream from GCN1 and GCN2 in the regulatory pathway that couples GCN4 expression to amino acid availability in Saccharomyces cerevisiae. Genetics 126(3):549-62 PMID:2249755
- Paddon CJ and Hinnebusch AG (1989) gcd12 mutations are gcn3-dependent alleles of GCD2, a negative regulator of GCN4 in the general amino acid control of Saccharomyces cerevisiae. Genetics 122(3):543-50 PMID:2668116
- Paddon CJ, et al. (1989) Amino acid sequence similarity between GCN3 and GCD2, positive and negative translational regulators of GCN4: evidence for antagonism by competition. Genetics 122(3):551-9 PMID:2668117
- Hannig EM and Hinnebusch AG (1988) Molecular analysis of GCN3, a translational activator of GCN4: evidence for posttranslational control of GCN3 regulatory function. Mol Cell Biol 8(11):4808-20 PMID:3062370
- Harashima S, et al. (1987) Interactions between positive and negative regulators of GCN4 controlling gene expression and entry into the yeast cell cycle. Genetics 117(3):409-19 PMID:3319768
- Mueller PP, et al. (1987) A segment of GCN4 mRNA containing the upstream AUG codons confers translational control upon a heterologous yeast transcript. Proc Natl Acad Sci U S A 84(9):2863-7 PMID:3554249
- Harashima S and Hinnebusch AG (1986) Multiple GCD genes required for repression of GCN4, a transcriptional activator of amino acid biosynthetic genes in Saccharomyces cerevisiae. Mol Cell Biol 6(11):3990-8 PMID:3540603
- Niederberger P, et al. (1986) Identification and characterization of four new GCD genes in Saccharomyces cerevisiae. Curr Genet 10(9):657-64 PMID:3329041
Related Literature
Genes that share literature (indicated by the purple circles) with the specified gene (indicated by yellow circle).
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Additional Literature
Papers that show experimental evidence for the gene or describe homologs in other species, but
for which the gene is not the paper’s principal focus.
No additional literature curated.
Download References (.nbib)
- Lanz MC, et al. (2021) In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Rep 22(2):e51121 PMID:33491328
- Nüske E, et al. (2020) Filament formation by the translation factor eIF2B regulates protein synthesis in starved cells. Biol Open 9(7) PMID:32554487
- Menconi G, et al. (2015) Global mapping of DNA conformational flexibility on Saccharomyces cerevisiae. PLoS Comput Biol 11(4):e1004136 PMID:25860149
- Liu Z, et al. (2014) Improved production of a heterologous amylase in Saccharomyces cerevisiae by inverse metabolic engineering. Appl Environ Microbiol 80(17):5542-50 PMID:24973076
- Browne CM, et al. (2013) The yeast eukaryotic translation initiation factor 2B translation initiation complex interacts with the fatty acid synthesis enzyme YBR159W and endoplasmic reticulum membranes. Mol Cell Biol 33(5):1041-56 PMID:23263984
- Jung PP, et al. (2011) Ploidy influences cellular responses to gross chromosomal rearrangements in Saccharomyces cerevisiae. BMC Genomics 12:331 PMID:21711526
- Rosenfeld AB and Racaniello VR (2010) Components of the multifactor complex needed for internal initiation by the IRES of hepatitis C virus in Saccharomyces cerevisiae. RNA Biol 7(5):596-605 PMID:20935471
- Watanabe R, et al. (2010) The eukaryotic initiation factor (eIF) 4G HEAT domain promotes translation re-initiation in yeast both dependent on and independent of eIF4A mRNA helicase. J Biol Chem 285(29):21922-33 PMID:20463023
- Nanda JS, et al. (2009) eIF1 controls multiple steps in start codon recognition during eukaryotic translation initiation. J Mol Biol 394(2):268-85 PMID:19751744
- Breslow DK, et al. (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8 PMID:18622397
- Kito K, et al. (2008) Discrimination between stable and dynamic components of protein complexes by means of quantitative proteomics. Proteomics 8(12):2366-70 PMID:18563728
- Campbell SG and Ashe MP (2007) An approach to studying the localization and dynamics of eukaryotic translation factors in live yeast cells. Methods Enzymol 431:33-45 PMID:17923229
- Kito K, et al. (2007) A synthetic protein approach toward accurate mass spectrometric quantification of component stoichiometry of multiprotein complexes. J Proteome Res 6(2):792-800 PMID:17269735
- Singh CR, et al. (2007) Change in nutritional status modulates the abundance of critical pre-initiation intermediate complexes during translation initiation in vivo. J Mol Biol 370(2):315-30 PMID:17512538
- Singh CR, et al. (2006) An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation. EMBO J 25(19):4537-46 PMID:16990799
- Campbell SG, et al. (2005) Dynamic cycling of eIF2 through a large eIF2B-containing cytoplasmic body: implications for translation control. J Cell Biol 170(6):925-34 PMID:16157703
- Flaherty P, et al. (2005) A latent variable model for chemogenomic profiling. Bioinformatics 21(15):3286-93 PMID:15919724
- Richardson JP, et al. (2004) Mutations causing childhood ataxia with central nervous system hypomyelination reduce eukaryotic initiation factor 2B complex formation and activity. Mol Cell Biol 24(6):2352-63 PMID:14993275
- Erickson FL, et al. (2001) Minimum requirements for the function of eukaryotic translation initiation factor 2. Genetics 158(1):123-32 PMID:11333223
- Krishnamoorthy T, et al. (2001) Tight binding of the phosphorylated alpha subunit of initiation factor 2 (eIF2alpha) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation. Mol Cell Biol 21(15):5018-30 PMID:11438658
- Linder P, et al. (1999) A systematic nomenclature for new translation initiation factor genes from S. pombe and other fungi. Yeast 15(10A):865-72 PMID:10407266
- Price NT, et al. (1996) eIF2B, the guanine nucleotide-exchange factor for eukaryotic initiation factor 2. Sequence conservation between the alpha, beta and delta subunits of eIF2B from mammals and yeast. Biochem J 318 ( Pt 2)(Pt 2):637-43 PMID:8929216
- Ohtake Y and Wickner RB (1995) Yeast virus propagation depends critically on free 60S ribosomal subunit concentration. Mol Cell Biol 15(5):2772-81 PMID:7739558
- Henderson RA, et al. (1994) The delta-subunit of murine guanine nucleotide exchange factor eIF-2B. Characterization of cDNAs predicts isoforms differing at the amino-terminal end. J Biol Chem 269(48):30517-23 PMID:7982969
- Vazquez de Aldana CR, et al. (1993) Mutations in the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2 alpha) that overcome the inhibitory effect of eIF-2 alpha phosphorylation on translation initiation. Proc Natl Acad Sci U S A 90(15):7215-9 PMID:8102207
- Holmberg S and Petersen JG (1988) Regulation of isoleucine-valine biosynthesis in Saccharomyces cerevisiae. Curr Genet 13(3):207-17 PMID:3289762
Reviews
No reviews curated.
Download References (.nbib)
- Merrick WC and Pavitt GD (2018) Protein Synthesis Initiation in Eukaryotic Cells. Cold Spring Harb Perspect Biol 10(12) PMID:29735639
- Dever TE, et al. (2016) Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae. Genetics 203(1):65-107 PMID:27183566
- Liu JL (2016) The Cytoophidium and Its Kind: Filamentation and Compartmentation of Metabolic Enzymes. Annu Rev Cell Dev Biol 32:349-372 PMID:27362644
- Wortham NC and Proud CG (2015) eIF2B: recent structural and functional insights into a key regulator of translation. Biochem Soc Trans 43(6):1234-40 PMID:26614666
- Carcamo WC, et al. (2014) Molecular cell biology and immunobiology of mammalian rod/ring structures. Int Rev Cell Mol Biol 308:35-74 PMID:24411169
- Immanuel TM, et al. (2012) A critical review of translation initiation factor eIF2α kinases in plants - regulating protein synthesis during stress. Funct Plant Biol 39(9):717-735 PMID:32480823
- Morano KA, et al. (2012) The response to heat shock and oxidative stress in Saccharomyces cerevisiae. Genetics 190(4):1157-95 PMID:22209905
- Simpson CE and Ashe MP (2012) Adaptation to stress in yeast: to translate or not? Biochem Soc Trans 40(4):794-9 PMID:22817736
- Yi C and Pan T (2011) Cellular dynamics of RNA modification. Acc Chem Res 44(12):1380-8 PMID:21615108
- Mohammad-Qureshi SS, et al. (2007) Purification of FLAG-tagged eukaryotic initiation factor 2B complexes, subcomplexes, and fragments from Saccharomyces cerevisiae. Methods Enzymol 431:1-13 PMID:17923227
- Campbell SG and Ashe MP (2006) Localization of the translational guanine nucleotide exchange factor eIF2B: a common theme for GEFs? Cell Cycle 5(7):678-80 PMID:16582624
- Hinnebusch AG (2005) Translational regulation of GCN4 and the general amino acid control of yeast. Annu Rev Microbiol 59:407-50 PMID:16153175
- Holcik M and Sonenberg N (2005) Translational control in stress and apoptosis. Nat Rev Mol Cell Biol 6(4):318-27 PMID:15803138
- Pavitt GD (2005) eIF2B, a mediator of general and gene-specific translational control. Biochem Soc Trans 33(Pt 6):1487-92 PMID:16246152
- Proud CG (2005) eIF2 and the control of cell physiology. Semin Cell Dev Biol 16(1):3-12 PMID:15659334
- Dever TE (2002) Gene-specific regulation by general translation factors. Cell 108(4):545-56 PMID:11909525
- Ganoza MC, et al. (2002) Evolutionary conservation of reactions in translation. Microbiol Mol Biol Rev 66(3):460-85, table of contents PMID:12209000
- McCarthy JE (1998) Posttranscriptional control of gene expression in yeast. Microbiol Mol Biol Rev 62(4):1492-553 PMID:9841679
- Hinnebusch AG (1997) Translational regulation of yeast GCN4. A window on factors that control initiator-trna binding to the ribosome. J Biol Chem 272(35):21661-4 PMID:9268289
- Hinnebusch AG (1994) Translational control of GCN4: an in vivo barometer of initiation-factor activity. Trends Biochem Sci 19(10):409-14 PMID:7817398
- Pain VM (1994) Translational control during amino acid starvation. Biochimie 76(8):718-28 PMID:7893822
- Price N and Proud C (1994) The guanine nucleotide-exchange factor, eIF-2B. Biochimie 76(8):748-60 PMID:7893825
- Hinnebusch A (1992) "General and Pathway-specific Regulatory Mechanisms Controlling the Synthesis of Amino Acid Biosynthetic Enzymes in Saccharomyces cerevisiae". Pp. 319-414 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression, edited by Jones EW, Pringle JR and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
- Lindahl L and Hinnebusch A (1992) Diversity of mechanisms in the regulation of translation in prokaryotes and lower eukaryotes. Curr Opin Genet Dev 2(5):720-6 PMID:1281027
Gene Ontology Literature
Paper(s) associated with one or more GO (Gene Ontology) terms in SGD for the specified gene.
No gene ontology literature curated.
Download References (.nbib)
- Yofe I, et al. (2016) One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. Nat Methods 13(4):371-378 PMID:26928762
- Pavitt GD, et al. (1997) Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2. Mol Cell Biol 17(3):1298-313 PMID:9032257
- Yang W and Hinnebusch AG (1996) Identification of a regulatory subcomplex in the guanine nucleotide exchange factor eIF2B that mediates inhibition by phosphorylated eIF2. Mol Cell Biol 16(11):6603-16 PMID:8887689
- Vazquez de Aldana CR and Hinnebusch AG (1994) Mutations in the GCD7 subunit of yeast guanine nucleotide exchange factor eIF-2B overcome the inhibitory effects of phosphorylated eIF-2 on translation initiation. Mol Cell Biol 14(5):3208-22 PMID:8164676
- Bushman JL, et al. (1993) Guanine nucleotide exchange factor for eukaryotic translation initiation factor 2 in Saccharomyces cerevisiae: interactions between the essential subunits GCD2, GCD6, and GCD7 and the regulatory subunit GCN3. Mol Cell Biol 13(8):4618-31 PMID:8336705
- Cigan AM, et al. (1993) A protein complex of translational regulators of GCN4 mRNA is the guanine nucleotide-exchange factor for translation initiation factor 2 in yeast. Proc Natl Acad Sci U S A 90(11):5350-4 PMID:8506384
- Foiani M, et al. (1991) GCD2, a translational repressor of the GCN4 gene, has a general function in the initiation of protein synthesis in Saccharomyces cerevisiae. Mol Cell Biol 11(6):3203-16 PMID:2038326
Phenotype Literature
Paper(s) associated with one or more pieces of classical phenotype evidence in SGD for the specified gene.
No phenotype literature curated.
Disease Literature
Paper(s) associated with one or more pieces of disease evidence in SGD, as found on the Disease page.
No disease literature curated.
Interaction Literature
Paper(s) associated with evidence supporting a physical or genetic interaction between the
specified gene and another gene in SGD. Currently, all interaction evidence is obtained from
BioGRID.
No interaction literature curated.
Download References (.nbib)
- Bertgen L, et al. (2024) Distinct types of intramitochondrial protein aggregates protect mitochondria against proteotoxic stress. Cell Rep 43(4):114018 PMID:38551959
- Marmorale LJ, et al. (2024) Fast-evolving cofactors regulate the role of HEATR5 complexes in intra-Golgi trafficking. J Cell Biol 223(3) PMID:38240799
- O'Brien MJ and Ansari A (2024) Protein interaction network revealed by quantitative proteomic analysis links TFIIB to multiple aspects of the transcription cycle. Biochim Biophys Acta Proteins Proteom 1872(1):140968 PMID:37863410
- Sekiguchi T, et al. (2024) Interaction between Gtr2p and ribosomal Rps31p affects the incorporation of Rps31p into ribosomes of Saccharomyces cerevisiae. Biochem Biophys Res Commun 699:149499 PMID:38281328
- Choudhry SK, et al. (2023) Nuclear pore complexes mediate subtelomeric gene silencing by regulating PCNA levels on chromatin. J Cell Biol 222(9) PMID:37358474
- Michaelis AC, et al. (2023) The social and structural architecture of the yeast protein interactome. Nature 624(7990):192-200 PMID:37968396
- Gavade JN, et al. (2022) Identification of 14-3-3 proteins, Polo kinase, and RNA-binding protein Pes4 as key regulators of meiotic commitment in budding yeast. Curr Biol 32(7):1534-1547.e9 PMID:35240051
- Lehner MH, et al. (2022) Yeast Smy2 and its human homologs GIGYF1 and -2 regulate Cdc48/VCP function during transcription stress. Cell Rep 41(4):111536 PMID:36288698
- Mattingly M, et al. (2022) Mediator recruits the cohesin loader Scc2 to RNA Pol II-transcribed genes and promotes sister chromatid cohesion. Curr Biol 32(13):2884-2896.e6 PMID:35654035
- Chang Y, et al. (2021) Analysis of the TORC1 interactome reveals a spatially distinct function of TORC1 in mRNP complexes. J Cell Biol 220(4) PMID:33566094
- Rössler I, et al. (2019) Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME. Nucleic Acids Res 47(13):6984-7002 PMID:31062022
- Izawa T, et al. (2017) Cytosolic Protein Vms1 Links Ribosome Quality Control to Mitochondrial and Cellular Homeostasis. Cell 171(4):890-903.e18 PMID:29107329
- Jungfleisch J, et al. (2017) A novel translational control mechanism involving RNA structures within coding sequences. Genome Res 27(1):95-106 PMID:27821408
- Costanzo M, et al. (2016) A global genetic interaction network maps a wiring diagram of cellular function. Science 353(6306) PMID:27708008
- Lakshminarasimhan M, et al. (2016) Proteomic and Genomic Analyses of the Rvb1 and Rvb2 Interaction Network upon Deletion of R2TP Complex Components. Mol Cell Proteomics 15(3):960-74 PMID:26831523
- Kırlı K, et al. (2015) A deep proteomics perspective on CRM1-mediated nuclear export and nucleocytoplasmic partitioning. Elife 4 PMID:26673895
- Gordiyenko Y, et al. (2014) eIF2B is a decameric guanine nucleotide exchange factor with a γ2ε2 tetrameric core. Nat Commun 5:3902 PMID:24852487
- Browne CM, et al. (2013) The yeast eukaryotic translation initiation factor 2B translation initiation complex interacts with the fatty acid synthesis enzyme YBR159W and endoplasmic reticulum membranes. Mol Cell Biol 33(5):1041-56 PMID:23263984
- Mitchell SF, et al. (2013) Global analysis of yeast mRNPs. Nat Struct Mol Biol 20(1):127-33 PMID:23222640
- van Pel DM, et al. (2013) Saccharomyces cerevisiae genetics predicts candidate therapeutic genetic interactions at the mammalian replication fork. G3 (Bethesda) 3(2):273-82 PMID:23390603
- Reid PJ, et al. (2012) Identification of intersubunit domain interactions within eukaryotic initiation factor (eIF) 2B, the nucleotide exchange factor for translation initiation. J Biol Chem 287(11):8275-85 PMID:22238343
- Costanzo M, et al. (2010) The genetic landscape of a cell. Science 327(5964):425-31 PMID:20093466
- Dev K, et al. (2010) The beta/Gcd7 subunit of eukaryotic translation initiation factor 2B (eIF2B), a guanine nucleotide exchange factor, is crucial for binding eIF2 in vivo. Mol Cell Biol 30(21):5218-33 PMID:20805354
- Batisse J, et al. (2009) Purification of nuclear poly(A)-binding protein Nab2 reveals association with the yeast transcriptome and a messenger ribonucleoprotein core structure. J Biol Chem 284(50):34911-7 PMID:19840948
- Kito K, et al. (2008) Discrimination between stable and dynamic components of protein complexes by means of quantitative proteomics. Proteomics 8(12):2366-70 PMID:18563728
- Tarassov K, et al. (2008) An in vivo map of the yeast protein interactome. Science 320(5882):1465-70 PMID:18467557
- Gavin AC, et al. (2006) Proteome survey reveals modularity of the yeast cell machinery. Nature 440(7084):631-6 PMID:16429126
- Krogan NJ, et al. (2006) Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440(7084):637-43 PMID:16554755
- Krogan NJ, et al. (2004) High-definition macromolecular composition of yeast RNA-processing complexes. Mol Cell 13(2):225-39 PMID:14759368
- Gavin AC, et al. (2002) Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415(6868):141-7 PMID:11805826
- Ho Y, et al. (2002) Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415(6868):180-3 PMID:11805837
- Ito T, et al. (2001) A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc Natl Acad Sci U S A 98(8):4569-74 PMID:11283351
- Gomez E and Pavitt GD (2000) Identification of domains and residues within the epsilon subunit of eukaryotic translation initiation factor 2B (eIF2Bepsilon) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation. Mol Cell Biol 20(11):3965-76 PMID:10805739
- Nika J, et al. (2000) Purification and kinetic analysis of eIF2B from Saccharomyces cerevisiae. J Biol Chem 275(34):26011-7 PMID:10852917
- Pavitt GD, et al. (1998) eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange. Genes Dev 12(4):514-26 PMID:9472020
- Pavitt GD, et al. (1997) Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2. Mol Cell Biol 17(3):1298-313 PMID:9032257
- Yang W and Hinnebusch AG (1996) Identification of a regulatory subcomplex in the guanine nucleotide exchange factor eIF2B that mediates inhibition by phosphorylated eIF2. Mol Cell Biol 16(11):6603-16 PMID:8887689
- Vazquez de Aldana CR and Hinnebusch AG (1994) Mutations in the GCD7 subunit of yeast guanine nucleotide exchange factor eIF-2B overcome the inhibitory effects of phosphorylated eIF-2 on translation initiation. Mol Cell Biol 14(5):3208-22 PMID:8164676
- Bushman JL, et al. (1993) Guanine nucleotide exchange factor for eukaryotic translation initiation factor 2 in Saccharomyces cerevisiae: interactions between the essential subunits GCD2, GCD6, and GCD7 and the regulatory subunit GCN3. Mol Cell Biol 13(8):4618-31 PMID:8336705
- Cigan AM, et al. (1993) A protein complex of translational regulators of GCN4 mRNA is the guanine nucleotide-exchange factor for translation initiation factor 2 in yeast. Proc Natl Acad Sci U S A 90(11):5350-4 PMID:8506384
- Cigan AM, et al. (1991) Complex formation by positive and negative translational regulators of GCN4. Mol Cell Biol 11(6):3217-28 PMID:2038327
- Paddon CJ and Hinnebusch AG (1989) gcd12 mutations are gcn3-dependent alleles of GCD2, a negative regulator of GCN4 in the general amino acid control of Saccharomyces cerevisiae. Genetics 122(3):543-50 PMID:2668116
- Harashima S, et al. (1987) Interactions between positive and negative regulators of GCN4 controlling gene expression and entry into the yeast cell cycle. Genetics 117(3):409-19 PMID:3319768
- Harashima S and Hinnebusch AG (1986) Multiple GCD genes required for repression of GCN4, a transcriptional activator of amino acid biosynthetic genes in Saccharomyces cerevisiae. Mol Cell Biol 6(11):3990-8 PMID:3540603
- Niederberger P, et al. (1986) Identification and characterization of four new GCD genes in Saccharomyces cerevisiae. Curr Genet 10(9):657-64 PMID:3329041
Regulation Literature
Paper(s) associated with one or more pieces of regulation evidence in SGD, as found on the
Regulation page.
No regulation literature curated.
Post-translational Modifications Literature
Paper(s) associated with one or more pieces of post-translational modifications evidence in SGD.
No post-translational modifications literature curated.
Download References (.nbib)
- Leutert M, et al. (2023) The regulatory landscape of the yeast phosphoproteome. Nat Struct Mol Biol 30(11):1761-1773 PMID:37845410
- Lanz MC, et al. (2021) In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Rep 22(2):e51121 PMID:33491328
- Zhou X, et al. (2021) Cross-compartment signal propagation in the mitotic exit network. Elife 10 PMID:33481703
- MacGilvray ME, et al. (2020) Phosphoproteome Response to Dithiothreitol Reveals Unique Versus Shared Features of Saccharomyces cerevisiae Stress Responses. J Proteome Res 19(8):3405-3417 PMID:32597660
- Swaney DL, et al. (2013) Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nat Methods 10(7):676-82 PMID:23749301
High-Throughput Literature
Paper(s) associated with one or more pieces of high-throughput evidence in SGD.
No high-throughput literature curated.
Download References (.nbib)
- Forster DT, et al. (2022) BIONIC: biological network integration using convolutions. Nat Methods 19(10):1250-1261 PMID:36192463
- Nicastro R, et al. (2021) Indole-3-acetic acid is a physiological inhibitor of TORC1 in yeast. PLoS Genet 17(3):e1009414 PMID:33690632
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