메뉴 건너뛰기




Volumn 24, Issue 6, 2004, Pages 2352-2363

Mutations Causing Childhood Ataxia with Central Nervous System Hypomyelination Reduce Eukaryotic Initiation Factor 2B Complex Formation and Activity

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR;

EID: 1542344340     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.24.6.2352-2363.2004     Document Type: Article
Times cited : (92)

References (55)
  • 3
    • 0035890059 scopus 로고    scopus 로고
    • A novel eIF2B-dependent mechanism of translational control in yeast as a response to fusel alcohols
    • Ashe, M. P., J. W. Slaven, S. K. De Long, S. Ibrahimo, and A. B. Sachs. 2001. A novel eIF2B-dependent mechanism of translational control in yeast as a response to fusel alcohols. EMBO J. 20:6464-6474.
    • (2001) EMBO J. , vol.20 , pp. 6464-6474
    • Ashe, M.P.1    Slaven, J.W.2    De Long, S.K.3    Ibrahimo, S.4    Sachs, A.B.5
  • 4
    • 0023484186 scopus 로고
    • 5-Fluoroorotic acid as a selective agent in yeast molecular genes
    • Boeke, J. D., J. Trueheart, G. Natsoulis, and G. R. Fink. 1987. 5-Fluoroorotic acid as a selective agent in yeast molecular genes. Methods Enzymol. 154: 164-175.
    • (1987) Methods Enzymol. , vol.154 , pp. 164-175
    • Boeke, J.D.1    Trueheart, J.2    Natsoulis, G.3    Fink, G.R.4
  • 5
    • 1542368830 scopus 로고    scopus 로고
    • Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue
    • DOI 10.1074/jbc.M311055200
    • Boesen, T., S. S. Mohammad, G. D. Pavitt, and G. R. Andersen. 2004. Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue. J. Biol. Chem. DOI 10.1074/jbc.M311055200.
    • (2004) J. Biol. Chem..
    • Boesen, T.S.1    Mohammad, S.2    Pavitt, G.D.3    Andersen, G.R.4
  • 6
    • 0027411601 scopus 로고
    • Evidence that GCD6 and GCD7, translational regulators of GCN4 are subunits of the guanine nucleotide exchange factor for eIF-2 in Saccharomyces cerevisiae
    • Bushman, J. L., A. I. Asuru, R. L. Matts, and A. G. Hinnebusch. 1993. Evidence that GCD6 and GCD7, translational regulators of GCN4 are subunits of the guanine nucleotide exchange factor for eIF-2 in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:1920-1932.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1920-1932
    • Bushman, J.L.1    Asuru, A.I.2    Matts, R.L.3    Hinnebusch, A.G.4
  • 8
    • 0025853453 scopus 로고
    • Complex formation by positive and negative translational regulators of GCN4
    • Cigan, A. M., M. Foiani, E. M. Hannig, and A. G. Hinnebusch. 1991. Complex formation by positive and negative translational regulators of GCN4. Mol. Cell. Biol. 11:3217-3228.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3217-3228
    • Cigan, A.M.1    Foiani, M.2    Hannig, E.M.3    Hinnebusch, A.G.4
  • 9
    • 0036167612 scopus 로고    scopus 로고
    • Molecular pathways of protein synthesis inhibition during brain reperfusion: Implications for neuronal survival or death
    • DeGracia, D. J., R. Kumar, C. R. Owen, G. S. Krause, and B. C. White. 2002. Molecular pathways of protein synthesis inhibition during brain reperfusion: implications for neuronal survival or death. J. Cereb. Blood Flow Metab. 22:127-141.
    • (2002) J. Cereb. Blood Flow Metab. , vol.22 , pp. 127-141
    • DeGracia, D.J.1    Kumar, R.2    Owen, C.R.3    Krause, G.S.4    White, B.C.5
  • 10
    • 0037154965 scopus 로고    scopus 로고
    • Gene-specific regulation by general translation factors
    • Dever, T. E. 2002. Gene-specific regulation by general translation factors. Cell 108:545-556.
    • (2002) Cell , vol.108 , pp. 545-556
    • Dever, T.E.1
  • 11
    • 0030907057 scopus 로고    scopus 로고
    • Using GCN4 as a reporter of eIF2α phosphorylation and translational regulation in yeast
    • Dever, T. E. 1997. Using GCN4 as a reporter of eIF2α phosphorylation and translational regulation in yeast. Methods 11:403-417.
    • (1997) Methods , vol.11 , pp. 403-417
    • Dever, T.E.1
  • 13
    • 0033858459 scopus 로고    scopus 로고
    • Pathways of leucine and valine catabolism in yeast
    • Dickinson, J. R. 2000. Pathways of leucine and valine catabolism in yeast. Methods Enzymol. 324:80-92.
    • (2000) Methods Enzymol. , vol.324 , pp. 80-92
    • Dickinson, J.R.1
  • 14
    • 0033118934 scopus 로고    scopus 로고
    • Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism
    • Eaglestone, S. S., B. S. Cox, and M. F. Tuite. 1999. Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism. EMBO J. 18:1974-1981.
    • (1999) EMBO J. , vol.18 , pp. 1974-1981
    • Eaglestone, S.S.1    Cox, B.S.2    Tuite, M.F.3
  • 15
    • 0037168792 scopus 로고    scopus 로고
    • A severe variant of childhood ataxia with central hypomyelination/vanishing white matter leukoencephalopathy related to EIF21B5 mutation
    • Fogli, A., C. Dionisi-Vici, F. Deodato, A. Bartuli, O. Boespflug-Tanguy, and E. Bertini. 2002. A severe variant of childhood ataxia with central hypomyelination/vanishing white matter leukoencephalopathy related to EIF21B5 mutation. Neurology 59:1966-1968.
    • (2002) Neurology , vol.59 , pp. 1966-1968
    • Fogli, A.1    Dionisi-Vici, C.2    Deodato, F.3    Bartuli, A.4    Boespflug-Tanguy, O.5    Bertini, E.6
  • 17
    • 0025869164 scopus 로고
    • GCD2, a translational repressor of the GCN4 gene, has a general function in the initiation of protein synthesis in Saccharomyces cerevisiae
    • Foiani, M., A. M. Cigan, C. J. Paddon, S. Harashima, and A. G. Hinnebusch. 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. 11:3203-3216.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3203-3216
    • Foiani, M.1    Cigan, A.M.2    Paddon, C.J.3    Harashima, S.4    Hinnebusch, A.G.5
  • 19
    • 0037023764 scopus 로고    scopus 로고
    • A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator
    • Gelman, M. S., E. S. Kannegaard, and R. R. Kopito. 2002. A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 277:11709-11714.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11709-11714
    • Gelman, M.S.1    Kannegaard, E.S.2    Kopito, R.R.3
  • 20
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure
    • Gietz, R. D., A. R. Willems, and R. A. Woods. 1995. Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 11:355-560.
    • (1995) Yeast , vol.11 , pp. 355-560
    • Gietz, R.D.1    Willems, A.R.2    Woods, R.A.3
  • 21
    • 0036790688 scopus 로고    scopus 로고
    • Characterization of the minimal catalytic domain within eIF2B: The guanine-nucleotide exchange factor for translation initiation
    • Gomez, E., S. S. Mohammad, and G. D. Pavitt. 2002. Characterization of the minimal catalytic domain within eIF2B: the guanine-nucleotide exchange factor for translation initiation. EMBO J. 21:5292-5301.
    • (2002) EMBO J. , vol.21 , pp. 5292-5301
    • Gomez, E.1    Mohammad, S.S.2    Pavitt, G.D.3
  • 22
    • 0034024628 scopus 로고    scopus 로고
    • Identification of domains and residues within the ε subunit of eukaryotic translation initiation factor 2B (eIF2Bε) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation
    • Gomez, E., and G. D. Pavitt. 2000. Identification of domains and residues within the ε subunit of eukaryotic translation initiation factor 2B (eIF2Bε) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation. Mol. Cell. Biol. 20:3965-3976.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3965-3976
    • Gomez, E.1    Pavitt, G.D.2
  • 23
    • 0025147469 scopus 로고
    • 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
    • Hannig, E. H., N. P. Williams, R. C. Wek, and A. G. Hinnebusch. 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 126:549-562.
    • (1990) Genetics , vol.126 , pp. 549-562
    • Hannig, E.H.1    Williams, N.P.2    Wek, R.C.3    Hinnebusch, A.G.4
  • 24
    • 0023797126 scopus 로고
    • Molecular analysis of GCN3, a translational activator of GCN4: Evidence for posttranslational control of GCN3 regulatory function
    • Hannig, E. M., and A. G. Hinnebusch. 1988. Molecular analysis of GCN3, a translational activator of GCN4: evidence for posttranslational control of GCN3 regulatory function. Mol. Cell. Biol. 8:4808-4820.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4808-4820
    • Hannig, E.M.1    Hinnebusch, A.G.2
  • 25
    • 0023442680 scopus 로고
    • Interactions between positive and negative regulators of GCN4 controlling gene expression and entry into the yeast cell cycle
    • Harashima, S., E. M. Hannig, and A. G. Hinnebusch. 1987. Interactions between positive and negative regulators of GCN4 controlling gene expression and entry into the yeast cell cycle. Genetics 117:409-419.
    • (1987) Genetics , vol.117 , pp. 409-419
    • Harashima, S.1    Hannig, E.M.2    Hinnebusch, A.G.3
  • 26
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding, H. P., I. Novoa, Y. Zhang, H. Zeng, R. Wek, M. Schapira, and D. Ron. 2000. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 6:1099-1108.
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 29
    • 0002470681 scopus 로고    scopus 로고
    • Mechanism and regulation of initiator methionyl-tRNA binding to ribosomes
    • N. Sonenberg, J. W. B. Hershey, and M. B Mathews (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Hinnebusch, A. G. 2000. Mechanism and regulation of initiator methionyl-tRNA binding to ribosomes, p. 185-243. In N. Sonenberg, J. W. B. Hershey, and M. B. Mathews (ed.), Translational control of gene expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (2000) Translational Control of Gene Expression , pp. 185-243
    • Hinnebusch, A.G.1
  • 30
    • 0000729653 scopus 로고    scopus 로고
    • Translational control of GCN4: Gene-specific regulation by phosphorylation of eIF
    • J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Hinnebusch, A. G. 1996. Translational control of GCN4: gene-specific regulation by phosphorylation of eIF2, p. 199-244. In J. W. B. Hershey, M. B. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1996) Translational Control , vol.2 , pp. 199-244
    • Hinnebusch, A.G.1
  • 31
    • 0038721896 scopus 로고    scopus 로고
    • Developmental changes of eukaryotic initiation factor 2B subunits in rat hippocampus
    • Inamura, N., H. Nawa, and N. Takei. 2003. Developmental changes of eukaryotic initiation factor 2B subunits in rat hippocampus. Neurosci. Lett. 346:117-119.
    • (2003) Neurosci. Lett. , vol.346 , pp. 117-119
    • Inamura, N.1    Nawa, H.2    Takei, N.3
  • 32
    • 0025974219 scopus 로고
    • Tackling the protease problem in Saccharomyces cerevisiae
    • Jones, E. W. 1991. Tackling the protease problem in Saccharomyces cerevisiae. Methods Enzymol. 194:428-453.
    • (1991) Methods Enzymol. , vol.194 , pp. 428-453
    • Jones, E.W.1
  • 33
    • 0035130605 scopus 로고    scopus 로고
    • Update on genetic disorders affecting white matter
    • Kaye, E. M. 2001. Update on genetic disorders affecting white matter. Pediatr. Neurol. 24:11-24.
    • (2001) Pediatr. Neurol. , vol.24 , pp. 11-24
    • Kaye, E.M.1
  • 34
    • 0034960171 scopus 로고    scopus 로고
    • Tight binding of the phosphorylated α subunit of initiation factor 2 (eIF2α) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation
    • Krishnamoorthy, T., G. D. Pavitt, F. Zhang, T. E. Dever, and A. G. Hinnebusch. 2001. Tight binding of the phosphorylated α subunit of initiation factor 2 (eIF2α) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation. Mol. Cell. Biol. 21:5018-5030.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5018-5030
    • Krishnamoorthy, T.1    Pavitt, G.D.2    Zhang, F.3    Dever, T.E.4    Hinnebusch, A.G.5
  • 36
    • 1842453031 scopus 로고    scopus 로고
    • Mutations linked to leukoencephalopathy with vanishing white matter impair the function the eukaryotic initiation factor 2B complex in diverse ways
    • in press
    • Li, W., X. Wang, M. S. van der Knaap, and C. G. Proud. Mutations linked to leukoencephalopathy with vanishing white matter impair the function the eukaryotic initiation factor 2B complex in diverse ways. Mol. Cell. Biol., in press.
    • Mol. Cell. Biol.
    • Li, W.1    Wang, X.2    Van Der Knaap, M.S.3    Proud, C.G.4
  • 37
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., K. Bryson, and D. T. Jones. 2000. The PSIPRED protein structure prediction server. Bioinformatics 16:404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 38
    • 0034973590 scopus 로고    scopus 로고
    • Transcriptional profiling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast
    • Natarajan, K., M. R. Meyer, B. M. Jackson, D. Slade, C. Roberts, A. G. Hinnebusch, and M. J. Marton. 2001. Transcriptional profiling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast. Mol. Cell. Biol. 21:4347-4368.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4347-4368
    • Natarajan, K.1    Meyer, M.R.2    Jackson, B.M.3    Slade, D.4    Roberts, C.5    Hinnebusch, A.G.6    Marton, M.J.7
  • 39
    • 0032519585 scopus 로고    scopus 로고
    • eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange
    • Pavitt, G. D., K. V. Ramaiah, S. R. Kimball, and A. G. Hinnebusch. 1998. eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange. Genes Dev. 12:514-526.
    • (1998) Genes Dev. , vol.12 , pp. 514-526
    • Pavitt, G.D.1    Ramaiah, K.V.2    Kimball, S.R.3    Hinnebusch, A.G.4
  • 40
    • 0031020341 scopus 로고    scopus 로고
    • Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2
    • Pavitt, G. D., W. Yang, and A. G. Hinnebusch. 1997. Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2. Mol. Cell. Biol. 17: 1298-1313.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1298-1313
    • Pavitt, G.D.1    Yang, W.2    Hinnebusch, A.G.3
  • 41
    • 0028867333 scopus 로고
    • The heat shock and ethanol stress responses of yeast exhibit extensive similarity and functional overlap
    • Piper, P. W. 1995. The heat shock and ethanol stress responses of yeast exhibit extensive similarity and functional overlap. FEMS Microbiol. Lett. 134:121-127.
    • (1995) FEMS Microbiol. Lett. , vol.134 , pp. 121-127
    • Piper, P.W.1
  • 42
    • 0037027950 scopus 로고    scopus 로고
    • Therapeutic approaches to repair defects in DeltaF508 CFTR folding and cellular targeting
    • Powell, K., and P. L. Zeitlin. 2002. Therapeutic approaches to repair defects in DeltaF508 CFTR folding and cellular targeting. Adv. Drug Delivery Rev. 54:1395-1408.
    • (2002) Adv. Drug Delivery Rev. , vol.54 , pp. 1395-1408
    • Powell, K.1    Zeitlin, P.L.2
  • 46
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 47
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 48
    • 0346736509 scopus 로고    scopus 로고
    • Misfolded proteins are competent to mediate a subset of the responses to heat shock in Saccharomyces cerevisiae
    • Trotter, E. W., C. M. Kao, L. Berenfeld, D. Botstein, G. A. Petsko, and J. V. Gray. 2002. Misfolded proteins are competent to mediate a subset of the responses to heat shock in Saccharomyces cerevisiae. J. Biol. Chem. 277: 44817-44825.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44817-44825
    • Trotter, E.W.1    Kao, C.M.2    Berenfeld, L.3    Botstein, D.4    Petsko, G.A.5    Gray, J.V.6
  • 49
    • 0036156978 scopus 로고    scopus 로고
    • Mutations in each of the five subunits of translation initiation factor eIF2B can cause leukoencephalopathy with vanishing white matter
    • van der Knaap, M. S., P. A. Leegwater, A. A. Konst, A. Visser, S. Naidu, C. B. Oudejans, R. B. Schutgens, and J. C. Pronk. 2002. Mutations in each of the five subunits of translation initiation factor eIF2B can cause leukoencephalopathy with vanishing white matter. Ann. Neurol. 51:264-270.
    • (2002) Ann. Neurol. , vol.51 , pp. 264-270
    • Van Der Knaap, M.S.1    Leegwater, P.A.2    Konst, A.A.3    Visser, A.4    Naidu, S.5    Oudejans, C.B.6    Schutgens, R.B.7    Pronk, J.C.8
  • 50
    • 0027186435 scopus 로고
    • 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
    • Vazquez de Aldana, C. R., T. E. Dever, and A. G. Hinnebusch. 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. USA 90:7215-7219.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7215-7219
    • Vazquez De Aldana, C.R.1    Dever, T.E.2    Hinnebusch, A.G.3
  • 51
    • 0000889541 scopus 로고
    • Mutations in the GCD7 subunit of yeast guanine nucleotide exchange factor eIF-2B overcome the inhibitory effects of phosphorylated eIF-2 on translation initiation
    • Vazquez de Aldana, C. R., and A. G. Hinnebusch. 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. 14:3208-3222.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3208-3222
    • Vazquez De Aldana, C.R.1    Hinnebusch, A.G.2
  • 52
    • 0035882047 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2B: Identification of multiple phosphorylation sites in the epsilon-subunit and their functions in vivo
    • Wang, X., F. E. Paulin, L. E. Campbell, E. Gomez, K. O'Brien, N. Morrice, and C. G. Proud. 2001. Eukaryotic initiation factor 2B: identification of multiple phosphorylation sites in the epsilon-subunit and their functions in vivo. EMBO J. 20:4349-4359.
    • (2001) EMBO J. , vol.20 , pp. 4349-4359
    • Wang, X.1    Paulin, F.E.2    Campbell, L.E.3    Gomez, E.4    O'Brien, K.5    Morrice, N.6    Proud, C.G.7
  • 53
    • 0035816596 scopus 로고    scopus 로고
    • Characterization of the mammalian initiation factor eIF2B complex as a GDP dissociation stimulator protein
    • Williams, D. D., N. T. Price, A. J. Loughlin, and C. G. Proud. 2001. Characterization of the mammalian initiation factor eIF2B complex as a GDP dissociation stimulator protein. J. Biol. Chem. 276:24697-24703.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24697-24703
    • Williams, D.D.1    Price, N.T.2    Loughlin, A.J.3    Proud, C.G.4
  • 55
    • 0029805459 scopus 로고    scopus 로고
    • Identification of a regulatory subcomplex in the guanine nucleotide exchange factor eIF2B that mediates inhibition by phosphorylated eIF2
    • Yang, W., and A. G. Hinnebusch. 1996. Identification of a regulatory subcomplex in the guanine nucleotide exchange factor eIF2B that mediates inhibition by phosphorylated eIF2. Mol. Cell. Biol. 16:6603-6616.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6603-6616
    • Yang, W.1    Hinnebusch, A.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.