메뉴 건너뛰기




Volumn 36, Issue 4, 2008, Pages 658-664

Clues to the mechanism of action of eIF2B, the guanine-nucleotide-exchange factor for translation initiation

Author keywords

Childhood ataxia with central nervous system hypomyelination (CACH); Eukaryotic initiation factor 2B (eIF2B); G protein; Guanine nucleotide exchange factor (GEF); Leukoencephalopathy with vanishing white matter (VWM); Translation initiation

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 1; ALANINE; ASPARTIC ACID; ELONGATION FACTOR TU; GLUTAMIC ACID; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; INITIATION FACTOR 2; INITIATION FACTOR 5; LEUCINE; MESSENGER RNA; METHIONINE TRANSFER RNA; SERINE; THREONINE; TRANSCRIPTION FACTOR GCN4; TRYPTOPHAN;

EID: 49349090915     PISSN: 03005127     EISSN: None     Source Type: Journal    
DOI: 10.1042/BST0360658     Document Type: Review
Times cited : (21)

References (47)
  • 1
    • 3943080710 scopus 로고    scopus 로고
    • The molecular mechanics of eukaryotic translation
    • Kapp, L.D. and Lorsch, J.R. (2004) The molecular mechanics of eukaryotic translation. Annu. Rev. Biochem. 73, 657-704
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 657-704
    • Kapp, L.D.1    Lorsch, J.R.2
  • 2
    • 28844478867 scopus 로고    scopus 로고
    • eIF2B, a mediator of general and gene-specific translational control
    • Pavitt, G.D. (2005) eIF2B, a mediator of general and gene-specific translational control. Biochem. Soc. Trans. 33, 1487-1492
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 1487-1492
    • Pavitt, G.D.1
  • 3
    • 12344305214 scopus 로고    scopus 로고
    • eIF2 and the control of cell physiology
    • Proud, C.G. (2005) eIF2 and the control of cell physiology. Semin. Cell Dev. Biol. 16, 3-12
    • (2005) Semin. Cell Dev. Biol , vol.16 , pp. 3-12
    • Proud, C.G.1
  • 4
    • 36748999400 scopus 로고    scopus 로고
    • New modes of translational control in development, behavior, and disease
    • Sonenberg, N. and Hinnebusch, A.G. (2007) New modes of translational control in development, behavior, and disease. Mol. Cell 28, 721-729
    • (2007) Mol. Cell , vol.28 , pp. 721-729
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 5
    • 27144510561 scopus 로고    scopus 로고
    • Translational regulation of GCN4 and the general amino acid control of yeast
    • Hinnebusch, A.G. (2005) Translational regulation of GCN4 and the general amino acid control of yeast. Annu. Rev. Microbiol. 59, 407-450
    • (2005) Annu. Rev. Microbiol , vol.59 , pp. 407-450
    • Hinnebusch, A.G.1
  • 6
    • 3843117589 scopus 로고    scopus 로고
    • Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells
    • Vattem, K.M. and Wek, R.C. (2004) Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells. Proc. Natl. Acad. Sci. U.S.A. 101, 11269-11274
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 11269-11274
    • Vattem, K.M.1    Wek, R.C.2
  • 7
    • 5044229348 scopus 로고    scopus 로고
    • molecular mechanisms of translational control
    • Gebauer, F. and Hentze, M.W. (2004) molecular mechanisms of translational control. Nat. Rev. Mol. Cell Biol. 5, 827-835
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 827-835
    • Gebauer, F.1    Hentze, M.W.2
  • 8
    • 32544438040 scopus 로고    scopus 로고
    • The large spectrum of eIF2B-related diseases
    • Fogli, A. and Boespflug-Tanguy, O. (2006) The large spectrum of eIF2B-related diseases. Biochem. Soc. Trans. 34, 22-29
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 22-29
    • Fogli, A.1    Boespflug-Tanguy, O.2
  • 9
    • 33646043141 scopus 로고    scopus 로고
    • Childhood ataxia with CNS hypomyelination/vanishing white matter disease: A common leukodystrophy caused by abnormal control of protein synthesis
    • Schiffmann, R. and Elroy-Stein, O. (2006) Childhood ataxia with CNS hypomyelination/vanishing white matter disease: a common leukodystrophy caused by abnormal control of protein synthesis. Mol. Genet, Metab. 88, 7-15
    • (2006) Mol. Genet, Metab , vol.88 , pp. 7-15
    • Schiffmann, R.1    Elroy-Stein, O.2
  • 12
    • 1542344340 scopus 로고    scopus 로고
    • Mutations causing childhood ataxia with central nervous system hypomyelination reduce eukaryotic initiation factor 2B complex formation and activity
    • Richardson, J.P., Mohammad, S.S. and Pavitt, G.D. (2004) Mutations causing childhood ataxia with central nervous system hypomyelination reduce eukaryotic initiation factor 2B complex formation and activity. Mol. Cell. Biol. 24, 2352-2363
    • (2004) Mol. Cell. Biol , vol.24 , pp. 2352-2363
    • Richardson, J.P.1    Mohammad, S.S.2    Pavitt, G.D.3
  • 13
    • 1842453031 scopus 로고    scopus 로고
    • Mutations linked to leukoencephalopathy with vanishing white matter impair the function of the eukaryotic initiation factor 2B complex in diverse ways
    • Li, W., Wang, X., van der Knaap, M.S. and Proud, C.G. (2004) Mutations linked to leukoencephalopathy with vanishing white matter impair the function of the eukaryotic initiation factor 2B complex in diverse ways. Mol. Cell. Biol. 24, 3295-3306
    • (2004) Mol. Cell. Biol , vol.24 , pp. 3295-3306
    • Li, W.1    Wang, X.2    van der Knaap, M.S.3    Proud, C.G.4
  • 14
    • 33646068185 scopus 로고    scopus 로고
    • Heightened stress response in primary fibroblasts expressing mutant eIF2B genes from CACH/VWM leukodystrophy patients
    • Kantor, L., Harding, H.P., Ron, D., Schiffmann, R., Kaneski, C.R, Kimball, S.R. and Elroy-Stein, O. (2005) Heightened stress response in primary fibroblasts expressing mutant eIF2B genes from CACH/VWM leukodystrophy patients. Hum. Genet. 118, 99-106
    • (2005) Hum. Genet , vol.118 , pp. 99-106
    • Kantor, L.1    Harding, H.P.2    Ron, D.3    Schiffmann, R.4    Kaneski, C.R.5    Kimball, S.R.6    Elroy-Stein, O.7
  • 16
    • 0032538317 scopus 로고    scopus 로고
    • Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide exchange and GTP-myristoyl switching
    • Goldberg, J. (1998) Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Cell 95, 237-248
    • (1998) Cell , vol.95 , pp. 237-248
    • Goldberg, J.1
  • 18
    • 36749037829 scopus 로고    scopus 로고
    • Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states
    • Yatime, L., Mechulam, Y., Blanquet, S. and Schmitt, E. (2007) Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states. Proc. Natl. Acad. Sci. U.S.A. 104, 18445-18450
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 18445-18450
    • Yatime, L.1    Mechulam, Y.2    Blanquet, S.3    Schmitt, E.4
  • 19
    • 0031057349 scopus 로고    scopus 로고
    • The ternary complex of EF-Tu and its role in protein biosynthesis
    • Clark, B.F. and Nyborg, J. (1997) The ternary complex of EF-Tu and its role in protein biosynthesis. Curr. Opin. Struct. Biol. 7, 110-116
    • (1997) Curr. Opin. Struct. Biol , vol.7 , pp. 110-116
    • Clark, B.F.1    Nyborg, J.2
  • 20
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu EF-Ts complex at 2.5Å resolution
    • Kawashima, T., Berthet-Colominas, C., Wulff, M., Cusack, S. and Leberman, R. (1996) The structure of the Escherichia coli EF-Tu EF-Ts complex at 2.5Å resolution. Nature 379, 511-518
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colominas, C.2    Wulff, M.3    Cusack, S.4    Leberman, R.5
  • 22
    • 0033638335 scopus 로고    scopus 로고
    • Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Bα
    • Andersen, G.R., Pedersen, L., Valente, L., Chatterjee, I., Kinzy, T.G., Kjeldgaard, M. and Nyborg, J. (2000) Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Bα. Mol. Cell 6, 1261-1266
    • (2000) Mol. Cell , vol.6 , pp. 1261-1266
    • Andersen, G.R.1    Pedersen, L.2    Valente, L.3    Chatterjee, I.4    Kinzy, T.G.5    Kjeldgaard, M.6    Nyborg, J.7
  • 23
    • 33644790001 scopus 로고    scopus 로고
    • Structural switch of the γ subunit in an archaeal aIF2αγ heterodimer
    • Yatime, L., Mechulam, Y., Blanquet, S. and Schmitt, E. (2006) Structural switch of the γ subunit in an archaeal aIF2αγ heterodimer. Structure 14, 119-128
    • (2006) Structure , vol.14 , pp. 119-128
    • Yatime, L.1    Mechulam, Y.2    Blanquet, S.3    Schmitt, E.4
  • 24
    • 1642304746 scopus 로고    scopus 로고
    • X-ray structure of translation initiation factor eIF2γ: Implications for tRNA and eIF2α binding
    • Roll-Mecak, A., Alone, P., Cao, C., Dever, T.E. and Burley, S.K. (2004) X-ray structure of translation initiation factor eIF2γ: implications for tRNA and eIF2α binding. J. Biol. Chem. 279, 10634-10642
    • (2004) J. Biol. Chem , vol.279 , pp. 10634-10642
    • Roll-Mecak, A.1    Alone, P.2    Cao, C.3    Dever, T.E.4    Burley, S.K.5
  • 25
    • 0035846821 scopus 로고    scopus 로고
    • Biochemical analysis of the eIF2βγ complex reveals a structural function for eIF2α in catalyzed nucleotide exchange
    • Nika, J., Rippel, S. and Hannig, E.M. (2001) Biochemical analysis of the eIF2βγ complex reveals a structural function for eIF2α in catalyzed nucleotide exchange. J. Biol. Chem. 276, 1051-1056
    • (2001) J. Biol. Chem , vol.276 , pp. 1051-1056
    • Nika, J.1    Rippel, S.2    Hannig, E.M.3
  • 27
    • 0037439198 scopus 로고    scopus 로고
    • Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo
    • Olsen, D.S., Savner, E.M., Mathew, A., Zhang, F., Krishnamoorthy, T., Phan, L. and Hinnebusch, A.G. (2003) Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo. EMBO J. 22, 193-204
    • (2003) EMBO J , vol.22 , pp. 193-204
    • Olsen, D.S.1    Savner, E.M.2    Mathew, A.3    Zhang, F.4    Krishnamoorthy, T.5    Phan, L.6    Hinnebusch, A.G.7
  • 28
    • 0033559265 scopus 로고    scopus 로고
    • Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2
    • Asano, K., Krishnamoorthy, T., Phan, L., Pavitt, G.D. and Hinnebusch, A.G. (1999) Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2. EMBO J. 18, 1673-1688
    • (1999) EMBO J , vol.18 , pp. 1673-1688
    • Asano, K.1    Krishnamoorthy, T.2    Phan, L.3    Pavitt, G.D.4    Hinnebusch, A.G.5
  • 29
    • 0036846237 scopus 로고    scopus 로고
    • Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo
    • Valasek, L., Nielsen, K.H. and Hinnebusch, A.G. (2002) Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation in vivo. EMBO J. 21, 5886-5898
    • (2002) EMBO J , vol.21 , pp. 5886-5898
    • Valasek, L.1    Nielsen, K.H.2    Hinnebusch, A.G.3
  • 30
    • 33744957161 scopus 로고    scopus 로고
    • Direct binding of translation initiation factor eIF2γ-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2bε
    • Alone, P.V. and Dever, T.E. (2006) Direct binding of translation initiation factor eIF2γ-G domain to its GTPase-activating and GDP-GTP exchange factors eIF5 and eIF2bε. J. Biol. Chem. 281, 12636-12644
    • (2006) J. Biol. Chem , vol.281 , pp. 12636-12644
    • Alone, P.V.1    Dever, T.E.2
  • 31
    • 0032519585 scopus 로고    scopus 로고
    • eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange
    • Pavitt, G.D., Ramaiah, K.V., Kimball, S.R. and Hinnebusch, A.G. (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
  • 32
    • 0034960171 scopus 로고    scopus 로고
    • Tight binding of the phosphorylated a 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., Pavitt, G.D., Zhang, F., Dever, T.E. and Hinnebusch, A.G. (2001) Tight binding of the phosphorylated a 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
  • 33
    • 34249699125 scopus 로고    scopus 로고
    • Change in nutritional status modulates the abundance of critical pre-initiation intermediate complexes during translation initiation in vivo
    • Singh, C.R., Udagawa, T., Lee, B., Wassink, S., He, H., Yamamoto, Y., Anderson, J.T., Pavitt, G.D. and Asano, K. (2007) Change in nutritional status modulates the abundance of critical pre-initiation intermediate complexes during translation initiation in vivo. J. Mol. Biol. 370, 315-330
    • (2007) J. Mol. Biol , vol.370 , pp. 315-330
    • Singh, C.R.1    Udagawa, T.2    Lee, B.3    Wassink, S.4    He, H.5    Yamamoto, Y.6    Anderson, J.T.7    Pavitt, G.D.8    Asano, K.9
  • 34
    • 33749340583 scopus 로고    scopus 로고
    • An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation
    • Singh, C.R., Lee, B., Udagawa, T., Mohammad-Qureshi, S.S., Yamamoto, Y., Pavitt, G.D. and Asano, K. (2006) An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation. EMBO J. 25, 4537-4546
    • (2006) EMBO J , vol.25 , pp. 4537-4546
    • Singh, C.R.1    Lee, B.2    Udagawa, T.3    Mohammad-Qureshi, S.S.4    Yamamoto, Y.5    Pavitt, G.D.6    Asano, K.7
  • 35
    • 0032538347 scopus 로고    scopus 로고
    • Invasion of the nucleotide snatchers: Structural insights into the mechanism of G protein GEFs
    • Sprang, S.R. and Coleman, D.E. (1998) Invasion of the nucleotide snatchers: structural insights into the mechanism of G protein GEFs. Cell 95, 155-158
    • (1998) Cell , vol.95 , pp. 155-158
    • Sprang, S.R.1    Coleman, D.E.2
  • 36
    • 13444252631 scopus 로고    scopus 로고
    • Rossman, K.L., Der, C.J. and Sondek, J. (2005) GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors. Nat. Rev. Mol. Cell Biol. 6, 167-180
    • Rossman, K.L., Der, C.J. and Sondek, J. (2005) GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors. Nat. Rev. Mol. Cell Biol. 6, 167-180
  • 37
    • 34249018367 scopus 로고    scopus 로고
    • GEFs and GAPs: Critical elements in the control of small G proteins
    • Bos, J.L., Rehmann, H. and Wittinghofer, A. (2007) GEFs and GAPs: critical elements in the control of small G proteins. Cell 129, 865-877
    • (2007) Cell , vol.129 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 38
    • 0346243924 scopus 로고    scopus 로고
    • Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor
    • Renault, L., Guibert, B. and Cherfils, J. (2003) Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor. Nature 426, 525-530
    • (2003) Nature , vol.426 , pp. 525-530
    • Renault, L.1    Guibert, B.2    Cherfils, J.3
  • 39
    • 0032549076 scopus 로고    scopus 로고
    • Mutational analysis of the roles of residues in Escherichia coli elongation factor Ts in the interaction with elongation factor Tu
    • Zhang, Y., Yu, N.J. and Spremulli, L.L. (1998) Mutational analysis of the roles of residues in Escherichia coli elongation factor Ts in the interaction with elongation factor Tu. J. Biol. Chem. 273, 4556-4562
    • (1998) J. Biol. Chem , vol.273 , pp. 4556-4562
    • Zhang, Y.1    Yu, N.J.2    Spremulli, L.L.3
  • 40
    • 0037155195 scopus 로고    scopus 로고
    • Mechanism of elongation factor (EF)-Ts-catalyzed nucleotide exchange in EF-Tu: Contribution of contacts at the guanine base
    • Wieden, H.J., Gromadski, K., Rodnin, D. and Rodnina, M.V. (2002) Mechanism of elongation factor (EF)-Ts-catalyzed nucleotide exchange in EF-Tu: contribution of contacts at the guanine base. J. Biol. Chem, 227, 6032-6036
    • (2002) J. Biol. Chem , vol.227 , pp. 6032-6036
    • Wieden, H.J.1    Gromadski, K.2    Rodnin, D.3    Rodnina, M.V.4
  • 41
    • 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 Pavitt, G.D. (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
  • 42
    • 0034697583 scopus 로고    scopus 로고
    • identification of domains within the E-subunit of the translation initiation factor eIF2B that are necessary for guanine nucleotide exchange activity and eIF2B holoprotein formation
    • Anthony, T.G., Fabian, J.R., Kimball, S.R. and Jefferson, L.S. (2000) identification of domains within the E-subunit of the translation initiation factor eIF2B that are necessary for guanine nucleotide exchange activity and eIF2B holoprotein formation. Biochim. Biophys. Acta 1492, 56-62
    • (2000) Biochim. Biophys. Acta , vol.1492 , pp. 56-62
    • Anthony, T.G.1    Fabian, J.R.2    Kimball, S.R.3    Jefferson, L.S.4
  • 43
    • 0036790688 scopus 로고    scopus 로고
    • Characterization of the minimal catalytic domain within eIF2B: The guanine-nucleotide exchange factor for translation initiation
    • Gomez, E., Mohammad, S.S. and Pavitt, G.D. (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
  • 44
    • 1542368830 scopus 로고    scopus 로고
    • Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue
    • Boesen, T., Mohammad, S.S., Pavitt, G.D. and Andersen, G.R. (2004) Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue. J. Biol. Chem. 279, 10584-10592
    • (2004) J. Biol. Chem , vol.279 , pp. 10584-10592
    • Boesen, T.1    Mohammad, S.S.2    Pavitt, G.D.3    Andersen, G.R.4
  • 45
    • 33746713880 scopus 로고    scopus 로고
    • The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5
    • Bieniossek, C., Schutz, P., Bumann, M., Limacher, A., Uson, I. and Baumann, U. (2006) The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5. J. Mol. Biol. 360, 457-465
    • (2006) J. Mol. Biol , vol.360 , pp. 457-465
    • Bieniossek, C.1    Schutz, P.2    Bumann, M.3    Limacher, A.4    Uson, I.5    Baumann, U.6
  • 46
    • 33646173651 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal domain of S. cerevisiae eIF5
    • Wei, Z., Xue, Y., Xu, H. and Gong, W. (2006) Crystal structure of the C-terminal domain of S. cerevisiae eIF5. J. Mol. Biol. 359, 1-9
    • (2006) J. Mol. Biol , vol.359 , pp. 1-9
    • Wei, Z.1    Xue, Y.2    Xu, H.3    Gong, W.4
  • 47
    • 34447514386 scopus 로고    scopus 로고
    • Critical contacts between the eukaryotic initiation factor 2B (eIF2B) catalytic domain and both eIF2β and -2γ mediate guanine nucleotide exchange
    • Mohammad-Qureshi, S.S., Haddad, R., Hemingway, E.J., Richardson, J.P. and Pavitt, G.D. (2007) Critical contacts between the eukaryotic initiation factor 2B (eIF2B) catalytic domain and both eIF2β and -2γ mediate guanine nucleotide exchange. Mol. Cell. Biol. 27, 5225-5234
    • (2007) Mol. Cell. Biol , vol.27 , pp. 5225-5234
    • Mohammad-Qureshi, S.S.1    Haddad, R.2    Hemingway, E.J.3    Richardson, J.P.4    Pavitt, G.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.