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Volumn 13, Issue 1, 2006, Pages 55-62

Dichotomous but stringent substrate selection by the dual-function Cdk7 complex revealed by chemical genetics

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE DERIVATIVE; CYCLIN DEPENDENT KINASE 7; CYCLIN DEPENDENT KINASE ACTIVATING KINASE; PEPTIDE; PROTEIN SPT5; RNA POLYMERASE II; TRANSCRIPTION ELONGATION FACTOR; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 30044438459     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb1028     Document Type: Article
Times cited : (86)

References (54)
  • 1
    • 0027296041 scopus 로고
    • The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues
    • Fesquet, D. et al. The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues. EMBO J. 12, 3111-3121 (1993).
    • (1993) EMBO J. , vol.12 , pp. 3111-3121
    • Fesquet, D.1
  • 4
    • 0027994603 scopus 로고
    • A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase
    • Fisher, R.P. & Morgan, D.O. A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase. Cell 78, 713-724 (1994).
    • (1994) Cell , vol.78 , pp. 713-724
    • Fisher, R.P.1    Morgan, D.O.2
  • 5
    • 0028070243 scopus 로고
    • A cyclin associated with the CDK-activating kinase MO15
    • Mäkelä, T.P. et al. A cyclin associated with the CDK-activating kinase MO15. Nature 371, 254-257 (1994).
    • (1994) Nature , vol.371 , pp. 254-257
    • Mäkelä, T.P.1
  • 6
    • 0028856425 scopus 로고
    • MAT1 ('ménage à trois') a new RING finger protein subunit stabilizing cyclin H-cdk7 complexes in starfish and Xenopus CAK
    • Devault, A. et al. MAT1 ('ménage à trois') a new RING finger protein subunit stabilizing cyclin H-cdk7 complexes in starfish and Xenopus CAK. EMBO J. 14, 5027-5036 (1995).
    • (1995) EMBO J. , vol.14 , pp. 5027-5036
    • Devault, A.1
  • 7
    • 0028807103 scopus 로고
    • Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase
    • Fisher, R.P., Jin, P., Chamberlin, H.M. & Morgan, D.O. Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase. Cell 83, 47-57 (1995).
    • (1995) Cell , vol.83 , pp. 47-57
    • Fisher, R.P.1    Jin, P.2    Chamberlin, H.M.3    Morgan, D.O.4
  • 8
    • 0028882228 scopus 로고
    • In vitro assembly of a functional human cdk7/cyclin H complex requires MAT1, a novel 36 kD RING finger protein
    • Tassan, J.-P. et al. In vitro assembly of a functional human cdk7/cyclin H complex requires MAT1, a novel 36 kD RING finger protein. EMBO J. 14, 5608-5617 (1995).
    • (1995) EMBO J. , vol.14 , pp. 5608-5617
    • Tassan, J.-P.1
  • 9
    • 0028600051 scopus 로고
    • The MO15 cell cycle kinase is associated with the TFIIH transcription-DNA repair factor
    • Roy, R. et al. The MO15 cell cycle kinase is associated with the TFIIH transcription-DNA repair factor. Cell 79, 1093-1101 (1994).
    • (1994) Cell , vol.79 , pp. 1093-1101
    • Roy, R.1
  • 10
    • 0028958673 scopus 로고
    • Association of Cdk-activating kinase subunits with transcription factor TFIIH
    • Serizawa, H. et al. Association of Cdk-activating kinase subunits with transcription factor TFIIH. Nature 374, 280-282 (1995).
    • (1995) Nature , vol.374 , pp. 280-282
    • Serizawa, H.1
  • 11
    • 0028954227 scopus 로고
    • Cdk-activating kinase (CAK) complex is a component of human transcription factor IIH
    • Shiekhattar, R. et al. Cdk-activating kinase (CAK) complex is a component of human transcription factor IIH. Nature 374, 283-287 (1995).
    • (1995) Nature , vol.374 , pp. 283-287
    • Shiekhattar, R.1
  • 12
    • 0032004973 scopus 로고    scopus 로고
    • The role of Cdk7 in CAK function, a retro-retrospective
    • Harper, J.W. & Elledge, S.J. The role of Cdk7 in CAK function, a retro-retrospective. Genes Dev. 12, 285-289 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 285-289
    • Harper, J.W.1    Elledge, S.J.2
  • 13
    • 0032005801 scopus 로고    scopus 로고
    • Cdk7 is essential for mitosis and for in vivo Cdk-activating kinase activity
    • Larochelle, S., Pandur, J., Fisher, R.P., Salz, H.K. & Suter, B. Cdk7 is essential for mitosis and for in vivo Cdk-activating kinase activity. Genes Dev. 12, 370-381 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 370-381
    • Larochelle, S.1    Pandur, J.2    Fisher, R.P.3    Salz, H.K.4    Suter, B.5
  • 14
    • 0032535290 scopus 로고    scopus 로고
    • Fission yeast Csk1 is a CAK-activating kinase (CAKAK)
    • Hermand, D. et al. Fission yeast Csk1 is a CAK-activating kinase (CAKAK). EMBO J. 17, 7230-7238 (1998).
    • (1998) EMBO J. , vol.17 , pp. 7230-7238
    • Hermand, D.1
  • 15
    • 0033594536 scopus 로고    scopus 로고
    • Cdc2 activation in fission yeast depends on Mcs6 and Csk1, two partially redundant Cdk-activating kinases CAKs
    • Lee, K.M., Saiz, J.E., Barton, W.A. & Fisher, R.P. Cdc2 activation in fission yeast depends on Mcs6 and Csk1, two partially redundant Cdk-activating kinases CAKs). Curr. Biol. 9, 441-444 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 441-444
    • Lee, K.M.1    Saiz, J.E.2    Barton, W.A.3    Fisher, R.P.4
  • 16
    • 0037046803 scopus 로고    scopus 로고
    • A CDK-activating kinase network is required in cell cycle control and transcription in fission yeast
    • Saiz, J.E. & Fisher, R.P. A CDK-activating kinase network is required in cell cycle control and transcription in fission yeast. Curr. Biol. 12, 1100-1105 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 1100-1105
    • Saiz, J.E.1    Fisher, R.P.2
  • 17
    • 0037117601 scopus 로고    scopus 로고
    • cdk-7 is required for mRNA transcription and cell cycle progression in Caenorhabditis elegans embryos
    • Wallenfang, M.R. & Seydoux, G. cdk-7 is required for mRNA transcription and cell cycle progression in Caenorhabditis elegans embryos. Proc. Natl. Acad. Sci. USA 99, 5527-5532 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5527-5532
    • Wallenfang, M.R.1    Seydoux, G.2
  • 18
    • 0029399072 scopus 로고
    • Innocent bystanders or chosen collaborators?
    • Poon, R.Y. & Hunter, T. Innocent bystanders or chosen collaborators? Curr. Biol. 5, 1243-1247 (1995).
    • (1995) Curr. Biol. , vol.5 , pp. 1243-1247
    • Poon, R.Y.1    Hunter, T.2
  • 19
    • 0034747803 scopus 로고    scopus 로고
    • Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T-loop
    • Garrett, S. et al. Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T-loop. Mol. Cell. Biol. 21, 88-99 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 88-99
    • Garrett, S.1
  • 20
    • 0032549653 scopus 로고    scopus 로고
    • Characterization of the residues phosphorylated in vitro by different C-terminal domain kinases
    • Trigon, S. et al. Characterization of the residues phosphorylated in vitro by different C-terminal domain kinases. J. Biol. Chem. 273, 6769-6775 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 6769-6775
    • Trigon, S.1
  • 21
    • 0035815612 scopus 로고    scopus 로고
    • Three RNA polymerase II carboxyl-terminal domain kinases display distinct substrate preferences
    • Ramanathan, Y. et al. Three RNA polymerase II carboxyl-terminal domain kinases display distinct substrate preferences. J. Biol. Chem. 276, 10913-10920 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 10913-10920
    • Ramanathan, Y.1
  • 22
    • 0030724673 scopus 로고    scopus 로고
    • MAT1-dependent manner
    • MAT1-dependent manner. Mol. Cell. Biol. 17, 7220-7229 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7220-7229
    • Ko, L.J.1
  • 23
    • 0031440878 scopus 로고    scopus 로고
    • Stimulation of RARα activation function AF-1 through binding to the general transcription factor TFIIH and phosphorylation by CDK7
    • Rochette-Egly, C., Adam, S., Rossignol, M., Egly, J.-M. & Chambon, P. Stimulation of RARα activation function AF-1 through binding to the general transcription factor TFIIH and phosphorylation by CDK7. Cell 90, 97-107 (1997).
    • (1997) Cell , vol.90 , pp. 97-107
    • Rochette-Egly, C.1    Adam, S.2    Rossignol, M.3    Egly, J.-M.4    Chambon, P.5
  • 24
    • 0033517132 scopus 로고    scopus 로고
    • Residues phosphorylated by TFIIH are required for E2F-1 degradation during S-phase
    • Vandel, L. & Kouzarides, T. Residues phosphorylated by TFIIH are required for E2F-1 degradation during S-phase. EMBO J. 18, 4280-4291 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4280-4291
    • Vandel, L.1    Kouzarides, T.2
  • 25
    • 0030669391 scopus 로고    scopus 로고
    • The cyclin-dependent kinase-activating kinase (CAK) assembly factor, MAT1, targets and enhances CAK activity on the POU domains of octamer transcription factors
    • Inamoto, S., Segil, N., Pan, Z.-Q., Kimura, M. & Roeder, R.G. The cyclin-dependent kinase-activating kinase (CAK) assembly factor, MAT1, targets and enhances CAK activity on the POU domains of octamer transcription factors. J. Biol. Chem. 272, 29852-29858 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 29852-29858
    • Inamoto, S.1    Segil, N.2    Pan, Z.-Q.3    Kimura, M.4    Roeder, R.G.5
  • 26
    • 0029147732 scopus 로고
    • Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase
    • Aprelikova, O., Xiong, Y. & Liu, E.T. Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase. J. Biol. Chem. 270, 18195-18197 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 18195-18197
    • Aprelikova, O.1    Xiong, Y.2    Liu, E.T.3
  • 27
    • 0242300176 scopus 로고    scopus 로고
    • Targets of the cyclin-dependent kinase Cdk1
    • Ubersax, J.A. et al. Targets of the cyclin-dependent kinase Cdk1. Nature 425, 859-864 (2003).
    • (2003) Nature , vol.425 , pp. 859-864
    • Ubersax, J.A.1
  • 28
    • 0035969559 scopus 로고    scopus 로고
    • Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication
    • Nash, P. et al. Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication. Nature 414, 514-521 (2001).
    • (2001) Nature , vol.414 , pp. 514-521
    • Nash, P.1
  • 29
    • 0030998712 scopus 로고    scopus 로고
    • Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH
    • Rossignol, M., Kolb-Cheynel, I. & Egly, J.-M. Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH. EMBO J. 16, 1628-1637 (1997).
    • (1997) EMBO J. , vol.16 , pp. 1628-1637
    • Rossignol, M.1    Kolb-Cheynel, I.2    Egly, J.-M.3
  • 30
    • 0030976052 scopus 로고    scopus 로고
    • Regulation of CDK7 substrate specificity by MAT1 and TFIIH
    • Yankulov, K.Y. & Bentley, D.L. Regulation of CDK7 substrate specificity by MAT1 and TFIIH. EMBO J. 16, 1638-1646 (1997).
    • (1997) EMBO J. , vol.16 , pp. 1638-1646
    • Yankulov, K.Y.1    Bentley, D.L.2
  • 31
    • 0035898652 scopus 로고    scopus 로고
    • T-loop phosphorylation stabilizes the CDK7-cyclin H-MAT1 complex in vivo and regulates its CTD kinase activity
    • Larochelle, S. et al. T-loop phosphorylation stabilizes the CDK7-cyclin H-MAT1 complex in vivo and regulates its CTD kinase activity. EMBO J. 20, 3749-3759 (2001).
    • (2001) EMBO J. , vol.20 , pp. 3749-3759
    • Larochelle, S.1
  • 32
    • 0030887842 scopus 로고    scopus 로고
    • Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates
    • Shah, K., Liu, Y., Deirmengian, C. & Shokat, K.M. Engineering unnatural nucleotide specificity for Rous sarcoma virus tyrosine kinase to uniquely label its direct substrates. Proc. Natl. Acad. Sci. USA 94, 3565-3570 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3565-3570
    • Shah, K.1    Liu, Y.2    Deirmengian, C.3    Shokat, K.M.4
  • 34
    • 0033638967 scopus 로고    scopus 로고
    • Identification and characterization of a novel cell cycle-regulated internal ribosome entry site
    • Cornelis, S. et al. Identification and characterization of a novel cell cycle-regulated internal ribosome entry site. Mol. Cell 5, 597-605 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 597-605
    • Cornelis, S.1
  • 35
    • 14444275279 scopus 로고    scopus 로고
    • DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs
    • Wada, T. et al. DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs. Genes Dev. 12, 343-356 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 343-356
    • Wada, T.1
  • 36
    • 0032534814 scopus 로고    scopus 로고
    • Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro
    • Wada, T., Takagi, T., Yamaguchi, Y., Watanabe, D. & Handa, H. Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro. EMBO J. 17, 7395-7403 (1998).
    • (1998) EMBO J. , vol.17 , pp. 7395-7403
    • Wada, T.1    Takagi, T.2    Yamaguchi, Y.3    Watanabe, D.4    Handa, H.5
  • 37
    • 0342748478 scopus 로고    scopus 로고
    • Domains in the SPT5 protein that modulate its transcriptional regulatory properties
    • Ivanov, D., Kwak, Y.T., Guo, J. & Gaynor, R.B. Domains in the SPT5 protein that modulate its transcriptional regulatory properties. Mol. Cell. Biol. 20, 2970-2983 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2970-2983
    • Ivanov, D.1    Kwak, Y.T.2    Guo, J.3    Gaynor, R.B.4
  • 38
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • Russo, A.A., Jeffrey, P.D. & Pavletich, N.P. Structural basis of cyclin-dependent kinase activation by phosphorylation. Nat. Struct. Biol. 3, 696-700 (1996).
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 696-700
    • Russo, A.A.1    Jeffrey, P.D.2    Pavletich, N.P.3
  • 39
    • 0036532116 scopus 로고    scopus 로고
    • The emerging power of chemical genetics
    • Specht, K.M. & Shokat, K.M. The emerging power of chemical genetics. Curr. Opin. Cell Biol. 14, 155-159 (2002).
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 155-159
    • Specht, K.M.1    Shokat, K.M.2
  • 40
    • 0028970682 scopus 로고
    • 160 by the cyclin-dependent kinase-interacting phosphatase KAP in the absence of cyclin
    • 160 by the cyclin-dependent kinase-interacting phosphatase KAP in the absence of cyclin. Science 270, 90-93 (1995).
    • (1995) Science , vol.270 , pp. 90-93
    • Poon, R.Y.1    Hunter, T.2
  • 41
    • 0032751695 scopus 로고    scopus 로고
    • Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases
    • Cheng, A., Ross, K.E., Kaldis, P. & Solomon, M.J. Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases. Genes Dev. 13, 2946-2957 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2946-2957
    • Cheng, A.1    Ross, K.E.2    Kaldis, P.3    Solomon, M.J.4
  • 42
    • 0038157142 scopus 로고    scopus 로고
    • Xpd/Ercc2 regulates CAK activity and mitotic progression
    • Chen, J., Larochelle, S., Li, X. & Suter, B. Xpd/Ercc2 regulates CAK activity and mitotic progression. Nature 424, 228-232 (2003).
    • (2003) Nature , vol.424 , pp. 228-232
    • Chen, J.1    Larochelle, S.2    Li, X.3    Suter, B.4
  • 43
    • 0035947671 scopus 로고    scopus 로고
    • Identification of new JNK substrate using ATP pocket mutant JNK and a corresponding ATP analogue
    • Habelhah, H. et al. Identification of new JNK substrate using ATP pocket mutant JNK and a corresponding ATP analogue. J. Biol. Chem. 276, 18090-18095 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 18090-18095
    • Habelhah, H.1
  • 44
    • 0842347413 scopus 로고    scopus 로고
    • Two cyclin-dependent kinases promote RNA polymerase II transcription and formation of the scaffold complex
    • Liu, Y. et al. Two cyclin-dependent kinases promote RNA polymerase II transcription and formation of the scaffold complex. Mol. Cell. Biol. 24, 1721-1735 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1721-1735
    • Liu, Y.1
  • 45
    • 0033611561 scopus 로고    scopus 로고
    • Cyclin C/CDK8 and cyclin H/CDK7/p36 are biochemically distinct CTD kinases
    • Rickert, P., Corden, J.L. & Lees, E. Cyclin C/CDK8 and cyclin H/CDK7/p36 are biochemically distinct CTD kinases. Oncogene 18, 1093-1102 (1999).
    • (1999) Oncogene , vol.18 , pp. 1093-1102
    • Rickert, P.1    Corden, J.L.2    Lees, E.3
  • 46
    • 1542284574 scopus 로고    scopus 로고
    • Three cyclin-dependent kinases preferentially phosphorylate different parts of the C-terminal domain of the large subunit of RNA polymerase II
    • Pinhero, R., Liaw, P., Bertens, K. & Yankulov, K. Three cyclin-dependent kinases preferentially phosphorylate different parts of the C-terminal domain of the large subunit of RNA polymerase II. Eur. J. Biochem. 271, 1004-1014 (2004).
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1004-1014
    • Pinhero, R.1    Liaw, P.2    Bertens, K.3    Yankulov, K.4
  • 48
    • 1842609933 scopus 로고    scopus 로고
    • Failure to proliferate and mitotic arrest of CDK11(p110/p58)-null mutant mice at the blastocyst stage of embryonic cell development
    • Li, T., Inoue, A., Lahti, J.M. & Kidd, V.J. Failure to proliferate and mitotic arrest of CDK11(p110/p58)-null mutant mice at the blastocyst stage of embryonic cell development. Mol. Cell. Biol. 24, 3188-3197 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3188-3197
    • Li, T.1    Inoue, A.2    Lahti, J.M.3    Kidd, V.J.4
  • 49
    • 0033566042 scopus 로고    scopus 로고
    • Transcription elongation factor hSPT5 stimulates mRNA capping
    • Wen, Y. & Shatkin, A.J. Transcription elongation factor hSPT5 stimulates mRNA capping. Genes Dev. 13, 1774-1779 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1774-1779
    • Wen, Y.1    Shatkin, A.J.2
  • 50
    • 0037205456 scopus 로고    scopus 로고
    • Interactions between fission yeast mRNA capping enzymes and elongation factor Spt5
    • Pei, Y. & Shuman, S. Interactions between fission yeast mRNA capping enzymes and elongation factor Spt5. J. Biol. Chem. 277, 19639-19648 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 19639-19648
    • Pei, Y.1    Shuman, S.2
  • 51
    • 0037154982 scopus 로고    scopus 로고
    • A unified theory of gene expression
    • Orphanides, G. & Reinberg, D. A unified theory of gene expression. Cell 108, 439-451 (2002).
    • (2002) Cell , vol.108 , pp. 439-451
    • Orphanides, G.1    Reinberg, D.2
  • 52
    • 0030855139 scopus 로고    scopus 로고
    • Reconstitution of mammalian CDK-activating kinase
    • Fisher, R.P. Reconstitution of mammalian CDK-activating kinase. Methods Enzymol. 283, 256-270 (1997).
    • (1997) Methods Enzymol. , vol.283 , pp. 256-270
    • Fisher, R.P.1
  • 53
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J.D., Lebovitz, R.M. & Roeder, R.G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11, 1475-1489 (1983).
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 54
    • 11844263936 scopus 로고    scopus 로고
    • The histone chaperone TAF-I/SET/INHAT is required for transcription in vitro of chromatin templates
    • Gamble, M.J., Erdjument-Bromage, H., Tempst, P., Freedman, L.P. & Fisher, R.P. The histone chaperone TAF-I/SET/INHAT is required for transcription in vitro of chromatin templates. Mol. Cell. Biol. 25, 797-807 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 797-807
    • Gamble, M.J.1    Erdjument-Bromage, H.2    Tempst, P.3    Freedman, L.P.4    Fisher, R.P.5


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