메뉴 건너뛰기




Volumn 335, Issue 2, 2004, Pages 415-424

Dephosphorylation of RNA Polymerase II by CTD-phosphatase FCP1 is Inhibited by Phospho-CTD Associating Proteins

Author keywords

Capping enzyme Hce1; CTD phosphatase FCP1; Prolyl isomerase Pin1; RNA polymerase II; Transcription

Indexed keywords

CARBOXYL TERMINAL DOMAIN PHOSPHATASE; CYCLOPHILIN; PHOSPHATASE; PHOSPHOTRANSFERASE; PROTEIN; PROTEIN CA150; PROTEIN HCE1; RNA POLYMERASE II; UNCLASSIFIED DRUG;

EID: 0345735669     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.10.036     Document Type: Article
Times cited : (25)

References (44)
  • 1
    • 0028924422 scopus 로고
    • Phosphorylation of the C-terminal domain of RNA polymerase II
    • Dahmus M.E. Phosphorylation of the C-terminal domain of RNA polymerase II. Biochim. Biophys. Acta. 1261:1995;171-182.
    • (1995) Biochim. Biophys. Acta , vol.1261 , pp. 171-182
    • Dahmus, M.E.1
  • 3
    • 0030249279 scopus 로고    scopus 로고
    • The multiple roles of transcription/repair factor TFIIH
    • Svejstrup J.Q., Vichi P., Egly J.-M. The multiple roles of transcription/repair factor TFIIH. Trends Biochem. Sci. 21:1996;346-350.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 346-350
    • Svejstrup, J.Q.1    Vichi, P.2    Egly, J.-M.3
  • 4
    • 0034111019 scopus 로고    scopus 로고
    • P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II
    • Price D.H. P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II. Mol. Cell. Biol. 20:2000;2629-2634.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2629-2634
    • Price, D.H.1
  • 5
    • 0028053812 scopus 로고
    • Purification and characterization of a phosphatase from HeLa cells that dephosphorylates the C-terminal domain of RNA polymerase II
    • Chambers R.S., Dahmus M.E. Purification and characterization of a phosphatase from HeLa cells that dephosphorylates the C-terminal domain of RNA polymerase II. J. Biol. Chem. 269:1994;26243-26248.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26243-26248
    • Chambers, R.S.1    Dahmus, M.E.2
  • 6
    • 0034815589 scopus 로고    scopus 로고
    • Transcription-independent RNA polymerase II dephosphorylation by the FCP1 CTD-phosphatase in Xenopus laevis early embryos
    • Palancade B., Dubois M.F., Dahmus M.E., Bensaude O. Transcription- independent RNA polymerase II dephosphorylation by the FCP1 CTD-phosphatase in Xenopus laevis early embryos. Mol. Cell. Biol. 21:2001;6359-6368.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6359-6368
    • Palancade, B.1    Dubois, M.F.2    Dahmus, M.E.3    Bensaude, O.4
  • 8
    • 0034685880 scopus 로고    scopus 로고
    • The sensitivity of RNA polymerase II in elongation complexes to C-terminal domain phosphatase
    • Lehman A.L., Dahmus M.E. The sensitivity of RNA polymerase II in elongation complexes to C-terminal domain phosphatase. J. Biol. Chem. 275:2000;14923-14932.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14923-14932
    • Lehman, A.L.1    Dahmus, M.E.2
  • 9
    • 0034693245 scopus 로고    scopus 로고
    • C-terminal domain phosphatase sensitivity of RNA polymerase II in early elongation complexes on the HIV-1 and adenovirus 2 major late templates
    • Marshall N.F., Dahmus M.E. C-terminal domain phosphatase sensitivity of RNA polymerase II in early elongation complexes on the HIV-1 and adenovirus 2 major late templates. J. Biol. Chem. 275:2000;32430-32437.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32430-32437
    • Marshall, N.F.1    Dahmus, M.E.2
  • 10
    • 0029748541 scopus 로고    scopus 로고
    • Purification and characterization of an RNA polymerase II phosphatase from yeast
    • Chambers R.S., Kane C.M. Purification and characterization of an RNA polymerase II phosphatase from yeast. J. Biol. Chem. 271:1996;24498-24504.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24498-24504
    • Chambers, R.S.1    Kane, C.M.2
  • 11
    • 0032538444 scopus 로고    scopus 로고
    • FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO
    • Archambault J., Pan G., Dahmus G.K., Cartier M., Marshall N.F., Zhang S., et al. FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO. J. Biol. Chem. 273:1998;27593-27601.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27593-27601
    • Archambault, J.1    Pan, G.2    Dahmus, G.K.3    Cartier, M.4    Marshall, N.F.5    Zhang, S.6
  • 12
    • 0033165865 scopus 로고    scopus 로고
    • An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae
    • Kobor M.S., Archambault J., Lester W., Holstege F.C., Gileadi O., Jansma D.B., et al. An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae. Mol. Cell. 4:1999;55-62.
    • (1999) Mol. Cell , vol.4 , pp. 55-62
    • Kobor, M.S.1    Archambault, J.2    Lester, W.3    Holstege, F.C.4    Gileadi, O.5    Jansma, D.B.6
  • 13
    • 0037184099 scopus 로고    scopus 로고
    • FCP1 phosphorylation by casein kinase 2 enhances binding to TFIIF and RNA polymerase II carboxyl-terminal domain phosphatase activity
    • Palancade B., Dubois M.-F., Bensaude O. FCP1 phosphorylation by casein kinase 2 enhances binding to TFIIF and RNA polymerase II carboxyl-terminal domain phosphatase activity. J. Biol. Chem. 277:2002;36061-36067.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36061-36067
    • Palancade, B.1    Dubois, M.-F.2    Bensaude, O.3
  • 14
    • 0345701299 scopus 로고    scopus 로고
    • The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation
    • Friedl E.M., Lane W.S., Erdjument-Bromage H., Tempst P., Reinberg D. The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation. Proc. Natl Acad. Sci. USA. 100:2003;2328-2333.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2328-2333
    • Friedl, E.M.1    Lane, W.S.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 15
    • 0038168110 scopus 로고    scopus 로고
    • A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5
    • Yeo M., Lin P.S., Dahmus M.E., Gill G.N. A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5. J. Biol. Chem. 278:2003;26078-26085.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26078-26085
    • Yeo, M.1    Lin, P.S.2    Dahmus, M.E.3    Gill, G.N.4
  • 16
    • 0141618451 scopus 로고    scopus 로고
    • Partial deficiency of the C-terminal-domain phosphatase of RNA polymerase II is associated with congenital cataracts facial dysmorphism neuropathy syndrome
    • Varon R., Gooding R., Steglich C., Marns L., Tang H., Angelicheva D., et al. Partial deficiency of the C-terminal-domain phosphatase of RNA polymerase II is associated with congenital cataracts facial dysmorphism neuropathy syndrome. Nature Genet. 35:2003;185-189.
    • (2003) Nature Genet. , vol.35 , pp. 185-189
    • Varon, R.1    Gooding, R.2    Steglich, C.3    Marns, L.4    Tang, H.5    Angelicheva, D.6
  • 17
    • 15644372864 scopus 로고    scopus 로고
    • 5′ Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated C-terminal domain of RNA polymerase II
    • McCracken S., Fong N., Rosonina E., Yankulov K., Brothers G., Siderovski D., et al. 5′ Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated C-terminal domain of RNA polymerase II. Genes Dev. 11:1997;3306-3318.
    • (1997) Genes Dev. , vol.11 , pp. 3306-3318
    • McCracken, S.1    Fong, N.2    Rosonina, E.3    Yankulov, K.4    Brothers, G.5    Siderovski, D.6
  • 18
    • 0031453408 scopus 로고    scopus 로고
    • MRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain
    • Cho E.J., Takagi T., Moore C.R., Buratowski S. mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain. Genes Dev. 15:1997;3319-3326.
    • (1997) Genes Dev. , vol.15 , pp. 3319-3326
    • Cho, E.J.1    Takagi, T.2    Moore, C.R.3    Buratowski, S.4
  • 19
    • 0030660264 scopus 로고    scopus 로고
    • Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II
    • Yue Z., Maldonado E., Pillutla R., Cho H., Reinberg D., Shatkin A.J. Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II. Proc. Natl Acad. Sci. USA. 94:1997;12898-12903.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12898-12903
    • Yue, Z.1    Maldonado, E.2    Pillutla, R.3    Cho, H.4    Reinberg, D.5    Shatkin, A.J.6
  • 20
    • 0029959435 scopus 로고    scopus 로고
    • The C-terminal domain of the largest subunit of RNA polymerase II interacts with a novel set of serine/arginine-rich proteins
    • Yuryev A., Patturajan M., Litingtung Y., Joshi R.V., Gentile C., Gebara M., Corden J.L. The C-terminal domain of the largest subunit of RNA polymerase II interacts with a novel set of serine/arginine-rich proteins. Proc. Natl Acad. Sci. USA. 93:1996;6975-6980.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6975-6980
    • Yuryev, A.1    Patturajan, M.2    Litingtung, Y.3    Joshi, R.V.4    Gentile, C.5    Gebara, M.6    Corden, J.L.7
  • 21
    • 0034704145 scopus 로고    scopus 로고
    • The splicing factor, Prp40, binds the phosphorylated carboxy-terminal domain of RNA polymerase II
    • Morris D., Greenleaf A.L. The splicing factor, Prp40, binds the phosphorylated carboxy-terminal domain of RNA polymerase II. J. Biol. Chem. 275:2000;39935-39943.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39935-39943
    • Morris, D.1    Greenleaf, A.L.2
  • 22
    • 0035895294 scopus 로고    scopus 로고
    • Cleavage/polyadenylation factor IA associates with the carboxyl-terminal domain of RNA polymerase II in Saccharomyces cerevisiae
    • Barillà D., Lee B.A., Proudfoot N.J. Cleavage/polyadenylation factor IA associates with the carboxyl-terminal domain of RNA polymerase II in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA. 2001;98.
    • (2001) Proc. Natl Acad. Sci. USA , pp. 98
    • Barillà, D.1    Lee, B.A.2    Proudfoot, N.J.3
  • 24
    • 0036179769 scopus 로고    scopus 로고
    • Requirements of the RNA polymerase II C-terminal domain for reconstituting pre-mRNA 3′ cleavage
    • Ryan K., Murthy K.G., Kaneko S., Manley J.L. Requirements of the RNA polymerase II C-terminal domain for reconstituting pre-mRNA 3′ cleavage. Mol. Cell. Biol. 22:2002;1684-1692.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1684-1692
    • Ryan, K.1    Murthy, K.G.2    Kaneko, S.3    Manley, J.L.4
  • 25
    • 0034255028 scopus 로고    scopus 로고
    • Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II
    • Carty S.M., Goldstrohm A.C., Suné C., Garcia-Blanco M.A., Greenleaf A.L. Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II. Proc. Natl Acad. Sci. USA. 97:2000;9015-9020.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9015-9020
    • Carty, S.M.1    Goldstrohm, A.C.2    Suné, C.3    Garcia-Blanco, M.A.4    Greenleaf, A.L.5
  • 26
    • 0032771752 scopus 로고    scopus 로고
    • A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pin1
    • Albert A., Lavoie S., Vincent M. A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pin1. J. Cell Sci. 112:1999;2493-2500.
    • (1999) J. Cell Sci. , vol.112 , pp. 2493-2500
    • Albert, A.1    Lavoie, S.2    Vincent, M.3
  • 27
    • 0033615705 scopus 로고    scopus 로고
    • Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3′-end formation
    • Morris D.P., Phatnani H.P., Greenleaf A.L. Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3′-end formation. J. Biol. Chem. 274:1999;31583-31587.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31583-31587
    • Morris, D.P.1    Phatnani, H.P.2    Greenleaf, A.L.3
  • 28
    • 0034679626 scopus 로고    scopus 로고
    • The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery
    • Wu X., Wilcox C.B., Devasahayam G., Hackett R.L., Arevalo-Rodriguez M., Cardenas M.E., et al. The Ess1 prolyl isomerase is linked to chromatin remodeling complexes and the general transcription machinery. EMBO J. 17:2000;3727-3738.
    • (2000) EMBO J. , vol.17 , pp. 3727-3738
    • Wu, X.1    Wilcox, C.B.2    Devasahayam, G.3    Hackett, R.L.4    Arevalo-Rodriguez, M.5    Cardenas, M.E.6
  • 29
  • 30
    • 0029043588 scopus 로고
    • The activity of COOH-terminal domain phosphatase is regulated by a docking site on RNA polymerase II and by the general transcription factors IIF and IIB
    • Chambers R.S., Wang B.Q., Burton Z.F., Dahmus M.E. The activity of COOH-terminal domain phosphatase is regulated by a docking site on RNA polymerase II and by the general transcription factors IIF and IIB. J. Biol. Chem. 270:1995;14962-14969.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14962-14969
    • Chambers, R.S.1    Wang, B.Q.2    Burton, Z.F.3    Dahmus, M.E.4
  • 31
    • 0036172151 scopus 로고    scopus 로고
    • Formation of a carboxy-terminal domain phosphatase (FCP1)/TFIIF/RNA polymerase II (pol II) complex in Schizosaccharomyces pombe involves direct interaction between Fcp1 and the Rpb4 subunit of pol II
    • Kimura M., Suzuki H., Ishihama A. Formation of a carboxy-terminal domain phosphatase (FCP1)/TFIIF/RNA polymerase II (pol II) complex in Schizosaccharomyces pombe involves direct interaction between Fcp1 and the Rpb4 subunit of pol II. Mol. Cell. Biol. 22:2002;1577-1588.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1577-1588
    • Kimura, M.1    Suzuki, H.2    Ishihama, A.3
  • 32
    • 0032540231 scopus 로고    scopus 로고
    • The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxy-terminal domain of RNA polymerase II
    • Ho C.K., Sriskanda V., McCracken S., Bentley D., Schwer B., Shuman S. The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxy-terminal domain of RNA polymerase II. J. Biol. Chem. 273:1998;9577-9585.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9577-9585
    • Ho, C.K.1    Sriskanda, V.2    McCracken, S.3    Bentley, D.4    Schwer, B.5    Shuman, S.6
  • 33
    • 2242454131 scopus 로고    scopus 로고
    • TFIIF-associating carboxyl-terminal domain phosphatase dephosphorylates phosphoserines 2 and 5 of RNA polymerase II
    • Lin P.S., Dubois M.F., Dahmus M.E. TFIIF-associating carboxyl-terminal domain phosphatase dephosphorylates phosphoserines 2 and 5 of RNA polymerase II. J. Biol. Chem. 277:2002;45949-45956.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45949-45956
    • Lin, P.S.1    Dubois, M.F.2    Dahmus, M.E.3
  • 34
    • 0033105914 scopus 로고    scopus 로고
    • Heat shock of HeLa cells inactivates a nuclear protein phosphatase specific for dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II
    • Dubois M.-F., Marshall N.F., Nguyen V.T., Dahmus G.K., Bonnet F., Dahmus M.E., Bensaude O. Heat shock of HeLa cells inactivates a nuclear protein phosphatase specific for dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II. Nucl. Acids Res. 27:1999;1338-1344.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 1338-1344
    • Dubois, M.-F.1    Marshall, N.F.2    Nguyen, V.T.3    Dahmus, G.K.4    Bonnet, F.5    Dahmus, M.E.6    Bensaude, O.7
  • 35
    • 0026672986 scopus 로고
    • The interaction of RNA polymerase II with the Adenovirus-2 major late promoter precluded by phosphorylation of the C-terminal domain of subunit IIa
    • Chesnut J.D., Stephens J.H., Dahmus M.E. The interaction of RNA polymerase II with the Adenovirus-2 major late promoter precluded by phosphorylation of the C-terminal domain of subunit IIa. J. Biol. Chem. 267:1992;10500-10506.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10500-10506
    • Chesnut, J.D.1    Stephens, J.H.2    Dahmus, M.E.3
  • 36
    • 0034050649 scopus 로고    scopus 로고
    • Requirement of the prolyl-isomerase Pin1 for the replication checkpoint
    • Winkler K.E., Swenson K.I., Kornbluth S., Means A.R. Requirement of the prolyl-isomerase Pin1 for the replication checkpoint. Science. 287:2000;1644-1647.
    • (2000) Science , vol.287 , pp. 1644-1647
    • Winkler, K.E.1    Swenson, K.I.2    Kornbluth, S.3    Means, A.R.4
  • 37
    • 0037181170 scopus 로고    scopus 로고
    • Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast FCP1
    • Kops O., Zhou X.Z., Lu K.P. Pin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast FCP1. FEBS Letters. 513:2002;305-311.
    • (2002) FEBS Letters , vol.513 , pp. 305-311
    • Kops, O.1    Zhou, X.Z.2    Lu, K.P.3
  • 38
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine- or phosphothreonine-binding modules
    • Lu P.J., Zhou X.Z., Shen M., Lu K.P. Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science. 283:1999;1325-1328.
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P.J.1    Zhou, X.Z.2    Shen, M.3    Lu, K.P.4
  • 39
    • 0035844058 scopus 로고    scopus 로고
    • Binding and regulation of the transcription factor NFAT by the peptidyl prolyl cis-trans isomerase Pin1
    • Liu W., Youn H.D., Zhou X.Z., Lu K.P., Liu J.O. Binding and regulation of the transcription factor NFAT by the peptidyl prolyl cis-trans isomerase Pin1. FEBS Letters. 496:2001;105-108.
    • (2001) FEBS Letters , vol.496 , pp. 105-108
    • Liu, W.1    Youn, H.D.2    Zhou, X.Z.3    Lu, K.P.4    Liu, J.O.5
  • 40
    • 0032039075 scopus 로고    scopus 로고
    • Selective inhibition of NFAT activation by a peptide spanning the calcineurin targeting site of NFAT
    • Aramburu J., Garcia-Cozar F., Raghavan A., Okamura H., Rao A., Hogan P.G. Selective inhibition of NFAT activation by a peptide spanning the calcineurin targeting site of NFAT. Mol. Cell. 1:1998;627-637.
    • (1998) Mol. Cell , vol.1 , pp. 627-637
    • Aramburu, J.1    Garcia-Cozar, F.2    Raghavan, A.3    Okamura, H.4    Rao, A.5    Hogan, P.G.6
  • 41
    • 0030728698 scopus 로고    scopus 로고
    • Pre-mRNA processing and the CTD of RNA polymerase II: The tail that wags the dog?
    • Steinmetz E.J. Pre-mRNA processing and the CTD of RNA polymerase II: the tail that wags the dog? Cell. 89:1997;491-494.
    • (1997) Cell , vol.89 , pp. 491-494
    • Steinmetz, E.J.1
  • 42
    • 0034307172 scopus 로고    scopus 로고
    • Dynamic association of capping enzymes with transcribing RNA polymerase II
    • Schroeder S.C., Schwer B., Shuman S., Bentley D. Dynamic association of capping enzymes with transcribing RNA polymerase II. Genes Dev. 14:2000;2435-2440.
    • (2000) Genes Dev. , vol.14 , pp. 2435-2440
    • Schroeder, S.C.1    Schwer, B.2    Shuman, S.3    Bentley, D.4
  • 43
    • 0035893314 scopus 로고    scopus 로고
    • Opposing effects of Ctk1 kinase and Fcp1 phosphatase at Ser2 of the RNA polymerase II C-terminal domain
    • Cho E.J., Kobor M.S., Kim M., Greenblatt J., Buratowski S. Opposing effects of Ctk1 kinase and Fcp1 phosphatase at Ser2 of the RNA polymerase II C-terminal domain. Genes Dev. 15:2001;3319-3329.
    • (2001) Genes Dev. , vol.15 , pp. 3319-3329
    • Cho, E.J.1    Kobor, M.S.2    Kim, M.3    Greenblatt, J.4    Buratowski, S.5
  • 44
    • 0035965126 scopus 로고    scopus 로고
    • The peptidyl-prolyl isomerase Pin1 interacts with hSPT5 phosphorylated by Cdk9
    • Lavoie S.B., Albert A.L., Handa H., Vincent M., Bensaude O. The peptidyl-prolyl isomerase Pin1 interacts with hSPT5 phosphorylated by Cdk9. J. Mol. Biol. 312:2001;675-685.
    • (2001) J. Mol. Biol. , vol.312 , pp. 675-685
    • Lavoie, S.B.1    Albert, A.L.2    Handa, H.3    Vincent, M.4    Bensaude, O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.