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Volumn 88, Issue 1, 2010, Pages 77-88

Comparison of the multiple oligomeric structures observed for the Rvb1 and Rvb2 proteins

Author keywords

AAA+; Pontin; Reptin; Rvb1; Rvb2

Indexed keywords

APOPTOSIS; CELLULAR ACTIVITIES; CELLULAR TRANSFORMATION; CHROMATIN REMODELING; COMPARATIVE ANALYSIS; NUCLEOLAR RNA; OLIGOMERIC STRUCTURE; PROTEIN STRUCTURES; STRUCTURAL STUDIES;

EID: 75349085062     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/O09-159     Document Type: Conference Paper
Times cited : (40)

References (36)
  • 1
    • 28144462571 scopus 로고    scopus 로고
    • Characterization of a human SWI2/SNF2 like protein hINO80: Demonstration of catalytic and DNA binding activity
    • PMID:16298340, doi:10.1016/j.bbrc.2005.10.206
    • Bakshi, R., Mehta, A.K., Sharma, R., Maiti, S., Pasha, S., and Brahmachari, V. 2006. Characterization of a human SWI2/SNF2 like protein hINO80: demonstration of catalytic and DNA binding activity. Biochem. Biophys. Res. Commun. 339(1): 313-320. doi:10.1016/j.bbrc.2005.10.206. PMID:16298340.
    • (2006) Biochem. Biophys. Res. Commun , vol.339 , Issue.1 , pp. 313-320
    • Bakshi, R.1    Mehta, A.K.2    Sharma, R.3    Maiti, S.4    Pasha, S.5    Brahmachari, V.6
  • 2
    • 0034669058 scopus 로고    scopus 로고
    • Pontin52 and reptin52 function as antagonistic regulators of beta-catenin signalling activity
    • PMID: 11080158, doi:10.1093/emboj/19.22.6121
    • Bauer, A., Chauvet, S., Huber, O., Usseglio, F., Rothbächer, U., Aragnol, D., et al. 2000. Pontin52 and reptin52 function as antagonistic regulators of beta-catenin signalling activity. EMBO J. 19(22): 6121-6130. doi:10.1093/emboj/19.22.6121. PMID: 11080158.
    • (2000) EMBO J , vol.19 , Issue.22 , pp. 6121-6130
    • Bauer, A.1    Chauvet, S.2    Huber, O.3    Usseglio, F.4    Rothbächer, U.5    Aragnol, D.6
  • 3
    • 0038475879 scopus 로고    scopus 로고
    • Reconstitution of the Mcm2-7p heterohexamer, subunit arrangement, and ATP site architecture
    • PMID:12480933, doi:10. 1074/jbc.M210511200
    • Davey, M.J., Indiani, C., and O'Donnell, M. 2003. Reconstitution of the Mcm2-7p heterohexamer, subunit arrangement, and ATP site architecture. J. Biol. Chem. 278(7): 4491-4499. doi:10. 1074/jbc.M210511200. PMID:12480933.
    • (2003) J. Biol. Chem , vol.278 , Issue.7 , pp. 4491-4499
    • Davey, M.J.1    Indiani, C.2    O'Donnell, M.3
  • 4
    • 0037336323 scopus 로고    scopus 로고
    • Fletcher, R.J., Bishop, B.E., Leon, R.P., Sclafani, R.A., Ogata, C.M., and Chen, X.S. 2003. The structure and function of MCM from archaeal M. Thermoautotrophicum. Nat. Struct. Biol. 10(3): 160-167. doi:10.1038/nsb893. PMID:12548282.
    • Fletcher, R.J., Bishop, B.E., Leon, R.P., Sclafani, R.A., Ogata, C.M., and Chen, X.S. 2003. The structure and function of MCM from archaeal M. Thermoautotrophicum. Nat. Struct. Biol. 10(3): 160-167. doi:10.1038/nsb893. PMID:12548282.
  • 5
    • 0035839104 scopus 로고    scopus 로고
    • The p400 complex is an essential E1A transformation target
    • PMID:11509179, doi:10.1016/S0092-8674(01) 00450-0
    • Fuchs, M., Gerber, J., Drapkin, R., Sif, S., Ikura, T., Ogryzko, V., et al. 2001. The p400 complex is an essential E1A transformation target. Cell, 106(3): 297-307. doi:10.1016/S0092-8674(01) 00450-0. PMID:11509179.
    • (2001) Cell , vol.106 , Issue.3 , pp. 297-307
    • Fuchs, M.1    Gerber, J.2    Drapkin, R.3    Sif, S.4    Ikura, T.5    Ogryzko, V.6
  • 6
    • 0141841630 scopus 로고    scopus 로고
    • The ATP-dependent helicase RUVBL1/TIP49a associates with tubulin during mitosis
    • PMID:14506706, doi:10.1002/cm.10136
    • Gartner, W., Rossbacher, J., Zierhut, B., Daneva, T., Base, W., Weissel, M., et al. 2003. The ATP-dependent helicase RUVBL1/TIP49a associates with tubulin during mitosis. Cell Motil. Cytoskeleton, 56(2): 79-93. doi:10.1002/cm.10136. PMID:14506706.
    • (2003) Cell Motil. Cytoskeleton , vol.56 , Issue.2 , pp. 79-93
    • Gartner, W.1    Rossbacher, J.2    Zierhut, B.3    Daneva, T.4    Base, W.5    Weissel, M.6
  • 7
    • 39049098269 scopus 로고    scopus 로고
    • Yeast Rvb1 and Rvb2 are ATP-dependent DNA helicases that form a heterohexameric complex
    • PMID:18234224, doi:10.1016/j.jmb.2007.12.049
    • Gribun, A., Cheung, K.L., Huen, J., Ortega, J., and Houry, W.A. 2008. Yeast Rvb1 and Rvb2 are ATP-dependent DNA helicases that form a heterohexameric complex. J. Mol. Biol. 376(5): 1320-1333. doi:10.1016/j.jmb.2007.12.049. PMID:18234224.
    • (2008) J. Mol. Biol , vol.376 , Issue.5 , pp. 1320-1333
    • Gribun, A.1    Cheung, K.L.2    Huen, J.3    Ortega, J.4    Houry, W.A.5
  • 8
    • 21744446127 scopus 로고    scopus 로고
    • AAA+ proteins: Have engine, will work
    • PMID:16072036, doi:10. 1038/nrm1684
    • Hanson, P.I., and Whiteheart, S.W. 2005. AAA+ proteins: have engine, will work. Nat. Rev. Mol. Cell Biol. 6(7): 519-529. doi:10. 1038/nrm1684. PMID:16072036.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , Issue.7 , pp. 519-529
    • Hanson, P.I.1    Whiteheart, S.W.2
  • 9
    • 75349105801 scopus 로고    scopus 로고
    • Huen, J., Kakihara, Y., Ugwu, F., Cheung, K., Ortega, J., and Houry, W.A. 2010. Rvb1/2: essential ATP-dependent hilcases for critical complexes. Biochem. Cell. Biol. 88: this issue.
    • Huen, J., Kakihara, Y., Ugwu, F., Cheung, K., Ortega, J., and Houry, W.A. 2010. Rvb1/2: essential ATP-dependent hilcases for critical complexes. Biochem. Cell. Biol. 88: this issue.
  • 10
    • 0034682736 scopus 로고    scopus 로고
    • Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis
    • PMID: 10966108, doi:10.1016/S0092- 8674(00)00051-9
    • Ikura, T., Ogryzko, V.V., Grigoriev, M., Groisman, R., Wang, J., Horikoshi, M., et al. 2000. Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell, 102(4): 463-473. doi:10.1016/S0092- 8674(00)00051-9. PMID: 10966108.
    • (2000) Cell , vol.102 , Issue.4 , pp. 463-473
    • Ikura, T.1    Ogryzko, V.V.2    Grigoriev, M.3    Groisman, R.4    Wang, J.5    Horikoshi, M.6
  • 11
    • 28144460300 scopus 로고    scopus 로고
    • A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex
    • PMID: 16230350, doi:10.1074/jbc.M509128200
    • Jin, J., Cai, Y., Yao, T., Gottschalk, A.J., Florens, L., Swanson, S.K., et al. 2005. A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex. J. Biol. Chem. 280(50): 41207-41212. doi:10.1074/jbc.M509128200. PMID: 16230350.
    • (2005) J. Biol. Chem , vol.280 , Issue.50 , pp. 41207-41212
    • Jin, J.1    Cai, Y.2    Yao, T.3    Gottschalk, A.J.4    Florens, L.5    Swanson, S.K.6
  • 12
    • 0037515607 scopus 로고    scopus 로고
    • Ordered ATP hydrolysis in the gamma complex clamp loader AAA+ machine
    • PMID:12582167, doi:10.1074/jbc.M212708200
    • Johnson, A., and O'Donnell, M. 2003. Ordered ATP hydrolysis in the gamma complex clamp loader AAA+ machine. J. Biol. Chem. 278(16): 14406-14413. doi:10.1074/jbc.M212708200. PMID:12582167.
    • (2003) J. Biol. Chem , vol.278 , Issue.16 , pp. 14406-14413
    • Johnson, A.1    O'Donnell, M.2
  • 13
    • 0033543650 scopus 로고    scopus 로고
    • Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH
    • PMID:10473576, doi:10.1074/jbc.274. 37.26225
    • Karata, K., Inagawa, T., Wilkinson, A.J., Tatsuta, T., and Ogura, T. 1999. Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH. J. Biol. Chem. 274(37): 26225-26232. doi:10.1074/jbc.274. 37.26225. PMID:10473576.
    • (1999) J. Biol. Chem , vol.274 , Issue.37 , pp. 26225-26232
    • Karata, K.1    Inagawa, T.2    Wilkinson, A.J.3    Tatsuta, T.4    Ogura, T.5
  • 14
    • 0034769951 scopus 로고    scopus 로고
    • A well-connected and conserved nucleoplasmic helicase is required for production of box C/D and H/ACA snoRNAs and localization of snoRNP proteins
    • PMID:11604509, doi:10.1128/MCB.21.22.7731-7746.2001
    • King, T.H., Decatur, W.A., Bertrand, E., Maxwell, E.S., and Fournier, M.J. 2001. A well-connected and conserved nucleoplasmic helicase is required for production of box C/D and H/ACA snoRNAs and localization of snoRNP proteins. Mol. Cell. Biol. 21(22): 7731-7746. doi:10.1128/MCB.21.22.7731-7746.2001. PMID:11604509.
    • (2001) Mol. Cell. Biol , vol.21 , Issue.22 , pp. 7731-7746
    • King, T.H.1    Decatur, W.A.2    Bertrand, E.3    Maxwell, E.S.4    Fournier, M.J.5
  • 15
    • 9144269660 scopus 로고    scopus 로고
    • A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1
    • PMID: 14690608, doi:10.1016/S1097-2765(03) 00497-0
    • Krogan, N.J., Keogh, M.C., Datta, N., Sawa, C., Ryan, O.W., Ding, H., et al. 2003. A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1. Mol. Cell, 12(6): 1565-1576. doi:10.1016/S1097-2765(03) 00497-0. PMID: 14690608.
    • (2003) Mol. Cell , vol.12 , Issue.6 , pp. 1565-1576
    • Krogan, N.J.1    Keogh, M.C.2    Datta, N.3    Sawa, C.4    Ryan, O.W.5    Ding, H.6
  • 16
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of Nethylmaleimide-sensitive fusion protein
    • PMID:9727495, doi:10.1016/S0092-8674(00)81593-7
    • Lenzen, C.U., Steinmann, D., Whiteheart, S.W., and Weis, W.I. 1998. Crystal structure of the hexamerization domain of Nethylmaleimide-sensitive fusion protein. Cell, 94(4): 525-536. doi:10.1016/S0092-8674(00)81593-7. PMID:9727495.
    • (1998) Cell , vol.94 , Issue.4 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 17
    • 0038700763 scopus 로고    scopus 로고
    • Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen
    • PMID:12774115, doi:10.1038/nature01691
    • Li, D., Zhao, R., Lilyestrom, W., Gai, D., Zhang, R., DeCaprio, J.A., et al. 2003. Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen. Nature, 423(6939): 512-518. doi:10.1038/nature01691. PMID:12774115.
    • (2003) Nature , vol.423 , Issue.6939 , pp. 512-518
    • Li, D.1    Zhao, R.2    Lilyestrom, W.3    Gai, D.4    Zhang, R.5    DeCaprio, J.A.6
  • 18
    • 0036914160 scopus 로고    scopus 로고
    • AAA proteins.
    • PMID:12504679, doi:10.1016/S0959-440X(02) 00388-3
    • Lupas, A.N., and Martin, J. 2002. AAA proteins. Curr. Opin. Struct. Biol. 12(6): 746-753. doi:10.1016/S0959-440X(02) 00388-3. PMID:12504679.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , Issue.6 , pp. 746-753
    • Lupas, A.N.1    Martin, J.2
  • 19
    • 33846007717 scopus 로고    scopus 로고
    • Crystal structure of the human AAA+ protein RuvBL1
    • PMID:17060327, doi:10.1074/jbc.M605625200
    • Matias, P.M., Gorynia, S., Donner, P., and Carrondo, M.A. 2006. Crystal structure of the human AAA+ protein RuvBL1. J. Biol. Chem. 281(50): 38918-38929. doi:10.1074/jbc.M605625200. PMID:17060327.
    • (2006) J. Biol. Chem , vol.281 , Issue.50 , pp. 38918-38929
    • Matias, P.M.1    Gorynia, S.2    Donner, P.3    Carrondo, M.A.4
  • 20
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • PMID: 14645854, doi:10.1126/science. 1090701
    • Mizuguchi, G., Shen, X., Landry, J., Wu, W.H., Sen, S., and Wu, C. 2004. ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science, 303(5656): 343-348. doi:10.1126/science. 1090701. PMID: 14645854.
    • (2004) Science , vol.303 , Issue.5656 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.2    Landry, J.3    Wu, W.H.4    Sen, S.5    Wu, C.6
  • 21
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • PMID:9927482
    • Neuwald, A.F., Aravind, L., Spouge, J.L., and Koonin, E.V. 1999. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9(1): 27-43. PMID:9927482.
    • (1999) Genome Res , vol.9 , Issue.1 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 22
    • 0034081813 scopus 로고    scopus 로고
    • Box C/D snoRNA-associated proteins: Two pairs of evolutionarily ancient proteins and possible links to replication and transcription
    • PMID:10864044, doi:10.1017/S1355838200992446
    • Newman, D.R., Kuhn, J.F., Shanab, G.M., and Maxwell, E.S. 2000. Box C/D snoRNA-associated proteins: two pairs of evolutionarily ancient proteins and possible links to replication and transcription. RNA, 6(6): 861-879. doi:10.1017/S1355838200992446. PMID:10864044.
    • (2000) RNA , vol.6 , Issue.6 , pp. 861-879
    • Newman, D.R.1    Kuhn, J.F.2    Shanab, G.M.3    Maxwell, E.S.4
  • 23
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure-diverse function
    • PMID:11473577, doi:10.1046/j.1365-2443.2001.00447.x
    • Ogura, T., and Wilkinson, A.J. 2001. AAA+ superfamily ATPases: common structure-diverse function. Genes Cells, 6(7): 575-597. doi:10.1046/j.1365-2443.2001.00447.x. PMID:11473577.
    • (2001) Genes Cells , vol.6 , Issue.7 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 24
    • 33846286030 scopus 로고    scopus 로고
    • Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex
    • PMID:17157868, doi:10.1016/j. jmb.2006.11.030
    • Puri, T., Wendler, P., Sigala, B., Saibil, H., and Tsaneva, I.R. 2007. Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex. J. Mol. Biol. 366(1): 179-192. doi:10.1016/j. jmb.2006.11.030. PMID:17157868.
    • (2007) J. Mol. Biol , vol.366 , Issue.1 , pp. 179-192
    • Puri, T.1    Wendler, P.2    Sigala, B.3    Saibil, H.4    Tsaneva, I.R.5
  • 25
    • 0035839032 scopus 로고    scopus 로고
    • Structure and mechanism of the RuvB Holliday junction branch migration motor
    • PMID:11478862, doi:10.1006/jmbi.2001. 4852
    • Putnam, C.D., Clancy, S.B., Tsuruta, H., Gonzalez, S., Wetmur, J.G., and Tainer, J.A. 2001. Structure and mechanism of the RuvB Holliday junction branch migration motor. J. Mol. Biol. 311(2): 297-310. doi:10.1006/jmbi.2001. 4852. PMID:11478862.
    • (2001) J. Mol. Biol , vol.311 , Issue.2 , pp. 297-310
    • Putnam, C.D.1    Clancy, S.B.2    Tsuruta, H.3    Gonzalez, S.4    Wetmur, J.G.5    Tainer, J.A.6
  • 26
    • 0032561183 scopus 로고    scopus 로고
    • An eukaryotic RuvB-like protein (RUVBL1) essential for growth
    • PMID:9774387, doi:10.1074/jbc.273.43.27786
    • Qiu, X.B., Lin, Y.L., Thome, K.C., Pian, P., Schlegel, B.P., Weremowicz, S., et al. 1998. An eukaryotic RuvB-like protein (RUVBL1) essential for growth. J. Biol. Chem. 273(43): 27786-27793. doi:10.1074/jbc.273.43.27786. PMID:9774387.
    • (1998) J. Biol. Chem , vol.273 , Issue.43 , pp. 27786-27793
    • Qiu, X.B.1    Lin, Y.L.2    Thome, K.C.3    Pian, P.4    Schlegel, B.P.5    Weremowicz, S.6
  • 27
    • 0032766242 scopus 로고    scopus 로고
    • MgATP binding and hydrolysis determinants of NtrC, a bacterial enhancer-binding protein
    • PMID:10419963
    • Rombel, I., Peters-Wendisch, P., Mesecar, A., Thorgeirsson, T., Shin, Y.K., and Kustu, S. 1999. MgATP binding and hydrolysis determinants of NtrC, a bacterial enhancer-binding protein. J. Bacteriol. 181(15): 4628-4638. PMID:10419963.
    • (1999) J. Bacteriol , vol.181 , Issue.15 , pp. 4628-4638
    • Rombel, I.1    Peters-Wendisch, P.2    Mesecar, A.3    Thorgeirsson, T.4    Shin, Y.K.5    Kustu, S.6
  • 28
    • 0033780164 scopus 로고    scopus 로고
    • Fitting atomic models into electron-microscopy maps
    • PMID:10998631, doi:10.1107/S0907444900009562
    • Rossmann, M.G. 2000. Fitting atomic models into electron-microscopy maps. Acta Crystallogr. D Biol. Crystallogr. 56(Pt 10): 1341-1349. doi:10.1107/S0907444900009562. PMID:10998631.
    • (2000) Acta Crystallogr. D Biol. Crystallogr , vol.56 , Issue.PART 10 , pp. 1341-1349
    • Rossmann, M.G.1
  • 29
    • 14844338484 scopus 로고    scopus 로고
    • Combining X-ray crystallography and electron microscopy
    • PMID:15766536, doi:10.1016/j.str.2005.01.005
    • Rossmann, M.G., Morais, M.C., Leiman, P.G., and Zhang, W. 2005. Combining X-ray crystallography and electron microscopy. Structure, 13(3): 355-362. doi:10.1016/j.str.2005.01.005. PMID:15766536.
    • (2005) Structure , vol.13 , Issue.3 , pp. 355-362
    • Rossmann, M.G.1    Morais, M.C.2    Leiman, P.G.3    Zhang, W.4
  • 30
    • 0034601464 scopus 로고    scopus 로고
    • A chromatin remodelling complex involved in transcription and DNA processing
    • PMID:10952318, doi:10.1038/35020123
    • Shen, X., Mizuguchi, G., Hamiche, A., and Wu, C. 2000. A chromatin remodelling complex involved in transcription and DNA processing. Nature, 406(6795): 541-544. doi:10.1038/35020123. PMID:10952318.
    • (2000) Nature , vol.406 , Issue.6795 , pp. 541-544
    • Shen, X.1    Mizuguchi, G.2    Hamiche, A.3    Wu, C.4
  • 31
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • PMID: 10892646, doi:10.1016/S0092-8674(00)80871-5
    • Singleton, M.R., Sawaya, M.R., Ellenberger, T., and Wigley, D.B. 2000. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell, 101(6): 589-600. doi:10.1016/S0092-8674(00)80871-5. PMID: 10892646.
    • (2000) Cell , vol.101 , Issue.6 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 32
    • 39449115385 scopus 로고    scopus 로고
    • AAA+ proteins: Diversity in function, similarity in structure
    • PMID:18208389, doi:10.1042/BST0360072
    • Snider, J., and Houry, W.A. 2008. AAA+ proteins: diversity in function, similarity in structure. Biochem. Soc. Trans. 36(Pt 1): 72-77. doi:10.1042/BST0360072. PMID:18208389.
    • (2008) Biochem. Soc. Trans , vol.36 , Issue.PART 1 , pp. 72-77
    • Snider, J.1    Houry, W.A.2
  • 33
    • 65149084160 scopus 로고    scopus 로고
    • The AAA+ superfamily of functionally diverse proteins
    • PMID:18466635, doi:10.1186/gb-2008-9-4-216
    • Snider, J., Thibault, G., and Houry, W.A. 2008. The AAA+ superfamily of functionally diverse proteins. Genome Biol. 9(4): 216. doi:10.1186/gb-2008-9-4-216. PMID:18466635.
    • (2008) Genome Biol , vol.9 , Issue.4 , pp. 216
    • Snider, J.1    Thibault, G.2    Houry, W.A.3
  • 34
    • 53049099436 scopus 로고    scopus 로고
    • Architecture of the pontin/reptin complex, essential in the assembly of several macromolecular complexes
    • PMID:18940606, doi:10.1016/j.str.2008.08. 009
    • Torreira, E., Jha, S., López-Blanco, J.R., Arias-Palomo, E., Chacón, P., Cañas, C., et al. 2008. Architecture of the pontin/reptin complex, essential in the assembly of several macromolecular complexes. Structure, 16(10): 1511-1520. doi:10.1016/j.str.2008.08. 009. PMID:18940606.
    • (2008) Structure , vol.16 , Issue.10 , pp. 1511-1520
    • Torreira, E.1    Jha, S.2    López-Blanco, J.R.3    Arias-Palomo, E.4    Chacón, P.5    Cañas, C.6
  • 35
    • 0033859666 scopus 로고    scopus 로고
    • An ATPase/helicase complex is an essential cofactor for oncogenic transformation by c-Myc
    • PMID:10882073, doi:10.1016/S1097-2765(00)80427-X
    • Wood, M.A., McMahon, S.B., and Cole, M.D. 2000. An ATPase/helicase complex is an essential cofactor for oncogenic transformation by c-Myc. Mol. Cell, 5(2): 321-330. doi:10.1016/S1097-2765(00)80427-X. PMID:10882073.
    • (2000) Mol. Cell , vol.5 , Issue.2 , pp. 321-330
    • Wood, M.A.1    McMahon, S.B.2    Cole, M.D.3
  • 36
    • 39049143941 scopus 로고    scopus 로고
    • Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation
    • PMID:18268103, doi:10. 1083/jcb.200709061
    • Zhao, R., Kakihara, Y., Gribun, A., Huen, J., Yang, G., Khanna, M., et al. 2008. Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. J. Cell Biol. 180(3): 563-578. doi:10. 1083/jcb.200709061. PMID:18268103.
    • (2008) J. Cell Biol , vol.180 , Issue.3 , pp. 563-578
    • Zhao, R.1    Kakihara, Y.2    Gribun, A.3    Huen, J.4    Yang, G.5    Khanna, M.6


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