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Volumn 368, Issue 1617, 2013, Pages 1-12

Chaperone-like activity of the AAAþproteins RVb1 and RVb2 in the assembly of various complexes

Author keywords

Ino80; PIKK; R2TP; RNA polymerase ii; Rvb1; Rvb2

Indexed keywords

CRITICAL ANALYSIS; ENZYME ACTIVITY; EUKARYOTE; HYDROLYSIS; PROTEIN; SIGNALING;

EID: 84883870558     PISSN: 09628436     EISSN: 14712970     Source Type: Journal    
DOI: 10.1098/rstb.2011.0399     Document Type: Review
Times cited : (79)

References (88)
  • 1
    • 0032969563 scopus 로고    scopus 로고
    • AAA{thorn}: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald AF, Aravind L, Spouge JL, Koonin EV. 1999 AAA{thorn}: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43.
    • (1999) Genome Res , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 2
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA{thorn} ATPases
    • doi:10.1016/j.jsb.2003.10.010
    • Iyer LM, Leipe DD, Koonin EV, Aravind L. 2004 Evolutionary history and higher order classification of AAA{thorn} ATPases. J. Struct. Biol. 146, 11-31. (doi:10.1016/j.jsb.2003.10.010)
    • (2004) J. Struct. Biol , vol.146 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 3
    • 65149084160 scopus 로고    scopus 로고
    • The AAA{thorn} superfamily of functionally diverse proteins
    • doi:10.1186/gb-2008-9-4-216
    • Snider J, Thibault G, Houry WA. 2008 The AAA{thorn} superfamily of functionally diverse proteins. Genome Biol. 9, 216. (doi:10.1186/gb-2008-9-4-216)
    • (2008) Genome Biol , vol.9 , pp. 216
    • Snider, J.1    Thibault, G.2    Houry, W.A.3
  • 4
    • 0001607723 scopus 로고
    • Distantly related sequences in the a-and b-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Saraste M, Runswick MJ, Gay NJ. 1982 Distantly related sequences in the a-and b-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 6
    • 0032411641 scopus 로고    scopus 로고
    • Pontin52, an interaction partner of beta-catenin, binds to the TATA box binding protein
    • 792, doi:10.1073/pnas.95.25.14787
    • Bauer A, Huber O, Kemler R. 1998 Pontin52, an interaction partner of beta-catenin, binds to the TATA box binding protein. Proc. Natl Acad. Sci. USA 95, 14 787-14 792. (doi:10.1073/pnas.95.25.14787)
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , Issue.14
    • Bauer, A.1    Huber, O.2    Kemler, R.3
  • 7
    • 0033859666 scopus 로고    scopus 로고
    • An ATPase/ helicase complex is an essential cofactor for oncogenic transformation by c-Myc
    • doi:10.1016/S1097-2765(00)80427-X
    • Wood MA, McMahon SB, Cole MD. 2000 An ATPase/ helicase complex is an essential cofactor for oncogenic transformation by c-Myc. Mol. Cell 5, 321-330. (doi:10.1016/S1097-2765(00)80427-X)
    • (2000) Mol. Cell , vol.5 , pp. 321-330
    • Wood, M.A.1    McMahon, S.B.2    Cole, M.D.3
  • 8
    • 0034669058 scopus 로고    scopus 로고
    • Pontin52 and reptin52 function as antagonistic regulators of beta-catenin signalling activity
    • doi:10.1093/emboj/19.22.6121
    • Bauer A, Chauvet S, Huber O, Usseglio F, Rothbacher U, Aragnol D, Kemler R, Pradel J. 2000 Pontin52 and reptin52 function as antagonistic regulators of beta-catenin signalling activity. EMBO J. 19, 6121-6130. (doi:10.1093/emboj/19.22.6121)
    • (2000) EMBO J , vol.19 , pp. 6121-6130
    • Bauer, A.1    Chauvet, S.2    Huber, O.3    Usseglio, F.4    Rothbacher, U.5    Aragnol, D.6    Kemler, R.7    Pradel, J.8
  • 9
    • 0035844141 scopus 로고    scopus 로고
    • Rvb1p and Rvb2p are essential components of a chromatin remodeling complex that regulates transcription of over 5% of yeast genes
    • doi:10.1074/jbc. M011523200
    • Jonsson ZO, Dhar SK, Narlikar GJ, Auty R, Wagle N, Pellman D, Pratt RE, Kingston R, Dutta A. 2001 Rvb1p and Rvb2p are essential components of a chromatin remodeling complex that regulates transcription of over 5% of yeast genes. J. Biol. Chem. 276, 16 279-16 288. (doi:10.1074/jbc. M011523200)
    • (2001) J. Biol. Chem , vol.276 , pp. 16279-16288
    • Jonsson, Z.O.1    Dhar, S.K.2    Narlikar, G.J.3    Auty, R.4    Wagle, N.5    Pellman, D.6    Pratt, R.E.7    Kingston, R.8    Dutta, A.9
  • 10
    • 0031560905 scopus 로고    scopus 로고
    • Molecular cloning of a rat 49-kDa TBP-interacting protein (TIP49) that is highly homologous to the bacterial RuvB
    • doi:10.1006/ bbrc.1997.6729
    • Kanemaki M et al. 1997 Molecular cloning of a rat 49-kDa TBP-interacting protein (TIP49) that is highly homologous to the bacterial RuvB. Biochem. Biophys. Res. Commun. 235, 64-68. (doi:10.1006/ bbrc.1997.6729)
    • (1997) Biochem. Biophys. Res. Commun , vol.235 , pp. 64-68
    • Kanemaki, M.1
  • 12
    • 0033529547 scopus 로고    scopus 로고
    • TIP49b, a new RuvB-like DNA helicase, is included in a complex together with another RuvB-like DNA helicase, TIP49a
    • doi:10.1074/jbc.274.32.22437
    • Kanemaki M, Kurokawa Y, Matsu-ura T, Makino Y, Masani A, Okazaki K, Morishita T, Tamura TA. 1999 TIP49b, a new RuvB-like DNA helicase, is included in a complex together with another RuvB-like DNA helicase, TIP49a. J. Biol. Chem. 274, 22437-22444. (doi:10.1074/jbc.274.32.22437)
    • (1999) J. Biol. Chem , vol.274 , pp. 22437-22444
    • Kanemaki, M.1    Kurokawa, Y.2    Matsu-Ura, T.3    Makino, Y.4    Masani, A.5    Okazaki, K.6    Morishita, T.7    Tamura, T.A.8
  • 13
    • 0035839032 scopus 로고    scopus 로고
    • Structure and mechanism of the RuvB Holliday junction branch migration motor
    • doi:10.1006/jmbi.2001.4852
    • Putnam CD, Clancy SB, Tsuruta H, Gonzalez S, Wetmur JG, Tainer JA. 2001 Structure and mechanism of the RuvB Holliday junction branch migration motor. J. Mol. Biol. 311, 297-310. (doi:10.1006/jmbi.2001.4852)
    • (2001) J. Mol. Biol , vol.311 , 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
  • 15
    • 0027476446 scopus 로고
    • RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro
    • doi:10.1073/pnas.90.4.1315
    • Tsaneva IR, Muller B, West SC. 1993 RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro. Proc. Natl Acad. Sci. USA 90, 1315-1319. (doi:10.1073/pnas.90.4.1315)
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 1315-1319
    • Tsaneva, I.R.1    Muller, B.2    West, S.C.3
  • 16
    • 34249000045 scopus 로고    scopus 로고
    • Functional and comparative characterization of Saccharomyces cerevisiae RVB1 and RVB2 genes with bacterial Ruv homologues
    • doi:10.1111/j.1567-1364.2006. 00205.x
    • Radovic S, Rapisarda VA, Tosato V, Bruschi CV. 2007 Functional and comparative characterization of Saccharomyces cerevisiae RVB1 and RVB2 genes with bacterial Ruv homologues. FEMS Yeast Res. 7, 527-539. (doi:10.1111/j.1567-1364.2006. 00205.x)
    • (2007) FEMS Yeast Res , vol.7 , pp. 527-539
    • Radovic, S.1    Rapisarda, V.A.2    Tosato, V.3    Bruschi, C.V.4
  • 17
    • 39049098269 scopus 로고    scopus 로고
    • Yeast Rvb1 and Rvb2 are ATP-dependent DNA helicases that form a heterohexameric complex
    • doi:10.1016/j.jmb. 2007.12.049
    • Gribun A, Cheung KL, Huen J, Ortega J, Houry WA. 2008 Yeast Rvb1 and Rvb2 are ATP-dependent DNA helicases that form a heterohexameric complex. J. Mol. Biol. 376, 1320-1333. (doi:10.1016/j.jmb. 2007.12.049)
    • (2008) J. Mol. Biol , vol.376 , pp. 1320-1333
    • Gribun, A.1    Cheung, K.L.2    Huen, J.3    Ortega, J.4    Houry, W.A.5
  • 18
    • 33846007717 scopus 로고    scopus 로고
    • Crystal structure of the human AAA{thorn} protein RuvBL1
    • doi:10.1074/jbc.M605625200
    • Matias PM, Gorynia S, Donner P, Carrondo MA. 2006 Crystal structure of the human AAA{thorn} protein RuvBL1. J. Biol. Chem. 281, 38918-38929. (doi:10.1074/jbc.M605625200)
    • (2006) J. Biol. Chem , vol.281 , pp. 38918-38929
    • Matias, P.M.1    Gorynia, S.2    Donner, P.3    Carrondo, M.A.4
  • 19
    • 66449130744 scopus 로고    scopus 로고
    • RVB1/RVB2: Running rings around molecular biology. Mol
    • (doi:10.1016/j.molcel.2009.05.016)
    • Jha S, Dutta A. 2009 RVB1/RVB2: running rings around molecular biology. Mol. Cell 34, 521-533. (doi:10.1016/j.molcel.2009.05.016)
    • (2009) Cell , vol.34 , pp. 521-533
    • Jha, S.1    Dutta, A.2
  • 20
    • 0034601464 scopus 로고    scopus 로고
    • A chromatin remodelling complex involved in transcription and DNA processing
    • doi:10.1038/35020123
    • Shen X, Mizuguchi G, Hamiche A, Wu C. 2000 A chromatin remodelling complex involved in transcription and DNA processing. Nature 406, 541-544. (doi:10.1038/35020123)
    • (2000) Nature , vol.406 , pp. 541-544
    • Shen, X.1    Mizuguchi, G.2    Hamiche, A.3    Wu, C.4
  • 21
    • 28144460300 scopus 로고    scopus 로고
    • A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex
    • doi:10.1074/jbc.M509128200
    • Jin J et al. 2005 A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex. J. Biol. Chem. 280, 41207-41212. (doi:10.1074/jbc.M509128200)
    • (2005) J. Biol. Chem , vol.280 , pp. 41207-41212
    • Jin, J.1
  • 22
    • 28144462571 scopus 로고    scopus 로고
    • Characterization of a human SWI2/SNF2 like protein hINO80: Demonstration of catalytic and DNA binding activity
    • doi:10. 1016/j.bbrc.2005.10.206
    • Bakshi R, Mehta AK, Sharma R, Maiti S, Pasha S, Brahmachari V. 2006 Characterization of a human SWI2/SNF2 like protein hINO80: demonstration of catalytic and DNA binding activity. Biochem. Biophys. Res. Commun. 339, 313-320. (doi:10. 1016/j.bbrc.2005.10.206)
    • (2006) Biochem. Biophys. Res. Commun , vol.339 , pp. 313-320
    • Bakshi, R.1    Mehta, A.K.2    Sharma, R.3    Maiti, S.4    Pasha, S.5    Brahmachari, V.6
  • 23
    • 70350701809 scopus 로고    scopus 로고
    • Cooperative action of TIP48 and TIP49 in H2A.Z exchange catalyzed by acetylation of nucleosomal H2A
    • doi:10.1093/nar/ gkp660)
    • Choi J, Heo K, An W. 2009 Cooperative action of TIP48 and TIP49 in H2A.Z exchange catalyzed by acetylation of nucleosomal H2A. Nucleic Acids Res. 37, 5993-6007. (doi:10.1093/nar/ gkp660)
    • (2009) Nucleic Acids Res , vol.37 , pp. 5993-6007
    • Choi, J.1    Heo, K.2    An, W.3
  • 24
    • 0038013975 scopus 로고    scopus 로고
    • Impairment of the DNA binding activity of the TATA-binding protein renders the transcriptional function of Rvb2p/Tih2p, the yeast RuvB-like protein, essential for cell growth
    • doi:10.1074/jbc. M213220200
    • Ohdate H, Lim CR, Kokubo T, Matsubara K, Kimata Y, Kohno K. 2003 Impairment of the DNA binding activity of the TATA-binding protein renders the transcriptional function of Rvb2p/Tih2p, the yeast RuvB-like protein, essential for cell growth. J. Biol. Chem. 278, 14647-14656. (doi:10.1074/jbc. M213220200)
    • (2003) J. Biol. Chem , vol.278 , pp. 14647-14656
    • Ohdate, H.1    Lim, C.R.2    Kokubo, T.3    Matsubara, K.4    Kimata, Y.5    Kohno, K.6
  • 25
    • 34748904017 scopus 로고    scopus 로고
    • A dynamic scaffold of pre-snoRNP factors facilitates human box C/D snoRNP assembly
    • doi:10.1128/MCB. 01097-07
    • McKeegan KS, Debieux CM, Boulon S, Bertrand E, Watkins NJ. 2007 A dynamic scaffold of pre-snoRNP factors facilitates human box C/D snoRNP assembly. Mol. Cell Biol. 27, 6782-6793. (doi:10.1128/MCB. 01097-07)
    • (2007) Mol. Cell Biol , vol.27 , pp. 6782-6793
    • McKeegan, K.S.1    Debieux, C.M.2    Boulon, S.3    Bertrand, E.4    Watkins, N.J.5
  • 26
    • 39049164474 scopus 로고    scopus 로고
    • The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery
    • doi:10. 1083/jcb.200708110
    • Boulon S et al. 2008 The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery. J. Cell Biol. 180, 579-595. (doi:10. 1083/jcb.200708110)
    • (2008) J. Cell Biol , vol.180 , pp. 579-595
    • Boulon, S.1
  • 27
    • 39049143941 scopus 로고    scopus 로고
    • Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation
    • doi:10. 1083/jcb.200709061
    • Zhao R et al. 2008 Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. J. Cell Biol. 180, 563-578. (doi:10. 1083/jcb.200709061)
    • (2008) J. Cell Biol , vol.180 , pp. 563-578
    • Zhao, R.1
  • 28
    • 70249098848 scopus 로고    scopus 로고
    • Evidence that the AAA{thorn} proteins TIP48 and TIP49 bridge interactions between 15.5K and the related NOP56 and NOP58 proteins during box C/D snoRNP biogenesis
    • doi:10. 1128/MCB.00752-09
    • McKeegan KS, Debieux CM, Watkins NJ. 2009 Evidence that the AAA{thorn} proteins TIP48 and TIP49 bridge interactions between 15.5K and the related NOP56 and NOP58 proteins during box C/D snoRNP biogenesis. Mol. Cell Biol. 29, 4971-4981. (doi:10. 1128/MCB.00752-09)
    • (2009) Mol. Cell Biol , vol.29 , pp. 4971-4981
    • McKeegan, K.S.1    Debieux, C.M.2    Watkins, N.J.3
  • 29
    • 77953771590 scopus 로고    scopus 로고
    • AAA{thorn} proteins RUVBL1 and RUVBL2 coordinate PIKK activity and function in nonsense-mediated mRNA decay
    • doi:10. 1126/scisignal.2000468
    • Izumi N, Yamashita A, Iwamatsu A, Kurata R, Nakamura H, Saari B, Hirano H, Anderson P, Ohno S. 2010 AAA{thorn} proteins RUVBL1 and RUVBL2 coordinate PIKK activity and function in nonsense-mediated mRNA decay. Sci. Signal. 3, ra27. (doi:10. 1126/scisignal.2000468)
    • (2010) Sci. Signal , vol.3 , pp. 27
    • Izumi, N.1    Yamashita, A.2    Iwamatsu, A.3    Kurata, R.4    Nakamura, H.5    Saari, B.6    Hirano, H.7    Anderson, P.8    Ohno, S.9
  • 31
    • 26844527774 scopus 로고    scopus 로고
    • Relocalization of human chromatin remodeling cofactor TIP48 in mitosis
    • doi:10.1016/j.yexcr.2005.07.030
    • Sigala B, Edwards M, Puri T, Tsaneva IR. 2005 Relocalization of human chromatin remodeling cofactor TIP48 in mitosis. Exp. Cell Res. 310, 357-369. (doi:10.1016/j.yexcr.2005.07.030)
    • (2005) Exp. Cell Res , vol.310 , pp. 357-369
    • Sigala, B.1    Edwards, M.2    Puri, T.3    Tsaneva, I.R.4
  • 32
    • 51349153303 scopus 로고    scopus 로고
    • Regulation of microtubule assembly and organization in mitosis by the AAA{thorn} ATPase Pontin
    • doi:10. 1091/mbc.E07-11-1202
    • Ducat D, Kawaguchi S, Liu H, Yates III JR, Zheng Y. 2008 Regulation of microtubule assembly and organization in mitosis by the AAA{thorn} ATPase Pontin. Mol. Biol. Cell 19, 3097-3110. (doi:10. 1091/mbc.E07-11-1202)
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3097-3110
    • Ducat, D.1    Kawaguchi, S.2    Liu, H.3    Yates III., J.R.4    Zheng, Y.5
  • 33
    • 40749135820 scopus 로고    scopus 로고
    • Identification of ATPases pontin and reptin as telomerase components essential for holoenzyme assembly
    • doi:10. 1016/j.cell.2008.01.019
    • Venteicher AS, Meng Z, Mason PJ, Veenstra TD, Artandi SE. 2008 Identification of ATPases pontin and reptin as telomerase components essential for holoenzyme assembly. Cell 132, 945-957. (doi:10. 1016/j.cell.2008.01.019)
    • (2008) Cell , vol.132 , pp. 945-957
    • Venteicher, A.S.1    Meng, Z.2    Mason, P.J.3    Veenstra, T.D.4    Artandi, S.E.5
  • 34
    • 78650077626 scopus 로고    scopus 로고
    • The protein interaction network of the human transcription machinery reveals a role for the conserved GTPase RPAP4/GPN1 and microtubule assembly in nuclear import and biogenesis of RNA polymerase II
    • doi:10.1074/mcp.M110.003616
    • Forget D et al. 2010 The protein interaction network of the human transcription machinery reveals a role for the conserved GTPase RPAP4/GPN1 and microtubule assembly in nuclear import and biogenesis of RNA polymerase II. Mol. Cell. Proteom. 9, 2827-2839. (doi:10.1074/mcp.M110.003616)
    • (2010) Mol. Cell. Proteom , vol.9 , pp. 2827-2839
    • Forget, D.1
  • 35
    • 80455176998 scopus 로고    scopus 로고
    • Structural and functional insights into a dodecameric molecular machine-the RuvBL1/RuvBL2 complex
    • doi:10.1016/j.jsb.2011.09.001
    • Gorynia S et al. 2011 Structural and functional insights into a dodecameric molecular machine-the RuvBL1/RuvBL2 complex. J. Struct. Biol. 176, 279-291. (doi:10.1016/j.jsb.2011.09.001)
    • (2011) J. Struct. Biol , vol.176 , pp. 279-291
    • Gorynia, S.1
  • 36
    • 33846286030 scopus 로고    scopus 로고
    • Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex
    • doi:10.1016/j.jmb.2006.11.030
    • Puri T, Wendler P, Sigala B, Saibil H, Tsaneva IR. 2007 Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex. J. Mol. Biol. 366, 179-192. (doi:10.1016/j.jmb.2006.11.030)
    • (2007) J. Mol. Biol , vol.366 , pp. 179-192
    • Puri, T.1    Wendler, P.2    Sigala, B.3    Saibil, H.4    Tsaneva, I.R.5
  • 37
    • 77954512714 scopus 로고    scopus 로고
    • Oligomeric assembly and interactions within the human RuvB-like RuvBL1 and RuvBL2 complexes
    • (doi:10.1042/BJ20100489)
    • Niewiarowski A, Bradley AS, Gor J, McKay AR, Perkins SJ, Tsaneva IR. 2010 Oligomeric assembly and interactions within the human RuvB-like RuvBL1 and RuvBL2 complexes. Biochem. J. 429, 113-125. (doi:10.1042/BJ20100489)
    • (2010) Biochem. J , vol.429 , pp. 113-125
    • Niewiarowski, A.1    Bradley, A.S.2    Gor, J.3    McKay, A.R.4    Perkins, S.J.5    Tsaneva, I.R.6
  • 38
    • 53049099436 scopus 로고    scopus 로고
    • Architecture of the pontin/reptin complex, essential in the assembly of several macromolecular complexes
    • doi:10.1016/ j.str.2008.08.009
    • Torreira E, Jha S, Lopez-Blanco JR, Arias-Palomo E, Chacon P, Canas C, Ayora S, Dutta A, Llorca O. 2008 Architecture of the pontin/reptin complex, essential in the assembly of several macromolecular complexes. Structure 16, 1511-1520. (doi:10.1016/ j.str.2008.08.009)
    • (2008) Structure , vol.16 , pp. 1511-1520
    • Torreira, E.1    Jha, S.2    Lopez-Blanco, J.R.3    Arias-Palomo, E.4    Chacon, P.5    Canas, C.6    Ayora, S.7    Dutta, A.8    Llorca, O.9
  • 39
    • 78349304846 scopus 로고    scopus 로고
    • Alternative oligomeric states of the yeast Rvb1/Rvb2 complex induced by histidine tags
    • (doi:10.1016/j.jmb. 2010.10.003)
    • Cheung KL, Huen J, Kakihara Y, Houry WA, Ortega J. 2010 Alternative oligomeric states of the yeast Rvb1/Rvb2 complex induced by histidine tags. J. Mol. Biol. 404, 478-492. (doi:10.1016/j.jmb. 2010.10.003)
    • (2010) J. Mol. Biol , vol.404 , pp. 478-492
    • Cheung, K.L.1    Huen, J.2    Kakihara, Y.3    Houry, W.A.4    Ortega, J.5
  • 40
    • 33947724287 scopus 로고    scopus 로고
    • Control of transcription by Pontin and Reptin
    • doi:10. 1016/j.tcb.2007.02.005
    • Gallant P. 2007 Control of transcription by Pontin and Reptin. Trends Cell Biol. 17, 187-192. (doi:10. 1016/j.tcb.2007.02.005)
    • (2007) Trends Cell Biol , vol.17 , pp. 187-192
    • Gallant, P.1
  • 41
    • 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
    • doi:10.1128/MCB.21.22.7731-7746.2001
    • King TH, Decatur WA, Bertrand E, Maxwell ES, Fournier MJ. 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, 7731-7746. (doi:10.1128/MCB.21.22.7731-7746.2001)
    • (2001) Mol. Cell Biol , vol.21 , pp. 7731-7746
    • King, T.H.1    Decatur, W.A.2    Bertrand, E.3    Maxwell, E.S.4    Fournier, M.J.5
  • 42
    • 0035204479 scopus 로고    scopus 로고
    • TIP49b, a regulator of activating transcription factor 2 response to stress and DNA damage
    • doi:10. 1128/MCB.21.24.8398-8413.2001
    • Cho SG, Bhoumik A, Broday L, Ivanov V, Rosenstein B, Ronai Z. 2001 TIP49b, a regulator of activating transcription factor 2 response to stress and DNA damage. Mol. Cell Biol. 21, 8398-8413. (doi:10. 1128/MCB.21.24.8398-8413.2001)
    • (2001) Mol. Cell Biol , vol.21 , pp. 8398-8413
    • Cho, S.G.1    Bhoumik, A.2    Broday, L.3    Ivanov, V.4    Rosenstein, B.5    Ronai, Z.6
  • 43
    • 18744395748 scopus 로고    scopus 로고
    • Reptin and pontin antagonistically regulate heart growth in zebrafish embryos
    • doi:10.1016/S0092-8674(02)01112-1
    • Rottbauer W et al. 2002 Reptin and pontin antagonistically regulate heart growth in zebrafish embryos. Cell 111, 661-672. (doi:10.1016/S0092-8674(02)01112-1)
    • (2002) Cell , vol.111 , pp. 661-672
    • Rottbauer, W.1
  • 44
    • 0346690269 scopus 로고    scopus 로고
    • TIP49 regulates b-catenin-mediated neoplastic transformation and T-cell factor target gene induction via effects on chromatin remodeling
    • Feng Y, Lee N, Fearon ER. 2003 TIP49 regulates b-catenin-mediated neoplastic transformation and T-cell factor target gene induction via effects on chromatin remodeling. Cancer Res. 63, 8726-8734.
    • (2003) Cancer Res , vol.63 , pp. 8726-8734
    • Feng, Y.1    Lee, N.2    Fearon, E.R.3
  • 45
    • 8644257491 scopus 로고    scopus 로고
    • Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin remodeling complex
    • doi:10.1016/j.molcel.2004.09.033
    • Jonsson ZO, Jha S, Wohlschlegel JA, Dutta A. 2004 Rvb1p/Rvb2p recruit Arp5p and assemble a functional Ino80 chromatin remodeling complex. Mol. Cell 16, 465-477. (doi:10.1016/j.molcel.2004.09.033)
    • (2004) Mol. Cell , vol.16 , pp. 465-477
    • Jonsson, Z.O.1    Jha, S.2    Wohlschlegel, J.A.3    Dutta, A.4
  • 46
    • 15944367756 scopus 로고    scopus 로고
    • Pontin and Reptin regulate cell proliferation in early Xenopus embryos in collaboration with c-Myc and Miz-1
    • doi:10.1016/j. mod.2004.11.010
    • Etard C, Gradl D, Kunz M, Eilers M, Wedlich D. 2005 Pontin and Reptin regulate cell proliferation in early Xenopus embryos in collaboration with c-Myc and Miz-1. Mech. Dev. 122, 545-556. (doi:10.1016/j. mod.2004.11.010)
    • (2005) Mech. Dev , vol.122 , pp. 545-556
    • Etard, C.1    Gradl, D.2    Kunz, M.3    Eilers, M.4    Wedlich, D.5
  • 47
    • 40249109998 scopus 로고    scopus 로고
    • Reptin and Pontin function antagonistically with PcG and TrxG complexes to mediate Hox gene control
    • doi:10.1038/embor.2008.8)
    • Diop SB et al. 2008 Reptin and Pontin function antagonistically with PcG and TrxG complexes to mediate Hox gene control. EMBO Rep. 9, 260-266. (doi:10.1038/embor.2008.8)
    • (2008) EMBO Rep , vol.9 , pp. 260-266
    • Diop, S.B.1
  • 48
    • 67449100986 scopus 로고    scopus 로고
    • RuvB-like protein 2 is a suppressor of influenza A virus polymerases
    • doi:10.1128/JVI.00293-09
    • Kakugawa S, Shimojima M, Neumann G, Goto H, Kawaoka Y. 2009 RuvB-like protein 2 is a suppressor of influenza A virus polymerases. J. Virol. 83, 6429-6434. (doi:10.1128/JVI.00293-09)
    • (2009) J. Virol , vol.83 , pp. 6429-6434
    • Kakugawa, S.1    Shimojima, M.2    Neumann, G.3    Goto, H.4    Kawaoka, Y.5
  • 49
    • 59649124959 scopus 로고    scopus 로고
    • The INO80 chromatin remodeling complex in transcription, replication and repair
    • doi:10.1016/j.tibs.2008.10.010
    • Conaway RC, Conaway JW. 2009 The INO80 chromatin remodeling complex in transcription, replication and repair. Trends Biochem. Sci. 34, 71-77. (doi:10.1016/j.tibs.2008.10.010)
    • (2009) Trends Biochem. Sci , vol.34 , pp. 71-77
    • Conaway, R.C.1    Conaway, J.W.2
  • 50
    • 0035313855 scopus 로고    scopus 로고
    • Mechanisms for ATP-dependent chromatin remodelling
    • doi:10.1016/S0959-437X(00)00172-6
    • Flaus A, Owen-Hughes T. 2001 Mechanisms for ATP-dependent chromatin remodelling. Curr. Opin. Genet. Dev. 11, 148-154. (doi:10.1016/S0959-437X(00)00172-6)
    • (2001) Curr. Opin. Genet. Dev , vol.11 , pp. 148-154
    • Flaus, A.1    Owen-Hughes, T.2
  • 51
    • 1942439629 scopus 로고    scopus 로고
    • Mechanisms for ATP-dependent chromatin remodelling: Farewell to the tuna-can octamer
    • doi:10.1016/j.gde.2004.01.007
    • Flaus A, Owen-Hughes T. 2004 Mechanisms for ATP-dependent chromatin remodelling: farewell to the tuna-can octamer? Curr. Opin. Genet. Dev. 14, 165-173. (doi:10.1016/j.gde.2004.01.007)
    • (2004) Curr. Opin. Genet. Dev , vol.14 , pp. 165-173
    • Flaus, A.1    Owen-Hughes, T.2
  • 52
    • 67349147423 scopus 로고    scopus 로고
    • Chromatin remodelling beyond transcription: The INO80 and SWR1 complexes
    • doi:10.1038/nrm2693
    • Morrison AJ, Shen X. 2009 Chromatin remodelling beyond transcription: the INO80 and SWR1 complexes. Nat. Rev. Mol. Cell Biol. 10, 373-384. (doi:10.1038/nrm2693)
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 373-384
    • Morrison, A.J.1    Shen, X.2
  • 53
    • 1342346531 scopus 로고    scopus 로고
    • Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans
    • doi:10. 1128/MCB.24.5.1884-1896.2004
    • Doyon Y, Selleck W, Lane WS, Tan S, Cote J. 2004 Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans. Mol. Cell Biol. 24, 1884-1896. (doi:10. 1128/MCB.24.5.1884-1896.2004)
    • (2004) Mol. Cell Biol , vol.24 , pp. 1884-1896
    • Doyon, Y.1    Selleck, W.2    Lane, W.S.3    Tan, S.4    Cote, J.5
  • 54
    • 19344372948 scopus 로고    scopus 로고
    • A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin
    • doi:10.1371/journal.pbio.0020131)
    • Kobor MS, Venkatasubrahmanyam S, Meneghini MD, Gin JW, Jennings JL, Link AJ, Madhani HD, Rine J. 2004 A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin. PLoS Biol. 2, E131. (doi:10.1371/journal.pbio.0020131)
    • (2004) PLoS Biol , vol.2
    • Kobor, M.S.1    Venkatasubrahmanyam, S.2    Meneghini, M.D.3    Gin, J.W.4    Jennings, J.L.5    Link, A.J.6    Madhani, H.D.7    Rine, J.8
  • 55
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • doi:10.1126/ science.1090701
    • Mizuguchi G, Shen X, Landry J, Wu WH, Sen S, Wu C. 2004 ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science 303, 343-348. (doi:10.1126/ science.1090701)
    • (2004) Science , vol.303 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.2    Landry, J.3    Wu, W.H.4    Sen, S.5    Wu, C.6
  • 56
    • 20244385811 scopus 로고    scopus 로고
    • The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes
    • doi:10.1074/jbc. M500001200
    • Cai Y et al. 2005 The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes. J. Biol. Chem. 280, 13665-13670. (doi:10.1074/jbc. M500001200)
    • (2005) J. Biol. Chem , vol.280 , pp. 13665-13670
    • Cai, Y.1
  • 57
    • 0242322038 scopus 로고    scopus 로고
    • Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex
    • doi:10.1074/jbc.C300389200
    • Cai Y, Jin J, Tomomori-Sato C, Sato S, Sorokina I, Parmely TJ, Conaway RC, Conaway JW. 2003 Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex. J. Biol. Chem. 278, 42733-42736. (doi:10.1074/jbc.C300389200)
    • (2003) J. Biol. Chem , vol.278 , pp. 42733-42736
    • Cai, Y.1    Jin, J.2    Tomomori-Sato, C.3    Sato, S.4    Sorokina, I.5    Parmely, T.J.6    Conaway, R.C.7    Conaway, J.W.8
  • 59
    • 33748897493 scopus 로고    scopus 로고
    • Drosophila Reptin and other TIP60 complex components promote generation of silent chromatin
    • doi:10.1534/genetics.106.059980
    • Qi D, Jin H, Lilja T, Mannervik M. 2006 Drosophila Reptin and other TIP60 complex components promote generation of silent chromatin. Genetics 174, 241-251. (doi:10.1534/genetics.106.059980)
    • (2006) Genetics , vol.174 , pp. 241-251
    • Qi, D.1    Jin, H.2    Lilja, T.3    Mannervik, M.4
  • 60
    • 79953170957 scopus 로고    scopus 로고
    • Subunit organization of the human INO80 chromatin remodeling complex: An evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling
    • doi:10.1074/jbc.M111.222505)
    • Chen L, Cai Y, Jin J, Florens L, Swanson SK, Washburn MP, Conaway JW, Conaway RC. 2011 Subunit organization of the human INO80 chromatin remodeling complex: an evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling. J. Biol. Chem. 286, 11283-11289. doi:10.1074/jbc.M111.222505)
    • (2011) J. Biol. Chem , vol.286 , pp. 11283-11289
    • Chen, L.1    Cai, Y.2    Jin, J.3    Florens, L.4    Swanson, S.K.5    Washburn, M.P.6    Conaway, J.W.7    Conaway, R.C.8
  • 61
    • 9144269660 scopus 로고    scopus 로고
    • A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1
    • doi:10.1016/ S1097-2765(03)00497-0
    • Krogan NJ et al. 2003 A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1. Mol. Cell 12, 1565-1576. (doi:10.1016/ S1097-2765(03)00497-0)
    • (2003) Mol. Cell , vol.12 , pp. 1565-1576
    • Krogan, N.J.1
  • 62
    • 28544442465 scopus 로고    scopus 로고
    • Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange
    • doi:10.1038/nsmb1023
    • Wu WH, Alami S, Luk E, Wu CH, Sen S, Mizuguchi G, Wei D, Wu C. 2005 Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange. Nat. Struct. Mol. Biol. 12, 1064-1071. (doi:10.1038/nsmb1023)
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 1064-1071
    • Wu, W.H.1    Alami, S.2    Luk, E.3    Wu, C.H.4    Sen, S.5    Mizuguchi, G.6    Wei, D.7    Wu, C.8
  • 63
    • 42149162883 scopus 로고    scopus 로고
    • Human Rvb1/Tip49 is required for the histone acetyltransferase activity of Tip60/NuA4 and for the downregulation of phosphorylation on H2AX after DNA damage
    • doi:10.1128/MCB.01983-07)
    • Jha S, Shibata E, Dutta A. 2008 Human Rvb1/Tip49 is required for the histone acetyltransferase activity of Tip60/NuA4 and for the downregulation of phosphorylation on H2AX after DNA damage. Mol. Cell Biol. 28, 2690-2700. (doi:10.1128/MCB.01983-07)
    • (2008) Mol. Cell Biol , vol.28 , pp. 2690-2700
    • Jha, S.1    Shibata, E.2    Dutta, A.3
  • 64
    • 24944516931 scopus 로고    scopus 로고
    • A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM
    • (doi:10.1073/pnas. 0504211102)
    • Sun Y, Jiang X, Chen S, Fernandes N, Price BD. 2005 A role for the Tip60 histone acetyltransferase in the acetylation and activation of ATM. Proc. Natl Acad. Sci. USA 102, 13182-13187. (doi:10.1073/pnas. 0504211102)
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 13182-13187
    • Sun, Y.1    Jiang, X.2    Chen, S.3    Fernandes, N.4    Price, B.D.5
  • 65
    • 0034682736 scopus 로고    scopus 로고
    • Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis
    • (doi:10.1016/S0092-8674(00)00051-9)
    • Ikura T, Ogryzko VV, Grigoriev M, Groisman R, Wang J, Horikoshi M, Scully R, Qin J, Nakatani Y. 2000 Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell 102, 463-473. (doi:10.1016/S0092-8674(00)00051-9)
    • (2000) Cell , vol.102 , pp. 463-473
    • Ikura, T.1    Ogryzko, V.V.2    Grigoriev, M.3    Groisman, R.4    Wang, J.5    Horikoshi, M.6    Scully, R.7    Qin, J.8    Nakatani, Y.9
  • 66
    • 33845656738 scopus 로고    scopus 로고
    • Acetylation of the p53 DNA-binding domain regulates apoptosis induction
    • doi:10.1016/j.molcel.2006.11.026)
    • Sykes SM, Mellert HS, Holbert MA, Li K, Marmorstein R, Lane WS, McMahon SB. 2006 Acetylation of the p53 DNA-binding domain regulates apoptosis induction. Mol. Cell 24, 841-851. doi:10.1016/j.molcel.2006.11.026)
    • (2006) Mol. Cell , vol.24 , pp. 841-851
    • Sykes, S.M.1    Mellert, H.S.2    Holbert, M.A.3    Li, K.4    Marmorstein, R.5    Lane, W.S.6    McMahon, S.B.7
  • 67
    • 0037067655 scopus 로고    scopus 로고
    • Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kB and b-amyloid precursor protein
    • (doi:10.1016/S0092-8674(02)00809-7)
    • Baek SH, Ohgi KA, Rose DW, Koo EH, Glass CK, Rosenfeld MG. 2002 Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kB and b-amyloid precursor protein. Cell 110, 55-67. (doi:10.1016/S0092-8674(02)00809-7)
    • (2002) Cell , vol.110 , pp. 55-67
    • Baek, S.H.1    Ohgi, K.A.2    Rose, D.W.3    Koo, E.H.4    Glass, C.K.5    Rosenfeld, M.G.6
  • 68
    • 20044382800 scopus 로고    scopus 로고
    • Navigating the chaperone network: An integrative map of physical and genetic interactions mediated by the hsp90 chaperone
    • doi:10.1016/j.cell.2004.12.024)
    • Zhao R et al. 2005 Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120, 715-727. (doi:10.1016/j.cell.2004.12.024)
    • (2005) Cell , vol.120 , pp. 715-727
    • Zhao, R.1
  • 69
    • 84857332083 scopus 로고    scopus 로고
    • Structure of minimal tetratricopeptide repeat domain protein tah1 reveals mechanism of its interaction with pih1 and hsp90
    • doi:10. 1074/jbc.M111.287458
    • Jimenez B, Ugwu F, Zhao R, Orti L, Makhnevych T, Pineda-Lucena A, Houry WA. 2012 Structure of minimal tetratricopeptide repeat domain protein tah1 reveals mechanism of its interaction with pih1 and hsp90. J. Biol. Chem. 287, 5698-5709. (doi:10. 1074/jbc.M111.287458)
    • (2012) J. Biol. Chem , vol.287 , pp. 5698-5709
    • Jimenez, B.1    Ugwu, F.2    Zhao, R.3    Orti, L.4    Makhnevych, T.5    Pineda-Lucena, A.6    Houry, W.A.7
  • 70
    • 77956898581 scopus 로고    scopus 로고
    • HSP90 and its R2TP/Prefoldin-like cochaperone are involved in the cytoplasmic assembly of RNA polymerase II
    • doi:10.1016/j.molcel.2010.08.023
    • Boulon S et al. 2010 HSP90 and its R2TP/Prefoldin-like cochaperone are involved in the cytoplasmic assembly of RNA polymerase II. Mol. Cell 39, 912-924. (doi:10.1016/j.molcel.2010.08.023)
    • (2010) Mol. Cell , vol.39 , pp. 912-924
    • Boulon, S.1
  • 71
    • 33847187076 scopus 로고    scopus 로고
    • Non-coding RNAs: Lessons from the small nuclear and small nucleolar RNAs
    • doi:10.1038/nrm2124
    • Matera AG, Terns RM, Terns MP. 2007 Non-coding RNAs: lessons from the small nuclear and small nucleolar RNAs. Nat. Rev. Mol. Cell Biol. 8, 209-220. (doi:10.1038/nrm2124)
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 209-220
    • Matera, A.G.1    Terns, R.M.2    Terns, M.P.3
  • 72
    • 0034721649 scopus 로고    scopus 로고
    • A common core RNP structure shared between the small nucleolar box C/D RNPs and the spliceosomal U4 snRNP
    • doi:10.1016/S0092-8674(00)00137-9)
    • Watkins NJ et al. 2000 A common core RNP structure shared between the small nucleolar box C/D RNPs and the spliceosomal U4 snRNP. Cell 103, 457-466 (doi:10.1016/S0092-8674(00)00137-9)
    • (2000) Cell , vol.103 , pp. 457-466
    • Watkins, N.J.1
  • 73
    • 0036773686 scopus 로고    scopus 로고
    • Exclusive interaction of the 15.5 kD protein with the terminal box C/D motif of a methylation guide snoRNP
    • doi:10. 1016/S1074-5521(02)00239-9)
    • Szewczak LB, DeGregorio SJ, Strobel SA, Steitz JA. 2002 Exclusive interaction of the 15.5 kD protein with the terminal box C/D motif of a methylation guide snoRNP. Chem. Biol. 9, 1095-1107. (doi:10. 1016/S1074-5521(02)00239-9)
    • (2002) Chem. Biol , vol.9 , pp. 1095-1107
    • Szewczak, L.B.1    Degregorio, S.J.2    Strobel, S.A.3    Steitz, J.A.4
  • 74
    • 0036889385 scopus 로고    scopus 로고
    • Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP. Mol
    • doi:10.1128/MCB.22.23.8342-8352.2002
    • Watkins NJ, Dickmanns A, Luhrmann R. 2002 Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP. Mol. Cell Biol. 22, 8342-8352. (doi:10.1128/MCB.22.23.8342-8352.2002)
    • (2002) Cell Biol , vol.22 , pp. 8342-8352
    • Watkins, N.J.1    Dickmanns, A.2    Luhrmann, R.3
  • 75
    • 9744222917 scopus 로고    scopus 로고
    • Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large dynamic multiprotein complex
    • doi:10.1016/j.molcel.2004.11.012
    • Watkins NJ, Lemm I, Ingelfinger D, Schneider C, Hossbach M, Urlaub H, Luhrmann R. 2004 Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large dynamic multiprotein complex. Mol. Cell 16, 789-798. (doi:10.1016/j.molcel.2004.11.012)
    • (2004) Mol. Cell , vol.16 , pp. 789-798
    • Watkins, N.J.1    Lemm, I.2    Ingelfinger, D.3    Schneider, C.4    Hossbach, M.5    Urlaub, H.6    Luhrmann, R.7
  • 76
    • 84855199318 scopus 로고    scopus 로고
    • The R2TP complex: Discovery and functions
    • (doi:10.1016/j.bbamcr.2011.08.016)
    • Kakihara Y, Houry WA. 2012 The R2TP complex: discovery and functions. Biochim. Biophys. Acta 1823, 101-107. (doi:10.1016/j.bbamcr.2011.08.016)
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 101-107
    • Kakihara, Y.1    Houry, W.A.2
  • 77
    • 68249113593 scopus 로고    scopus 로고
    • Common mechanisms of PIKK regulation
    • (doi:10.1016/j.dnarep.2009.04.006)
    • Lovejoy CA, Cortez D. 2009 Common mechanisms of PIKK regulation. DNA Repair (Amst.) 8, 1004-1008. (doi:10.1016/j.dnarep.2009.04.006)
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 1004-1008
    • Lovejoy, C.A.1    Cortez, D.2
  • 78
    • 84855490644 scopus 로고    scopus 로고
    • Heat shock protein 90 regulates phosphatidylinositol 3-kinase-related protein kinase family proteins together with the RUVBL1/2 and Tel2-containing co-factor complex
    • doi:10. 1111/j.1349-7006.2011.02112.x
    • Izumi N, Yamashita A, Hirano H, Ohno S. 2012 Heat shock protein 90 regulates phosphatidylinositol 3-kinase-related protein kinase family proteins together with the RUVBL1/2 and Tel2-containing co-factor complex. Cancer Sci. 103, 50-57. (doi:10. 1111/j.1349-7006.2011.02112.x)
    • (2012) Cancer Sci , vol.103 , pp. 50-57
    • Izumi, N.1    Yamashita, A.2    Hirano, H.3    Ohno, S.4
  • 79
    • 79955602011 scopus 로고    scopus 로고
    • The complete spectrum of yeast chromosome instability genes identifies candidate CIN cancer genes and functional roles for ASTRA complex components
    • (doi:10.1371/journal.pgen.1002057
    • Stirling PC et al. 2011 The complete spectrum of yeast chromosome instability genes identifies candidate CIN cancer genes and functional roles for ASTRA complex components. PLoS Genet. 7, e1002057. (doi:10.1371/journal.pgen.1002057)
    • (2011) PLoS Genet , vol.7
    • Stirling, P.C.1
  • 80
    • 0015844590 scopus 로고
    • A theory of marginotomy. The incomplete copying of template margin in enzymic synthesis of polynucleotides and biological significance of the phenomenon
    • (doi:10.1016/0022-5193(73)90198-7)
    • Olovnikov AM. 1973 A theory of marginotomy. The incomplete copying of template margin in enzymic synthesis of polynucleotides and biological significance of the phenomenon. J. Theor. Biol. 41, 181-190. (doi:10.1016/0022-5193(73)90198-7)
    • (1973) J. Theor. Biol , vol.41 , pp. 181-190
    • Olovnikov, A.M.1
  • 81
    • 77954036420 scopus 로고    scopus 로고
    • Reptin is required for the transcription of telomerase reverse transcriptase and over-expressed in gastric cancer
    • doi:10.1186/1476-4598-9-132
    • Li W, Zeng J, Li Q, Zhao L, Liu T, Bjorkholm M, Jia J, Xu D. 2010 Reptin is required for the transcription of telomerase reverse transcriptase and over-expressed in gastric cancer. Mol. Cancer 9, 132. (doi:10.1186/1476-4598-9-132)
    • (2010) Mol. Cancer , vol.9 , pp. 132
    • Li, W.1    Zeng, J.2    Li, Q.3    Zhao, L.4    Liu, T.5    Bjorkholm, M.6    Jia, J.7    Xu, D.8
  • 82
    • 57949091054 scopus 로고    scopus 로고
    • Chromatin Central: Towards the comparative proteome by accurate mapping of the yeast proteomic environment
    • doi:10.1186/gb-2008-9-11-r167
    • Shevchenko A et al. 2008 Chromatin Central: towards the comparative proteome by accurate mapping of the yeast proteomic environment. Genome Biol. 9, R167. (doi:10.1186/gb-2008-9-11-r167)
    • (2008) Genome Biol , vol.9
    • Shevchenko, A.1
  • 83
    • 52049115398 scopus 로고    scopus 로고
    • Pontin and reptin, two related ATPases with multiple roles in cancer
    • doi:10.1158/0008-5472. CAN-08-0547
    • Huber O, Menard L, Haurie V, Nicou A, Taras D, Rosenbaum J. 2008 Pontin and reptin, two related ATPases with multiple roles in cancer. Cancer Res. 68, 6873-6876. (doi:10.1158/0008-5472. CAN-08-0547)
    • (2008) Cancer Res , vol.68 , pp. 6873-6876
    • Huber, O.1    Menard, L.2    Haurie, V.3    Nicou, A.4    Taras, D.5    Rosenbaum, J.6
  • 84
    • 17244378084 scopus 로고    scopus 로고
    • Transcriptional regulation of a metastasis suppressor gene by Tip60 and b-catenin complexes
    • doi:10.1038/ nature03452
    • Kim JH et al. 2005 Transcriptional regulation of a metastasis suppressor gene by Tip60 and b-catenin complexes. Nature 434, 921-926. (doi:10.1038/ nature03452)
    • (2005) Nature , vol.434 , pp. 921-926
    • Kim, J.H.1
  • 85
    • 23844441846 scopus 로고    scopus 로고
    • The histidine triad protein Hint1 interacts with Pontin and Reptin and inhibits TCF-b-catenin-mediated transcription
    • doi:10.1242/jcs.02437)
    • Weiske J, Huber O. 2005 The histidine triad protein Hint1 interacts with Pontin and Reptin and inhibits TCF-b-catenin-mediated transcription. J. Cell Sci. 118, 3117-3129. (doi:10.1242/jcs.02437)
    • (2005) J. Cell Sci , vol.118 , pp. 3117-3129
    • Weiske, J.1    Huber, O.2
  • 86
    • 84864860915 scopus 로고    scopus 로고
    • {thorn} TIP49 ATPases
    • doi:10.1016/j. str.2012.05.012
    • {thorn} TIP49 ATPases. Structure 20, 1321-1331. (doi:10.1016/j. str.2012.05.012)
    • (2012) Structure , vol.20 , pp. 1321-1331
    • Petukhov, M.1
  • 87
    • 84870626295 scopus 로고    scopus 로고
    • Conformational transitions regulate the exposure of a DNA-binding domain in the RuvBL1-RuvBL2 complex
    • (doi:10.1093/nar/gks871)
    • López-Perrote A, Muñoz-Hernández H, Gil D, Llorca O. 2012 Conformational transitions regulate the exposure of a DNA-binding domain in the RuvBL1-RuvBL2 complex. Nucleic Acids Res. 40, 11086-11099. (doi:10.1093/nar/gks871)
    • (2012) Nucleic Acids Res , vol.40 , pp. 11086-11099
    • López-Perrote, A.1    Muñoz-Hernández, H.2    Gil, D.3    Llorca, O.4
  • 88
    • 84866604898 scopus 로고    scopus 로고
    • {thorn} ATPases pontin and reptin in the biogenesis of H/ACA RNPs
    • doi:10.1261/rna.034942.112
    • {thorn} ATPases pontin and reptin in the biogenesis of H/ACA RNPs. RNA 18, 1833-1845. (doi:10.1261/rna.034942.112)
    • (2012) RNA , vol.18 , pp. 1833-1845
    • Machado-Pinilla, R.1    Liger, D.2    Leulliot, N.3    Meier, U.T.4


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