메뉴 건너뛰기




Volumn 15, Issue 3, 2014, Pages 216-224

Molecular chaperone-mediated nuclear protein dynamics

Author keywords

Molecular chaperone; Nucleus; Protein DNA dynamics; Transcription

Indexed keywords

AROMATIC HYDROCARBON RECEPTOR; BRG1 PROTEIN; CELL CYCLE PROTEIN 37; CHAPERONE; CHAPERONIN 60; DNA BINDING PROTEIN; ESTRADIOL; ESTROGEN RECEPTOR; FIBRILLARIN; GREEN FLUORESCENT PROTEIN; HEAT SHOCK PROTEIN 90; HIGH MOBILITY GROUP N2 PROTEIN; HISTONE ACETYLTRANSFERASE; HYPOXIA INDUCIBLE FACTOR 1; MYOD1 PROTEIN; NUCLEAR PROTEIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR BINDING PROTEIN; PROTEIN P23; RIBOSOME RNA; RNA POLYMERASE; SMALL HEAT SHOCK PROTEIN;

EID: 84904506503     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/1389203715666140331112230     Document Type: Article
Times cited : (8)

References (95)
  • 1
    • 0035793376 scopus 로고    scopus 로고
    • Protein dynamics: Implications for nuclear architecture and gene expression
    • Misteli, T. Protein dynamics: implications for nuclear architecture and gene expression. Science, 2001, 291, 843-847.
    • (2001) Science , vol.291 , pp. 843-847
    • Misteli, T.1
  • 2
    • 34247351481 scopus 로고    scopus 로고
    • Can visco-elastic phase separation, macromolecular crowding and colloidal physics explain nuclear organisation?
    • Iborra, F.J. Can visco-elastic phase separation, macromolecular crowding and colloidal physics explain nuclear organisation? Theor. Biol. Med. Model., 2007, 4, 15.
    • (2007) Theor. Biol. Med. Model , vol.4 , pp. 15
    • Iborra, F.J.1
  • 3
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • Ellis, R.J. Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci., 2001, 26, 597-604.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 4
    • 53249113141 scopus 로고    scopus 로고
    • Macromolecular crowding and its potential impact on nuclear function
    • Richter, K.; Nessling, M.; Lichter, P. Macromolecular crowding and its potential impact on nuclear function. Biochim. Biophys. Acta, 2008, 1783, 2100-2107.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 2100-2107
    • Richter, K.1    Nessling, M.2    Lichter, P.3
  • 5
    • 0014525216 scopus 로고
    • Self-assembly of biological structures
    • Kushner, D.J. Self-assembly of biological structures. Bacteriol. Rev., 1969, 33, 302-345.
    • (1969) Bacteriol. Rev , vol.33 , pp. 302-345
    • Kushner, D.J.1
  • 6
    • 0021551283 scopus 로고
    • Role of subunit interactions in the self-assembly of oligomeric proteins
    • Garel, J.R.; Martel, A.; Muller, K.; Ikai, A.; Morishima, N.; Sutoh, K. Role of subunit interactions in the self-assembly of oligomeric proteins. Adv. Biophys., 1984, 18, 91-113.
    • (1984) Adv. Biophys , vol.18 , pp. 91-113
    • Garel, J.R.1    Martel, A.2    Muller, K.3    Ikai, A.4    Morishima, N.5    Sutoh, K.6
  • 8
    • 0035338418 scopus 로고    scopus 로고
    • Continuous recycling: A mechanism for modulatory signal transduction
    • Freeman, B.C.; Yamamoto, K.R. Continuous recycling: a mechanism for modulatory signal transduction. Trends Biochem. Sci., 2001, 26, 285-290.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 285-290
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 9
    • 33746813983 scopus 로고    scopus 로고
    • How can biochemical reactions within cells differ from those in test tubes?
    • Minton, A.P. How can biochemical reactions within cells differ from those in test tubes? J. Cell Sci., 2006, 119, 2863-2869.
    • (2006) J. Cell Sci , vol.119 , pp. 2863-2869
    • Minton, A.P.1
  • 10
    • 84934438837 scopus 로고    scopus 로고
    • Protein misassembly: Macromolecular crowding and molecular chaperones
    • Ellis, R.J. Protein misassembly: macromolecular crowding and molecular chaperones. Adv. Exp. Med. Biol., 2007, 594, 1-13.
    • (2007) Adv. Exp. Med. Biol , vol.594 , pp. 1-13
    • Ellis, R.J.1
  • 11
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heatshock proteins
    • Hendrick, J.P.; Hartl, F.U. Molecular chaperone functions of heatshock proteins. Annu. Rev. Biochem., 1993, 62, 349-384.
    • (1993) Annu. Rev. Biochem , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 12
    • 43549102208 scopus 로고    scopus 로고
    • Hsp90: The Rosetta Stone of cellular protein dynamics
    • DeZwaan, D.C.; Freeman, B.C. Hsp90: The Rosetta Stone of cellular protein dynamics? Cell Cycle, 2008, 7, 1006-101.
    • (2008) Cell Cycle , vol.7 , pp. 1006-1101
    • Dezwaan, D.C.1    Freeman, B.C.2
  • 13
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt, W.B.; Toft, D.O. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med., 2003, 228, 111-133.
    • (2003) Exp. Biol. Med , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 15
    • 0004247764 scopus 로고    scopus 로고
    • New Haven, Conn., Yale University Press
    • Harris, H. The Birth of the Cell, New Haven, Conn., Yale University Press, 1999.
    • (1999) The Birth of the Cell
    • Harris, H.1
  • 17
    • 79960622503 scopus 로고    scopus 로고
    • Biogenesis and function of nuclear bodies
    • Mao, Y.S.; Zhang, B.; Spector, D.L. Biogenesis and function of nuclear bodies. Trends Genet., 2011, 27, 295-306.
    • (2011) Trends Genet , vol.27 , pp. 295-306
    • Mao, Y.S.1    Zhang, B.2    Spector, D.L.3
  • 18
    • 67649503031 scopus 로고    scopus 로고
    • Cajal's contribution to the knowledge of the neuronal cell nucleus
    • Lafarga, M.; Casafont, I.; Bengoechea, R.; Tapia, O.; Berciano, M.T. Cajal's contribution to the knowledge of the neuronal cell nucleus. Chromosoma, 2009, 118, 437-443.
    • (2009) Chromosoma , vol.118 , pp. 437-443
    • Lafarga, M.1    Casafont, I.2    Bengoechea, R.3    Tapia, O.4    Berciano, M.T.5
  • 20
    • 84865628181 scopus 로고    scopus 로고
    • Paraspeckle nuclear bodies-useful uselessness?
    • Nakagawa, S.; Hirose, T. Paraspeckle nuclear bodies-useful uselessness? Cell Mol. Life Sci., 2012, 69(18), 3027-3036.
    • (2012) Cell Mol. Life Sci , vol.69 , Issue.18 , pp. 3027-3036
    • Nakagawa, S.1    Hirose, T.2
  • 21
    • 0000394947 scopus 로고
    • The relation of a particular chromosomal element to the development of the nucleoli in Zea mays
    • McClintock, B. The relation of a particular chromosomal element to the development of the nucleoli in Zea mays. Zeitschrift fur Zellforschung und Mikroskopische Anatomie, 1934, 21, 294-328.
    • (1934) Zeitschrift Fur Zellforschung Und Mikroskopische Anatomie , vol.21 , pp. 294-328
    • McClintock, B.1
  • 22
    • 16844372528 scopus 로고    scopus 로고
    • Birth of a nucleolus: The evolution of nucleolar compartments
    • Thiry, M.; Lafontaine, D.L. Birth of a nucleolus: the evolution of nucleolar compartments. Trends Cell Biol., 2005, 15, 194-199.
    • (2005) Trends Cell Biol , vol.15 , pp. 194-199
    • Thiry, M.1    Lafontaine, D.L.2
  • 23
    • 11144328968 scopus 로고    scopus 로고
    • Cajal bodies, nucleoli, and speckles in the Xenopus oocyte nucleus have a low-density, sponge-like structure
    • Handwerger, K.E.; Cordero, J.A.; Gall, J.G. Cajal bodies, nucleoli, and speckles in the Xenopus oocyte nucleus have a low-density, sponge-like structure. Mol. Biol. Cell, 2005, 16, 202-211.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 202-211
    • Handwerger, K.E.1    Cordero, J.A.2    Gall, J.G.3
  • 24
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair, R.D.; Misteli, T. High mobility of proteins in the mammalian cell nucleus. Nature, 2000, 404, 604-609.
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 25
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
    • Freeman, B.C.; Morimoto, R.I. The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J., 1996, 15, 2969-2979.
    • (1996) EMBO J , vol.15 , pp. 2969-2979
    • Freeman, B.C.1    Morimoto, R.I.2
  • 26
    • 0029858706 scopus 로고    scopus 로고
    • Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis
    • Hayer-Hartl, M.K.; Weber, F.; Hartl, F.U. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. EMBO J., 1996, 15, 6111-6121.
    • (1996) EMBO J , vol.15 , pp. 6111-6121
    • Hayer-Hartl, M.K.1    Weber, F.2    Hartl, F.U.3
  • 27
    • 14544280757 scopus 로고    scopus 로고
    • Transcriptional regulation and the role of diverse coactivators in animal cells
    • Roeder, R.G. Transcriptional regulation and the role of diverse coactivators in animal cells. FEBS Lett., 2005, 579, 909-915.
    • (2005) FEBS Lett , vol.579 , pp. 909-915
    • Roeder, R.G.1
  • 28
    • 36549078554 scopus 로고    scopus 로고
    • Dynamics of coactivator recruitment and chromatin modifications during nuclear receptor mediated transcription
    • Aoyagi, S.; Archer, T.K. Dynamics of coactivator recruitment and chromatin modifications during nuclear receptor mediated transcription. Mol. Cell. Endocrinol., 2008, 280, 1-5.
    • (2008) Mol. Cell. Endocrinol , vol.280 , pp. 1-5
    • Aoyagi, S.1    Archer, T.K.2
  • 29
    • 33746641324 scopus 로고    scopus 로고
    • Nucleosome displacement in transcription
    • Workman, J.L. Nucleosome displacement in transcription. Genes & Dev., 2006, 20, 2009-2017.
    • (2006) Genes & Dev , vol.20 , pp. 2009-2017
    • Workman, J.L.1
  • 30
    • 0038022718 scopus 로고    scopus 로고
    • Targeting genes and transcription factors to segregated nuclear compartments
    • Isogai, Y.; Tjian, R. Targeting genes and transcription factors to segregated nuclear compartments. Curr. Opin. Cell Biol., 2003, 15, 296-303.
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 296-303
    • Isogai, Y.1    Tjian, R.2
  • 32
    • 71849119231 scopus 로고    scopus 로고
    • Nuclear organization in the 3D space of the nucleus - cause or consequence?
    • Nunez, E.; Fu, X.D.; Rosenfeld, M.G. Nuclear organization in the 3D space of the nucleus - cause or consequence? Curr. Opin. Genet. Dev., 2009, 19, 424-436.
    • (2009) Curr. Opin. Genet. Dev , vol.19 , pp. 424-436
    • Nunez, E.1    Fu, X.D.2    Rosenfeld, M.G.3
  • 33
    • 79952631797 scopus 로고    scopus 로고
    • An ending is a new beginning: Transcription termination supports re-initiation
    • Lykke-Andersen, S.; Mapendano, C.K.; Jensen TH. An ending is a new beginning: transcription termination supports re-initiation. Cell Cycle, 2011, 10, 863-865.
    • (2011) Cell Cycle , vol.10 , pp. 863-865
    • Lykke-Andersen, S.1    Mapendano, C.K.2    Jensen, T.H.3
  • 34
    • 77955500692 scopus 로고    scopus 로고
    • Modulation of steroid hormone receptor activity
    • Stanisi-, V.; Lonard, D.M.; O'Malley, B.W. Modulation of steroid hormone receptor activity. Prog. Brain Res., 2010, 181, 153-176.
    • (2010) Prog. Brain Res , vol.181 , pp. 153-176
    • Stanisi-, V.1    Lonard, D.M.2    O'Malley, B.W.3
  • 35
    • 21744435965 scopus 로고    scopus 로고
    • Controlling nuclear receptors: The circular logic of cofactor cycles
    • Perissi, V.; Rosenfeld, M.G. Controlling nuclear receptors: the circular logic of cofactor cycles. Nat. Rev. Mol. Cell. Biol., 2005, 6, 542-554.
    • (2005) Nat. Rev. Mol. Cell. Biol , vol.6 , pp. 542-554
    • Perissi, V.1    Rosenfeld, M.G.2
  • 36
    • 0033305547 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Cellular and molecular biology
    • McKenna, N.J.; Lanz, R.B.l.; O'Malley, B.W. Nuclear receptor coregulators: cellular and molecular biology. Endocr. Rev., 1999, 20, 321-344.
    • (1999) Endocr. Rev , vol.20 , pp. 321-344
    • McKenna, N.J.1    Lanz, R.B.L.2    O'Malley, B.W.3
  • 37
    • 0037192501 scopus 로고    scopus 로고
    • Molecular determinants for the tissue specificity of SERMs
    • Shang, Y.; Brown, M. Molecular determinants for the tissue specificity of SERMs. Science, 2002, 295, 2465-2468.
    • (2002) Science , vol.295 , pp. 2465-2468
    • Shang, Y.1    Brown, M.2
  • 39
    • 0033617334 scopus 로고    scopus 로고
    • Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- and developmentally regulated promoter
    • Cosma, M.P.; Tanaka, T.; Nasmyth, K. Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- and developmentally regulated promoter. Cell, 1999, 97, 299-311.
    • (1999) Cell , vol.97 , pp. 299-311
    • Cosma, M.P.1    Tanaka, T.2    Nasmyth, K.3
  • 40
    • 0033681250 scopus 로고    scopus 로고
    • Ordered recruitment of chromatin modifying and general transcription factors to the IFN-beta promoter
    • Agalioti, T.; Lomvardas, S.; Parekh, B.; Yie, J.; Maniatis, T.; Thanos, D. Ordered recruitment of chromatin modifying and general transcription factors to the IFN-beta promoter. Cell, 2000, 103, 667-678.
    • (2000) Cell , vol.103 , pp. 667-678
    • Agalioti, T.1    Lomvardas, S.2    Parekh, B.3    Yie, J.4    Maniatis, T.5    Thanos, D.6
  • 41
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Shang, Y.; Hu, X.; DiRenzo, J.; Lazar, M.A.; Brown, M. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell, 2000, 103, 843-852.
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.1    Hu, X.2    Direnzo, J.3    Lazar, M.A.4    Brown, M.5
  • 42
    • 0037062460 scopus 로고    scopus 로고
    • Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormoneresponsive promoters in vivo
    • Sharma, D.; Fondell, J.D. Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormoneresponsive promoters in vivo. Proc. Nat.l Acad. Sci. U.S.A., 2002, 99, 7934-7939.
    • (2002) Proc. Nat.l Acad. Sci. U.S.A , vol.99 , pp. 7934-7939
    • Sharma, D.1    Fondell, J.D.2
  • 43
    • 0037716755 scopus 로고    scopus 로고
    • Independent recruitment in vivo by Gal4 of two complexes required for transcription
    • Bryant, G.O.; Ptashne, M. Independent recruitment in vivo by Gal4 of two complexes required for transcription. Mol. Cell, 2003, 11, 1301-1309.
    • (2003) Mol. Cell , vol.11 , pp. 1301-1309
    • Bryant, G.O.1    Ptashne, M.2
  • 44
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen Receptor-_ directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Metivier, R.; Penot, G.; Hubner, M.R.; Reid, G.; Brand, H.; Kos, M.; Gannon, F. Estrogen Receptor-_ directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell, 2003, 115, 751-763.
    • (2003) Cell , vol.115 , pp. 751-763
    • Metivier, R.1    Penot, G.2    Hubner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 45
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasomemediated turnover of unliganded and liganded ERalpha on responsive promoters is an integral feature of estrogen signaling
    • Reid, G.; Hübner, M.R.; Métivier, R.; Brand, H.; Denger, S.; Manu, D.; Beaudouin, J.; Ellenberg, J.; Gannon, F. Cyclic, proteasomemediated turnover of unliganded and liganded ERalpha on responsive promoters is an integral feature of estrogen signaling. Mol. Cell, 2003, 11, 695-707.
    • (2003) Mol. Cell , vol.11 , pp. 695-707
    • Reid, G.1    Hübner, M.R.2    Métivier, R.3    Brand, H.4    Denger, S.5    Manu, D.6    Beaudouin, J.7    Ellenberg, J.8    Gannon, F.9
  • 46
    • 33645820442 scopus 로고    scopus 로고
    • Transcription in four dimensions: Nuclear receptor-directed initiation of gene expression
    • Métivier, R.; Reid, G.; Gannon, F. Transcription in four dimensions: nuclear receptor-directed initiation of gene expression. EMBO Rep., 2006, 7, 161-167.
    • (2006) EMBO Rep , vol.7 , pp. 161-167
    • Métivier, R.1    Reid, G.2    Gannon, F.3
  • 47
    • 1942502336 scopus 로고    scopus 로고
    • The coactivator LXXLL nuclear receptor recognition motif
    • Savkur, R.S.; Burris, T.P. The coactivator LXXLL nuclear receptor recognition motif. J. Pept. Res., 2004, 63, 207-212.
    • (2004) J. Pept. Res , vol.63 , pp. 207-212
    • Savkur, R.S.1    Burris, T.P.2
  • 48
    • 0025007114 scopus 로고
    • Quantitative analysis of the glucocorticoid receptor-DNA interaction at the mouse mammary tumor virus glucocorticoid response element
    • Perlmann T.; Eriksson, P.; Wrange, O. Quantitative analysis of the glucocorticoid receptor-DNA interaction at the mouse mammary tumor virus glucocorticoid response element. J. Biol. Chem., 1990, 265, 17222-17229.
    • (1990) J. Biol. Chem , vol.265 , pp. 17222-17229
    • Perlmann, T.1    Eriksson, P.2    Wrange, O.3
  • 49
    • 0343415609 scopus 로고    scopus 로고
    • The glucocorticoid receptor: Rapid exchange with regulatory sites in living cells
    • McNally, J.G.; Müller, W.G.; Walker, D.; Wolford, R.; Hager, G.L. The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. Science, 2000, 287, 1262-1265.
    • (2000) Science , vol.287 , pp. 1262-1265
    • McNally, J.G.1    Müller, W.G.2    Walker, D.3    Wolford, R.4    Hager, G.L.5
  • 50
  • 52
    • 0037809279 scopus 로고    scopus 로고
    • Dynamic shuttling and intranuclear mobility of nuclear hormone receptors
    • Maruvada, P.; Baumann, C.T.; Hager, G.L.; Yen, P.M. Dynamic shuttling and intranuclear mobility of nuclear hormone receptors. J. Biol. Chem., 2003, 278, 12425-12432.
    • (2003) J. Biol. Chem , vol.278 , pp. 12425-12432
    • Maruvada, P.1    Baumann, C.T.2    Hager, G.L.3    Yen, P.M.4
  • 54
    • 14844348177 scopus 로고    scopus 로고
    • Ligand-specific dynamics of the progesterone receptor in living cells and during chromatin remodelling in vitro
    • Rayasam, G.V.; Elbi, C.; Walker, D.A.; Wolford, R.; Fletcher, T.M.; Edwards, D.P.; Hager, G.L. Ligand-specific dynamics of the progesterone receptor in living cells and during chromatin remodelling in vitro. Mol. Cell. Biol., 2005, 25, 2406-2418.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 2406-2418
    • Rayasam, G.V.1    Elbi, C.2    Walker, D.A.3    Wolford, R.4    Fletcher, T.M.5    Edwards, D.P.6    Hager, G.L.7
  • 56
    • 2142823918 scopus 로고    scopus 로고
    • On the movements of nuclear components in living cells
    • Bubulya, P.A.; Spector, D.L. On the movements of nuclear components in living cells. Exp. Cell Res., 2004, 296, 4-11.
    • (2004) Exp. Cell Res , vol.296 , pp. 4-11
    • Bubulya, P.A.1    Spector, D.L.2
  • 58
    • 82355190137 scopus 로고    scopus 로고
    • Assembly of the transcription machinery: Ordered and stable, random and dynamic, or both?
    • Stasevich, T.J.; McNally, J.G. Assembly of the transcription machinery: ordered and stable, random and dynamic, or both? Chromosoma, 2011, 120, 533-545.
    • (2011) Chromosoma , vol.120 , pp. 533-545
    • Stasevich, T.J.1    McNally, J.G.2
  • 59
    • 0036532111 scopus 로고    scopus 로고
    • Protein dynamics in the nuclear compartment
    • Hager, G.L.; Elbi, C.; Becker, M. Protein dynamics in the nuclear compartment. Curr. Opin. Genet. Dev., 2002, 12, 137-141.
    • (2002) Curr. Opin. Genet. Dev , vol.12 , pp. 137-141
    • Hager, G.L.1    Elbi, C.2    Becker, M.3
  • 60
    • 3042760021 scopus 로고    scopus 로고
    • Global nature of dynamic protein-chromatin interactions in vivo: Three-dimensional genome scanning and dynamic interaction networks of chromatin proteins
    • Phair, R.D.; Scaffidi, P.; Elbi, C.; Vecerová, J.; Dey, A.; Ozato, K.; Brown, D.T.; Hager, G.; Bustin, M.; Misteli, T. Global nature of dynamic protein-chromatin interactions in vivo: three-dimensional genome scanning and dynamic interaction networks of chromatin proteins. Mol. Cell. Biol., 2004, 24, 6393-6402.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 6393-6402
    • Phair, R.D.1    Scaffidi, P.2    Elbi, C.3    Vecerová, J.4    Dey, A.5    Ozato, K.6    Brown, D.T.7    Hager, G.8    Bustin, M.9    Misteli, T.10
  • 61
    • 0018221572 scopus 로고
    • Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA
    • Laskey, R.A.; Honda, B.M.; Mills, A.D.; Finch, J.T. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA. Nature, 1978, 275, 416-420.
    • (1978) Nature , vol.275 , pp. 416-420
    • Laskey, R.A.1    Honda, B.M.2    Mills, A.D.3    Finch, J.T.4
  • 62
    • 0019333950 scopus 로고
    • Protein synthesis in chloroplasts. IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts
    • Barraclough, R.; Ellis, R.J. Protein synthesis in chloroplasts. IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts. Biochim. Biophys. Acta, 1980, 608, 19-31.
    • (1980) Biochim. Biophys. Acta , vol.608 , pp. 19-31
    • Barraclough, R.1    Ellis, R.J.2
  • 63
    • 0022969885 scopus 로고
    • Speculations on the functions of the major heat shock and glucose-regulated proteins
    • Pelham, H.R. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell, 1986, 46, 959-961.
    • (1986) Cell , vol.46 , pp. 959-961
    • Pelham, H.R.1
  • 64
    • 0018193766 scopus 로고
    • Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication
    • Yochem, J.; Uchida, H.; Sunshine, M.; Saito, H.; Georgopoulos, C.P.; Feiss, M. Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication. Mol. Gen. Genet., 1978, 164, 9-14.
    • (1978) Mol. Gen. Genet , vol.164 , pp. 9-14
    • Yochem, J.1    Uchida, H.2    Sunshine, M.3    Saito, H.4    Georgopoulos, C.P.5    Feiss, M.6
  • 65
    • 0021835596 scopus 로고
    • Initiation of DNA replication on single-stranded DNA templates catalyzed by purified replication proteins of bacteriophage lambda and Escherichia coli
    • LeBowitz, J.H.; Zylicz, M.; Georgopoulos, C.; McMacken, R. Initiation of DNA replication on single-stranded DNA templates catalyzed by purified replication proteins of bacteriophage lambda and Escherichia coli. Proc. Nat.l Acad. Sci. USA., 1985, 82, 3988-3992.
    • (1985) Proc. Nat.l Acad. Sci. USA , vol.82 , pp. 3988-3992
    • Lebowitz, J.H.1    Zylicz, M.2    Georgopoulos, C.3    McMacken, R.4
  • 66
    • 0012749458 scopus 로고
    • Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication
    • Liberek, K.; Georgopoulos, C.; Zylicz, M. Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication. Proc. Nat.l Acad. Sci. U.S.A., 1988, 85, 6632-6636.
    • (1988) Proc. Nat.l Acad. Sci. U.S.A , vol.85 , pp. 6632-6636
    • Liberek, K.1    Georgopoulos, C.2    Zylicz, M.3
  • 67
    • 58149271606 scopus 로고    scopus 로고
    • Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms
    • Johnson, J.L.; Brown, C. Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms. Cell Stress Chaperones, 2009, 14, 83-94.
    • (2009) Cell Stress Chaperones , vol.14 , pp. 83-94
    • Johnson, J.L.1    Brown, C.2
  • 68
    • 0024421221 scopus 로고
    • Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
    • Borkovich, K.A.; Farrelly, F.W.; Finkelstein, D.B.; Taulien, J.; Lindquist, S. Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol. Cell Biol., 1989, 9, 3919-3930.
    • (1989) Mol. Cell Biol , vol.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farrelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 69
    • 0024044382 scopus 로고
    • Ancient heat shock gene is dispensable
    • Bardwell, J.C.; Craig, E.A. Ancient heat shock gene is dispensable. J. Bacteriol., 1988, 170, 2977-2983.
    • (1988) J. Bacteriol , vol.170 , pp. 2977-2983
    • Bardwell, J.C.1    Craig, E.A.2
  • 70
    • 84857058279 scopus 로고    scopus 로고
    • Expanding the cellular molecular chaperone network through the ubiquitous cochaperones
    • Echtenkamp, F.J.; Freeman, B.C. Expanding the cellular molecular chaperone network through the ubiquitous cochaperones. Biochim. Biophys. Acta, 2012, 1823, 668-673.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 668-673
    • Echtenkamp, F.J.1    Freeman, B.C.2
  • 71
    • 84857042271 scopus 로고    scopus 로고
    • The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
    • Li, J.; Soroka, J.; Buchner, J. The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones. Biochim. Biophys. Acta, 2012, 1823, 624-635.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 624-635
    • Li, J.1    Soroka, J.2    Buchner, J.3
  • 73
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor associated protein, p23
    • Freeman, B.C.; Toft, T.O.; Morimoto, R.I. Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor associated protein, p23. Science, 1996, 274, 1718-1720.
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, T.O.2    Morimoto, R.I.3
  • 74
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of Hsp90-associated proteins
    • Bose, S.; Weikl, T.; Bügl, H.; Buchner, J. Chaperone function of Hsp90-associated proteins. Science, 1996, 274, 1715-1717.
    • (1996) Science , vol.274 , pp. 1715-1717
    • Bose, S.1    Weikl, T.2    Bügl, H.3    Buchner, J.4
  • 75
    • 79960452274 scopus 로고    scopus 로고
    • Global functional map of the yeast p23 homolog reveals extensive nuclear molecular chaperone activities
    • Echtenkamp, F.; Woo, J.I.; Oxelmark, E.; Zelin, E.; Andrews, B.; Garabedian, M.J.; Freeman, B.C. Global functional map of the yeast p23 homolog reveals extensive nuclear molecular chaperone activities. Mol. Cell, 2011, 43, 229-241.
    • (2011) Mol. Cell , vol.43 , pp. 229-241
    • Echtenkamp, F.1    Woo, J.I.2    Oxelmark, E.3    Zelin, E.4    Andrews, B.5    Garabedian, M.J.6    Freeman, B.C.7
  • 76
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • Freeman, B.C.; Yamamoto, K.R. Disassembly of transcriptional regulatory complexes by molecular chaperones. Science, 2002, 296, 2232-2235.
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 77
    • 34347249238 scopus 로고    scopus 로고
    • The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation
    • Toogun, O.A.; Zeiger, W.; Freeman, B.C. The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation. Proc. Nat.l Acad. Sci. U.S.A., 2007, 104, 5765-5770.
    • (2007) Proc. Nat.l Acad. Sci. U.S.A , vol.104 , pp. 5765-5770
    • Toogun, O.A.1    Zeiger, W.2    Freeman, B.C.3
  • 78
    • 0022342203 scopus 로고
    • Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein
    • Sanchez, E.R.; Toft, D.O.; Schlesinger, M.J.; Pratt, W.B. Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein. J. Biol. Chem., 1985, 260, 12398-12401.
    • (1985) J. Biol. Chem , vol.260 , pp. 12398-12401
    • Sanchez, E.R.1    Toft, D.O.2    Schlesinger, M.J.3    Pratt, W.B.4
  • 79
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
    • Pratt, W.B. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J. Biol. Chem., 1993, 268, 21455-21458.
    • (1993) J. Biol. Chem , vol.268 , pp. 21455-21458
    • Pratt, W.B.1
  • 80
    • 0032915842 scopus 로고    scopus 로고
    • Chromatin recycling of glucocorticoid receptors: Implications for multiple roles of heat shock protein 90
    • Liu, J.; DeFranco, D.B. Chromatin recycling of glucocorticoid receptors: implications for multiple roles of heat shock protein 90. Mol. Endocrinol., 1999, 13, 355-365.
    • (1999) Mol. Endocrinol , vol.13 , pp. 355-365
    • Liu, J.1    Defranco, D.B.2
  • 81
    • 0033502429 scopus 로고    scopus 로고
    • Geldanamycin as a potential anti-cancer agent: Its molecular target and biochemical activity
    • Neckers, L.; Schulte, T.W.; Mimnaugh, E. Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity. Invest. New Drugs, 1999, 17, 361-373.
    • (1999) Invest. New Drugs , vol.17 , pp. 361-373
    • Neckers, L.1    Schulte, T.W.2    Mimnaugh, E.3
  • 83
    • 12144290835 scopus 로고    scopus 로고
    • Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes
    • Stavreva, D.A.; Muller, W.G.; Hager, G.L.; Smith, C.L.; McNally, J.G. Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes. Mol. Cell. Biol., 2004, 24, 2682-2697.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 2682-2697
    • Stavreva, D.A.1    Muller, W.G.2    Hager, G.L.3    Smith, C.L.4    McNally, J.G.5
  • 84
    • 0026722373 scopus 로고
    • Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84)
    • Shaknovich, R.; Shue, G.; Kohtz, D.S. Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84). Mol. Cell. Biol., 1992, 12, 5059-5068.
    • (1992) Mol. Cell. Biol , vol.12 , pp. 5059-5068
    • Shaknovich, R.1    Shue, G.2    Kohtz, D.S.3
  • 85
    • 0028858813 scopus 로고
    • Distinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains
    • Antonsson, C.; Whitelaw, M.L.; McGuire, J.; Gustafsson, J.A.; Poellinger, L. Distinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains. Mol. Cell. Biol., 1995, 15, 756-765.
    • (1995) Mol. Cell. Biol , vol.15 , pp. 756-765
    • Antonsson, C.1    Whitelaw, M.L.2    McGuire, J.3    Gustafsson, J.A.4    Poellinger, L.5
  • 86
    • 0036841843 scopus 로고    scopus 로고
    • Reduction of hypoxiainduced transcription through the repression of hypoxia-inducible factor-1alpha/aryl hydrocarbon receptor nuclear translocator DNA binding by the 90-kDa heat-shock protein inhibitor radicicol
    • Hur, E.; Kim, H.H.; Choi, S.M.; Kim, J.H.; Yim, S.; Kwon, H.J.; Choi, Y.; Kim, D.K.; Lee, M.O.; Park, H. Reduction of hypoxiainduced transcription through the repression of hypoxia-inducible factor-1alpha/aryl hydrocarbon receptor nuclear translocator DNA binding by the 90-kDa heat-shock protein inhibitor radicicol. Mol. Pharmacol., 2002, 62, 975-982.
    • (2002) Mol. Pharmacol , vol.62 , pp. 975-982
    • Hur, E.1    Kim, H.H.2    Choi, S.M.3    Kim, J.H.4    Yim, S.5    Kwon, H.J.6    Choi, Y.7    Kim, D.K.8    Lee, M.O.9    Park, H.10
  • 87
    • 10344243547 scopus 로고    scopus 로고
    • Hsp90 regulates the activity of wild type p53 under physiological and elevated temperatures
    • Muller, L.; Schaupp, A.; Walerych, D.; Wegele, H.; Buchner, J. Hsp90 regulates the activity of wild type p53 under physiological and elevated temperatures. J. Biol. Chem., 2004, 279, 48846-48854.
    • (2004) J. Biol. Chem , vol.279 , pp. 48846-48854
    • Muller, L.1    Schaupp, A.2    Walerych, D.3    Wegele, H.4    Buchner, J.5
  • 89
    • 0034102339 scopus 로고    scopus 로고
    • The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
    • Freeman, B.C.; Felts, S.J.; Toft, D.O.; Yamamoto, K.R. The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies. Genes & Dev., 2000, 14, 422-434.
    • (2000) Genes & Dev , vol.14 , pp. 422-434
    • Freeman, B.C.1    Felts, S.J.2    Toft, D.O.3    Yamamoto, K.R.4
  • 90
    • 27744495040 scopus 로고    scopus 로고
    • A putative stimulatory role for activator turnover in gene expression
    • Lipford, J.R.; Smith, G.T.; Chi, Y.; Deshaies, R.J. A putative stimulatory role for activator turnover in gene expression. Nature, 2005, 438, 113-116.
    • (2005) Nature , vol.438 , pp. 113-116
    • Lipford, J.R.1    Smith, G.T.2    Chi, Y.3    Deshaies, R.J.4
  • 91
    • 33748331286 scopus 로고    scopus 로고
    • Proteolytic turnover of the Gal4 transcription factor is not required for function in vivo
    • Nalley, K.; Johnston, S.A.; Kodadek, T. Proteolytic turnover of the Gal4 transcription factor is not required for function in vivo. Nature, 2006, 442, 1054-1057.
    • (2006) Nature , vol.442 , pp. 1054-1057
    • Nalley, K.1    Johnston, S.A.2    Kodadek, T.3
  • 93
    • 0035900780 scopus 로고    scopus 로고
    • Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids
    • Wallace, A.D.; Cidlowski, J.A. Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids. J. Biol. Chem., 2001, 276, 42714-42721.
    • (2001) J. Biol. Chem , vol.276 , pp. 42714-42721
    • Wallace, A.D.1    Cidlowski, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.