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Volumn 124, Issue 18, 2011, Pages 3164-3173

The myosin-binding UCS domain but not the Hsp90-binding TPR domain of the UNC-45 chaperone is essential for function in Caenorhabditis elegans

Author keywords

Accumulation; Assembly; Hsp90; Myosin; UNC 45

Indexed keywords

BINDING PROTEIN; CHAPERONE; MYOSIN; PROTEIN UNC 45; UNCLASSIFIED DRUG;

EID: 80052365659     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.087320     Document Type: Article
Times cited : (32)

References (57)
  • 1
    • 2342456308 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: terminating erroneous gene expression
    • Baker, K. E. and Parker, R. (2004). Nonsense-mediated mRNA decay: terminating erroneous gene expression. Curr. Opin. Cell Biol. 16, 293-299.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 293-299
    • Baker, K.E.1    Parker, R.2
  • 2
    • 0032583155 scopus 로고    scopus 로고
    • Unc-45 mutations in Caenorhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly
    • Barral, J. M., Bauer, C. C., Ortiz, I. and Epstein, H. F. (1998). Unc-45 mutations in Caenorhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly. J. Cell Biol. 143, 1215-1225.
    • (1998) J. Cell Biol. , vol.143 , pp. 1215-1225
    • Barral, J.M.1    Bauer, C.C.2    Ortiz, I.3    Epstein, H.F.4
  • 3
    • 0037169028 scopus 로고    scopus 로고
    • Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin
    • Barral, J. M., Hutagalung, A. H., Brinker, A., Hartl, F. U. and Epstein, H. F. (2002). Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin. Science 295, 669-671.
    • (2002) Science , vol.295 , pp. 669-671
    • Barral, J.M.1    Hutagalung, A.H.2    Brinker, A.3    Hartl, F.U.4    Epstein, H.F.5
  • 4
    • 77957801950 scopus 로고    scopus 로고
    • Knockdown and overexpression of Unc-45b result in defective myofibril organization in skeletal muscles of zebrafish embryos
    • Bernick, E. P., Zhang, P. J. and Du, S. (2010). Knockdown and overexpression of Unc-45b result in defective myofibril organization in skeletal muscles of zebrafish embryos. BMC Cell Biol. 11, 70.
    • (2010) BMC Cell Biol , vol.11 , pp. 70
    • Bernick, E.P.1    Zhang, P.J.2    Du, S.3
  • 5
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner, S. (1974). The genetics of Caenorhabditis elegans. Genetics 77, 71-94.
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 7
    • 0037184045 scopus 로고    scopus 로고
    • Folding of the striated muscle myosin motor domain
    • Chow, D., Srikakulam, R., Chen, Y. and Winkelmann, D. A. (2002). Folding of the striated muscle myosin motor domain. J. Biol. Chem. 277, 36799-36807.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36799-36807
    • Chow, D.1    Srikakulam, R.2    Chen, Y.3    Winkelmann, D.A.4
  • 8
    • 19344374029 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: molecular insights and mechanistic variations across species
    • Conti, E. and Izaurralde, E. (2005). Nonsense-mediated mRNA decay: molecular insights and mechanistic variations across species. Curr. Opin. Cell Biol. 17, 316-325.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 316-325
    • Conti, E.1    Izaurralde, E.2
  • 9
    • 38649104452 scopus 로고    scopus 로고
    • Heat-shock protein 90alpha1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos
    • Du, S. J., Li, H., Bian, Y. and Zhong, Y. (2008). Heat-shock protein 90alpha1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos. Proc. Natl. Acad. Sci. USA 105, 554-559.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 554-559
    • Du, S.J.1    Li, H.2    Bian, Y.3    Zhong, Y.4
  • 10
    • 0024396222 scopus 로고
    • Chimaeras of myc oncoprotein and steroid receptors cause hormone-dependent transformation of cells
    • Eilers, M., Picard, D., Yamamoto, K. R. and Bishop, J. M. (1989). Chimaeras of myc oncoprotein and steroid receptors cause hormone-dependent transformation of cells. Nature 340, 66-68.
    • (1989) Nature , vol.340 , pp. 66-68
    • Eilers, M.1    Picard, D.2    Yamamoto, K.R.3    Bishop, J.M.4
  • 11
    • 0016358187 scopus 로고
    • Temperature-sensitive mutation affecting myofilament assembly in Caenorhabditis elegans
    • Epstein, H. F. and Thomson, J. N. (1974). Temperature-sensitive mutation affecting myofilament assembly in Caenorhabditis elegans. Nature 250, 579-580.
    • (1974) Nature , vol.250 , pp. 579-580
    • Epstein, H.F.1    Thomson, J.N.2
  • 12
    • 41549132154 scopus 로고    scopus 로고
    • Shuttling of the chaperones Unc45b and Hsp90a between the A band and the Z line of the myofibril
    • Etard, C., Roostalu, U. and Strähle, U. (2008). Shuttling of the chaperones Unc45b and Hsp90a between the A band and the Z line of the myofibril. J. Cell Biol. 180, 1163-1175.
    • (2008) J. Cell Biol. , vol.180 , pp. 1163-1175
    • Etard, C.1    Roostalu, U.2    Strähle, U.3
  • 13
    • 77951875791 scopus 로고    scopus 로고
    • Lack of Apobec2-related proteins causes a dystrophic muscle phenotype in zebrafish embryos
    • Etard, C., Roostalu, U. and Strä̈hle, U. (2010). Lack of Apobec2-related proteins causes a dystrophic muscle phenotype in zebrafish embryos. J. Cell Biol. 189, 527-539.
    • (2010) J. Cell Biol. , vol.189 , pp. 527-539
    • Etard, C.1    Roostalu, U.2    Strä̈hle, U.3
  • 14
    • 27744485422 scopus 로고    scopus 로고
    • A proteomic snapshot of the human heat shock protein 90 interactome
    • Falsone, S. F., Gesslbauer, B., Tirk, F., Piccinini, A. M. and Kungl, A. J. (2005). A proteomic snapshot of the human heat shock protein 90 interactome. FEBS Lett. 579, 6350-6354.
    • (2005) FEBS Lett. , vol.579 , pp. 6350-6354
    • Falsone, S.F.1    Gesslbauer, B.2    Tirk, F.3    Piccinini, A.M.4    Kungl, A.J.5
  • 15
    • 0025606427 scopus 로고
    • The unc-86 gene product couples cell lineage and cell identity in C. elegans
    • Finney, M. and Ruvkun, G. (1990). The unc-86 gene product couples cell lineage and cell identity in C. elegans. Cell 63, 895-905.
    • (1990) Cell , vol.63 , pp. 895-905
    • Finney, M.1    Ruvkun, G.2
  • 16
    • 0001705247 scopus 로고
    • Integrative transformation of Caenorhabditis elegans
    • Fire, A. (1986). Integrative transformation of Caenorhabditis elegans. EMBO J. 5, 2673-2680.
    • (1986) EMBO J. , vol.5 , pp. 2673-2680
    • Fire, A.1
  • 17
    • 0024436981 scopus 로고
    • Proper expression of myosin genes in transgenic nematodes
    • Fire, A. and Waterston, R. H. (1989). Proper expression of myosin genes in transgenic nematodes. EMBO J. 8, 3419-3428.
    • (1989) EMBO J. , vol.8 , pp. 3419-3428
    • Fire, A.1    Waterston, R.H.2
  • 18
    • 33644856260 scopus 로고    scopus 로고
    • New insights into myosin evolution and classification
    • Foth, B. J., Goedecke, M. C. and Soldati, D. (2006). New insights into myosin evolution and classification. Proc. Natl. Acad. Sci. USA 103, 3681-3686.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 3681-3686
    • Foth, B.J.1    Goedecke, M.C.2    Soldati, D.3
  • 19
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • Freeman, B. C. and Yamamoto, K. R. (2002). Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 296, 2232-2235.
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 20
    • 0024444026 scopus 로고
    • A new kind of informational suppression in the nematode Caenorhabditis elegans
    • Hodgkin, J., Papp, A., Pulak, R., Ambros, V. and Anderson, P. (1989). A new kind of informational suppression in the nematode Caenorhabditis elegans. Genetics 123, 301-313.
    • (1989) Genetics , vol.123 , pp. 301-313
    • Hodgkin, J.1    Papp, A.2    Pulak, R.3    Ambros, V.4    Anderson, P.5
  • 21
    • 4043096960 scopus 로고    scopus 로고
    • Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans
    • Hoppe, T., Cassata, G., Barral, J. M., Springer, W., Hutagalung, A. H., Epstein, H. F. and Baumeister, R. (2004). Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans. Cell 118, 337-349.
    • (2004) Cell , vol.118 , pp. 337-349
    • Hoppe, T.1    Cassata, G.2    Barral, J.M.3    Springer, W.4    Hutagalung, A.H.5    Epstein, H.F.6    Baumeister, R.7
  • 22
    • 0026658220 scopus 로고
    • Cell cycle regulation of glucocorticoid receptor function
    • Hsu, S. C., Qi, M. and DeFranco, D. B. (1992). Cell cycle regulation of glucocorticoid receptor function. EMBO J. 11, 3457-3468.
    • (1992) EMBO J. , vol.11 , pp. 3457-3468
    • Hsu, S.C.1    Qi, M.2    DeFranco, D.B.3
  • 24
    • 0028149532 scopus 로고
    • Elements regulating cell- and stage-specific expression of the C. elegans MyoD family homolog hlh-1
    • Krause, M., Harrison, S. W., Xu, S. Q., Chen, L. and Fire, A. (1994). Elements regulating cell- and stage-specific expression of the C. elegans MyoD family homolog hlh-1. Dev. Biol. 166, 133-148.
    • (1994) Dev. Biol. , vol.166 , pp. 133-148
    • Krause, M.1    Harrison, S.W.2    Xu, S.Q.3    Chen, L.4    Fire, A.5
  • 25
    • 34247466028 scopus 로고    scopus 로고
    • The UNC-45 chaperone mediates sarcomere assembly through myosin degradation in Caenorhabditis elegans
    • Landsverk, M. L., Li, S., Hutagalung, A. H., Najafov, A., Hoppe, T., Barral, J. M. and Epstein, H. F. (2007). The UNC-45 chaperone mediates sarcomere assembly through myosin degradation in Caenorhabditis elegans. J. Cell Biol. 177, 205-210.
    • (2007) J. Cell Biol. , vol.177 , pp. 205-210
    • Landsverk, M.L.1    Li, S.2    Hutagalung, A.H.3    Najafov, A.4    Hoppe, T.5    Barral, J.M.6    Epstein, H.F.7
  • 27
    • 45149115936 scopus 로고    scopus 로고
    • Unc45 activates Hsp90-dependent folding of the myosin motor domain
    • Liu, L., Srikakulam, R. and Winkelmann, D. A. (2008). Unc45 activates Hsp90-dependent folding of the myosin motor domain. J. Biol. Chem. 283, 13185-13193.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13185-13193
    • Liu, L.1    Srikakulam, R.2    Winkelmann, D.A.3
  • 28
    • 7244226219 scopus 로고    scopus 로고
    • UCS protein Rng3p activates actin filament gliding by fission yeast myosin-II
    • Lord, M. and Pollard, T. D. (2004). UCS protein Rng3p activates actin filament gliding by fission yeast myosin-II. J. Cell Biol. 167, 315-325.
    • (2004) J. Cell Biol. , vol.167 , pp. 315-325
    • Lord, M.1    Pollard, T.D.2
  • 29
    • 45249089995 scopus 로고    scopus 로고
    • Yeast UCS proteins promote actomyosin interactions and limit myosin turnover in cells
    • Lord, M., Sladewski, T. E. and Pollard, T. D. (2008). Yeast UCS proteins promote actomyosin interactions and limit myosin turnover in cells. Proc. Natl. Acad. Sci. USA 105, 8014-8019.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8014-8019
    • Lord, M.1    Sladewski, T.E.2    Pollard, T.D.3
  • 30
    • 2042515635 scopus 로고
    • Coexpression and assembly of myosin heavy chain and myosin light chain in Escherichia coli
    • McNally, E. M., Goodwin, E. B., Spudich, J. A. and Leinwand, L. A. (1988). Coexpression and assembly of myosin heavy chain and myosin light chain in Escherichia coli. Proc. Natl. Acad. Sci. USA 85, 7270-7273.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7270-7273
    • McNally, E.M.1    Goodwin, E.B.2    Spudich, J.A.3    Leinwand, L.A.4
  • 31
    • 0029443103 scopus 로고
    • DNA transformation
    • Mello, C. and Fire, A. (1995). DNA transformation. Methods Cell Biol. 48, 451-482.
    • (1995) Methods Cell Biol , vol.48 , pp. 451-482
    • Mello, C.1    Fire, A.2
  • 32
    • 0020825822 scopus 로고
    • Differential localization of two myosins within nematode thick filaments
    • Miller, D. M., Ortiz, I., Berliner, G. C. and Epstein, H. F. (1983). Differential localization of two myosins within nematode thick filaments. Cell 34, 477-490.
    • (1983) Cell , vol.34 , pp. 477-490
    • Miller, D.M.1    Ortiz, I.2    Berliner, G.C.3    Epstein, H.F.4
  • 33
    • 15244348370 scopus 로고    scopus 로고
    • Hsp90 protein in fission yeast Swo1p and UCS protein Rng3p facilitate myosin II assembly and function
    • Mishra, M., D'Souza, V. M., Chang, K. C., Huang, Y. and Balasubramanian, M. K. (2005). Hsp90 protein in fission yeast Swo1p and UCS protein Rng3p facilitate myosin II assembly and function. Eukaryot. Cell 4, 567-576.
    • (2005) Eukaryot. Cell , vol.4 , pp. 567-576
    • Mishra, M.1    D'Souza, V.M.2    Chang, K.C.3    Huang, Y.4    Balasubramanian, M.K.5
  • 35
    • 0027451263 scopus 로고
    • Sequence requirements for myosin gene expression and regulation in Caenorhabditis elegans
    • Okkema, P. G., Harrison, S. W., Plunger, V., Aryana, A. and Fire, A. (1993). Sequence requirements for myosin gene expression and regulation in Caenorhabditis elegans. Genetics 135, 385-404.
    • (1993) Genetics , vol.135 , pp. 385-404
    • Okkema, P.G.1    Harrison, S.W.2    Plunger, V.3    Aryana, A.4    Fire, A.5
  • 36
    • 0023441954 scopus 로고
    • Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor
    • Picard, D. and Yamamoto, K. R. (1987). Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor. EMBO J. 6, 3333-3340.
    • (1987) EMBO J , vol.6 , pp. 3333-3340
    • Picard, D.1    Yamamoto, K.R.2
  • 37
    • 0023789310 scopus 로고
    • A movable and regulable inactivation function within the steroid binding domain of the glucocorticoid receptor
    • Picard, D., Salser, S. J. and Yamamoto, K. R. (1988). A movable and regulable inactivation function within the steroid binding domain of the glucocorticoid receptor. Cell 54, 1073-1080.
    • (1988) Cell , vol.54 , pp. 1073-1080
    • Picard, D.1    Salser, S.J.2    Yamamoto, K.R.3
  • 38
    • 1842833926 scopus 로고    scopus 로고
    • Two mammalian UNC-45 isoforms are related to distinct cytoskeletal and muscle-specific functions
    • Price, M. G., Landsverk, M. L., Barral, J. M. and Epstein, H. F. (2002). Two mammalian UNC-45 isoforms are related to distinct cytoskeletal and muscle-specific functions. J. Cell Sci. 115, 4013-4023.
    • (2002) J. Cell Sci. , vol.115 , pp. 4013-4023
    • Price, M.G.1    Landsverk, M.L.2    Barral, J.M.3    Epstein, H.F.4
  • 39
    • 0027382460 scopus 로고
    • mRNA surveillance by the Caenorhabditis elegans smg genes
    • Pulak, R. and Anderson, P. (1993). mRNA surveillance by the Caenorhabditis elegans smg genes. Genes Dev. 7, 1885-1897.
    • (1993) Genes Dev. , vol.7 , pp. 1885-1897
    • Pulak, R.1    Anderson, P.2
  • 40
    • 0024360979 scopus 로고
    • v-mos oncoproteins affect the nuclear retention and reutilization of glucocorticoid receptors
    • Qi, M., Hamilton, B. J. and DeFranco, D. (1989). v-mos oncoproteins affect the nuclear retention and reutilization of glucocorticoid receptors. Mol. Endocrinol. 3, 1279-1288.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1279-1288
    • Qi, M.1    Hamilton, B.J.2    DeFranco, D.3
  • 42
    • 0033575232 scopus 로고    scopus 로고
    • Identification of conserved residues required for the binding of a tetratricopeptide repeat domain to heat shock protein 90
    • Russell, L. C., Whitt, S. R., Chen, M.-S. and Chinkers, M. (1999). Identification of conserved residues required for the binding of a tetratricopeptide repeat domain to heat shock protein 90. J. Biol. Chem. 274, 20060-20063.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20060-20063
    • Russell, L.C.1    Whitt, S.R.2    Chen, M.-S.3    Chinkers, M.4
  • 43
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U. and Moarefi, I. (2000). Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101, 199-210.
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 44
    • 0034677906 scopus 로고    scopus 로고
    • Myosins: a diverse superfamily
    • Sellers, J. R. (2000). Myosins: a diverse superfamily. Biochim. Biophys. Acta 1496, 3-22.
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 3-22
    • Sellers, J.R.1
  • 45
    • 78650730499 scopus 로고    scopus 로고
    • UNC-45/CRO1/She4p (UCS) protein forms elongated dimer and joins two myosin heads near their actin binding region
    • Shi, H. and Blobel, G. (2010). UNC-45/CRO1/She4p (UCS) protein forms elongated dimer and joins two myosin heads near their actin binding region. Proc. Natl. Acad. Sci. USA 107, 21382-21387.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 21382-21387
    • Shi, H.1    Blobel, G.2
  • 47
    • 0022348755 scopus 로고
    • Extrachromosomal DNA transformation of Caenorhabditis elegans
    • Stinchcomb, D. T., Shaw, J. E., Carr, S. H. and Hirsh, D. (1985). Extrachromosomal DNA transformation of Caenorhabditis elegans. Mol. Cell. Biol. 5, 3484-3496.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3484-3496
    • Stinchcomb, D.T.1    Shaw, J.E.2    Carr, S.H.3    Hirsh, D.4
  • 48
    • 0016067224 scopus 로고
    • The DNA of Caenorhabditis elegans
    • Sulston, J. E. and Brenner, S. (1974). The DNA of Caenorhabditis elegans. Genetics 77, 95-104.
    • (1974) Genetics , vol.77 , pp. 95-104
    • Sulston, J.E.1    Brenner, S.2
  • 49
    • 0020858899 scopus 로고
    • The embryonic cell lineage of the nematode Caenorhabditis elegans
    • Sulston, J. E., Schierenberg, E., White, J. G. and Thomson, J. N. (1983). The embryonic cell lineage of the nematode Caenorhabditis elegans. Dev. Biol. 100, 64-119.
    • (1983) Dev. Biol. , vol.100 , pp. 64-119
    • Sulston, J.E.1    Schierenberg, E.2    White, J.G.3    Thomson, J.N.4
  • 50
    • 0038128252 scopus 로고    scopus 로고
    • She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast Saccharomyces cerevisiae
    • Toi, H., Fujimura-Kamada, K., Irie, K., Takai, Y., Todo, S. and Tanaka, K. (2003). She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast, Saccharomyces cerevisiae. Mol. Biol. Cell 14, 2237-2249.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2237-2249
    • Toi, H.1    Fujimura-Kamada, K.2    Irie, K.3    Takai, Y.4    Todo, S.5    Tanaka, K.6
  • 51
    • 0025028910 scopus 로고
    • The unc-45 gene of Caenorhabditis elegans is an essential muscle-affecting gene with maternal expression
    • Venolia, L. andWaterston, R. H. (1990). The unc-45 gene of Caenorhabditis elegans is an essential muscle-affecting gene with maternal expression. Genetics 126, 345-353.
    • (1990) Genetics , vol.126 , pp. 345-353
    • Venolia, L.1    Waterston, R.H.2
  • 52
    • 0024150160 scopus 로고
    • Ligand-regulated nonspecific inactivation of receptor function: a versatile mechanism for signal transduction
    • Yamamoto, K. R., Godowski, P. J. and Picard, D. (1988). Ligand-regulated nonspecific inactivation of receptor function: a versatile mechanism for signal transduction. Cold Spring Harb. Symp. Quant. Biol. 53, 803-811.
    • (1988) Cold Spring Harb. Symp. Quant. Biol. , vol.53 , pp. 803-811
    • Yamamoto, K.R.1    Godowski, P.J.2    Picard, D.3
  • 53
    • 0642377466 scopus 로고    scopus 로고
    • More than folding: localized functions of cytosolic chaperones
    • Young, J. C., Barral, J. M. and Hartl, F. U. (2003). More than folding: localized functions of cytosolic chaperones. Trends Biochem. Sci. 28, 541-547.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 541-547
    • Young, J.C.1    Barral, J.M.2    Hartl, F.U.3
  • 54
    • 0018818291 scopus 로고
    • Mutants altering coordinate synthesis of specific myosins during nematode muscle development
    • Zengel, J. M. and Epstein, H. F. (1980). Mutants altering coordinate synthesis of specific myosins during nematode muscle development. Proc. Natl. Acad. Sci. USA 77, 852-856.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 852-856
    • Zengel, J.M.1    Epstein, H.F.2
  • 55
    • 84934439633 scopus 로고    scopus 로고
    • Molecular interaction network of the Hsp90 chaperone system
    • Zhao, R. and Houry, W. A. (2007). Molecular interaction network of the Hsp90 chaperone system. Adv. Exp. Med. Biol. 594, 27-36.
    • (2007) Adv. Exp. Med. Biol. , vol.594 , pp. 27-36
    • Zhao, R.1    Houry, W.A.2
  • 56
    • 20044382800 scopus 로고    scopus 로고
    • Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone
    • Zhao, R., Davey, M., Hsu, Y. C., Kaplanek, P., Tong, A., Parsons, A. B., Krogan, N., Cagney, G., Mai, D., Greenblatt, J. et al. (2005). Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120, 715-727.
    • (2005) Cell , vol.120 , pp. 715-727
    • Zhao, R.1    Davey, M.2    Hsu, Y.C.3    Kaplanek, P.4    Tong, A.5    Parsons, A.B.6    Krogan, N.7    Cagney, G.8    Mai, D.9    Greenblatt, J.10
  • 57
    • 0035980061 scopus 로고    scopus 로고
    • Hsp90 phosphorylation is linked to its chaperoning function Assembly of the retrovirus cell attachment protein
    • Zhao, Y. G., Gilmore, R., Leone, G., Coffey, M. C., Weber, B. and Lee, P. W. (2001). Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the retrovirus cell attachment protein. J. Biol. Chem. 276, 32822-32827.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32822-32827
    • Zhao, Y.G.1    Gilmore, R.2    Leone, G.3    Coffey, M.C.4    Weber, B.5    Lee, P.W.6


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