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Volumn 27, Issue 9, 2013, Pages 3594-3607

Stress-inducible phosphoprotein 1 has unique cochaperone activity during development and regulates cellular response to ischemia via the prion protein

(22)  Beraldo, Flavio H a,b   Soares, Iaci N a,b,c   Goncalves, Daniela F a,c   Fan, Jue a   Thomas, Anu A a,b   Santos, Tiago G d   Mohammad, Amro H a,b   Roffé, Martin d   Calder, Michele D b,e   Nikolova, Simona a   Hajj, Glaucia N d   Guimaraes, Andre L a,f   Massensini, Andre R c   Welch, Ian b   Betts, Dean H b,e   Gros, Robert a,b   Drangova, Maria a,b   Watson, Andrew J b,e   Bartha, Robert a,b   Prado, Vania F a,b   more..


Author keywords

Hsp70; Hsp90; Maternal effect gene; Prion protein; Stroke

Indexed keywords

CASPASE 3; CHAPERONE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PHOSPHOPROTEIN; PRION PROTEIN; STRESS INDUCIBLE PHOSPHOPROTEIN 1; UNCLASSIFIED DRUG;

EID: 84883352804     PISSN: None     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.13-232280     Document Type: Article
Times cited : (68)

References (63)
  • 1
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • Picard, D. (2002) Heat-shock protein 90, a chaperone for folding and regulation. Cell. Mol. Life Sci. 59, 1640-1648
    • (2002) Cell. Mol. Life Sci , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 3
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl, L. H., and Prodromou, C. (2006) Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75, 271-294
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 5
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: Emerging mechanistic insights
    • Taipale, M., Jarosz, D. F., and Lindquist, S. (2010) HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat. Rev. Mol. Cell Biol. 11, 515-528
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 6
    • 0037518202 scopus 로고    scopus 로고
    • Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle
    • Richter, K., Muschler, P., Hainzl, O., Reinstein, J., and Buchner, J. (2003) Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle. J. Biol. Chem. 278, 10328-10333
    • (2003) J. Biol. Chem , vol.278 , pp. 10328-10333
    • Richter, K.1    Muschler, P.2    Hainzl, O.3    Reinstein, J.4    Buchner, J.5
  • 7
    • 79959344309 scopus 로고    scopus 로고
    • Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90: Hop complex
    • Southworth, D. R., and Agard, D. A. (2011) Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90: Hop complex. Mol. Cell 42, 771-781
    • (2011) Mol. Cell , vol.42 , pp. 771-781
    • Southworth, D.R.1    Agard, D.A.2
  • 8
    • 79251560849 scopus 로고    scopus 로고
    • Drosophila Piwi functions in Hsp90-mediated suppression of phenotypic variation
    • Gangaraju, V. K., Yin, H., Weiner, M. M., Wang, J., Huang, X. A., and Lin, H. (2011) Drosophila Piwi functions in Hsp90-mediated suppression of phenotypic variation. Nat. Genet. 43, 153-158
    • (2011) Nat. Genet , vol.43 , pp. 153-158
    • Gangaraju, V.K.1    Yin, H.2    Weiner, M.M.3    Wang, J.4    Huang, X.A.5    Lin, H.6
  • 10
    • 79958748545 scopus 로고    scopus 로고
    • Extracellular heat shock proteins, cellular export vesicles, and the stress observation system: A form of communication during injury, infection, and cell damage
    • De Maio, A. (2011) Extracellular heat shock proteins, cellular export vesicles, and the stress observation system: a form of communication during injury, infection, and cell damage. Cell Stress Chaperones 16, 235-249
    • (2011) Cell Stress Chaperones , vol.16 , pp. 235-249
    • De Maio, A.1
  • 11
    • 36448998174 scopus 로고    scopus 로고
    • Cellular prion protein expression in astrocytes modulates neuronal survival and differentiation
    • Lima, F. R., Arantes, C. P., Muras, A. G., Nomizo, R., Brentani, R. R., and Martins, V. R. (2007) Cellular prion protein expression in astrocytes modulates neuronal survival and differentiation. J. Neurochem. 103, 2164-2176
    • (2007) J. Neurochem , vol.103 , pp. 2164-2176
    • Lima, F.R.1    Arantes, C.P.2    Muras, A.G.3    Nomizo, R.4    Brentani, R.R.5    Martins, V.R.6
  • 12
    • 70349144046 scopus 로고    scopus 로고
    • Prion protein and its ligand stress inducible protein 1 regulate astrocyte development
    • Arantes, C., Nomizo, R., Lopes, M. H., Hajj, G. N., Lima, F. R., and Martins, V. R. (2009) Prion protein and its ligand stress inducible protein 1 regulate astrocyte development. Glia 57, 1439-1449
    • (2009) Glia , vol.57 , pp. 1439-1449
    • Arantes, C.1    Nomizo, R.2    Lopes, M.H.3    Hajj, G.N.4    Lima, F.R.5    Martins, V.R.6
  • 14
    • 78449232159 scopus 로고    scopus 로고
    • Role of alpha7 nicotinic acetylcholine receptor in calcium signaling induced by prion protein interaction with stress-inducible protein 1
    • Beraldo, F. H., Arantes, C. P., Santos, T. G., Queiroz, N. G., Young, K., Rylett, R. J., Markus, R. P., Prado, M. A., and Martins, V. R. (2010) Role of alpha7 nicotinic acetylcholine receptor in calcium signaling induced by prion protein interaction with stress-inducible protein 1. J. Biol. Chem. 285, 36542-36550
    • (2010) J. Biol. Chem , vol.285 , pp. 36542-36550
    • Beraldo, F.H.1    Arantes, C.P.2    Santos, T.G.3    Queiroz, N.G.4    Young, K.5    Rylett, R.J.6    Markus, R.P.7    Prado, M.A.8    Martins, V.R.9
  • 16
    • 78449232159 scopus 로고    scopus 로고
    • Role of α7 nicotinic acetylcholine receptor in calcium signaling induced by prion protein interaction with stress-inducible protein 1
    • Beraldo, F. H., Arantes, C. P., Santos, T. G., Queiroz, N. G., Young, K., Rylett, R. J., Markus, R. P., Prado, M. A., and Martins, V. R. (2010) Role of α7 nicotinic acetylcholine receptor in calcium signaling induced by prion protein interaction with stress-inducible protein 1. J. Biol. Chem. 19, 36542-36550
    • (2010) J. Biol. Chem , vol.19 , pp. 36542-36550
    • Beraldo, F.H.1    Arantes, C.P.2    Santos, T.G.3    Queiroz, N.G.4    Young, K.5    Rylett, R.J.6    Markus, R.P.7    Prado, M.A.8    Martins, V.R.9
  • 17
    • 30544444183 scopus 로고    scopus 로고
    • Interaction of cellular prion and stress-inducible protein 1 promotes neuritogenesis and neuroprotection by distinct signaling pathways
    • Lopes, M. H., Hajj, G. N., Muras, A. G., Mancini, G. L., Castro, R. M., Ribeiro, K. C., Brentani, R. R., Linden, R., and Martins, V. R. (2005) Interaction of cellular prion and stress-inducible protein 1 promotes neuritogenesis and neuroprotection by distinct signaling pathways. J. Neurosci. 7, 11330-11339
    • (2005) J. Neurosci , vol.7 , pp. 11330-11339
    • Lopes, M.H.1    Hajj, G.N.2    Muras, A.G.3    Mancini, G.L.4    Castro, R.M.5    Ribeiro, K.C.6    Brentani, R.R.7    Linden, R.8    Martins, V.R.9
  • 18
    • 0031013723 scopus 로고    scopus 로고
    • In vivo analysis of the hsp90 cochaperone sti1 p60
    • Chang, H. C., Nathan, D. F., and Lindquist, S. (1997) In vivo analysis of the Hsp90 cochaperone Sti1 (p60). Mol. Cell. Biol. 17, 318-325
    • (1997) Mol. Cell. Biol , vol.17 , pp. 318-325
    • Chang, H.C.1    Nathan, D.F.2    Lindquist, S.3
  • 19
    • 67649365446 scopus 로고    scopus 로고
    • C. Elegans STI-1, the homolog of Sti1/Hop, is involved in aging and stress response
    • Song, H. O., Lee, W., An, K., Lee, H. S., Cho, J. H., Park, Z. Y., and Ahnn, J. (2009) C. elegans STI-1, the homolog of Sti1/Hop, is involved in aging and stress response. J. Mol. Biol. 390, 604-617
    • (2009) J. Mol. Biol , vol.390 , pp. 604-617
    • Song, H.O.1    Lee, W.2    An, K.3    Lee, H.S.4    Cho, J.H.5    Park, Z.Y.6    Ahnn, J.7
  • 24
    • 77953648269 scopus 로고    scopus 로고
    • Rapid 3D phenotyping of cardiovascular development in mouse embryos by micro-CT with iodine staining
    • Degenhardt, K., Wright, A. C., Horng, D., Padmanabhan, A., and Epstein, J. A. (2010) Rapid 3D phenotyping of cardiovascular development in mouse embryos by micro-CT with iodine staining. Circ. Cardiovasc. Imaging 3, 314-322
    • (2010) Circ. Cardiovasc. Imaging , vol.3 , pp. 314-322
    • Degenhardt, K.1    Wright, A.C.2    Horng, D.3    Padmanabhan, A.4    Epstein, J.A.5
  • 25
    • 51849131434 scopus 로고    scopus 로고
    • In vivo small-animal imaging using micro-CT and digital subtraction angiography
    • Badea, C. T., Drangova, M., Holdsworth, D. W., and Johnson, G. A. (2008) In vivo small-animal imaging using micro-CT and digital subtraction angiography. Phys. Med. Biol. 53, R319-R350
    • (2008) Phys. Med. Biol , vol.53
    • Badea, C.T.1    Drangova, M.2    Holdsworth, D.W.3    Johnson, G.A.4
  • 26
    • 0024494427 scopus 로고
    • Reversible middle cerebral artery occlusion without craniectomy in rats
    • Longa, E. Z., Weinstein, P. R., Carlson, S., and Cummins, R. (1989) Reversible middle cerebral artery occlusion without craniectomy in rats. Stroke 20, 84-91
    • (1989) Stroke , vol.20 , pp. 84-91
    • Longa, E.Z.1    Weinstein, P.R.2    Carlson, S.3    Cummins, R.4
  • 27
    • 0022483434 scopus 로고
    • Rat middle cerebral artery occlusion: Evaluation of the model and development of a neurologic examination
    • Bederson, J. B., Pitts, L. H., Tsuji, M., Nishimura, M. C., Davis, R. L., and Bartkowski, H. (1986) Rat middle cerebral artery occlusion: evaluation of the model and development of a neurologic examination. Stroke 17, 472-476
    • (1986) Stroke , vol.17 , pp. 472-476
    • Bederson, J.B.1    Pitts, L.H.2    Tsuji, M.3    Nishimura, M.C.4    Davis, R.L.5    Bartkowski, H.6
  • 30
    • 84865788598 scopus 로고    scopus 로고
    • Secreted stress-induced phosphoprotein 1 activates the ALK2-SMAD signaling pathways and promotes cell proliferation of ovarian cancer cells
    • Tsai, C. L., Tsai, C. N., Lin, C. Y., Chen, H. W., Lee, Y. S., Chao, A., Wang, T. H., Wang, H. S., and Lai, C. H. (2012) Secreted stress-induced phosphoprotein 1 activates the ALK2-SMAD signaling pathways and promotes cell proliferation of ovarian cancer cells. Cell Rep. 2, 283-293
    • (2012) Cell Rep , vol.2 , pp. 283-293
    • Tsai, C.L.1    Tsai, C.N.2    Lin, C.Y.3    Chen, H.W.4    Lee, Y.S.5    Chao, A.6    Wang, T.H.7    Wang, H.S.8    Lai, C.H.9
  • 32
    • 0024469206 scopus 로고
    • Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae
    • Nicolet, C. M., and Craig, E. A. (1989) Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae. Mol. Cell. Biol. 9, 3638-3646
    • (1989) Mol. Cell. Biol , vol.9 , pp. 3638-3646
    • Nicolet, C.M.1    Craig, E.A.2
  • 36
    • 80053555789 scopus 로고    scopus 로고
    • More than just a focus: The chromatin response to DNA damage and its role in genome integrity maintenance
    • Lukas, J., Lukas, C., and Bartek, J. (2011) More than just a focus: The chromatin response to DNA damage and its role in genome integrity maintenance. Nat. Cell Biol. 13, 1161-1169
    • (2011) Nat. Cell Biol , vol.13 , pp. 1161-1169
    • Lukas, J.1    Lukas, C.2    Bartek, J.3
  • 37
    • 36949005417 scopus 로고    scopus 로고
    • DNA damage signalling guards against activated oncogenes and tumour progression
    • Bartek, J., Bartkova, J., and Lukas, J. (2007) DNA damage signalling guards against activated oncogenes and tumour progression. Oncogene 26, 7773-7779
    • (2007) Oncogene , vol.26 , pp. 7773-7779
    • Bartek, J.1    Bartkova, J.2    Lukas, J.3
  • 38
    • 43549110056 scopus 로고    scopus 로고
    • Nuclear translocation of the phosphoprotein Hop (Hsp70/Hsp90 organizing protein) occurs under heat shock, and its proposed nuclear localization signal is involved in Hsp90 binding
    • Daniel, S., Bradley, G., Longshaw, V. M., Söti, C., Csermely, P., and Blatch, G. L. (2008) Nuclear translocation of the phosphoprotein Hop (Hsp70/Hsp90 organizing protein) occurs under heat shock, and its proposed nuclear localization signal is involved in Hsp90 binding. Biochim. Biophys. Acta 1783, 1003- 1014
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1003-1014
    • Daniel, S.1    Bradley, G.2    Longshaw, V.M.3    Söti, C.4    Csermely, P.5    Blatch, G.L.6
  • 39
    • 1342283935 scopus 로고    scopus 로고
    • Nuclear translocation of the Hsp70/ Hsp90 organizing protein mSTI1 is regulated by cell cycle kinases
    • Longshaw, V. M., Chapple, J. P., Balda, M. S., Cheetham, M. E., and Blatch, G. L. (2004) Nuclear translocation of the Hsp70/ Hsp90 organizing protein mSTI1 is regulated by cell cycle kinases. J. Cell Sci. 15, 701-710
    • (2004) J. Cell Sci , vol.15 , pp. 701-710
    • Longshaw, V.M.1    Chapple, J.P.2    Balda, M.S.3    Cheetham, M.E.4    Blatch, G.L.5
  • 42
    • 25644433562 scopus 로고    scopus 로고
    • Overexpression of PrPC by adenovirus-mediated gene targeting reduces ischemic injury in a stroke rat model
    • Shyu, W. C., Lin, S. Z., Chiang, M. F., Ding, D. C., Li, K. W., Chen, S. F., Yang, H. I., and Li, H. (2005) Overexpression of PrPC by adenovirus-mediated gene targeting reduces ischemic injury in a stroke rat model. J. Neurosci. 25, 8967-8977
    • (2005) J. Neurosci , vol.25 , pp. 8967-8977
    • Shyu, W.C.1    Lin, S.Z.2    Chiang, M.F.3    Ding, D.C.4    Li, K.W.5    Chen, S.F.6    Yang, H.I.7    Li, H.8
  • 43
    • 72149127389 scopus 로고    scopus 로고
    • The alpha-secretase-derived N-terminal product of cellular prion, N1 displays neuroprotective function, in vitro and in vivo
    • Guillot-Sestier, M. V., Sunyach, C., Druon, C., Scarzello, S., and Checler, F. (2009) The alpha-secretase-derived N-terminal product of cellular prion, N1 displays neuroprotective function, in vitro and in vivo. J. Biol. Chem. 284, 35973-35986
    • (2009) J. Biol. Chem , vol.284 , pp. 35973-35986
    • Guillot-Sestier, M.V.1    Sunyach, C.2    Druon, C.3    Scarzello, S.4    Checler, F.5
  • 44
    • 0033621681 scopus 로고    scopus 로고
    • Mice lacking HSP90β fail to develop a placental labyrinth
    • Voss, A. K., Thomas, T., and Gruss, P. (2000) Mice lacking HSP90β fail to develop a placental labyrinth. Development 127, 1-11
    • (2000) Development , vol.127 , pp. 1-11
    • Voss, A.K.1    Thomas, T.2    Gruss, P.3
  • 45
    • 80053620191 scopus 로고    scopus 로고
    • Heat shock protein 90 (HSP90) contributes to cytosolic translocation of extracellular antigen for cross-presentation by dendritic cells
    • Imai, T., Kato, Y., Kajiwara, C., Mizukami, S., Ishige, I., Ichiyanagi, T., Hikida, M., Wang, J. Y., and Udono, H. (2011) Heat shock protein 90 (HSP90) contributes to cytosolic translocation of extracellular antigen for cross-presentation by dendritic cells. Proc. Natl. Acad. Sci. U. S. A. 108, 16363-16368
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 16363-16368
    • Imai, T.1    Kato, Y.2    Kajiwara, C.3    Mizukami, S.4    Ishige, I.5    Ichiyanagi, T.6    Hikida, M.7    Wang, J.Y.8    Udono, H.9
  • 46
    • 84862816993 scopus 로고    scopus 로고
    • Dynamics of the regulation of Hsp90 by the co-chaperone Sti1
    • Lee, C. T., Graf, C., Mayer, F. J., Richter, S. M., and Mayer, M. P. (2012) Dynamics of the regulation of Hsp90 by the co-chaperone Sti1. EMBO. J. 31, 1518-1528
    • (2012) EMBO. J. , vol.31 , pp. 1518-1528
    • Lee, C.T.1    Graf, C.2    Mayer, F.J.3    Richter, S.M.4    Mayer, M.P.5
  • 48
    • 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
  • 50
    • 79960075550 scopus 로고    scopus 로고
    • Enhanced neural progenitor/ stem cells self-renewal via the interaction of stress-inducible protein 1 with the prion protein
    • Santos, T. G., Silva, I. R., Costa-Silva, B., Lepique, A. P., Martins, V. R., and Lopes, M. H. (2011) Enhanced neural progenitor/ stem cells self-renewal via the interaction of stress-inducible protein 1 with the prion protein. Stem Cells 29, 1126-1136
    • (2011) Stem Cells , vol.29 , pp. 1126-1136
    • Santos, T.G.1    Silva, I.R.2    Costa-Silva, B.3    Lepique, A.P.4    Martins, V.R.5    Lopes, M.H.6
  • 52
  • 53
    • 34249727193 scopus 로고    scopus 로고
    • Hsp90 regulates the Fanconi anemia DNA damage response pathway
    • Oda, T., Hayano, T., Miyaso, H., Takahashi, N., and Yamashita, T. (2007) Hsp90 regulates the Fanconi anemia DNA damage response pathway. Blood 109, 5016-5026
    • (2007) Blood , vol.109 , pp. 5016-5026
    • Oda, T.1    Hayano, T.2    Miyaso, H.3    Takahashi, N.4    Yamashita, T.5
  • 54
    • 79960134213 scopus 로고    scopus 로고
    • Hsp90 inhibitormediated disruption of chaperone association of ATR with hsp90 sensitizes cancer cells to DNA damage
    • Ha, K., Fiskus, W., Rao, R., Balusu, R., Venkannagari, S., Nalabothula, N. R., and Bhalla, K. N. (2011) Hsp90 inhibitormediated disruption of chaperone association of ATR with hsp90 sensitizes cancer cells to DNA damage. Mol. Cancer Ther. 10, 1194-1206
    • (2011) Mol. Cancer Ther , vol.10 , pp. 1194-1206
    • Ha, K.1    Fiskus, W.2    Rao, R.3    Balusu, R.4    Venkannagari, S.5    Nalabothula, N.R.6    Bhalla, K.N.7
  • 55
    • 84863371816 scopus 로고    scopus 로고
    • Heat shock protein 90alpha (Hsp90alpha) is phosphorylated in response to DNA damage and accumulates in repair foci
    • Quanz, M., Herbette, A., Sayarath, M., de, K. L., Dubois, T., Sun, J. S., and Dutreix, M. (2012) Heat shock protein 90alpha (Hsp90alpha) is phosphorylated in response to DNA damage and accumulates in repair foci. J. Biol. Chem. 287, 8803-8815
    • (2012) J. Biol. Chem , vol.287 , pp. 8803-8815
    • Quanz, M.1    Herbette, A.2    Sayarath, M.3    De, K.L.4    Dubois, T.5    Sun, J.S.6    Dutreix, M.7
  • 56
    • 84857943078 scopus 로고    scopus 로고
    • Quantitative proteomics reveals that Hsp90 inhibition preferentially targets kinases and the DNA damage response
    • Sharma, K., Vabulas, R. M., Macek, B., Pinkert, S., Cox, J., Mann, M., and Hartl, F. U. (2012) Quantitative proteomics reveals that Hsp90 inhibition preferentially targets kinases and the DNA damage response. Mol. Cell. Proteomics 11, M111
    • (2012) Mol. Cell. Proteomics , vol.11
    • Sharma, K.1    Vabulas, R.M.2    Macek, B.3    Pinkert, S.4    Cox, J.5    Mann, M.6    Hartl, F.U.7
  • 58
    • 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
  • 59
    • 0037160084 scopus 로고    scopus 로고
    • Interactions of STAT3 with caveolin-1 and heat shock protein 90 in plasma membrane raft and cytosolic complexes. Preservation of cytokine signaling during fever
    • Shah, M., Patel, K., Fried, V. A., and Sehgal, P. B. (2002) Interactions of STAT3 with caveolin-1 and heat shock protein 90 in plasma membrane raft and cytosolic complexes. Preservation of cytokine signaling during fever. J. Biol. Chem. 277, 45662- 45669
    • (2002) J. Biol. Chem , vol.277 , pp. 45662-45669
    • Shah, M.1    Patel, K.2    Fried, V.A.3    Sehgal, P.B.4
  • 60
    • 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., and Buchner, J. (2004) Hsp90 regulates the activity of wild type p53 under physiological and elevated temperatures. J. Biol. Chem. 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
  • 61
    • 0345803950 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase interaction with Hsp90 mediates kinase maturation
    • Luo, J., and Benovic, J. L. (2003) G protein-coupled receptor kinase interaction with Hsp90 mediates kinase maturation. J. Biol. Chem. 278, 50908-50914
    • (2003) J. Biol. Chem , vol.278 , pp. 50908-50914
    • Luo, J.1    Benovic, J.L.2
  • 62
    • 82955169612 scopus 로고    scopus 로고
    • A compound that inhibits the HOP-Hsp90 complex formation and has unique killing effects in breast cancer cell lines
    • Pimienta, G., Herbert, K. M., and Regan, L. (2011) A compound that inhibits the HOP-Hsp90 complex formation and has unique killing effects in breast cancer cell lines. Mol. Pharm. 8, 2252-2261
    • (2011) Mol. Pharm , vol.8 , pp. 2252-2261
    • Pimienta, G.1    Herbert, K.M.2    Regan, L.3


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