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Volumn 6, Issue 10, 2011, Pages

An interaction network predicted from public data as a discovery tool: Application to the Hsp90 molecular chaperone machine

Author keywords

[No Author keywords available]

Indexed keywords

AHA1 PROTEIN; BINDING PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 90; UNCLASSIFIED DRUG;

EID: 80053976720     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0026044     Document Type: Article
Times cited : (188)

References (62)
  • 1
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: emerging mechanistic insights
    • Taipale M, Jarosz DF, 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
  • 2
    • 65549138976 scopus 로고    scopus 로고
    • The complex dance of the molecular chaperone Hsp90
    • Neckers L, Mollapour M, Tsutsumi S, (2009) The complex dance of the molecular chaperone Hsp90. Trends Biochem Sci 34: 223-226.
    • (2009) Trends Biochem Sci , vol.34 , pp. 223-226
    • Neckers, L.1    Mollapour, M.2    Tsutsumi, S.3
  • 5
    • 0030667932 scopus 로고    scopus 로고
    • In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
    • Nathan DF, Vos MH, Lindquist S, (1997) In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc Natl Acad Sci USA 94: 12949-12956.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12949-12956
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 7
    • 77952551024 scopus 로고    scopus 로고
    • Discovery and development of Hsp90 inhibitors: a promising pathway for cancer therapy
    • Porter JR, Fritz CC, Depew KM, (2010) Discovery and development of Hsp90 inhibitors: a promising pathway for cancer therapy. Curr Opin Chem Biol 14: 412-420.
    • (2010) Curr Opin Chem Biol , vol.14 , pp. 412-420
    • Porter, J.R.1    Fritz, C.C.2    Depew, K.M.3
  • 8
    • 30344462410 scopus 로고    scopus 로고
    • Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
    • Albanèse V, Yam AY, Baughman J, Parnot C, Frydman J, (2006) Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells. Cell 124: 75-88.
    • (2006) Cell , vol.124 , pp. 75-88
    • Albanèse, V.1    Yam, A.Y.2    Baughman, J.3    Parnot, C.4    Frydman, J.5
  • 9
    • 34848844683 scopus 로고    scopus 로고
    • Systems analysis of chaperone networks in the malarial parasite Plasmodium falciparum
    • Pavithra SR, Kumar R, Tatu U, (2007) Systems analysis of chaperone networks in the malarial parasite Plasmodium falciparum. PLoS Comput Biol 3: 1701-1715.
    • (2007) PLoS Comput Biol , vol.3 , pp. 1701-1715
    • Pavithra, S.R.1    Kumar, R.2    Tatu, U.3
  • 10
    • 42949165604 scopus 로고    scopus 로고
    • Chaperones as integrators of cellular networks: changes of cellular integrity in stress and diseases
    • Palotai R, Szalay MS, Csermely P, (2008) Chaperones as integrators of cellular networks: changes of cellular integrity in stress and diseases. IUBMB Life 60: 10-18.
    • (2008) IUBMB Life , vol.60 , pp. 10-18
    • Palotai, R.1    Szalay, M.S.2    Csermely, P.3
  • 11
    • 67650681847 scopus 로고    scopus 로고
    • An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell
    • Gong Y, Kakihara Y, Krogan N, Greenblatt J, Emili A, et al. (2009) An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Mol Syst Biol 5: 275.
    • (2009) Mol Syst Biol , vol.5 , pp. 275
    • Gong, Y.1    Kakihara, Y.2    Krogan, N.3    Greenblatt, J.4    Emili, A.5
  • 12
    • 20044382800 scopus 로고    scopus 로고
    • Navigating the chaperone network: integrative map of physical and genetic interactions mediated by the Hsp90 chaperone
    • Zhao R, Davey M, Hsu YC, Kaplanek P, Tong A, et al. (2005) Navigating the chaperone network: 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
  • 13
    • 18944365231 scopus 로고    scopus 로고
    • A two-hybrid screen of the yeast proteome for hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p)
    • Millson SH, Truman AW, King V, Prodromou C, Pearl LH, et al. (2005) A two-hybrid screen of the yeast proteome for hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p). Eukaryot Cell 4: 849-860.
    • (2005) Eukaryot Cell , vol.4 , pp. 849-860
    • Millson, S.H.1    Truman, A.W.2    King, V.3    Prodromou, C.4    Pearl, L.H.5
  • 15
    • 34848926209 scopus 로고    scopus 로고
    • Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches
    • McClellan AJ, Xia Y, Deutschbauer AM, Davis RW, Gerstein M, et al. (2007) Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell 131: 121-135.
    • (2007) Cell , vol.131 , pp. 121-135
    • McClellan, A.J.1    Xia, Y.2    Deutschbauer, A.M.3    Davis, R.W.4    Gerstein, M.5
  • 16
    • 34249317189 scopus 로고    scopus 로고
    • Novel subunits of the mammalian Hsp90 signal transduction chaperone
    • Te J, Jia L, Rogers J, Miller A, Hartson SD, (2007) Novel subunits of the mammalian Hsp90 signal transduction chaperone. J Proteome Res 6: 1963-1973.
    • (2007) J Proteome Res , vol.6 , pp. 1963-1973
    • Te, J.1    Jia, L.2    Rogers, J.3    Miller, A.4    Hartson, S.D.5
  • 17
    • 34547229135 scopus 로고    scopus 로고
    • A proteomic approach towards the Hsp90-dependent ubiquitinylated proteome
    • Falsone SF, Gesslbauer B, Rek A, Kungl AJ, (2007) A proteomic approach towards the Hsp90-dependent ubiquitinylated proteome. Proteomics 7: 2375-2383.
    • (2007) Proteomics , vol.7 , pp. 2375-2383
    • Falsone, S.F.1    Gesslbauer, B.2    Rek, A.3    Kungl, A.J.4
  • 18
    • 66249138886 scopus 로고    scopus 로고
    • Hsp90 inhibitor PU-H71, a multimodal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models
    • Caldas-Lopes E, Cerchietti L, Ahn JH, Clement CC, Robles AI, et al. (2009) Hsp90 inhibitor PU-H71, a multimodal inhibitor of malignancy, induces complete responses in triple-negative breast cancer models. Proc Natl Acad Sci USA 106: 8368-8373.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 8368-8373
    • Caldas-Lopes, E.1    Cerchietti, L.2    Ahn, J.H.3    Clement, C.C.4    Robles, A.I.5
  • 20
    • 76649103378 scopus 로고    scopus 로고
    • A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein
    • Gano JJ, Simon JA, (2010) A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein. Mol Cell Proteomics 9: 255-270.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 255-270
    • Gano, J.J.1    Simon, J.A.2
  • 22
    • 79953713220 scopus 로고    scopus 로고
    • Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5
    • Skarra DV, Goudreault M, Choi H, Mullin M, Nesvizhskii AI, et al. (2011) Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5. Proteomics 11: 1508-1516.
    • (2011) Proteomics , vol.11 , pp. 1508-1516
    • Skarra, D.V.1    Goudreault, M.2    Choi, H.3    Mullin, M.4    Nesvizhskii, A.I.5
  • 23
    • 80053958392 scopus 로고    scopus 로고
    • Approaches for defining the Hsp90-dependent proteome
    • in press
    • Hartson SD, Matts RL, (2011) Approaches for defining the Hsp90-dependent proteome. Biochim Biophys Acta in press.
    • (2011) Biochim Biophys Acta
    • Hartson, S.D.1    Matts, R.L.2
  • 24
    • 38449101120 scopus 로고    scopus 로고
    • Integration of biological networks and gene expression data using Cytoscape
    • Cline MS, Smoot M, Cerami E, Kuchinsky A, Landys N, et al. (2007) Integration of biological networks and gene expression data using Cytoscape. Nat Protoc 2: 2366-2382.
    • (2007) Nat Protoc , vol.2 , pp. 2366-2382
    • Cline, M.S.1    Smoot, M.2    Cerami, E.3    Kuchinsky, A.4    Landys, N.5
  • 25
    • 34547101963 scopus 로고    scopus 로고
    • Characterization of protein-interaction networks in tumors
    • Platzer A, Perco P, Lukas A, Mayer B, (2007) Characterization of protein-interaction networks in tumors. BMC Bioinformatics 8: 224.
    • (2007) BMC Bioinformatics , vol.8 , pp. 224
    • Platzer, A.1    Perco, P.2    Lukas, A.3    Mayer, B.4
  • 26
    • 64549104807 scopus 로고    scopus 로고
    • ClueGO: a Cytoscape plug-in to decipher functionally grouped gene ontology and pathway annotation networks
    • Bindea G, Mlecnik B, Hackl H, Charoentong P, Tosolini M, et al. (2009) ClueGO: a Cytoscape plug-in to decipher functionally grouped gene ontology and pathway annotation networks. Bioinformatics 25: 1091-1093.
    • (2009) Bioinformatics , vol.25 , pp. 1091-1093
    • Bindea, G.1    Mlecnik, B.2    Hackl, H.3    Charoentong, P.4    Tosolini, M.5
  • 27
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner NC, Campbell RE, Steinbach PA, Giepmans BN, Palmer AE, et al. (2004) Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat Biotechnol 22: 1567-1572.
    • (2004) Nat Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5
  • 28
    • 65549102777 scopus 로고    scopus 로고
    • Protein-protein interaction databases: keeping up with growing interactomes
    • Lehne B, Schlitt T, (2009) Protein-protein interaction databases: keeping up with growing interactomes. Hum Genomics 3: 291-297.
    • (2009) Hum Genomics , vol.3 , pp. 291-297
    • Lehne, B.1    Schlitt, T.2
  • 29
    • 77955505357 scopus 로고    scopus 로고
    • Protein-protein interactions essentials: key concepts to building and analyzing interactome networks
    • De Las Rivas J, Fontanillo C, (2010) Protein-protein interactions essentials: key concepts to building and analyzing interactome networks. PLoS Comput Biol 6: e1000807.
    • (2010) PLoS Comput Biol , vol.6
    • De Las Rivas, J.1    Fontanillo, C.2
  • 30
    • 0035222942 scopus 로고    scopus 로고
    • Protein interaction maps for model organisms
    • Walhout AJ, Vidal M, (2001) Protein interaction maps for model organisms. Nat Rev Mol Cell Biol 2: 55-62.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 55-62
    • Walhout, A.J.1    Vidal, M.2
  • 31
    • 57649199632 scopus 로고    scopus 로고
    • The prediction of protein-protein interaction networks in rice blast fungus
    • He F, Zhang Y, Chen H, Zhang Z, Peng YL, (2008) The prediction of protein-protein interaction networks in rice blast fungus. BMC genomics 9: 519.
    • (2008) BMC Genomics , vol.9 , pp. 519
    • He, F.1    Zhang, Y.2    Chen, H.3    Zhang, Z.4    Peng, Y.L.5
  • 32
    • 73249119966 scopus 로고    scopus 로고
    • Towards the mammalian interactome: Inference of a core mammalian interaction set in mouse
    • Shin CJ, Davis MJ, Ragan MA, (2009) Towards the mammalian interactome: Inference of a core mammalian interaction set in mouse. Proteomics 9: 5256-5266.
    • (2009) Proteomics , vol.9 , pp. 5256-5266
    • Shin, C.J.1    Davis, M.J.2    Ragan, M.A.3
  • 33
    • 79959241188 scopus 로고    scopus 로고
    • A predicted protein-protein interaction network of the filamentous fungus Neurospora crassa
    • Wang TY, He F, Hu QW, Zhang Z, (2011) A predicted protein-protein interaction network of the filamentous fungus Neurospora crassa. Molecular bioSystems 7: 2278-2285.
    • (2011) Molecular BioSystems , vol.7 , pp. 2278-2285
    • Wang, T.Y.1    He, F.2    Hu, Q.W.3    Zhang, Z.4
  • 39
    • 0037245913 scopus 로고    scopus 로고
    • BIND: the Biomolecular Interaction Network Database
    • Bader GD, Betel D, Hogue CW, (2003) BIND: the Biomolecular Interaction Network Database. Nucleic Acids Res 31: 248-250.
    • (2003) Nucleic Acids Res , vol.31 , pp. 248-250
    • Bader, G.D.1    Betel, D.2    Hogue, C.W.3
  • 40
    • 66449084442 scopus 로고    scopus 로고
    • Infrastructure for the life sciences: design and implementation of the UniProt website
    • Jain E, Bairoch A, Duvaud S, Phan I, Redaschi N, et al. (2009) Infrastructure for the life sciences: design and implementation of the UniProt website. BMC Bioinformatics 10: 136.
    • (2009) BMC Bioinformatics , vol.10 , pp. 136
    • Jain, E.1    Bairoch, A.2    Duvaud, S.3    Phan, I.4    Redaschi, N.5
  • 41
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da W, Sherman BT, Lempicki RA, (2009) Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 4: 44-57.
    • (2009) Nat Protoc , vol.4 , pp. 44-57
    • da Huang, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 42
    • 0034069495 scopus 로고    scopus 로고
    • Gene ontology: tool for the unification of biology. The Gene Ontology Consortium
    • Ashburner M, Ball CA, Blake JA, Botstein D, Butler H, et al. (2000) Gene ontology: tool for the unification of biology. The Gene Ontology Consortium. Nat Genet 25: 25-29.
    • (2000) Nat Genet , vol.25 , pp. 25-29
    • Ashburner, M.1    Ball, C.A.2    Blake, J.A.3    Botstein, D.4    Butler, H.5
  • 43
    • 58749109023 scopus 로고    scopus 로고
    • Genevestigator v3: a reference expression database for the meta-analysis of transcriptomes
    • Hruz T, Laule O, Szabo G, Wessendorp F, Bleuler S, et al. (2008) Genevestigator v3: a reference expression database for the meta-analysis of transcriptomes. Adv Bioinformatics 2008: 420747.
    • (2008) Adv Bioinformatics , vol.2008 , pp. 420747
    • Hruz, T.1    Laule, O.2    Szabo, G.3    Wessendorp, F.4    Bleuler, S.5
  • 44
    • 0037012880 scopus 로고    scopus 로고
    • Specificity and stability in topology of protein networks
    • Maslov S, Sneppen K, (2002) Specificity and stability in topology of protein networks. Science 296: 910-913.
    • (2002) Science , vol.296 , pp. 910-913
    • Maslov, S.1    Sneppen, K.2
  • 45
    • 34247623628 scopus 로고    scopus 로고
    • Getting connected: analysis and principles of biological networks
    • Zhu X, Gerstein M, Snyder M, (2007) Getting connected: analysis and principles of biological networks. Genes Dev 21: 1010-1024.
    • (2007) Genes Dev , vol.21 , pp. 1010-1024
    • Zhu, X.1    Gerstein, M.2    Snyder, M.3
  • 47
    • 79952689290 scopus 로고    scopus 로고
    • SnapShot: Protein-Protein Interaction Networks
    • 1000-1000.e1001
    • Seebacher J, Gavin AC, (2011) SnapShot: Protein-Protein Interaction Networks. Cell 144: 1000-1000.e1001.
    • (2011) Cell , vol.144
    • Seebacher, J.1    Gavin, A.C.2
  • 49
    • 0038718854 scopus 로고    scopus 로고
    • The structure and function of complex networks
    • Newman MEJ, (2003) The structure and function of complex networks. SIAM Review 45: 167-256.
    • (2003) SIAM Review , vol.45 , pp. 167-256
    • Newman, M.E.J.1
  • 50
    • 67149133632 scopus 로고    scopus 로고
    • Heat shock proteins and immune system
    • Tsan MF, Gao B, (2009) Heat shock proteins and immune system. J Leukoc Biol 85: 905-910.
    • (2009) J Leukoc Biol , vol.85 , pp. 905-910
    • Tsan, M.F.1    Gao, B.2
  • 51
    • 77953020807 scopus 로고    scopus 로고
    • Molecular chaperones, essential partners of steroid hormone receptors for activity and mobility
    • Echeverría PC, Picard D, (2010) Molecular chaperones, essential partners of steroid hormone receptors for activity and mobility. Biochim Biophys Acta 1803: 641-649.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 641-649
    • Echeverría, P.C.1    Picard, D.2
  • 53
    • 79251495443 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90α is required for meiotic progression of spermatocytes beyond pachytene in the mouse
    • Grad I, Cederroth CR, Walicki J, Grey C, Barluenga S, et al. (2010) The molecular chaperone Hsp90α is required for meiotic progression of spermatocytes beyond pachytene in the mouse. PLoS ONE 5: e15770.
    • (2010) PLoS ONE , vol.5
    • Grad, I.1    Cederroth, C.R.2    Walicki, J.3    Grey, C.4    Barluenga, S.5
  • 54
    • 77953027874 scopus 로고    scopus 로고
    • Transport of proteins across or into the mitochondrial outer membrane
    • Endo T, Yamano K, (2010) Transport of proteins across or into the mitochondrial outer membrane. Biochim Biophys Acta 1803: 706-714.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 706-714
    • Endo, T.1    Yamano, K.2
  • 55
    • 77953022036 scopus 로고    scopus 로고
    • Protein import into chloroplasts: the Tic complex and its regulation
    • Kovacs-Bogdan E, Soll J, Bolter B, (2010) Protein import into chloroplasts: the Tic complex and its regulation. Biochim Biophys Acta 1803: 740-747.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 740-747
    • Kovacs-Bogdan, E.1    Soll, J.2    Bolter, B.3
  • 56
    • 78651320914 scopus 로고    scopus 로고
    • Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore
    • Galigniana MD, Echeverría PC, Erlejman A, Piwien-Pilipuk G, (2010) Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore. Nucleus 1: 299-308.
    • (2010) Nucleus , vol.1 , pp. 299-308
    • Galigniana, M.D.1    Echeverría, P.C.2    Erlejman, A.3    Piwien-Pilipuk, G.4
  • 57
    • 2342447986 scopus 로고    scopus 로고
    • Importin 7 and importin α/importin β are nuclear import receptors for the glucocorticoid receptor
    • Freedman ND, Yamamoto KR, (2004) Importin 7 and importin α/importin β are nuclear import receptors for the glucocorticoid receptor. Mol Biol Cell 15: 2276-2286.
    • (2004) Mol Biol Cell , vol.15 , pp. 2276-2286
    • Freedman, N.D.1    Yamamoto, K.R.2
  • 58
    • 68849118800 scopus 로고    scopus 로고
    • Nuclear import of the glucocorticoid receptor-Hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β
    • Echeverria PC, Mazaira G, Erlejman A, Gomez-Sanchez C, Piwien Pilipuk G, et al. (2009) Nuclear import of the glucocorticoid receptor-Hsp90 complex through the nuclear pore complex is mediated by its interaction with Nup62 and importin β. Mol Cell Biol 29: 4788-4797.
    • (2009) Mol Cell Biol , vol.29 , pp. 4788-4797
    • Echeverria, P.C.1    Mazaira, G.2    Erlejman, A.3    Gomez-Sanchez, C.4    Piwien Pilipuk, G.5
  • 59
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt WB, Toft DO, (1997) Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 18: 306-360.
    • (1997) Endocr Rev , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 61
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: from nascent chain to folded protein
    • Hartl FU, Hayer-Hartl M, (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295: 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 62
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: life on the verge of death
    • Richter K, Haslbeck M, Buchner J, (2010) The heat shock response: life on the verge of death. Mol Cell 40: 253-266.
    • (2010) Mol Cell , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3


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