Bagatell R, Paine-Murrieta GD, Taylor CW, Pulcini EJ, Akinaga S, Benjamin IJ, Whitesell L (2000) Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90-binding agents. Clin Cancer Res 6:3312–3318
Google Scholar
Calderwood SK, Khaleque MA, Sawyer DB, Ciocca DR (2006) Heat shock proteins in cancer: chaperones of tumorigenesis. Trends Biochem Sci 31:164–172. doi:10.1016/j.tibs.2006.01.006
Article
Google Scholar
Caplan AJ, Mandal AK, Theodoraki MA (2007) Molecular chaperones and protein kinase quality control trends. Cell Biol 17:87–92. doi:10.1016/j.tcb.2006.12.002
Article
Google Scholar
Cutforth T, Rubin GM (1994) Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. Cell 77:1027–1036
Article
Google Scholar
d’Auvergne EJ, Gooley PR (2008a) Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces. J Biomol NMR 40:107–119. doi:10.1007/s10858-007-9214-2
Article
Google Scholar
d’Auvergne EJ, Gooley PR (2008b) Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor. J Biomol NMR 40:121–133. doi:10.1007/s10858-007-9213-3
Article
Google Scholar
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293
Article
Google Scholar
Eliezer D, Chung J, Dyson HJ, Wright PE (2000) Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin. Biochemistry 39:2894–2901
Article
Google Scholar
Farrow NA et al (1994) Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. Biochemistry 33:5984–6003
Article
Google Scholar
Guntert P (2004) Automated NMR structure calculation with CYANA. Methods Mol Biol 278:353–378. doi:10.1385/1-59259-809-9:353
Google Scholar
Jhaveri K, Taldone T, Modi S, Chiosis G (2012) Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancers. Biochim Biophys Acta 1823:742–755. doi:10.1016/j.bbamcr.2011.10.008
Article
Google Scholar
Karnitz LM, Felts SJ (2007) Cdc37 regulation of the kinome: when to hold’em and when to fold’em. Sci Signal 2007:pe22. doi:10.1126/stke.3852007pe22
Google Scholar
Kay LE, Torchia DA, Bax A (1989) Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28:8972–8979
Article
Google Scholar
Lefevre JF, Dayie KT, Peng JW, Wagner G (1996) Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions. Biochemistry 35:2674–2686. doi:10.1021/bi9526802
Article
Google Scholar
McCollum AK, Teneyck CJ, Sauer BM, Toft DO, Erlichman C (2006) Up-regulation of heat shock protein 27 induces resistance to 17-allylamino-demethoxygeldanamycin through a glutathione-mediated mechanism. Cancer Res 66:10967–10975. doi:10.1158/0008-5472.CAN-06-1629
Article
Google Scholar
O’Sullivan DB, Jones CE, Abdelraheim SR, Brazier MW, Toms H, Brown DR, Viles JH (2009) Dynamics of a truncated prion protein, PrP(113-231), from (15)N NMR relaxation: order parameters calculated and slow conformational fluctuations localized to a distinct region. Protein Sci 18:410–423. doi:10.1002/pro.44
Article
Google Scholar
Ottiger M, Delaglio F, Bax A (1998) Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J Magn Reson 131:373–378. doi:10.1006/jmre.1998.1361
Article
ADS
Google Scholar
Pearl LH (2005) Hsp90 and Cdc37—a chaperone cancer conspiracy. Curr Opin Genet Dev 15:55–61. doi:10.1016/j.gde.2004.12.011
Article
Google Scholar
Pearl LH, Prodromou C (2006) Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem 75:271–294. doi:10.1146/annurev.biochem.75.103004.142738
Article
Google Scholar
Polier S, Samant RS, Clarke PA, Workman P, Prodromou C, Pearl LH (2013) ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system. Nat Chem Biol 9:307–312. doi:10.1038/nchembio.1212
Article
Google Scholar
Roe SM, Prodromou C, O’Brien R, Ladbury JE, Piper PW, Pearl LH (1999) Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 42:260–266. doi:10.1021/jm980403y
Article
Google Scholar
Roe SM et al (2004) The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37). Cell 116:87–98
Article
Google Scholar
Rohl A, Rohrberg J, Buchner J (2013) The chaperone Hsp90: changing partners for demanding clients. Trends Biochem Sci 38:253–262. doi:10.1016/j.tibs.2013.02.003
Article
Google Scholar
Schwarze SR, Fu VX, Jarrard DF (2003) Cdc37 enhances proliferation and is necessary for normal human prostate epithelial cell survival. Cancer Res 63:4614–4619
Google Scholar
Seiler CY et al (2014) DNASU plasmid and PSI: biology-materials repositories— resources to accelerate biological research. Nucleic Acids Res 42:D1253–D1260. doi:10.1093/nar/gkt1060
Article
Google Scholar
Shao J, Irwin A, Hartson SD, Matts RL (2003a) Functional dissection of cdc37: characterization of domain structure and amino acid residues critical for protein kinase binding. Biochemistry 42:12577–12588. doi:10.1021/bi035138j
Article
Google Scholar
Shao J, Prince T, Hartson SD, Matts RL (2003b) Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37. J Biol Chem 278:38117–38120. doi:10.1074/jbc.C300330200
Article
Google Scholar
Shen Y, Bax A (2013) Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks. J Biomol NMR 56:227–241. doi:10.1007/s10858-013-9741-y
Article
Google Scholar
Sreeramulu S, Gande SL, Gobel M, Schwalbe H (2009a) Molecular mechanism of inhibition of the human protein complex Hsp90-Cdc37, a kinome chaperone-cochaperone, by triterpene celastrol. Angew Chem Int Ed Engl 48:5853–5855. doi:10.1002/anie.200900929
Article
Google Scholar
Sreeramulu S, Jonker HR, Langer T, Richter C, Lancaster CR, Schwalbe H (2009b) The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy. J Biol Chem 284:3885–3896. doi:10.1074/jbc.M806715200
Article
Google Scholar
Stepanova L, Finegold M, DeMayo F, Schmidt EV, Harper JW (2000a) The oncoprotein kinase chaperone CDC37 functions as an oncogene in mice and collaborates with both c-myc and cyclin D1 in transformation of multiple tissues. Mol Cell Biol 20:4462–4473
Article
Google Scholar
Stepanova L, Yang G, DeMayo F, Wheeler TM, Finegold M, Thompson TC, Harper JW (2000b) Induction of human Cdc37 in prostate cancer correlates with the ability of targeted Cdc37 expression to promote prostatic hyperplasia. Oncogene 19:2186–2193. doi:10.1038/sj.onc.1203561
Article
Google Scholar
Vaughan CK et al (2006) Structure of an Hsp90-Cdc37-Cdk4 complex. Mol Cell 23:697–707. doi:10.1016/j.molcel.2006.07.016
Article
Google Scholar
Wen Y et al (2010) Unique structural characteristics of the rabbit prion protein. J Biol Chem 285:31682–31693. doi:10.1074/jbc.M110.118844
Article
Google Scholar
Whitesell L, Lindquist SL (2005) HSP90 and the chaperoning of cancer. Nat Rev Cancer 5:761–772. doi:10.1038/nrc1716
Article
Google Scholar
Xu W et al (2012) Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine. Mol Cell 47:434–443. doi:10.1016/j.molcel.2012.05.015
Article
Google Scholar