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Structure and mechanism of the Hsp90 molecular chaperone machinery.
Pearl LH, Prodromou C. Pearl LH, et al. Among authors: prodromou c. Annu Rev Biochem. 2006;75:271-94. doi: 10.1146/annurev.biochem.75.103004.142738. Annu Rev Biochem. 2006. PMID: 16756493 Review.
Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.
Siligardi G, Panaretou B, Meyer P, Singh S, Woolfson DN, Piper PW, Pearl LH, Prodromou C. Siligardi G, et al. Among authors: prodromou c. J Biol Chem. 2002 Jun 7;277(23):20151-9. doi: 10.1074/jbc.M201287200. Epub 2002 Mar 26. J Biol Chem. 2002. PMID: 11916974
Backbone resonance assignments of the 25kD N-terminal ATPase domain from the Hsp90 chaperone.
Salek RM, Williams MA, Prodromou C, Pearl LH, Ladbury JE. Salek RM, et al. Among authors: prodromou c. J Biomol NMR. 2002 Aug;23(4):327-8. doi: 10.1023/a:1020268712347. J Biomol NMR. 2002. PMID: 12398355 No abstract available.
Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1.
Panaretou B, Siligardi G, Meyer P, Maloney A, Sullivan JK, Singh S, Millson SH, Clarke PA, Naaby-Hansen S, Stein R, Cramer R, Mollapour M, Workman P, Piper PW, Pearl LH, Prodromou C. Panaretou B, et al. Among authors: prodromou c. Mol Cell. 2002 Dec;10(6):1307-18. doi: 10.1016/s1097-2765(02)00785-2. Mol Cell. 2002. PMID: 12504007
Yeast is selectively hypersensitised to heat shock protein 90 (Hsp90)-targetting drugs with heterologous expression of the human Hsp90beta, a property that can be exploited in screens for new Hsp90 chaperone inhibitors.
Piper PW, Panaretou B, Millson SH, Truman A, Mollapour M, Pearl LH, Prodromou C. Piper PW, et al. Among authors: prodromou c. Gene. 2003 Jan 2;302(1-2):165-70. doi: 10.1016/s0378-1119(02)01102-2. Gene. 2003. PMID: 12527207
Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions.
Meyer P, Prodromou C, Hu B, Vaughan C, Roe SM, Panaretou B, Piper PW, Pearl LH. Meyer P, et al. Among authors: prodromou c. Mol Cell. 2003 Mar;11(3):647-58. doi: 10.1016/s1097-2765(03)00065-0. Mol Cell. 2003. PMID: 12667448
Structure and functional relationships of Hsp90.
Prodromou C, Pearl LH. Prodromou C, et al. Curr Cancer Drug Targets. 2003 Oct;3(5):301-23. doi: 10.2174/1568009033481877. Curr Cancer Drug Targets. 2003. PMID: 14529383 Review.
Sensitivity to Hsp90-targeting drugs can arise with mutation to the Hsp90 chaperone, cochaperones and plasma membrane ATP binding cassette transporters of yeast.
Piper PW, Millson SH, Mollapour M, Panaretou B, Siligardi G, Pearl LH, Prodromou C. Piper PW, et al. Among authors: prodromou c. Eur J Biochem. 2003 Dec;270(23):4689-95. doi: 10.1046/j.1432-1033.2003.03866.x. Eur J Biochem. 2003. PMID: 14622256
The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37).
Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, Prodromou C, Pearl LH. Roe SM, et al. Among authors: prodromou c. Cell. 2004 Jan 9;116(1):87-98. doi: 10.1016/s0092-8674(03)01027-4. Cell. 2004. PMID: 14718169
Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.
Meyer P, Prodromou C, Liao C, Hu B, Mark Roe S, Vaughan CK, Vlasic I, Panaretou B, Piper PW, Pearl LH. Meyer P, et al. Among authors: prodromou c. EMBO J. 2004 Feb 11;23(3):511-9. doi: 10.1038/sj.emboj.7600060. Epub 2004 Jan 22. EMBO J. 2004. PMID: 14739935 Free PMC article. Corrected and republished.
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