Prodromou Lab

Publications

Dr Chrisostomos Prodromou

  • Minghao Zhang; Yasuhiro Kadota; Chrisostomos Prodromou; Ken Shirasu; Laurence Pearl, (2010). Structural basis for assembly of Hsp90 - Sgt1 - CHORD protein complexes: implications for chaperoning of NLR innate immunity receptors. Mol. Cell, 39(2), 269-81
  • Day JE, Sharp SY, Rowlands MG, Aherne W, Lewis W, Roe SM, Prodromou C, Pearl LH, Workman P, Moody CJ. (2010). Inhibition of Hsp90 with resorcylic acid macrolactones: synthesis and binding studies. Chemistry, 10;16(34):10366-72.
  • Mollapour M, Tsutsumi S, Donnelly AC, Beebe K, Tokita MJ, Lee MJ, Lee S, Morra G, Bourboulia D, Scroggins BT, Colombo G, Blagg BS, Panaretou B, Stetler-Stevenson WG, Trepel JB, Piper PW, Prodromou C, Pearl LH, Neckers L. Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function. Mol Cell, 2010 Feb 12;37(3):333-43.
  • Rowlands M, McAndrew C, Prodromou C, Pearl L, Kalusa A, Jones K, Workman P, Aherne W. (2010). Detection of the ATPase activity of the molecular chaperones Hsp90 and Hsp72 using the TranscreenerTM ADP assay kit. J Biomol Screen. 2010 Mar;15(3):279-86.
  • Millson SH, Prodromou C, Piper PW. (2010). A simple yeast-based system for analyzing inhibitor resistance in the human cancer drug targets Hsp90alpha/beta. Biochem Pharmacol., 79(11):1581-8.
  • Prodromou, C. (2009). Strategies for stalling malignancy: targeting cancer's addiction to Hsp90. Curr Top Med Chem. 2009;9(15):1352-68.
  • Tsutsumi S, Mollapour M, Graf C, Lee CT, Scroggins BT, Xu W, Haslerova L, Hessling M, Konstantinova AA, Trepel JB, Panaretou B, Buchner J, Mayer MP, Prodromou C, Neckers L. (2009). Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain. Nat. Struct. Mol. Biol., 16(11), 1141-7.
  • Nilapwar S, Williams E, Fu C, Prodromou C, Pearl LH, Williams MA, Ladbury JE. (2009). Structural-thermodynamic relationships of interactions in the N-terminal ATP-binding domain of Hsp90. J Mol Biol., 392(4):923-36.
  • Prodromou C, Nuttall JM, Millson SH, Roe SM, Sim TS, Tan D, Workman P, Pearl LH, Piper PW. (2009). Structural basis of the radicicol resistance displayed by a fungal hsp90. ACS Chem Biol., 4(4):289-97.
  • Mayer MP, Prodromou C, Frydman J. (2009). The Hsp90 mosaic: a picture emerges. Nat. Struct. Mol. Biol., 16(1):2-6.
  • Vaughan CK, Piper PW, Pearl LH, Prodromou C. (2009). A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s. FEBS J., 276(1):199-209.
  • Vaughan CK, Mollapour M, Smith JR, Truman A, Hu B, Good VM, Panaretou B, Neckers L, Clarke PA, Workman P, Piper PW, Prodromou C, Pearl LH. (2008). Hsp90-dependent activation of protein kinases is regulated arril X, Borgognoni J, Boxall K, Cansfield JE, Cheung KM, Collins I, Davies NG, Drysdale MJ, Dymock B, Eccles SA, Finch H, Fink A, Hayes A, Howes R, Hubbard RE, James K, Jordan AM, Lockie A, Martins V, Massey A, Matthews TP, McDonald E, Northfield CJ, Pearl LH, Prodromou C, Ray S, Raynaud FI, Roughley SD, Sharp SY, Surgenor A, Walmsley DL, Webb P, Wood M, Workman P, Wright L. (2008). 4,5-Diarylisoxazole Hsp90 Chaperone Inhibitors: Potential Therapeutic Agents for the Treatment of Cancer, J Med Chem. 51(2), 196-218.
  • Savva R, Prodromou C, Driscoll PC. (2007). DNA fragmentation based combinatorial approaches to soluble protein expression Part II: library expression, screening and scale-up. Drug Discov Today, 12(21-22):939-47.
  • Prodromou C, Savva R, Driscoll PC. (2007). DNA fragmentation-based combinatorial approaches to soluble protein expression Part I. Generating DNA fragment libraries. Drug Discov Today, 12(21-22):931-8.
  • Sharp SY, Prodromou C, Boxall K, Powers MV, Holmes JL, Box G, Matthews TP, Cheung KM, Kalusa A, James K, Hayes A, Hardcastle A, Dymock B, Brough PA, Barril X, Cansfield JE, Wright L, Surgenor A, Foloppe N, Hubbard RE, Aherne W, Pearl L, Jones K, McDonald E, Raynaud F, Eccles S, Drysdale M, Workman P. (2007) nhibition of the heat shock protein 90 molecular chaperone in vitro and in vivo by novel, synthetic, potent resorcinylic pyrazole/isoxazole amide analogues. Mol Cancer Ther., 6, 1198-1211.
  • Truman AW, Millson SH, Nuttall JM, Mollapour M, Prodromou C and Piper PW (2007). In the yeast heat shock response Hsf1-directed induction of Hsp90 facilitates the activation of the Slt2(Mpk1) cell integrity MAP kinase. Eukaryot Cell., 6, 744-752.
  • Sharp SY, Boxall K, Rowlands M, Prodromou C, Roe SM, Maloney A, Powers M, Clarke PA, Box G, Sanderson S, Patterson L, Matthews TP, Cheung KM, Ball K, Hayes A, Raynaud F, Marais R, Pearl L, Eccles A, Aherne W, McDonald E and Workman P (2006). In vitro Biological Characterization of a Novel, Synthetic Diaryl Pyrazole Resorcinol Class of Heat Shock Protein 90 Inhibitors. Cancer Res. 2007 Mar 1;67(5):2206-16.
  • Poisy N, Sharp SY, Boxall K, Connelly S, Roe SM, Prodromou C, Slawin AM, Pearl LH, Workman P and Moody CJ (2006). Inhibition of Hsp90 with synthetic macrolactones: synthesis and structural and biological evaluation of ring and conformational analogs of radicicol. Chem Biol., 13, 1203-1215.
  • Reich S, Puckey LH, Cheetham CL, Harris R, Ali AA, Bhattacharyya U, Mclagan K, Powell KA, Prodromou C, Pearl LH, Driscoll PC and Savva R (2006). Combinatorial Domain Hunting: An effective approach for the identification of soluble protein domains adaptable to high-throughput applications. Protein Sci., 15, 2356-2365.
  • Truman AW, Millson SH, Nuttall JM, King V, Mollapour M, Prodromou C, Pearl LH and Piper PW (2006). Expressed in the yeast Saccharomyces cerevisiae, human ERK5 is a client of the Hsp90 chaperone that complements loss of the Slt2p (Mpk1p) cell integrity stress-activated protein kinase. Eukaryot Cell.,5, 1914-1924.
  • Vaughan CK, Gohlke U, Sobott F, Good VM, Ali MM, Prodromou C, Robinson CV, Saibil HR and Pearl LH (2006). Structure of an Hsp90-Cdc37-Cdk4 complex. Mol Cell, 23, 697-707.
  • Pearl L. H. and Prodromou C. (2006). Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem., 75, 271-294.
  • M. M. U. Ali, S. M. Roe, C. K. Vaughan, P. Meyer, B. Panaretou, P. W. Piper, C. Prodromou and L. H. Pearl (2006). Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone. Nature 440, 1013-1017.
  • M. Zhang, M. Windheim, S. M. Roe, M. Peggie, P. Cohen, C. Prodromou and L. H. Pearl (2005). Chaperoned ubiquitylation - Crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex. Mol. Cell, 20, 525-538.
  • Cheung KM, Matthews TP, James K, Rowlands MG, Boxall KJ, Sharp SY, Maloney A, Roe SM, Prodromou C, Pearl LH, Aherne GW, McDonald E, Workman P. (2005). The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors. Bioorg Med Chem Lett., 15(14):3338-43.
  • Millson SH, Truman AW, King V, Prodromou C, Pearl LH, Piper PW. (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(5):849-60.
  • Hu B, Liao C, Millson SH, Mollapour M, Prodromou C, Pearl LH, Piper PW, Panaretou B. (2005). Qri2/Nse4, a component of the essential Smc5/6 DNA repair complex. Mol Microbiol., 55(6):1735-50.
  • Millson SH, Truman AW, Wolfram F, King V, Panaretou B, Prodromou C, Pearl LH, Piper PW. (2004). Investigating the protein-protein interactions of the yeast Hsp90 chaperone system by two-hybrid analysis: potential uses and limitations of this approach. Cell Stress Chaperones, 9(4):359-68.
  • Siligardi G, Hu B, Panaretou B, Piper PW, Pearl LH, Prodromou C. (2004). Co-chaperone Regulation of Conformational Switching in the Hsp90 ATPase Cycle. J Biol Chem., 279(50):51989-51998.
  • Rowlands MG, Newbatt YM, Prodromou C, Pearl LH, Workman P, Aherne W. (2004). High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Anal Biochem., 327(2):176-83.
  • Meyer P, Prodromou C, Liao C, Hu B, Mark Roe S, Vaughan CK, Vlasic I, Panaretou B, Piper PW, Pearl LH. (2004). Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J., 23(3):511-9.
  • Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, Prodromou C, Pearl LH. (2004). The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37). Cell., 116(1):87-98.
  • Piper PW, Millson SH, Mollapour M, Panaretou B, Siligardi G, Pearl LH, Prodromou C (2003). Sensitivity to Hsp90-targeting drugs can arise with mutation to the Hsp90 chaperone, cochaperones and plasma membrane ATP binding cassette transporters of yeast. Eur. J. Biochem. 270, 4689-4695.
  • Prodromou C. and Pearl L. H. (2003). Structure and functional relationships of Hsp90. Curr. Cancer Drug Targets, 3, 301-323.
  • Aherne W, Maloney A, Prodromou C, Rowlands MG, Hardcastle A, Boxall K, Clarke P, Walton MI, Pearl L, Workman P. (2003). Assays for HSP90 and inhibitors. Methods Mol Med. 85:149-161.
  • Meyer P, Prodromou C, Hu B, Vaughan C, Roe SM, Panaretou B, Piper PW, Pearl LH. (2003). Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol Cell. 11(3), 647-58.
  • Piper PW, Panaretou B, Millson SH, Trumana A, Mollapour M, Pearl LH, Prodromou C. (2003). 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. Gene. 302(1-2), 165-170.
  • Davis B, Collier A, Dymock B, Finch H, Pearl L; Prodromou C, Surgenor A, Wood M, Workman P and Wright L. (2002). Approaches to structure-based drug discovery for the HSP-90 family [abstract]. Eur J Cancer 38: 336.
  • 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. (2002). Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol Cell. 10(6), 1307-1318.
  • Sale RM, William MA, Prodromou C, Pearl LH, Ladbury JE. (2002). Backbone resonance assignments of the 25kD N-terminal ATPase domain from the Hsp90 chaperone. J Biomol NMR. 23(4), 327-328.
  • Siligardi G, Panaretou B, Meyer P, Singh S, Woolfson DN, Piper PW, Pearl LH, Prodromou C. (2002). Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37. J Biol Chem. 277(23), 20151-20159.
  • Rowlands MG; Newbatt YM; Turlais F; Prodromou C; Pearl L; Workman P and Aherne W (2001). High throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Clin Cancer Res, 7: 475.
  • L. H. Pearl and C. Prodromou. (2001). Structure, function and mechanism of the Hsp90 molecular chaperone. Adv. Prot. Chem. 59, 157-186.
  • C. Prodromou, B. Panaretou, S. Chohan, G. Siligardi, R O'Brien, J.E Ladbury, S.M. Roe, PW. Piper and L.H. Pearl. (2000). EMBO J. 19, 4383-439.
  • L. H. Pearl and C. Prodromou. (2000). Structure and in vivo function of Hsp90. Curr. Opin. Struc Biol. 10, 46-51.
  • C. Prodromou, G. Siligardi, R. O'Brien, D. N. Woolfson, L. Regan, Barry Panaretou, J. E. Ladbury, P. W. Piper and L. H. Pearl. (1999). Regulation of Hsp90 ATPase activity by TPR-domain co-chaperones. EMBO J, 18, 754-762.
  • S.M. Roe , C. Prodromou, P.W. piper and L.H. Pearl. (1999). The structural basis for inhibition of the Hsp90 molecular chaperone by the anti-tumour antibiotics radicicol and geldanamycin. J. Med. Chem. 42, 260-266.
  • B. Panaretou, C. Prodromou, S.M. Roe , P.W. Piper and L.H. Pearl. (1998). ATP binding and hydrolysis are essential for the function of the Hsp90 molecular chaperone in vivo. EMBO J., 17, 4829-4836.
  • C. Prodromou, S.M. Roe, R. O'Brien, J.E. Ladbury, P.W. Piper and L.H. Pearl. (1997). Identification and structural characterisation of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell, 90, 65-75.
  • C. Prodromou, S.M. Roe, P.W. piper and L.H. Pearl. (1997). A molecular 'clamp' in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Nature structural Biology, 4 (6), 477482.
  • A. G. Headley, C. Prodromou and L. H. Pearl (1997). X-ray and enzymatic studies on mutant human lysozymes. Protein Engineering 10, 62.
  • C. Prodromou, P.W. piper and L.H. Pearl. (1996). Expression and crystallisation of the yeast Hsp82 chaperone, and preliminary X-ray diffraction studies of the amino-terminal domain. Proteins: Structure, Function, and Genetics, 25, 517-522.
  • V. Wheeler, C. Prodromou, L.H. Pearl, R. Williamson and C. Coutelle. (1996). Synthesis of a modified gene encoding human ornithine transcarbolyase for the expression in mammalian mitochondrial and universal translation systems - A novel approach towards correction of a genetic defect. Gene, 169 (2), 252-255.
  • C. Prodromou and L.H. Pearl, (1992). Recursive PCR: a novel technique for total gene synthesis. Protein Engineering, 5 (8), 827-829.
  • C. Prodromou, P.J. Artymuik and J.R. Guest, 1992). The aconitase of E. coli: Nucleotide sequence of the aconitase gene and amino acid similarity with mitochondrial aconitases, the iron-responsive-element binding protein and isopropylmalate isomerases. Eur. J. Biochem, 204, 599-609.
  • C. Prodromou, M.J. Haynes and J.R. Guest, (1991). The aconitase of E. coli: Purification of the enzyme and cloning and mapping of the gene. J. General Microbiology, 137, 2505-2515.
  • C. Prodromou, I.P. Wright, I.H. Evans and E.A. Bevan, (1991). Cloning of the HIS3 gene of Y. lipolytica. Antonie Van Leeuwenhoek, 60, 95-99.
  • J.R Guest, J. Green, S. Spiro, C. Prodromou and A.D. Sharrocks. Regulation of Gene Expression by Oxygen in E. coli. Eds G. Hauska and R. Thauer. In '41. Colloquium Mosbach 1990. The molecular basis of bacterial metabolism'. Springer-Verlag Berlin Heildelberg 1990.