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Hsp90 inhibition differentially destabilises MAP kinase and TGF-beta signalling components in cancer cells revealed by kinase-targeted chemoproteomics.

Haupt A, Joberty G, Bantscheff M, Fröhlich H, Stehr H, Schweiger MR, Fischer A, Kerick M, Boerno ST, Dahl A, Lappe M, Lehrach H, Gonzalez C, Drewes G, Lange BM.

BMC Cancer. 2012 Jan 25;12:38. doi: 10.1186/1471-2407-12-38.


Heat shock protein 90 (Hsp90) regulates the stability of transforming growth factor beta-activated kinase 1 (TAK1) in interleukin-1beta-induced cell signaling.

Shi L, Zhang Z, Fang S, Xu J, Liu J, Shen J, Fang F, Luo L, Yin Z.

Mol Immunol. 2009 Feb;46(4):541-50. doi: 10.1016/j.molimm.2008.07.019.


Heat shock protein 90 maintains the tumour-like character of rheumatoid synovial cells by stabilizing integrin-linked kinase, extracellular signal-regulated kinase and protein kinase B.

Hashiramoto A, Murata M, Kawazoe T, Yoshida K, Akiyama C, Shiozawa K, Shiozawa S.

Rheumatology (Oxford). 2011 May;50(5):852-61. doi: 10.1093/rheumatology/keq385.


Heat shock protein 90 (Hsp90) inhibition targets canonical TGF-β signalling to prevent fibrosis.

Tomcik M, Zerr P, Pitkowski J, Palumbo-Zerr K, Avouac J, Distler O, Becvar R, Senolt L, Schett G, Distler JH.

Ann Rheum Dis. 2014 Jun;73(6):1215-22. doi: 10.1136/annrheumdis-2012-203095.


Inhibition of heat shock protein 90 impairs epidermal growth factor-mediated signaling in gastric cancer cells and reduces tumor growth and vascularization in vivo.

Lang SA, Klein D, Moser C, Gaumann A, Glockzin G, Dahlke MH, Dietmaier W, Bolder U, Schlitt HJ, Geissler EK, Stoeltzing O.

Mol Cancer Ther. 2007 Mar;6(3):1123-32.


Distinct regulation of insulin receptor substrate-1 and -2 by 90-kDa heat-shock protein in adrenal chromaffin cells.

Yoshikawa N, Nemoto T, Satoh S, Maruta T, Yanagita T, Chosa E, Wada A.

Neurochem Int. 2010 Jan;56(1):42-50. doi: 10.1016/j.neuint.2009.08.013.


Hsp90 inhibition transiently activates Src kinase and promotes Src-dependent Akt and Erk activation.

Koga F, Xu W, Karpova TS, McNally JG, Baron R, Neckers L.

Proc Natl Acad Sci U S A. 2006 Jul 25;103(30):11318-22.


Heat shock protein 90 inhibition is cytotoxic to primary AML cells expressing mutant FLT3 and results in altered downstream signalling.

Al Shaer L, Walsby E, Gilkes A, Tonks A, Walsh V, Mills K, Burnett A, Rowntree C.

Br J Haematol. 2008 May;141(4):483-93. doi: 10.1111/j.1365-2141.2008.07053.x.


Drug-mediated targeted disruption of multiple protein activities through functional inhibition of the Hsp90 chaperone complex.

Stravopodis DJ, Margaritis LH, Voutsinas GE.

Curr Med Chem. 2007;14(29):3122-38. Review.


Proteome-wide changes induced by the Hsp90 inhibitor, geldanamycin in anaplastic large cell lymphoma cells.

Schumacher JA, Crockett DK, Elenitoba-Johnson KS, Lim MS.

Proteomics. 2007 Aug;7(15):2603-16.


Heat shock protein 90 is a promising target for effective growth inhibition of gastrointestinal neuroendocrine tumors.

Gloesenkamp C, Nitzsche B, Lim AR, Normant E, Vosburgh E, Schrader M, Ocker M, Scherübl H, Höpfner M.

Int J Oncol. 2012 May;40(5):1659-67. doi: 10.3892/ijo.2012.1328.


Heat shock protein 90-sheltered overexpression of insulin-like growth factor 1 receptor contributes to malignancy of thymic epithelial tumors.

Breinig M, Mayer P, Harjung A, Goeppert B, Malz M, Penzel R, Neumann O, Hartmann A, Dienemann H, Giaccone G, Schirmacher P, Kern MA, Chiosis G, Rieker RJ.

Clin Cancer Res. 2011 Apr 15;17(8):2237-49. doi: 10.1158/1078-0432.CCR-10-1689.


Inhibition of RPE cell sterile inflammatory responses and endotoxin-induced uveitis by a cell-impermeable HSP90 inhibitor.

Qin S, Ni M, Wang X, Maurier-Mahé F, Shurland DL, Rodrigues GA.

Exp Eye Res. 2011 Dec;93(6):889-97. doi: 10.1016/j.exer.2011.10.002.


The Hsp90-specific inhibitor geldanamycin selectively disrupts kinase-mediated signaling events of T-lymphocyte activation.

Schnaider T, Somogyi J, Csermely P, Szamel M.

Cell Stress Chaperones. 2000 Jan;5(1):52-61.


Molecular signature of response and potential pathways related to resistance to the HSP90 inhibitor, 17AAG, in breast cancer.

Zajac M, Gomez G, Benitez J, Martínez-Delgado B.

BMC Med Genomics. 2010 Oct 4;3:44. doi: 10.1186/1755-8794-3-44.


High-content, high-throughput analysis of cell cycle perturbations induced by the HSP90 inhibitor XL888.

Lyman SK, Crawley SC, Gong R, Adamkewicz JI, McGrath G, Chew JY, Choi J, Holst CR, Goon LH, Detmer SA, Vaclavikova J, Gerritsen ME, Blake RA.

PLoS One. 2011 Mar 7;6(3):e17692. doi: 10.1371/journal.pone.0017692. Erratum in: PLoS One. 2011;6(3). doi: 10.1371/annotation/73d83e95-8f14-48ed-bb67-2310a33e4ecc.


Efficacy of Hsp90 inhibition for induction of apoptosis and inhibition of growth in cervical carcinoma cells in vitro and in vivo.

Schwock J, Pham NA, Cao MP, Hedley DW.

Cancer Chemother Pharmacol. 2008 Apr;61(4):669-81.


HSP90 inhibitors induce desensitization of EGF receptor via p38 MAPK-mediated phosphorylation at Ser1046/1047 in human pancreatic cancer cells.

Adachi S, Yasuda I, Nakashima M, Yamauchi T, Yamauchi J, Natsume H, Moriwaki H, Kozawa O.

Oncol Rep. 2010 Jun;23(6):1709-14.

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