نتایج جستجو برای: جهش hsp27

تعداد نتایج: 4533  

2017
Chin-Sheng Hung Chien-Yu Huang Chia-Hwa Lee Wei-Yu Chen Ming-Te Huang Po-Li Wei Yu-Jia Chang

Heat shock protein 27 (Hsp27) is a key chaperone that interacts with over 200 client proteins. The expression of Hsp27 might be correlated with poor outcome in many types of cancer. Previous study indicated that Hsp27 might be an important biomarker in hepatocellular carcinoma (HCC). However, the detailed mechanism is less well understood. The shRNA-mediated silencing of Hsp27 decreased the pro...

Journal: :Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology 1998
M A Fanelli F D Cuello Carrión J Dekker J Schoemaker D R Ciocca

Heat shock protein Mr 27,000 (hsp27) is found in many human breast cancer cells and tissues; its expression is associated with the presence of estrogen receptors, lower cell proliferation, and resistance to certain chemotherapies. The purpose of this study was to assess whether hsp27 may be present in sera from women with primary breast cancer and to know whether autoantibodies to hsp27 may be ...

Journal: :Cancer research 2004
Palma Rocchi Alan So Satoko Kojima Maxim Signaevsky Eliana Beraldi Ladan Fazli Antonio Hurtado-Coll Kazuki Yamanaka Martin Gleave

Heat shock protein 27 (Hsp27) is a chaperone implicated as an independent predictor of clinical outcome in prostate cancer. Our aim was to characterize changes in Hsp27 after androgen withdrawal and during androgen-independent progression in prostate xenografts and human prostate cancer to assess the functional significance of these changes using antisense inhibition of Hsp27. A tissue microarr...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2012
Oddbjørn Straume Takeshi Shimamura Michael J G Lampa Julian Carretero Anne M Øyan Di Jia Christa L Borgman Margaret Soucheray Sean R Downing Sarah M Short Soo-Young Kang Souming Wang Liang Chen Karin Collett Ingeborg Bachmann Kwok-Kin Wong Geoffrey I Shapiro Karl Henning Kalland Judah Folkman Randolph S Watnick Lars A Akslen George N Naumov

The mechanisms underlying tumor dormancy have been elusive and not well characterized. We recently published an experimental model for the study of human tumor dormancy and the role of angiogenesis, and reported that the angiogenic switch was preceded by a local increase in VEGF-A and basic fibroblast growth factor. In this breast cancer xenograft model (MDA-MB-436 cells), analysis of different...

Journal: :The American journal of physiology 1997
Janice K Larsen Ilia A Yamboliev Lee A Weber William T Gerthoffer

The 27-kDa heat shock protein (HSP27) is expressed in a variety of tissues in the absence of stress and is thought to regulate actin filament dynamics, possibly by a phosphorylation/dephosphorylation mechanism. HSP27 has also been suggested to be involved in contraction of intestinal smooth muscle. We have investigated phosphorylation of HSP27 in airway smooth muscle in response to the muscarin...

Journal: :Journal of B.U.ON. : official journal of the Balkan Union of Oncology 2013
D M Marinova Y G Slavova N Trifonova D Kostadinov V Maksimov D Petrov

PURPOSE Heat shock protein (Hsp)27 is overexpressed in a range of human cancers and is implicated in tumor cell proliferation, differentiation, invasion, metastasis, and survival. The aim of the present study was to determine the prognostic significance of Hsp27 expression in small cell lung carcinoma (SCLC) and large cell neuroendocrine carcinoma (LCNEC). METHODS Surgically resected SCLCs (N...

Journal: :dental research journal 0
parviz deyhimi faezeh azmoudeh

background: heat shock proteins (hsps) are a family of proteins that are known to play a significant role in the repair of denatured proteins in the cell. it seems that cytoprotective properties of hsps may help in malignant progression by facilitating tumor cell growth and survival. the purpose of this study is to evaluate hsp27 and hsp70 expression in various histopathological grades of squam...

Journal: :Molecular and cellular biology 1995
J N Lavoie H Lambert E Hickey L A Weber J Landry

Phosphorylation of heat shock protein 27 (HSP27) can modulate actin filament dynamics in response to growth factors. During heat shock, HSP27 is phosphorylated at the same sites and by the same protein kinase as during mitogenic stimulation. This suggests that the same function of the protein may be activated during growth factor stimulation and the stress response. To determine the role of HSP...

Journal: :The Journal of neuroscience : the official journal of the Society for Neuroscience 2008
R Anne Stetler Guodong Cao Yanqin Gao Feng Zhang Suping Wang Zhongfang Weng Peter Vosler Lili Zhang Armando Signore Steven H Graham Jun Chen

Heat shock protein 27 (Hsp27), a recently discovered member of the heat shock protein family, is markedly induced in the brain after cerebral ischemia and other injury states. In non-neuronal systems, Hsp27 has potent cell death-suppressing functions. However, the mechanism of Hsp27-mediated neuroprotection has not yet been elucidated. Using transgenic and viral overexpression of Hsp27, we inve...

Journal: :Cancer research 2006
Andrea K McCollum Cynthia J Teneyck Brian M Sauer David O Toft Charles Erlichman

17-Allylamino-demethoxygeldanamycin (17-AAG), currently in phase I and II clinical trials as an anticancer agent, binds to the ATP pocket of heat shock protein (Hsp90). This binding induces a cellular stress response that up-regulates many proteins including Hsp27, a member of the small heat shock protein family that has cytoprotective roles, including chaperoning of cellular proteins, regulati...

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