نتایج جستجو برای: hsp90 alpha

تعداد نتایج: 207548  

Journal: :journal of paramedical sciences 0
zarin sharifnia biothecnology department, school of medicine, tabriz university of medical sciences, tabriz nariman mosaffa immunology department, school of medicine, shahid beheshti university of medical sciences, tehran mahvash khodabandeh national institute of genetics engineering for biological researches, tehran roya yaraee immunology department, shahed university, tehran bahram kazemi cellular & molecular research center, school of medicine, shahid beheshti university of medical sciences, tehran mojgan bandehpour cellular & molecular research center, school of medicine, shahid beheshti university of medical sciences, tehran

there are more than 350 million individuals with hepatitis c in the world. one of the important problems in vaccine project is development of effective and suitable adjuvant in human vaccines. at present research we applied human βhsp90 protein as an adjuvant in recombinant hcv vaccine design. the thermal vector of pgp1-2 was used for human heat shock protein 90 expression. this protein injecte...

2013
Jiahong Wang Shuzhong Cui Xiangliang Zhang Yinbing Wu Hongsheng Tang

The heat shock protein 90 (HSP90) is overexpressed and highly associated with poor prognosis in many malignancies. However, the role of HSP90 in gastric cancer has not been thoroughly elucidated. The aim of this study is to investigate the relationship of HSP90 expression with clinicopathological parameters and prognosis in advanced gastric cancer, and estimate the alteration of HSP90 expressio...

Journal: :Molecular and biochemical parasitology 2009
Diana Wider Marie-Pierre Péli-Gulli Pierre-André Briand Utpal Tatu Didier Picard

Developing novel drugs against the unicellular parasite Plasmodium is complicated by the paucity of simple screening systems. Heat-shock proteins are an essential class of proteins for the parasite's cyclical life style between different cellular milieus and temperatures. The molecular chaperone Hsp90 assists a large variety of proteins, but its supporting functions for many proteins that are i...

2016
Agnieszka Góral Paweł Bieganowski Wiktor Prus Łucja Krzemień-Ojak Beata Kądziołka Hanna Fabczak Anna Filipek

The Hsp90 chaperone activity is tightly regulated by interaction with many co-chaperones. Since CacyBP/SIP shares some sequence homology with a known Hsp90 co-chaperone, Sgt1, in this work we performed a set of experiments in order to verify whether CacyBP/SIP can interact with Hsp90. By applying the immunoprecipitation assay we have found that CacyBP/SIP binds to Hsp90 and that the middle (M) ...

Journal: :Journal of visualized experiments : JoVE 2011
Patrick J M Murphy Hannah R Franklin Nathan W Furukawa

Hsp90 is an essential and highly abundant molecular chaperone protein that has been found to regulate more than 150 eukaryotic signaling proteins, including transcription factors (e.g. nuclear receptors, p53) and protein kinases (e.g. Src, Raf, Akt kinase) involved in cell cycling, tumorigenesis, apoptosis, and multiple eukaryotic signaling pathways (1,2). Of these many 'client' proteins for hs...

Journal: :The Journal of biological chemistry 1992
Y Miyata I Yahara

We found that a preparation of the 90-kDa heat shock protein, HSP90, purified to apparent homogeneity, contains a serine/threonine kinase which phosphorylates HSP90. The protein kinase was identified as casein kinase II (CKII) according to its properties. The protein kinase was separable from HSP90 by adsorption to heparin-Sepharose or phosphocellulose. CKII was coimmunoprecipitated with HSP90 ...

2015
Thomas L. Prince Toshiki Kijima Manabu Tatokoro Sunmin Lee Shinji Tsutsumi Kendrick Yim Candy Rivas Sylvia Alarcon Harvey Schwartz Kofi Khamit-Kush Bradley T. Scroggins Kristin Beebe Jane B. Trepel Len Neckers Jeffrey L Brodsky

The two cytosolic/nuclear isoforms of the molecular chaperone HSP90, stress-inducible HSP90α and constitutively expressed HSP90β, fold, assemble and maintain the three-dimensional structure of numerous client proteins. Because many HSP90 clients are important in cancer, several HSP90 inhibitors have been evaluated in the clinic. However, little is known concerning possible unique isoform or con...

2015
Stephanie Diezmann Michelle D. Leach Leah E. Cowen Robert Alan Arkowitz

Candida albicans is among the most prevalent opportunistic fungal pathogens. Its capacity to cause life-threatening bloodstream infections is associated with the ability to form biofilms, which are intrinsically drug resistant reservoirs for dispersal. A key regulator of biofilm drug resistance and dispersal is the molecular chaperone Hsp90, which stabilizes many signal transducers. We previous...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1999
K I Kang X Meng J Devin-Leclerc I Bouhouche A Chadli F Cadepond E E Baulieu M G Catelli

Hsp90, a molecular chaperone required for the functioning of glucocorticosteroid receptor (GR), ensures, by direct interaction, the conformational competence of the steroid-binding pocket. In addition to having this positive function, Hsp90 maintains steroid receptors in an inactive form in the absence of hormone. However, neither the participation of Hsp90 once the pathway has been activated b...

Journal: :Molecular cell 2010
Mehdi Mollapour Shinji Tsutsumi Alison C Donnelly Kristin Beebe Mari J Tokita Min-Jung Lee Sunmin Lee Giulia Morra Dimitra Bourboulia Bradley T Scroggins Giorgio Colombo Brian S Blagg Barry Panaretou William G Stetler-Stevenson Jane B Trepel Peter W Piper Chrisostomos Prodromou Laurence H Pearl Len Neckers

Saccharomyces WEE1 (Swe1), the only "true" tyrosine kinase in budding yeast, is an Hsp90 client protein. Here we show that Swe1(Wee1) phosphorylates a conserved tyrosine residue (Y24 in yeast Hsp90 and Y38 in human Hsp90alpha) in the N domain of Hsp90. Phosphorylation is cell-cycle associated and modulates the ability of Hsp90 to chaperone a selected clientele, including v-Src and several other...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید