Results 51 to 60 of about 132,845 (313)

Hsp90: From Cellular to Organismal Proteostasis

Cells, 2022
Assuring a healthy proteome is indispensable for survival and organismal health. Proteome disbalance and the loss of the proteostasis buffer are hallmarks of various diseases.
Milán Somogyvári, Saba Khatatneh, Csaba Sőti   +2 more
doaj   +1 more source

The Role of Heat Shock Proteins in Regulating Receptor Signal Transduction

Molecular Pharmacology, 2019
Heat shock proteins (Hsp) are a class of stress-inducible proteins that mainly act as molecular protein chaperones. This chaperone activity is diverse, including assisting in nascent protein folding and regulating client protein location and ...
J. Streicher
semanticscholar   +1 more source

A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity. [PDF]

, 2014
Hsp90 is a conserved chaperone that facilitates protein homeostasis. Our crystal structure of the mitochondrial Hsp90, TRAP1, revealed an extension of the N-terminal β-strand previously shown to cross between protomers in the closed state. In this study,
Agard, David A, Cooke, Roger, Elnatan, Daniel, Lavery, Laura A, Naber, Nariman, Partridge, James R   +5 more
core   +2 more sources

Cell Stress Induced Stressome Release Including Damaged Membrane Vesicles and Extracellular HSP90 by Prostate Cancer Cells

Cells, 2020
Tumor cells exhibit therapeutic stress resistance-associated secretory phenotype involving extracellular vesicles (EVs) such as oncosomes and heat shock proteins (HSPs). Such a secretory phenotype occurs in response to cell stress and cancer therapeutics.
Takanori Eguchi, Chiharu Sogawa, Kisho Ono, Masaki Matsumoto, Manh Tien Tran, Yuka Okusha, Benjamin J. Lang, Kuniaki Okamoto, Stuart K. Calderwood   +8 more
doaj   +1 more source

Targeting GRP75 improves HSP90 inhibitor efficacy by enhancing p53-mediated apoptosis in hepatocellular carcinoma. [PDF]

PLoS ONE, 2014
Heat shock protein 90 (HSP90) inhibitors are potential drugs for cancer therapy. The inhibition of HSP90 on cancer cell growth largely through degrading client proteins, like Akt and p53, therefore, triggering cancer cell apoptosis.
Weiwei Guo, Lichong Yan, Ling Yang, Xiaoyu Liu, Qiukai E, Peiye Gao, Xiaofei Ye, Wen Liu, Ji Zuo   +8 more
doaj   +1 more source

Regulation of CLC-1 chloride channel biosynthesis by FKBP8 and Hsp90β. [PDF]

, 2016
Mutations in human CLC-1 chloride channel are associated with the skeletal muscle disorder myotonia congenita. The disease-causing mutant A531V manifests enhanced proteasomal degradation of CLC-1.
Chen, Shu-Ching, Chen, Tsung-Yu, Hsieh, Hsin-Ying, Huang, Jing-Jia, Peng, Yi-Jheng, Tang, Chih-Yung, Wu, Chia-Ying, Wu, Hao-Han   +7 more
core   +1 more source

Heat Shock Proteins in Alzheimer’s Disease: Role and Targeting

International Journal of Molecular Sciences, 2018
Among diseases whose cure is still far from being discovered, Alzheimer’s disease (AD) has been recognized as a crucial medical and social problem. A major issue in AD research is represented by the complexity of involved biochemical pathways, including ...
C. Campanella, A. Pace, Celeste Caruso Bavisotto, Paola Marzullo, A. Marino Gammazza, S. Buscemi, Antonio Palumbo Piccionello   +6 more
semanticscholar   +1 more source

Heat-Shock Protein 90 Controls the Expression of Cell-Cycle Genes by Stabilizing Metazoan-Specific Host-Cell Factor HCFC1

Cell Reports, 2019
Summary: Molecular chaperones such as heat-shock proteins (HSPs) help in protein folding. Their function in the cytosol has been well studied. Notably, chaperones are also present in the nucleus, a compartment where proteins enter after completing de ...
Aneliya Antonova, Barbara Hummel, Ashkan Khavaran, Desiree M. Redhaber, Fernando Aprile-Garcia, Prashant Rawat, Kathrin Gundel, Megan Schneck, Erik C. Hansen, Jan Mitschke, Gerhard Mittler, Cornelius Miething, Ritwick Sawarkar   +12 more
doaj   +1 more source

Heat Shock Proteins in Cancer Immunotherapy

Journal of Oncology, 2019
Heat shock proteins (HSPs) are highly conserved molecular chaperones with divergent roles in various cellular processes. The HSPs are classified according to their molecular size as HSP27, HSP40, HSP60, HSP70, and HSP90.
J. Das, Xiaofang Xiong, X. Ren, Jin-Ming Yang, Jianxun Song   +4 more
semanticscholar   +1 more source

Geldanamycin and its derivatives as Hsp90 inhibitors [PDF]

, 2012
The Hsp90 molecule, one of the most abundant heat shock proteins in mammalian cells, maintains homeostasis and prevents stress-induced cellular damage.
BUCCHIERI, Fabio, CICERO, Giuseppe, Gorska, M., Knap, N., Kuban Jankowska, A., Popowska, U., Sawczuk, W., Sielicka Dudzin, A., Wozniak, F.   +8 more
core   +1 more source