Results 31 to 40 of about 138,190 (352)

Hsp90-binding immunophilins link p53 to dynein during p53 transport to the nucleus [PDF]

, 2004
The tumor suppressor protein p53 is known to be transported to the nucleus along microtubular tracks by cytoplasmic dynein. However, the connection between p53 and the dynein motor protein complex has not been established.
Galigniana, Mario Daniel, Harrell, Jennifer M., Ljungman, Mats, O´Hagen, Heather M., Pratt, William B.   +4 more
core   +1 more source

Heat Shock Protein 90 (Hsp90) Expression and Breast Cancer

Pharmaceuticals, 2012
Hsp90 is an abundant protein in mammalian cells. It forms several discrete complexes, each containing distinct groups of co-chaperones that assist protein folding and refolding during stress, protein transport and degradation. It interacts with a variety
Christos A. Papadimitriou, Konstantinos Koutsoukos, Evangelos Bournakis, Flora Zagouri   +3 more
doaj   +1 more source

In Vitro Inhibition of Hsp90 Protein by Benzothiazoloquinazolinequinones Is Enhanced in The Presence of Ascorbate. A Preliminary In Vivo Antiproliferative Study

Molecules, 2020
A series of benzo[g]benzothiazolo[2,3-b]quinazoline-7,12-quinones were prepared from 2-acylnaphthohydroquinones and 2-aminobenzothiazoles and were evaluated for their in vitro antiproliferative activity.
Jaime A. Valderrama, David Ríos, Giulio G. Muccioli, Pedro Buc Calderon, Julio Benites   +4 more
doaj   +1 more source

Hsp90‐mediated regulation of DYRK3 couples stress granule disassembly and growth via mTORC1 signaling

EMBO Reports, 2021
Stress granules (SGs) are dynamic condensates associated with protein misfolding diseases. They sequester stalled mRNAs and signaling factors, such as the mTORC1 subunit raptor, suggesting that SGs coordinate cell growth during and after stress. However,
L. Mediani, Francesco Antoniani, Veronica Galli, J. Vinet, A. Carrá, Ilaria Bigi, Vadreenath Tripathy, Tatiana Tiago, Marco Cimino, G. Leo, Triana Amen, D. Kaganovich, Cristina Cereda, O. Pansarasa, J. Mandrioli, P. Tripathi, D. Troost, E. Aronica, J. Buchner, A. Goswami, J. Sterneckert, S. Alberti, Serena Carra   +22 more
semanticscholar   +1 more source

Triple knockdown of CDC37, HSP90-alpha and HSP90-beta diminishes extracellular vesicles-driven malignancy events and macrophage M2 polarization in oral cancer

Journal of Extracellular Vesicles, 2020
Evidence has been accumulating to indicate that extracellular vesicles (EVs), including exosomes, released by cancer cells can foster tumour progression.
Kisho Ono, Chiharu Sogawa, Hotaka Kawai, Manh Tien Tran, Eman A. Taha, Yanyin Lu, May Wathone Oo, Yuka Okusha, Hirohiko Okamura, Soichiro Ibaragi, Masaharu Takigawa, Ken-Ichi Kozaki, Hitoshi Nagatsuka, Akira Sasaki, Kuniaki Okamoto, Stuart K. Calderwood, Takanori Eguchi   +16 more
doaj   +1 more source

The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease

International Journal of Molecular Sciences, 2018
The mammalian HSP90 family of proteins is a cluster of highly conserved molecules that are involved in myriad cellular processes. Their distribution in various cellular compartments underlines their essential roles in cellular homeostasis.
Abdullah Hoter, M. El-Sabban, H. Naim
semanticscholar   +1 more source

Post-translational modifications of Hsp90 and translating the chaperone code

Journal of Biological Chemistry, 2020
Cells have a remarkable ability to synthesize large amounts of protein in a very short period of time. Under these conditions, many hydrophobic surfaces on proteins may be transiently exposed, and the likelihood of deleterious interactions is quite high.
Sarah J Backe, Rebecca A. Sager, Mark R. Woodford, A. Makedon, M. Mollapour   +4 more
semanticscholar   +1 more source

The Development of Hsp90β-Selective Inhibitors to Overcome Detriments Associated with pan-Hsp90 Inhibition.

Journal of Medicinal Chemistry, 2021
The 90 kD heat shock proteins (Hsp90) are molecular chaperones that are responsible for the folding of select proteins, many of which are directly associated with cancer progression. Consequently, inhibition of the Hsp90 protein folding machinery results
Sanket J. Mishra, Weiya Liu, K. Beebe, Monimoy Banerjee, C. Kent, Vitumbiko Munthali, J. Koren, John A. Taylor, L. Neckers, J. Holzbeierlein, B. Blagg   +10 more
semanticscholar   +1 more source

Assay strategies for the discovery and validation of therapeutics targeting Brugia pahangi Hsp90 [PDF]

, 2010
The chemotherapy of lymphatic filariasis relies upon drugs such as diethylcarbamazine and ivermectin that largely target the microfilarial stages of the parasite, necessitating continued treatment over the long reproductive life span of the adult worm ...
A Hoerauf, A Kamal, A Rodina, AA Sayed, Anna Rodina, BA Sheehy, C Bourguinat, C Gloeckner, CL David, D Addiss, DF Cully, DH Molyneux, E Caldas-Lopes, E Devaney, E Ghedin, Eileen Devaney, F Aguero, G Chiosis, Gabriela Chiosis, H He, JA Dent, JA Frearson, JA Frearson, JE Day, JH Zhang, K Moulick, Kerry O'Neill, Kirsty Maitland, L Neckers, L Neckers, L Timmons, LE Cowen, M Peroval, M Vilenchik, Matty Knight, N Kato, NA Him, P Workman, Pallav Patel, PJ Hotez, PW Piper, R Kumar, RE Howells, RI Hewitt, RK Allan, S Kumar, S Nwaka, SN Chen, SN Shelton, T Stiernagle, T Supali, T Taldone, T Taldone, T Taldone, TG Geary, Tony Taldone, V Gillan, Victoria Gillan, W Grant, W Luo, Weilin Sun, Y Du   +61 more
core   +3 more sources

Detecting HSP90 Phosphorylation [PDF]

, 2011
Heat-shock protein 90 (HSP90) is an essential molecular chaperone in eukaryotes. It is important for chaperoning proteins that are important determinants of multistep carcinogenesis. HSP90's ATPase activity is associated with its chaperone function.
Mehdi, Mollapour, Len, Neckers
openaire   +2 more sources