Results 41 to 50 of about 6,022 (190)

Targeting the oncogene and kinome chaperone CDC37 [PDF]

Nature Reviews Cancer, 2008
CDC37 is a molecular chaperone that physically stabilizes the catalytic domains found in protein kinases and is therefore a wide-spectrum regulator of protein phosphorylation. It is also an overexpressed oncoprotein that mediates carcinogenesis by stabilizing the compromised structures of mutant and/or overexpressed oncogenic kinases. Recent work shows
Phillip J, Gray, Thomas, Prince, Jinrong, Cheng, Mary Ann, Stevenson, Stuart K, Calderwood   +4 more
openaire   +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

Cdc37 goes beyond Hsp90 and kinases

Cell Stress & Chaperones, 2003
Cdc37 is a relatively poorly conserved and yet essential molecular chaperone. It has long been thought to function primarily as an accessory factor for Hsp90, notably directing Hsp90 to kinases as substrates. More recent discoveries challenge this simplistic view.
MacLean, Morag, Picard, Didier
openaire   +4 more sources

Structural Bioinformatics and Protein Docking Analysis of the Molecular Chaperone-Kinase Interactions: Towards Allosteric Inhibition of Protein Kinases by Targeting the Hsp90-Cdc37 Chaperone Machinery

Pharmaceuticals, 2013
A fundamental role of the Hsp90-Cdc37 chaperone system in mediating maturation of protein kinase clients and supporting kinase functional activity is essential for the integrity and viability of signaling pathways involved in cell cycle control and ...
Gennady Verkhivker, Elizabeth Berrigan, Nathan Lawless, Kristin Blacklock   +3 more
doaj   +1 more source

Role and Regulation of Myeloid Zinc Finger Protein 1 in Cancer [PDF]

, 2015
Myeloid zinc finger 1 (MZF1) belongs to the SCAN-Zinc Finger (SCAN-ZF) transcription factor family that has recently been implicated in a number of types of cancer.
Anders, Asiedu, Bernardi, Bettermann, Briers, Bunch, Calderwood, Cappadocia, Cerami, Chang, Chen, Cheng, Dellaire, Deng, Derynck, Driver, Edelstein, Euskirchen, Fujii, Gaboli, Gao, Gray, Heun, Hromas, Hromas, Hromas, Hsieh, Huang, Hudson, Inoue, Iyengar, Jensen, Massague, Mudduluru, Murai, Noll, Ogawa, Ogawa, Perrotti, Peterson, Rafn, Raman, Redon, Reymann, Sander, Sander, Sironen, Stepanova, Stielow, Subramonian, Takahashi, Tanaka, Tsai, Tsai, Uhlen, Uhlen, Van Damme, Weber, Williams   +58 more
core   +1 more source

Mapping differential interactomes by affinity purification coupled with data independent mass spectrometry acquisition [PDF]

, 2013
Characterizing changes in protein-protein interactions associated with sequence variants (e.g. disease-associated mutations or splice forms) or following exposure to drugs, growth factors or hormones is critical to understanding how protein complexes are
AC Gingras, AC Gingras, AC Gingras, Amber L Couzens, Anne-Claude Gingras, B Schuster-Böckler, BM Bolstad, Brett Larsen, C Jeronimo, C Prodromou, D Mellacheruvu, DL Tabb, G Liu, GL Andrews, Gordana Ivosev, HS Yang, IV Shilov, JD Venable, JE Delmore, Jean-Philippe Lambert, KG Coleman, L Reiter, L Zuo, LC Gillet, M Barrios-Rodiles, M Serrano, M Taipale, M Taipale, Marc Vidal, Mikko Taipale, MJ Kean, N Bisson, OM Grbovic, P Lahiry, P Picotti, PA Brough, Q Zhong, Quan Zhong, RE Steward, Ron Bonner, Ruedi Aebersold, S da Rocha Dias, S Luke-Glaser, S Tate, Stephen Tate, Susan Lindquist, T Ideker, T Shimamura, T Wölfel, TA Addona, Tony Pawson, V Vacic, WH Dunham, Y Liu, Y Zheng, Zhen-Yuan Lin   +55 more
core   +5 more sources

How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches [PDF]

Trends in Biochemical Sciences, 2017
The Hsp90/Cdc37 chaperone system interacts with and supports 60% of the human kinome. Not only are Hsp90 and Cdc37 generally required for initial folding, but many kinases rely on the Hsp90/Cdc37 throughout their lifetimes. A large fraction of these 'client' kinases are key oncoproteins, and their interactions with the Hsp90/Cdc37 machinery are crucial
Verba, Kliment A, Agard, David A
openaire   +4 more sources

A Thermodynamic-Based Interpretation of Protein Expression Heterogeneity in Different Glioblastoma Multiforme Tumors Identifies Tumor-Specific Unbalanced Processes [PDF]

, 2016
We describe a thermodynamic-motivated, information theoretic analysis of proteomic data collected from a series of 8 glioblastoma multiforme (GBM) tumors. GBMs are considered here as prototypes of heterogeneous cancers.
Heath, James R., Johnson, Hannah, Kravchenko-Balasha, Nataly, Levine, R. D., White, Forest M.   +4 more
core   +3 more sources

Cdc37 and protein kinase folding

RSC Advances, 2007
Cdc37 is a molecular chaperone that collaborates with Hsp90 to fold protein kinases and other clients including transcription factors. Cdc37 function in protein kinase folding is dependent on direct interaction between the chaperone and the N-lobe of the kinase catalytic domain.
Robert Matts, Avrom J. Caplan
openaire   +2 more sources

HSP-90/kinase complexes are stabilized by the large PPIase FKB-6

Scientific Reports, 2021
Protein kinases are important regulators in cellular signal transduction. As one major type of Hsp90 client, protein kinases rely on the ATP-dependent molecular chaperone Hsp90, which maintains their structure and supports their activation.
Siyuan Sima, Katalin Barkovits, Katrin Marcus, Lukas Schmauder, Stephan M. Hacker, Nils Hellwig, Nina Morgner, Klaus Richter   +7 more
doaj   +1 more source