Results 31 to 40 of about 3,736 (194)

Physical Interaction of Mammalian CDC37 with CDK4 [PDF]

Journal of Biological Chemistry, 1996
CDC37 was originally identified as a Start gene in budding yeast and has been shown to be required for association of CDC28 with cyclins. The exact functional mechanism by which CDC37 promotes this association, however, remains unknown. CDK4 is a cyclin D-dependent kinase that controls progression through G1 of the mammalian cell cycle.
K, Dai, R, Kobayashi, D, Beach
openaire   +2 more sources

Hsp90 modulates human sperm capacitation via the Erk1/2 and p38 MAPK signaling pathways

Reproductive Biology and Endocrinology, 2021
Background Heat shock protein 90 (Hsp90) is a highly abundant eukaryotic molecular chaperone that plays important roles in client protein maturation, protein folding and degradation, and signal transduction.
Peibei Sun, Yayan Wang, Tian Gao, Kun Li, Dongwang Zheng, Ajuan Liu, Ya Ni   +6 more
doaj   +1 more source

Rational design, synthesis and structural characterization of peptides and peptidomimetics to target Hsp90/Cdc37 interaction for treating hepatocellular carcinoma

Computational and Structural Biotechnology Journal, 2023
Heat shock protein 90 (Hsp90) and cell division cycle 37 (Cdc37) work together as a molecular chaperone complex to regulate the activity of a multitude of client protein kinases.
Surya Sukumaran, Mingdian Tan, Shulamit Fluss Ben-Uliel, Hui Zhang, Marta De Zotti, Mei-Sze Chua, Samuel K. So, Nir Qvit   +7 more
doaj   +1 more source

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

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

Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains. [PDF]

PLoS ONE, 2017
A fundamental role of the Hsp90 and Cdc37 chaperones in mediating conformational development and activation of diverse protein kinase clients is essential in signal transduction. There has been increasing evidence that the Hsp90-Cdc37 system executes its
Josh Czemeres, Kurt Buse, Gennady M Verkhivker   +2 more
doaj   +1 more source

Elaiophylin Is a Potent Hsp90/ Cdc37 Protein Interface Inhibitor with K-Ras Nanocluster Selectivity

Biomolecules, 2021
The natural product elaiophylin is a macrodiolide with a broad range of biological activities. However, no direct target of elaiophylin in eukaryotes has been described so far, which hinders a systematic explanation of its astonishing activity range.
Farid A. Siddiqui, Vladimir Vukic, Tiina A. Salminen, Daniel Abankwa   +3 more
doaj   +1 more source

Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery

Journal of Hematology & Oncology, 2018
Heat shock protein 90 (Hsp90) is a critical molecular chaperone protein that regulates the folding, maturation, and stability of a wide variety of proteins.
Ting Li, Hu-Lin Jiang, Yun-Guang Tong, Jin-Jian Lu   +3 more
doaj   +1 more source

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

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