Results 1 to 10 of about 844,423 (151)

Cell division cycle 37 change after bortezomib-based induction therapy helps to predict clinical response and prognosis in multiple myeloma patients

Hematology, 2023
Objective Cell division cycle 37 (CDC37) modulates disease progression and bortezomib resistance in multiple myeloma by regulating X-box binding protein 1, nuclear factor-kappa-B, etc.
Wuqiang Lin, Xiuli Chen, Heyong Zheng, Zhenjie Cai   +3 more
doaj   +3 more sources

Cdc37 (Cell Division Cycle 37) Restricts Hsp90 (Heat Shock Protein 90) Motility by Interaction with N-terminal and Middle Domain Binding Sites [PDF]

Journal of Biological Chemistry, 2013
The ATPase-driven dimeric molecular Hsp90 (heat shock protein 90) and its cofactor Cdc37 (cell division cycle 37 protein) are crucial to prevent the cellular depletion of many protein kinases. In complex with Hsp90, Cdc37 is thought to bind an important lid structure in the ATPase domain of Hsp90 and inhibit ATP turnover by Hsp90.
Eckl, J., Rutz, D., Haslbeck, V., Zierer, B., Reinstein, J., Richter, K.   +5 more
openaire   +4 more sources

Computational Discovery of Niclosamide Ethanolamine, a Repurposed Drug Candidate That Reduces Growth of Hepatocellular Carcinoma Cells In Vitro and in Mice by Inhibiting Cell Division Cycle 37 Signaling [PDF]

Gastroenterology, 2017
Drug repositioning offers a shorter approval process than new drug development. We therefore searched large public datasets of drug-induced gene expression signatures to identify agents that might be effective against hepatocellular carcinoma (HCC).We searched public databases of messenger RNA expression patterns reported from HCC specimens from ...
Chen, Bin, Wei, Wei, Ma, Li, Yang, Bin, Gill, Ryan M, Chua, Mei-Sze, Butte, Atul J, So, Samuel   +7 more
openaire   +4 more sources

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

Identification of co-chaperone Cdc37 in Penaeus monodon: coordination with Hsp90 can reduce cadmium stress-induced lipid peroxidation

Ecotoxicology and Environmental Safety, 2021
Cell division cycle 37 (Cdc37) is an important cytoplasmic phosphoprotein, which usually functions as a complex with heat shock protein 90 (Hsp90), to effectively reduce the damage caused by heavy metals, such as cadmium (Cd), in aquatic animals.
Chao Zhao, Chao Peng, Pengfei Wang, Sigang Fan, Lulu Yan, Lihua Qiu   +5 more
doaj   +1 more source

Interaction of Mouse Pem Protein and Cell Division Cycle 37 Homolog [PDF]

Acta Biochimica et Biophysica Sinica, 2005
Mouse Pem, a homeobox gene, encodes a protein consisting of 210 amino acid residues. To study the function of mouse Pem protein, we used the yeast two-hybrid system to screen the library of 7-day mouse embryo with full-length mouse Pem cDNA. Fifty-two colonies were obtained after 1.57 x 10(8) colonies were screened by nutrition limitation and beta ...
Fen, Guo, Yue-Qin, Li, Shi-Qian, Li, Zhi-Wen, Luo, Xin, Zhang, Dong-Sheng, Tang, Tian-Hong, Zhou   +6 more
openaire   +2 more sources

Direct Interaction of the Cell Division Cycle 37 Homolog Inhibits Endothelial Nitric Oxide Synthase Activity [PDF]

Circulation Research, 2006
Endothelial NO synthase (eNOS) via the production of NO in the endothelium plays a key role in cardiovascular biology and is tightly regulated by co- and posttranslational mechanisms, phosphorylation, and protein–protein interactions. The cell division cycle 37 homolog (Cdc37) is a key heat shock protein 90 (Hsp90) cochaperone for protein kinase ...
M Brennan, Harris, Manuela, Bartoli, Sarika G, Sood, Robert L, Matts, Richard C, Venema   +4 more
openaire   +2 more sources

Cdc48 and cofactors Npl4-Ufd1 are important for G1 progression during heat stress by maintaining cell wall integrity in Saccharomyces cerevisiae. [PDF]

PLoS ONE, 2011
The ubiquitin-selective chaperone Cdc48, a member of the AAA (ATPase Associated with various cellular Activities) ATPase superfamily, is involved in many processes, including endoplasmic reticulum-associated degradation (ERAD), ubiquitin- and proteasome ...
Meng-Ti Hsieh, Rey-Huei Chen
doaj   +1 more source

Ginsenoside Rg5 enhances the radiosensitivity of lung adenocarcinoma via reducing HSP90-CDC37 interaction and promoting client protein degradation

Journal of Pharmaceutical Analysis, 2023
Ginsenoside Rg5 is a rare ginsenoside showing promising tumor-suppressive effects. This study aimed to explore its radio-sensitizing effects and the underlying mechanisms. Human lung adenocarcinoma cell lines A549 and Calu-3 were used for in vitro and in 
Hansong Bai, Jiahua Lyu, Xinyu Nie, Hao Kuang, Long Liang, Hongyuan Jia, Shijie Zhou, Churong Li, Tao Li   +8 more
doaj   +1 more source

Recognition of BRAF by CDC37 and Re-Evaluation of the Activation Mechanism for the Class 2 BRAF-L597R Mutant

Biomolecules, 2022
The kinome specific co-chaperone, CDC37 (cell division cycle 37), is responsible for delivering BRAF (B-Rapidly Accelerated Fibrosarcoma) to the Hsp90 (heat shock protein 90) complex, where it is then translocated to the RAS (protooncogene product p21 ...
Dennis M. Bjorklund, R. Marc L. Morgan, Jasmeen Oberoi, Katie L. I. M. Day, Panagiota A. Galliou, Chrisostomos Prodromou   +5 more
doaj   +1 more source