Results 101 to 110 of about 3,509 (196)

Hsp90^.Cdc37 complexes with protein kinases form cooperatively with multiple distinct interaction sites.

, 2015
Protein kinases are the most prominent group of heat shock protein 90 (Hsp90) clients and are recruited to the molecular chaperone by the kinase-specific cochaperone cell division cycle 37 (Cdc37).
Daake, M.A., Scherr, M.J., Eckl, J.M., Richter, K., Sattler, M., Freiburger, L.   +5 more
core   +1 more source

Integrated analysis of disulfidptosis-related immune genes signature to boost the efficacy of prognostic prediction in gastric cancer

Cancer Cell International
Background Gastric cancer (GC) remains a malignant tumor with high morbidity and mortality, accounting for approximately 1,080,000 diagnosed cases and 770,000 deaths worldwide annually.
Jie Li, Tian Yu, Juan Sun, Mingwei Ma, Zicheng Zheng, Yixuan He, Weiming Kang, Xin Ye   +7 more
doaj   +1 more source

PINK1-Interacting Proteins: Proteomic Analysis of Overexpressed PINK1

Parkinson's Disease, 2011
Recent publications suggest that the Parkinson's disease- (PD-) related PINK1/Parkin pathway promotes elimination of dysfunctional mitochondria by autophagy.
Aleksandar Rakovic, Anne Grünewald, Lisa Voges, Sarah Hofmann, Slobodanka Orolicki, Katja Lohmann, Christine Klein   +6 more
doaj   +1 more source

Cdc37 is involved in MDA-MB 231 cell invasion.

, 2012
A, Wound healing assay. Images obtained at 0 hours and 24 hours after scratch formation. Cells were let to migrate in control conditions as described in Materials and Methods or in the presence of 200 µg/ml of anti-Cdc37 antibody.
Evangelia Patsavoudi (140964), Avraam El Hamidieh (140953), Nicholas Grammatikakis (140959)   +2 more
core   +1 more source

Effect of the CSFV NS5A protein on key proteins in the MAPK and PI3K-mTOR signaling pathways in porcine macrophages

Frontiers in Microbiology
Classical swine fever (CSF) is a highly contagious disease caused by classical swine fever virus (CSFV). NS5A, a non-structural protein of CSFV, plays an important role in regulating viral replication and protein translation.
Yidan Wang, Xiaoru Zheng, Yingying Yang, Xinru Zhao, Min Li, Juan Huang, Qiaoya Zhang, Xiaobing Qin, Ying Yu, Qing Pan, Zhi Cao   +10 more
doaj   +1 more source

DYRK1B mutations associated with metabolic syndrome impair the chaperone-dependent maturation of the kinase domain

Scientific Reports, 2017
Two missense mutations of the DYRK1B gene have recently been found to co-segregate with a rare autosomal-dominant form of metabolic syndrome. This gene encodes a member of the DYRK family of protein kinases, which depend on tyrosine autophosphorylation ...
Samira Abu Jhaisha, Esti W. Widowati, Isao Kii, Rie Sonamoto, Stefan Knapp, Chrisovalantis Papadopoulos, Walter Becker   +6 more
doaj   +1 more source

ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system

, 2013
Protein kinase clients are recruited to the Hsp90 molecular chaperone system via Cdc37, which simultaneously binds Hsp90 and kinases and regulates the Hsp90 chaperone cycle.
Paul Workman, Chrisostomos Prodromou, Paul A Clarke, Laurence Pearl (4462603), Paul A Clarke (16083338), Paul Workman (54973), Rahul S Samant (13160922), Rahul S Samant, Laurence H Pearl, Sigrun Polier (16062746), Sigrun Polier, Chrisostomos Prodromou (4463035)   +11 more
core   +1 more source

Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37

, 2016
Despite the essential functions of Hsp90, little is known about the mechanism that controls substrate entry into its chaperone cycle. We show that the role of Cdc37 cochaperone reaches beyond that of an adaptor protein and find that it participates in ...
Zhang, Ziming, Liu, Wenjun, Marshall, Devon, Landgraf, Ralf, Larsen, Randy W., Larsen, Randy W, Keramisanou, Dimitra, Diviney, Andrea, Gelis, Ioannis, Aboalroub, Adam   +9 more
core   +2 more sources

Cdc37 is involved in MDA-MB 453 cell invasion.

, 2012
A, Wound healing assay. Images obtained at 0 hours and 24 hours after scratch formation. Cells were let to migrate in control conditions or in the presence of 200 µg/ml of anti-Cdc37 antibody.
Evangelia Patsavoudi (140964), Avraam El Hamidieh (140953), Nicholas Grammatikakis (140959)   +2 more
core   +1 more source

The role of the HSP90 cochaperone CDC37 and its therapeutic potential in cancer

, 2009
The cochaperone CDC37 promotes recruitment of a subset of client proteins, predominantly protein kinases, to the HSP90 chaperone, thereby regulating the activity of several signalling pathways including those altered in malignancy. Here, an investigation
Smith, Jennifer Rachel
core