Results 1 to 10 of about 3,509 (196)

Tumor‐Derived CDC37 Inhibits Antigen Cross‐Presentation in Dendritic Cells and Impairs Anti‐Tumor Immunity in Breast Cancer [PDF]

Advanced Science
Tumor mutational burden (TMB), usually representing high immunogenicity, cannot always predict treatment response of immune checkpoint blockade (ICB).
Ruxin Wang, Yunyi Zhang, Xiangyu Meng, Jianli Zhao, Yue Xing, Qian Ouyang, Ning Zhang, Huiping Chen, Nanyan Miao, Erwei Song, Di Huang   +10 more
doaj   +3 more sources

HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation

Nature Communications, 2022
Binding to HSP90-CDC37 is essential for the activity of many protein kinases, but its function is unclear. Here, the authors show that HSP90-CDC37 provides a structural platform for the phosphatase PP5 to dephosphorylate a bound kinase, ‘factory ...
Jasmeen Oberoi, Xavi Aran Guiu, Emily A. Outwin, Pascale Schellenberger, Theodoros I. Roumeliotis, Jyoti S. Choudhary, Laurence H. Pearl   +6 more
doaj   +7 more sources

Differential Regulation of G1 CDK Complexes by the Hsp90-Cdc37 Chaperone System

Cell Reports, 2017
Summary: Selective recruitment of protein kinases to the Hsp90 system is mediated by the adaptor co-chaperone Cdc37. We show that assembly of CDK4 and CDK6 into protein complexes is differentially regulated by the Cdc37-Hsp90 system.
MARTYNA W Pastok, Stephen R Wedge, Chrisostomos Prodromou   +2 more
exaly   +5 more sources

Structure of an Hsp90-Cdc37-Cdk4 Complex [PDF]

Molecular Cell, 2006
Activation of many protein kinases depends on their interaction with the Hsp90 molecular chaperone system. Recruitment of protein kinase clients to the Hsp90 chaperone system is mediated by the cochaperone adaptor protein Cdc37, which acts as a scaffold, simultaneously binding protein kinases and Hsp90. We have now expressed and purified an Hsp90-Cdc37-
Vaughan, C, Gohlke, U, Sobott, F, Good, V, Ali, M, Prodromou, C, Robinson, C, Saibil, H, Pearl, L   +8 more
openaire   +5 more sources

Comparative analysis of the impact of Heat shock protein 90 kDa or Cdc37 mutation on the yeast proteome [PDF]

Cell Stress & Chaperones
Hsp90 is an abundant and essential molecular chaperone that is required for the folding and/or activity of up to 15%-20% of all yeast proteins. Hsp90 and its cochaperone Cdc37 are of interest due to their cooperative role in chaperoning oncogenic protein
Erick I. Rios, Jill L. Johnson
doaj   +2 more sources

Design of Disruptors of the Hsp90–Cdc37 Interface [PDF]

Molecules, 2020
The molecular chaperone Hsp90 is a ubiquitous ATPase-directed protein responsible for the activation and structural stabilization of a large clientele of proteins.
Ilda D’Annessa, Naama Hurwitz, Valentina Pirota, Giovanni Luca Beretta, Stella Tinelli, Mark Woodford, Mauro Freccero, Mehdi Mollapour, Nadia Zaffaroni, Haim Wolfson, Giorgio Colombo   +10 more
doaj   +5 more sources

Self-Assembled Dictamni Cortex Nanoparticles Ameliorate Psoriasis by Epigenetic Modulation of HSP90AB1 and Suppression of the Inflammatory Response. [PDF]

Adv Sci (Weinh)
This study develops self‐assembled Dictamni Cortex (BXP)‐Fe(III) infinite coordination polymer nanoparticles (NB) to improve BXP's solubility and bioavailability for psoriasis. NB transdermally treats psoriasis by targeting the epigenetic regulator CTCF (CCCTC‐binding factor), suppressing HSP90AB1 (heat shock protein 90 alpha family class B member 1 ...
Zhang Z, Du W, Zhang X, Cui H, Cheng B, Han X, He K, Yin T, Liu X, Xian N, Wang Z, Liu M, Han D, Liu J, Zheng Y, Wang Y.   +15 more
europepmc   +2 more sources

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   +6 more sources

The oncolytic avian reovirus p17 protein triggers chaperone-mediated autophagy by modulating Hsp90 and the T-complex protein-1 ring complex chaperones and co-chaperones to activate the IKK/NF-κB signaling [PDF]

Journal of Virology
This study is the first to reveal that oncolytic avian reovirus (ARV) modulates the IKK/NF-κB signaling through the Hsp90-Cdc37, T-complex protein-1 ring complex (TRiC)/Hsc70, and TRiC-phosducin-like protein 1 (PhLP1) chaperone complexes, thereby ...
Wei‐Ru Huang, Jyun-Yi Li, Tsai-Ling Liao, Lon-Fye Lye, Muhammad Munir, Hung-Jen Liu   +5 more
doaj   +2 more sources

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   +3 more sources