Cargando…

The Alpha Isoform of Heat Shock Protein 90 and the Co-chaperones p23 and Cdc37 Promote Opioid Anti-nociception in the Brain

Opioid activation of the mu opioid receptor (MOR) promotes signaling cascades that evoke both analgesic responses to pain and side effects like addiction and dependence. Manipulation of these cascades, such as by biased agonism, has great promise to improve opioid therapy. However, the signaling cas...

Descripción completa

Detalles Bibliográficos
Autores principales:	Lei, Wei, Duron, David I., Stine, Carrie, Mishra, Sanket, Blagg, Brian S. J., Streicher, John M.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Frontiers Media S.A. 2019
Materias:	Neuroscience
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6895903/ https://www.ncbi.nlm.nih.gov/pubmed/31849607 http://dx.doi.org/10.3389/fnmol.2019.00294

Ejemplares similares

Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
por: Li, Ting, et al.
Publicado: (2018)

Hsp90-Dependent Activation of Protein Kinases Is Regulated by Chaperone-Targeted Dephosphorylation of Cdc37
por: Vaughan, Cara K., et al.
Publicado: (2008)

Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins
por: Smith, Jennifer R., et al.
Publicado: (2013)

Differential Regulation of G1 CDK Complexes by the Hsp90-Cdc37 Chaperone System
por: Hallett, Stephen T., et al.
Publicado: (2017)

The co-chaperone Cdc37 regulates the rabies virus phosphoprotein stability by targeting to Hsp90AA1 machinery
por: Xu, Yunbin, et al.
Publicado: (2016)

Design of Disruptors of the Hsp90–Cdc37 Interface
por: D’Annessa, Ilda, et al.
Publicado: (2020)

Hsp90/Cdc37 Chaperone/co-chaperone complex, a novel junction anticancer target elucidated by the mode of action of herbal drug Withaferin A
por: Grover, Abhinav, et al.
Publicado: (2011)

Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System
por: Bunney, Tom D., et al.
Publicado: (2018)

Stability of the Human Hsp90-p50(Cdc37) Chaperone Complex against Nucleotides and Hsp90 Inhibitors, and the Influence of Phosphorylation by Casein Kinase 2
por: Olesen, Sanne H., et al.
Publicado: (2015)

Hsp90 S-nitrosylation at Cys521, as a conformational switch, modulates cycling of Hsp90-AHA1-CDC37 chaperone machine to aggravate atherosclerosis
por: Zhao, Shuang, et al.
Publicado: (2022)

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
por: Lawless, Nathan, et al.
Publicado: (2013)

Therapeutic Potential of the Hsp90/Cdc37 Interaction in Neurodegenerative Diseases
por: Gracia, Liam, et al.
Publicado: (2019)

Assembly mechanism of early Hsp90-Cdc37-kinase complexes
por: Keramisanou, Dimitra, et al.
Publicado: (2022)

Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor
por: Khandelwal, Anuj, et al.
Publicado: (2018)

Nematode CDC-37 and DNJ-13 form complexes and can interact with HSP-90
por: Schmauder, Lukas, et al.
Publicado: (2021)

Isoform-selective Hsp90 inhibition rescues model of hereditary open-angle glaucoma
por: Stothert, Andrew R., et al.
Publicado: (2017)

Ensemble-based modeling and rigidity decomposition of allosteric interaction networks and communication pathways in cyclin-dependent kinases: Differentiating kinase clients of the Hsp90-Cdc37 chaperone
por: Stetz, Gabrielle, et al.
Publicado: (2017)

The Activity and Stability of p56Lck and TCR Signaling Do Not Depend on the Co-Chaperone Cdc37
por: Kowallik, Sarah, et al.
Publicado: (2020)

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
por: Czemeres, Josh, et al.
Publicado: (2017)

Cell Surface Cdc37 Participates in Extracellular HSP90 Mediated Cancer Cell Invasion
por: El Hamidieh, Avraam, et al.
Publicado: (2012)

HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation
por: Oberoi, Jasmeen, et al.
Publicado: (2022)

The disruption of protein−protein interactions with co-chaperones and client substrates as a strategy towards Hsp90 inhibition
por: Serwetnyk, Michael A., et al.
Publicado: (2021)

Hsp90β inhibition upregulates interferon response and enhances immune checkpoint blockade therapy in murine tumors
por: Rahmy, Sharif, et al.
Publicado: (2022)

Silencing the cochaperone CDC37 destabilises kinase clients and sensitises cancer cells to HSP90 inhibitors
por: Smith, Jennifer R., et al.
Publicado: (2008)

Small-molecule inhibitor targeting the Hsp90-Cdc37 protein-protein interaction in colorectal cancer
por: Wang, Lei, et al.
Publicado: (2019)

Identification of Isoform-Selective Ligands for the Middle Domain of Heat Shock Protein 90 (Hsp90)
por: Mak, Oi Wei, et al.
Publicado: (2019)

Novel Small Molecule Hsp90/Cdc37 Interface Inhibitors Indirectly Target K-Ras-Signaling
por: Siddiqui, Farid Ahmad, et al.
Publicado: (2021)

Elaiophylin Is a Potent Hsp90/ Cdc37 Protein Interface Inhibitor with K-Ras Nanocluster Selectivity
por: Siddiqui, Farid A., et al.
Publicado: (2021)

CDC37 as a novel target for the treatment of NPM1-ALK expressing anaplastic large cell lymphomas
por: Kuravi, Sudhakiranmayi, et al.
Publicado: (2019)

Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle
por: Biebl, Maximilian M., et al.
Publicado: (2021)

Regulation of SKP2 protein stability by heat shock protein 90 chaperone machinery
por: Cai, Lili, et al.
Publicado: (2021)

Tenth International Symposium on the Hsp90 chaperone machine: Switzerland, October 19-23, 2022
por: Edkins, Adrienne L., et al.
Publicado: (2023)

Rational design, synthesis and structural characterization of peptides and peptidomimetics to target Hsp90/Cdc37 interaction for treating hepatocellular carcinoma
por: Sukumaran, Surya, et al.
Publicado: (2023)

Triple knockdown of CDC37, HSP90-alpha and HSP90-beta diminishes extracellular vesicles-driven malignancy events and macrophage M2 polarization in oral cancer
por: Ono, Kisho, et al.
Publicado: (2020)

Mutations Y493G and K546D in human HSP90 disrupt binding of celastrol and reduce interaction with Cdc37
por: Peng, Bin, et al.
Publicado: (2016)

Small Molecule Inhibitors to Disrupt Protein-protein Interactions of Heat Shock Protein 90 Chaperone Machinery
por: Seo, Young Ho
Publicado: (2015)

Heat Shock Protein 90 Chaperone Regulates the E3 Ubiquitin-Ligase Hakai Protein Stability
por: Díaz-Díaz, Andrea, et al.
Publicado: (2020)

Comprehensive molecular pharmacology screening reveals potential new receptor interactions for clinically relevant opioids
por: Olson, Keith M., et al.
Publicado: (2019)

Identification of a DYRK1A Inhibitor that Induces Degradation of the Target Kinase using Co-chaperone CDC37 fused with Luciferase nanoKAZ
por: Sonamoto, Rie, et al.
Publicado: (2015)

FW-04-806 inhibits proliferation and induces apoptosis in human breast cancer cells by binding to N-terminus of Hsp90 and disrupting Hsp90-Cdc37 complex formation
por: Huang, Wei, et al.
Publicado: (2014)

Cannot write session to /tmp/vufind_sessions/sess_rdhsnsao3knso14vlildi6a23v