Cargando…

Small-molecule inhibitor targeting the Hsp90-Cdc37 protein-protein interaction in colorectal cancer

Disrupting the interactions between Hsp90 and Cdc37 is emerging as an alternative and specific way to regulate the Hsp90 chaperone cycle in a manner not involving adenosine triphosphatase inhibition. Here, we identified DDO-5936 as a small-molecule inhibitor of the Hsp90-Cdc37 protein-protein intera...

Descripción completa

Detalles Bibliográficos
Autores principales:	Wang, Lei, Zhang, Lixiao, Li, Li, Jiang, Jingsheng, Zheng, Zhen, Shang, Jialin, Wang, Chengxiang, Chen, Weilin, Bao, Qichao, Xu, Xiaoli, Jiang, Zhengyu, Zhang, Jian, You, Qidong
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	American Association for the Advancement of Science 2019
Materias:	Research Articles
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6750927/ https://www.ncbi.nlm.nih.gov/pubmed/31555737 http://dx.doi.org/10.1126/sciadv.aax2277

Ejemplares similares

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

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

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)

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)

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

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

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

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

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

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

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)

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

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)

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)

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

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

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)

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)

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)

Modulation of protein fate decision by small molecules: targeting molecular chaperone machinery
por: Wang, Lei, et al.
Publicado: (2020)

(20S) Ginsenoside Rh2 Exerts Its Anti-Tumor Effect by Disrupting the HSP90A-Cdc37 System in Human Liver Cancer Cells
por: Chen, Chen, et al.
Publicado: (2021)

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)

Apigenin inhibits proliferation and induces apoptosis in human multiple myeloma cells through targeting the trinity of CK2, Cdc37 and Hsp90
por: Zhao, Ming, et al.
Publicado: (2011)

Identification and Characterization of Three Heat Shock Protein 90 (Hsp90) Homologs in the Brown Planthopper
por: Chen, Xuan, et al.
Publicado: (2020)

Y‐632 inhibits heat shock protein 90 (Hsp90) function by disrupting the interaction between Hsp90 and Hsp70/Hsp90 organizing protein, and exerts antitumor activity in vitro and in vivo
por: Wang, Wenqian, et al.
Publicado: (2016)

Circulating heat shock protein 90 (Hsp90) and autoantibodies to Hsp90 are increased in patients with atopic dermatitis
por: Sitko, Krzysztof, et al.
Publicado: (2021)

Regulation of Vascular Endothelial Cell Polarization and Migration by Hsp70/Hsp90-Organizing Protein
por: Li, Jingyu, et al.
Publicado: (2012)

The Ribosomal Biogenesis Protein Utp21 Interacts with Hsp90 and Has Differing Requirements for Hsp90-Associated Proteins
por: Tenge, Victoria R., et al.
Publicado: (2014)

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)

Hsp40s Specify Functions of Hsp104 and Hsp90 Protein Chaperone Machines
por: Reidy, Michael, et al.
Publicado: (2014)

HSP90 proteins in the scenario of tumor complexity
por: Rasola, Andrea
Publicado: (2017)

Heat Shock Protein 90 (Hsp90) Expression and Breast Cancer
por: Zagouri, Flora, et al.
Publicado: (2012)

Traditional and Novel Mechanisms of Heat Shock Protein 90 (HSP90) Inhibition in Cancer Chemotherapy Including HSP90 Cleavage
por: Park, Sangkyu, et al.
Publicado: (2019)

The Alpha Isoform of Heat Shock Protein 90 and the Co-chaperones p23 and Cdc37 Promote Opioid Anti-nociception in the Brain
por: Lei, Wei, et al.
Publicado: (2019)

Cdc7-Dbf4-mediated phosphorylation of HSP90-S164 stabilizes HSP90-HCLK2-MRN complex to enhance ATR/ATM signaling that overcomes replication stress in cancer
por: Cheng, An Ning, 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)

Heat Shock Protein 90 (Hsp90) and Hsp70 as Potential Therapeutic Targets in Autoimmune Skin Diseases
por: Tukaj, Stefan, et al.
Publicado: (2022)

Modelling the Role of the Hsp70/Hsp90 System in the Maintenance of Protein Homeostasis
por: Proctor, Carole J., et al.
Publicado: (2011)

Cannot write session to /tmp/vufind_sessions/sess_7ts0ppmv7r9e4qqe02dpml8bfu