Cargando…

Discovery of new molecular entities able to strongly interfere with Hsp90 C-terminal domain

Heat shock protein 90 (Hsp90) is an ATP dependent molecular chaperone deeply involved in the complex network of cellular signaling governing some key functions, such as cell proliferation and survival, invasion and angiogenesis. Over the past years the N-terminal protein domain has been fully invest...

Descripción completa

Detalles Bibliográficos
Autores principales:	Terracciano, Stefania, Russo, Alessandra, Chini, Maria G., Vaccaro, Maria C., Potenza, Marianna, Vassallo, Antonio, Riccio, Raffaele, Bifulco, Giuseppe, Bruno, Ines
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Nature Publishing Group UK 2018
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5786060/ https://www.ncbi.nlm.nih.gov/pubmed/29374167 http://dx.doi.org/10.1038/s41598-017-14902-y

Ejemplares similares

Natural Iminosugar (+)-Lentiginosine Inhibits ATPase and Chaperone Activity of Hsp90
por: Dal Piaz, Fabrizio, et al.
Publicado: (2012)

Identification of the Plant Compound Geraniin as a Novel Hsp90 Inhibitor
por: Vassallo, Antonio, et al.
Publicado: (2013)

Limonoids from Guarea guidonia and Cedrela odorata: Heat Shock Protein 90 (Hsp90) Modulator Properties of Chisomicine D
por: Bellone, Maria Laura, et al.
Publicado: (2021)

Hsp90 N- and C-terminal double inhibition synergistically suppresses Bcr-Abl-positive human leukemia cells
por: Chen, Chun, et al.
Publicado: (2016)

The HSP90 inhibitor KW-2478 depletes the malignancy of BCR/ABL and overcomes the imatinib-resistance caused by BCR/ABL amplification
por: Zeng, Dachuan, et al.
Publicado: (2022)

HSP90 inhibitor AUY922 induces cell death by disruption of the Bcr-Abl, Jak2 and HSP90 signaling network complex in leukemia cells
por: Tao, Wenjing, et al.
Publicado: (2015)

Identification of 2-(thiophen-2-yl)acetic Acid-Based Lead Compound for mPGES-1 Inhibition
por: Di Micco, Simone, et al.
Publicado: (2021)

SUV39H1 is a New Client Protein of Hsp90 Degradated by Chaetocin as a Novel C-Terminal Inhibitor of Hsp90
por: Lian, Bin, et al.
Publicado: (2021)

HSP90 Interacts with the Fibronectin N-terminal Domains and Increases Matrix Formation
por: Chakraborty, Abir, et al.
Publicado: (2020)

Retraction Note: Disruption of the Bcr-Abl/Hsp90 protein complex: a possible mechanism to inhibit Bcr-Abl-positive human leukemic blasts by novobiocin
por: Wu, L. X., et al.
Publicado: (2020)

Hsp90 C-Terminal Inhibitors Exhibit Antimigratory Activity by Disrupting the Hsp90α/Aha1 Complex in PC3-MM2 Cells
por: Ghosh, Suman, et al.
Publicado: (2014)

Exploring the Anticancer Potential of Premna resinosa (Hochst.) Leaf Surface Extract: Discovering New Diterpenes as Heat Shock Protein 70 (Hsp70) Binding Agents
por: Parisi, Valentina, et al.
Publicado: (2023)

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

Structure-Activity Relationships of Benzothiazole-Based Hsp90 C-Terminal-Domain Inhibitors
por: Dernovšek, Jaka, et al.
Publicado: (2021)

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

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)

Hsp-90 and the biology of nematodes
por: Him, Nik AIIN, et al.
Publicado: (2009)

Mechanisms of Hsp90 regulation
por: Prodromou, Chrisostomos
Publicado: (2016)

Regulatory Mechanisms of Hsp90
por: Prodromou, Chrisostomos
Publicado: (2017)

Inhibitors of HSP90 in melanoma
por: Mielczarek-Lewandowska, Aleksandra, et al.
Publicado: (2019)

Role of HSP90 in Cancer
por: Birbo, Bereket, et al.
Publicado: (2021)

Organismal Roles of Hsp90
por: van Oosten-Hawle, Patricija
Publicado: (2023)

Inhibition of N-terminal ATPase on HSP90 attenuates colitis through enhanced Treg function
por: Collins, Colm B., et al.
Publicado: (2013)

A Dynamic View of ATP-coupled Functioning Cycle of Hsp90 N-terminal Domain
por: Zhang, Huaqun, et al.
Publicado: (2015)

Development of a First-in-Class Small-Molecule Inhibitor of the C-Terminal Hsp90 Dimerization
por: Bhatia, Sanil, et al.
Publicado: (2022)

Repositioning of Quinazolinedione-Based Compounds on Soluble Epoxide Hydrolase (sEH) through 3D Structure-Based Pharmacophore Model-Driven Investigation
por: Gazzillo, Erica, et al.
Publicado: (2022)

The Distinct Assignments for Hsp90α and Hsp90β: More Than Skin Deep
por: Chang, Cheng, et al.
Publicado: (2023)

Hsp110 Chaperones Control Client Fate Determination in the Hsp70–Hsp90 Chaperone System
por: Mandal, Atin K., et al.
Publicado: (2010)

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

Identification of 2-Aminoacyl-1,3,4-thiadiazoles as Prostaglandin E(2) and Leukotriene Biosynthesis Inhibitors
por: Potenza, Marianna, et al.
Publicado: (2022)

HSP90 inhibitors disrupt a transient HSP90-HSF1 interaction and identify a noncanonical model of HSP90-mediated HSF1 regulation
por: Kijima, Toshiki, et al.
Publicado: (2018)

The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases
por: Lackie, Rachel E., et al.
Publicado: (2017)

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

USP22-dependent HSP90AB1 expression promotes resistance to HSP90 inhibition in mammary and colorectal cancer
por: Kosinsky, Robyn Laura, et al.
Publicado: (2019)

Structural Refinement of 2,4-Thiazolidinedione Derivatives as New Anticancer Agents Able to Modulate the BAG3 Protein
por: Ruggiero, Dafne, et al.
Publicado: (2022)

Resolving Hot Spots in the C-Terminal Dimerization Domain that Determine the Stability of the Molecular Chaperone Hsp90
por: Ciglia, Emanuele, et al.
Publicado: (2014)

C-terminal domain of SMYD3 serves as a unique HSP90-regulated motif in oncogenesis
por: Brown, Mark A., et al.
Publicado: (2015)

Modulation of Human Hsp90α Conformational Dynamics by Allosteric Ligand Interaction at the C-Terminal Domain
por: Penkler, David L., et al.
Publicado: (2019)

Global Dynamics of Yeast Hsp90 Middle and C-Terminal Dimer Studied by Advanced Sampling Simulations
por: Kandzia, Florian, et al.
Publicado: (2019)

In Silico Discovery and Optimisation of a Novel Structural Class of Hsp90 C-Terminal Domain Inhibitors
por: Zajec, Živa, et al.
Publicado: (2022)

Cannot write session to /tmp/vufind_sessions/sess_c865ct29tphh2bt5o39cme0jbk