Results 61 to 70 of about 3,509 (196)

ITC data for CDC37-BRAF interactions for paper: Recognition of BRAF by CDC37 and Re-evaluation of the Activation mechanism for the Class 2 BRAF-L597R Mutant

open access: yes, 2022
Data for paper published in Biomolecules June 2022  Isothermal Titration Calorimetry results for CDC37-BRAF interactions. dil in the filename donates the heat of dilution. Heats of dilution are in to buffer.
Dennis Bjorklund (6517310)   +5 more
core   +1 more source

Structural biology of HER2/ERBB2 dimerization: mechanistic insights and differential roles in healthy versus cancerous cells

open access: yesExploration of Medicine
Aim: Present study was done to understand the dimerization of HER2/ERBB2 in normal and cancer cells using in-silico study. Methods: Pathway analysis was done using Reactome.
Jayasree Santhanakrishnan   +2 more
doaj   +1 more source

AUY922 induces retinal toxicity through attenuating TRPM1

open access: yesJournal of Biomedical Science, 2021
Background Ocular adverse events are common dose-limiting toxicities in cancer patients treated with HSP90 inhibitors, such as AUY922; however, the pathology and molecular mechanisms that mediate AUY922-induced retinal toxicity remain undescribed ...
Che-Hung Shen   +9 more
doaj   +1 more source

Structural dynamics of RAF1-HSP90-CDC37 and HSP90 complexes reveal asymmetric client interactions and key structural elements

open access: yesCommunications Biology
RAF kinases are integral to the RAS-MAPK signaling pathway, and proper RAF1 folding relies on its interaction with the chaperone HSP90 and the cochaperone CDC37.
Lorenzo I. Finci   +11 more
doaj   +1 more source

Screening the Active Phytochemicals From Eclipta prostrata and Unraveling Their Molecular Insight Into Human Malignancies

open access: yesCancer Innovation, Volume 4, Issue 6, December 2025.
This review comprehensively analyses the phytochemicals from Eclipta prostrata, identifying 25 active compounds with chemotherapeutic potential against 15 different human malignancies. These compounds modulate diverse and complex mechanisms, including targeting critical signaling pathways (e.g., PI3K/AKT/mTOR), inducing regulated cell death (e.g., FAS,
Md. Sakhawat Hossain   +13 more
wiley   +1 more source

Hsp90/Cdc37 Chaperone/co-chaperone complex, a novel junction anticancer target elucidated by the mode of action of herbal drug Withaferin A

open access: yesBMC Bioinformatics, 2011
Background HSPs (Heat shock proteins) are highly conserved ubiquitous proteins among species which are involved in maintaining appropriate folding and conformation of other proteins and are thus referred to as molecular chaperones.
Bisaria Virendra S   +6 more
doaj   +1 more source

Renoprotective Role and Mechanisms of Luteolin in Chronic Kidney Disease: Insights From NHANES Data, Network Pharmacology, Mendelian Randomization, and Molecular Docking Techniques

open access: yesFood Science &Nutrition, Volume 13, Issue 12, December 2025.
This study identified luteolin as a key flavonoid linked to lower CKD risk. Mediation analysis indicated that lower systemic inflammation, reduced serum uric acid, and higher bicarbonate and albumin levels collectively account for part of this relationship.
Mengjin Li   +5 more
wiley   +1 more source

Nematode CDC-37 and DNJ-13 form complexes and can interact with HSP-90

open access: yesScientific Reports, 2021
The molecular chaperones Hsc70 and Hsp90 are required for proteostasis control and specific folding of client proteins in eukaryotic and prokaryotic organisms.
Lukas Schmauder   +5 more
doaj   +1 more source

Tumour Cell Size Control and Its Impact on Tumour Cell Function

open access: yesCell Proliferation, Volume 58, Issue 12, December 2025.
The regulatory mechanism of the size of tumour cells and its impact on the functions of tumour cells, as well as a summary of potential therapeutic targets for the corresponding mechanisms. ABSTRACT Cell size is an important component of cell morphological characteristics.
Min Zhou, Mei Zhou, Yang Jin
wiley   +1 more source

Identification and Characterization of Harc, a Novel Hsp90-associating Relative of Cdc37 [PDF]

open access: yesJournal of Biological Chemistry, 2001
Although little is known about the precise mechanisms by which the molecular chaperone Hsp90 recognizes its client proteins, Cdc37 has been shown to play a critical role in the targeting of Hsp90 to client protein kinases. Described here is the identification and characterization of a novel 35-kDa human protein that is 31% identical to Cdc37.
G M, Scholz, K, Cartledge, N E, Hall
openaire   +2 more sources

Home - About - Disclaimer - Privacy