Characterization of HSP90 isoforms in transformed bovine leukocytes infected with Theileria annulata [PDF]
, 2016 HSP90 chaperones are essential regulators of cellular function, as they ensure the appropriate conformation of multiple key client proteins. Four HSP90 isoforms were identified in the protozoan parasite Theileria annulata.
Calder, Ewen D.D. +8 more
core +2 more sources
Transcriptional regulation of human NMNAT2: insights from 3D genome sequencing and bioinformatics
The FEBS Journal, EarlyView.NMNAT2 is a valuable drug target, as low levels increase the risk of neurodegeneration. We employed 4C‐seq to identify NMNAT2 regulatory regions in the human genome, revealing distinct interactomes of the NMNAT2 promoter in undifferentiated and neuron‐like SH‐SY5Y cells. Additionally, we uncovered NMNAT2‐associated genes and transcription factors. This
Yu Chen Chang +5 more
wiley +1 more source
A dajkafehérjék az öregedési folyamatokban = Molecular chaperones in the ageing process [PDF]
, 2008 A stresszválasz fontos szerepet játszik az öregedésben, és terápiás célpont a korfüggő betegségek kezelésében. Pályázatunkban kimutattuk, hogy (1) az öregedés kóroki tényezőjeként ismert oxidatív stressz osztódó sejtekben nem vezet fehérje denaturációhoz
Amere Subbarao, Sreedhar +3 more
core
Μελέτη της πρωτεΐνης heat shock protein 90 (HSP90) σε καρκινικά φαινόμενα [PDF]
, 2009 Dimitris Stellas
openalex +1 more source
Deletion of heat shock protein 60 in adult mouse cardiomyocytes perturbs mitochondrial protein homeostasis and causes heart failure. [PDF]
, 2020 To maintain healthy mitochondrial enzyme content and function, mitochondria possess a complex protein quality control system, which is composed of different endogenous sets of chaperones and proteases.
Chen, Ju +13 more
core
Design of Allosteric Stimulators of the Hsp90 ATPase as New Anticancer Leads [PDF]
, 2017 Allosteric compounds that stimulate Hsp90 adenosine triphosphatase (ATPase) activity were rationally designed, showing anticancer potencies in the low micromolar to nanomolar range.
Agard, Da +10 more
core +1 more source
The ribosome‐associated complex regulates cytosolic translation upon mitoprotein‐induced stress
The FEBS Journal, EarlyView.Defects in mitochondrial protein import trigger a stress response. The contribution of translation regulation to such a response is only partially understood. We demonstrate that the deletion of mitochondrial surface proteins (TOM70/TOM71) leads to defects in mitochondrial biogenesis and slow growth.
Jiaxin Qian +7 more
wiley +1 more source
Mechanisms of Resistance to Hsp90 Inhibitor Drugs: A Complex Mosaic Emerges
Pharmaceuticals, 2011 The molecular chaperone Hsp90 holds great promise as a cancer drug target, despite some of the initial clinical trials of Hsp90 inhibitor drugs having not lived up to expectation.
Peter W. Piper, Stefan H. Millson
doaj +1 more source
The ALS‐associated E425K mutation uncouples DNAJC7 from the Hsp70 chaperone cycle
The FEBS Journal, EarlyView.DNAJC7 is a J‐domain protein that plays a key role in protein quality control by regulating Hsp70 activity and preventing protein aggregation. We find that the ALS‐associated E425K mutation in DNAJC7 disrupts productive interaction and activation of Hsp70, thereby blocking the transfer and refolding of client proteins such as TDP‐43.
Bar Elmaleh +2 more
wiley +1 more source
New Insights into Hsp90 Structural Plasticity Revealed by cryoEM
BioChemHeat Shock Protein 90 (Hsp90) acts as a crucial molecular chaperone, playing an essential role in activating numerous signaling proteins. The intricate mechanism of Hsp90 involving ATPase-coupled conformational changes and interactions with cochaperone ...
Karine Minari +2 more
doaj +1 more source