Cell Reports, 2019 Summary: The extracellular molecular chaperone heat shock protein 90 (eHSP90) stabilizes protease client the matrix metalloproteinase 2 (MMP2), leading to tumor cell invasion.
Alexander J. Baker-Williams +15 more
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Thermodynamic bounds on the ultra- and infra-affinity of Hsp70 for its substrates [PDF]
, 2017 The 70 kDa Heat Shock Proteins Hsp70 have several essential functions in living systems, such as protecting cells against protein aggregation, assisting protein folding, remodeling protein complexes and driving the translocation into organelles.
Hartich, David +3 more
core +2 more sources
Myelin pathology: Involvement of molecular chaperones and the promise of chaperonotherapy [PDF]
, 2019 The process of axon myelination involves various proteins including molecular chaperones. Myelin alteration is a common feature in neurological diseases due to structural and functional abnormalities of one or more myelin proteins.
Cappello F. +4 more
core +1 more source
Donor-strand exchange in chaperone-assisted pilus assembly revealed in atomic detail by molecular dynamics [PDF]
, 2008 Adhesive multi-subunit fibres are assembled on the surface of many pathogenic bacteria via the chaperone-usher pathway. In the periplasm, a chaperone donates a β-strand to a pilus subunit to complement its incomplete immunoglobulin-like fold.
Ashcroft, A.E. +5 more
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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. [PDF]
PLoS ONE, 2017 The overarching goal of delineating molecular principles underlying differentiation of protein kinase clients and chaperone-based modulation of kinase activity is fundamental to understanding activity of many oncogenic kinases that require chaperoning of
Gabrielle Stetz +2 more
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Updates on Aβ Processing by Hsp90, BRICHOS, and Newly Reported Distinctive Chaperones
Biomolecules, 2023 Alzheimer’s disease (AD) is an extremely devastating neurodegenerative disease, and there is no cure for it. AD is specified as the misfolding and aggregation of amyloid-β protein (Aβ) and abnormalities in hyperphosphorylated tau protein.
Mohammed Iqbal +3 more
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Could Upregulated Hsp70 Protein Compensate for the Hsp90-Silence-Induced Cell Death in Glioma Cells? [PDF]
, 2014 The molecular chaperone heat shock protein 90 alpha (Hsp90α) has been recognized in various tumours including glioma. This pilot study using a proteomic approach analyses the downstream effects of Hsp90 inhibition using 17-allylamino-17 ...
Khan, Zarine Jamsher +3 more
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Structure of the TPR Domain of AIP: Lack of Client Protein Interaction with the C-Terminal alpha-7 Helix of the TPR Domain of AIP Is Sufficient for Pituitary Adenoma Predisposition [PDF]
, 2012 PMCID: PMC3534021This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are ...
A Laenger +62 more
core +6 more sources
Hsp83/Hsp90 Physically Associates with Insulin Receptor to Promote Neural Stem Cell Reactivation
Stem Cell Reports, 2018 Summary: Neural stem cells (NSCs) have the ability to exit quiescence and reactivate in response to physiological stimuli. In the Drosophila brain, insulin receptor (InR)/phosphatidylinositol 3-kinase (PI3K)/Akt pathway triggers NSC reactivation. However,
Jiawen Huang, Hongyan Wang
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Probing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics. [PDF]
PLoS ONE, 2012 Deciphering functional mechanisms of the Hsp90 chaperone machinery is an important objective in cancer biology aiming to facilitate discovery of targeted anti-cancer therapies.
Anshuman Dixit, Gennady M Verkhivker
doaj +1 more source