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Editorial: Molecular Chaperones and Neurodegeneration [PDF]

Frontiers in Neuroscience, 2017
Peer ...
Roodveldt, Cintia, Outeiro, Tiago F., Braun, Janice E. A.   +2 more
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BAG5 Promotes Alpha-Synuclein Oligomer Formation and Functionally Interacts With the Autophagy Adaptor Protein p62

Frontiers in Cell and Developmental Biology, 2020
Molecular chaperones are critical to maintaining intracellular proteostasis and have been shown to have a protective role against alpha-synuclein-mediated toxicity.
Erik L. Friesen, Erik L. Friesen, Yu Tong Zhang, Yu Tong Zhang, Rebecca Earnshaw, Rebecca Earnshaw, Mitch L. De Snoo, Mitch L. De Snoo, Darren M. O’Hara, Darren M. O’Hara, Victoria Agapova, Hien Chau, Sophie Ngana, Sophie Ngana, Kevin S. Chen, Kevin S. Chen, Lorraine V. Kalia, Lorraine V. Kalia, Lorraine V. Kalia, Suneil K. Kalia, Suneil K. Kalia, Suneil K. Kalia   +21 more
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Functional Characterization of an Arabidopsis Profilin Protein as a Molecular Chaperone under Heat Shock Stress

Molecules, 2022
Profilins (PFNs) are actin monomer-binding proteins that function as antimicrobial agents in plant phloem sap. Although the roles of Arabidopsis thaliana profilin protein isoforms (AtPFNs) in regulating actin polymerization have already been described ...
Hyosuk Son, Young Jun Jung, Seong-Cheol Park, Il Ryong Kim, Joung Hun Park, Mi-Kyeong Jang, Jung Ro Lee   +6 more
doaj   +1 more source

Molecular Chaperone Receptors [PDF]

, 2017
Extracellular heat shock proteins (HSP) play important roles in cell signaling and immunity. Many of these effects are mediated by surface receptors expressed on a wide range of cell types. We have investigated the nature of such proteins by cloning candidate receptors into cells (CHO-K1) with the rare property of being null for HSP binding. Using this
Ayesha, Murshid, Jimmy, Theriault, Jianlin, Gong, Stuart K, Calderwood   +3 more
openaire   +2 more sources

Role of Subunit Exchange and Electrostatic Interactions on the Chaperone Activity of Mycobacterium leprae HSP18. [PDF]

PLoS ONE, 2015
Mycobacterium leprae HSP18, a major immunodominant antigen of M. leprae pathogen, is a small heat shock protein. Previously, we reported that HSP18 is a molecular chaperone that prevents aggregation of different chemically and thermally stressed client ...
Sandip Kumar Nandi, Alok Kumar Panda, Ayon Chakraborty, Sougata Sinha Ray, Ashis Biswas   +4 more
doaj   +1 more source

αA-Crystallin-derived mini-chaperone modulates stability and function of cataract causing αAG98R-crystallin. [PDF]

PLoS ONE, 2012
A substitution mutation in human αA-crystallin (αAG98R) is associated with autosomal dominant cataract. The recombinant mutant αAG98R protein exhibits altered structure, substrate-dependent chaperone activity, impaired oligomer stability and aggregation ...
Murugesan Raju, Puttur Santhoshkumar, K Krishna Sharma   +2 more
doaj   +1 more source

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

Pharmaceuticals, 2013
A fundamental role of the Hsp90-Cdc37 chaperone system in mediating maturation of protein kinase clients and supporting kinase functional activity is essential for the integrity and viability of signaling pathways involved in cell cycle control and ...
Gennady Verkhivker, Elizabeth Berrigan, Nathan Lawless, Kristin Blacklock   +3 more
doaj   +1 more source

Functions and Therapeutic Potential of Extracellular Hsp60, Hsp70, and Hsp90 in Neuroinflammatory Disorders

Applied Sciences, 2021
Neuroinflammation is implicated in central nervous system (CNS) diseases, but the molecular mechanisms involved are poorly understood. Progress may be accelerated by developing a comprehensive view of the pathogenesis of CNS disorders, including the ...
Giusi Alberti, Letizia Paladino, Alessandra Maria Vitale, Celeste Caruso Bavisotto, Everly Conway de Macario, Claudia Campanella, Alberto J. L. Macario, Antonella Marino Gammazza   +7 more
doaj   +1 more source

Co-chaperones TIMP2 and AHA1 Competitively Regulate Extracellular HSP90:Client MMP2 Activity and Matrix Proteolysis

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, Fiza Hashmi, Marek A. Budzyński, Mark R. Woodford, Stephanie Gleicher, Samu V. Himanen, Alan M. Makedon, Derek Friedman, Stephanie Cortes, Sara Namek, William G. Stetler-Stevenson, Gennady Bratslavsky, Alaji Bah, Mehdi Mollapour, Lea Sistonen, Dimitra Bourboulia   +15 more
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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