Results 11 to 20 of about 227,395 (295)
The APE2 Exonuclease Is a Client of the Hsp70–Hsp90 Axis in Yeast and Mammalian Cells
Biomolecules, 2022 Molecular chaperones such as Hsp70 and Hsp90 help fold and activate proteins in important signal transduction pathways that include DNA damage response (DDR).
Siddhi Omkar +4 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 +3 more
openaire +2 more sources
Metabolic and Chaperone Gene Loss Marks the Origin of Animals: Evidence for Hsp104 and Hsp78 Sharing Mitochondrial Clients [PDF]
, 2015 The evolution of animals involved acquisition of an emergent gene repertoire for gastrulation. Whether loss of genes also co-evolved with this developmental reprogramming has not yet been addressed.
Erives, Albert, Fassler, Jan
core +5 more sources
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 +21 more
doaj +1 more source
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 +4 more
doaj +1 more source
Small heat-shock proteins: important players in regulating cellular proteostasis [PDF]
, 2015 Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection.
Carver, John A. +3 more
core +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 +2 more
doaj +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
core +1 more source
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 +3 more
doaj +1 more source
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 +7 more
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