Chaperone-Based Therapies for Disease Modification in Parkinson’s Disease
Parkinson's Disease, 2017 Parkinson’s disease (PD) is the second most common neurodegenerative disorder and is characterized by the presence of pathological intracellular aggregates primarily composed of misfolded α-synuclein.
Erik L. Friesen +4 more
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Control of steroid receptor dynamics and function by genomic actions of the cochaperones p23 and Bag-1L [PDF]
, 2014 Molecular chaperones encompass a group of unrelated proteins that facilitate the correct assembly and disassembly of other macromolecular structures, which they themselves do not remain a part of.
Brown, Myles +3 more
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The Chlamydia trachomatis Type III Secretion Chaperone Slc1 Engages Multiple Early Effectors, Including TepP, a Tyrosine-phosphorylated Protein Required for the Recruitment of CrkI-II to Nascent Inclusions and Innate Immune Signaling [PDF]
, 2014 Chlamydia trachomatis, the causative agent of trachoma and sexually transmitted infections, employs a type III secretion (T3S) system to deliver effector proteins into host epithelial cells to establish a replicative vacuole.
Bastidas, Robert J. +6 more
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Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates. [PDF]
, 2015 Molecular chaperones are key components of the arsenal of cellular defence mechanisms active against protein aggregation. In addition to their established role in assisting protein folding, increasing evidence indicates that molecular chaperones are able
Aprile, Francesco A +5 more
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Molecular chaperones and selection against mutations
Biology Direct, 2008 Background Molecular chaperones help to restore the native states of proteins after their destabilization by external stress. It has been proposed that another function of chaperones is to maintain the activity of proteins destabilized by mutation ...
Korona Ryszard, Tomala Katarzyna
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Expression patterns of molecular chaperone genes in Antarctic psychrophilic yeast, Glaciozyma antarctica PI12 in response to heat stress [PDF]
Polish Polar Research, 2019 Microbes living in the polar regions have some common and unique strategies to respond to thermal stress. Nevertheless, the amount of information available, especially at the molecular level is lacking for some organisms such as Antarctic psychrophilic ...
Nur Athirah Yusof +7 more
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Protein trafficking in the mitochondrial intermembrane space: mechanisms and links to human disease [PDF]
, 2017 Mitochondria fulfill a diverse range of functions in cells including oxygen metabolism, homeostasis of inorganic ions and execution of apoptosis. Biogenesis of mitochondria relies on protein import pathways that are ensured by dedicated multiprotein ...
MacPherson, Lisa +1 more
core +1 more source
Cells, 2019 Heat shock protein 90 (HSP90) molecular chaperones are a family of ubiquitous proteins participating in several cellular functions through the regulation of folding and/or assembly of large multiprotein complexes and client proteins.
V. Condelli +7 more
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Molecular chaperone genes in the sugarcane expressed sequence database (SUCEST)
Genetics and Molecular Biology, 2001 Some newly synthesized proteins require the assistance of molecular chaperones for their correct folding. Chaperones are also involved in the dissolution of protein aggregates making their study significant for both biotechnology and medicine and the ...
Júlio C. Borges +2 more
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Life, 2020 The property of molecular chaperones to dissolve protein aggregates of Parkinson-related α-synuclein has been known for some time. Recent findings point to an even more active role of molecular chaperones preventing the transformation of α-synuclein into
Emelie E. Aspholm +2 more
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