The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution [PDF]
NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a ...
El-Mkami, H. +31 more
core +1 more source
Human molecular chaperones share with SARS-CoV-2 antigenic epitopes potentially capable of eliciting autoimmunity against endothelial cells: possible role of molecular mimicry in COVID-19 [PDF]
Severe acute respiratory syndrome corona virus 2 (SARS-CoV-2), the cause of COVID-19 disease, has the potential to elicit autoimmunity because mimicry of human molecular chaperones by viral proteins.
Legare S. +7 more
core +1 more source
Chaperone-Based Therapies for Disease Modification in Parkinson’s Disease
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
doaj +1 more source
Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones. [PDF]
When massively expressed in bacteria, recombinant proteins often tend to misfold and accumulate as soluble and insoluble nonfunctional aggregates. A general strategy to improve the native folding of recombinant proteins is to increase the cellular ...
Diamant, S. +3 more
core +1 more source
A Novel Method for Assessing the Chaperone Activity of Proteins. [PDF]
Protein chaperones are molecular machines which function both during homeostasis and stress conditions in all living organisms. Depending on their specific function, molecular chaperones are involved in a plethora of cellular processes by playing key ...
Nevena Hristozova +2 more
doaj +1 more source
Molecular chaperones and hypoxic-ischemic encephalopathy
Hypoxic-ischemic encephalopathy (HIE) is a disease that occurs when the brain is subjected to hypoxia, resulting in neuronal death and neurological deficits, with a poor prognosis.
Cong Hua +4 more
doaj +1 more source
Gymnastics of Molecular Chaperones [PDF]
Molecular chaperones assist folding processes and conformational changes in many proteins. In order to do so, they progress through complex conformational cycles themselves. In this review, I discuss the diverse conformational dynamics of the ATP-dependent chaperones of the Hsp60, Hsp70, Hsp90, and Hsp100 families.
openaire +2 more sources
Hsp70 in mitochondrial biogenesis [PDF]
The family of hsp70 (70 kilodalton heat shock protein) molecular chaperones plays an essential and diverse role in cellular physiology, Hsp70 proteins appear to elicit their effects by interacting with polypeptides that present domains which exhibit non ...
Stuart, Rosemary A. +2 more
core +1 more source
Expression patterns of molecular chaperone genes in Antarctic psychrophilic yeast, Glaciozyma antarctica PI12 in response to heat stress [PDF]
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
doaj +1 more source
Molecular Chaperones in Parkinson's Disease – Present and Future
Parkinson's disease, like many other neurodegenerative disorders, is characterized by the progressive accumulation of pathogenic protein species and the formation of intracellular inclusion bodies.
Darius Ebrahimi-Fakhari +2 more
doaj +1 more source

