The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution [PDF]
, 2013 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
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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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A Novel Method for Assessing the Chaperone Activity of Proteins. [PDF]
PLoS ONE, 2016 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
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Gymnastics of Molecular Chaperones [PDF]
Molecular Cell, 2010 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
Molecular chaperones and hypoxic-ischemic encephalopathy
Neural Regeneration Research, 2017 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
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Single-molecule fluorescence studies of Protein Folding and Molecular Chaperones [PDF]
, 2011 Folding of newly synthesized proteins is an essential part of protein biosynthesis and misfolding can result in protein aggregation which can also lead to several severe diseases.
Sikor, Martin
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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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Molecular Chaperones in Parkinson's Disease – Present and Future
Journal of Parkinson’s Disease, 2011 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
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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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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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