Results 31 to 40 of about 146,944 (294)

Chaperone-Based Therapies for Disease Modification in Parkinson’s Disease

open access: yesParkinson'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
doaj   +1 more source

A Novel Method for Assessing the Chaperone Activity of Proteins. [PDF]

open access: yesPLoS 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
doaj   +1 more source

Control of steroid receptor dynamics and function by genomic actions of the cochaperones p23 and Bag-1L [PDF]

open access: yes, 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
core   +2 more sources

Molecular chaperones and hypoxic-ischemic encephalopathy

open access: yesNeural 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
doaj   +1 more source

Thermodynamic bounds on the ultra- and infra-affinity of Hsp70 for its substrates [PDF]

open access: yes, 2017
The 70 kDa Heat Shock Proteins Hsp70 have several essential functions in living systems, such as protecting cells against protein aggregation, assisting protein folding, remodeling protein complexes and driving the translocation into organelles.
Hartich, David   +3 more
core   +2 more sources

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]

open access: yes, 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
core   +3 more sources

Protein trafficking in the mitochondrial intermembrane space: mechanisms and links to human disease [PDF]

open access: yes, 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

Molecular chaperones and selection against mutations

open access: yesBiology 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
doaj   +1 more source

Expression patterns of molecular chaperone genes in Antarctic psychrophilic yeast, Glaciozyma antarctica PI12 in response to heat stress [PDF]

open access: yesPolish 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
doaj   +1 more source

Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates. [PDF]

open access: yes, 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
core   +3 more sources

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