[HTML][HTML] Small heat shock proteins: role in cellular functions and pathology
Small heat shock proteins (sHsps) are conserved across species and are important in stress
tolerance. Many sHsps exhibit chaperone-like activity in preventing aggregation of target …
tolerance. Many sHsps exhibit chaperone-like activity in preventing aggregation of target …
[HTML][HTML] α-Synuclein misfolding and Parkinson's disease
L Breydo, JW Wu, VN Uversky - … et Biophysica Acta (BBA)-Molecular Basis …, 2012 - Elsevier
Substantial evidence links α-synuclein, a small highly conserved presynaptic protein with
unknown function, to both familial and sporadic Parkinson's disease (PD). α-Synuclein has …
unknown function, to both familial and sporadic Parkinson's disease (PD). α-Synuclein has …
The scientific and clinical basis for the treatment of Parkinson disease (2009)
CW Olanow, MB Stern, K Sethi - Neurology, 2009 - AAN Enterprises
Parkinson disease (PD) is an age-related neurodegenerative disorder that affects as many
as 1–2% of persons aged 60 years and older. With the aging of the population, the …
as 1–2% of persons aged 60 years and older. With the aging of the population, the …
[HTML][HTML] Alpha-synuclein and tau: teammates in neurodegeneration?
S Moussaud, DR Jones… - Molecular …, 2014 - Springer
The accumulation of α-synuclein aggregates is the hallmark of Parkinson's disease, and
more generally of synucleinopathies. The accumulation of tau aggregates however is …
more generally of synucleinopathies. The accumulation of tau aggregates however is …
Sirtuin 2 inhibitors rescue α-synuclein-mediated toxicity in models of Parkinson's disease
TF Outeiro, E Kontopoulos, SM Altmann, I Kufareva… - science, 2007 - science.org
The sirtuins are members of the histone deacetylase family of proteins that participate in a
variety of cellular functions and play a role in aging. We identified a potent inhibitor of sirtuin …
variety of cellular functions and play a role in aging. We identified a potent inhibitor of sirtuin …
Large potentials of small heat shock proteins
EV Mymrikov, AS Seit-Nebi… - Physiological …, 2011 - journals.physiology.org
Modern classification of the family of human small heat shock proteins (the so-called HSPB)
is presented, and the structure and properties of three members of this family are analyzed …
is presented, and the structure and properties of three members of this family are analyzed …
[HTML][HTML] Formation of toxic oligomeric α-synuclein species in living cells
TF Outeiro, P Putcha, JE Tetzlaff, R Spoelgen, M Koker… - PloS one, 2008 - journals.plos.org
Background Misfolding, oligomerization, and fibrillization of α-synuclein are thought to be
central events in the onset and progression of Parkinson's disease (PD) and related …
central events in the onset and progression of Parkinson's disease (PD) and related …
[HTML][HTML] Molecular chaperones: a double-edged sword in neurodegenerative diseases
J Tittelmeier, E Nachman… - Frontiers in aging …, 2020 - frontiersin.org
Aberrant accumulation of misfolded proteins into amyloid deposits is a hallmark in many age-
related neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's …
related neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's …
Heat shock proteins: cellular and molecular mechanisms in the central nervous system
Emerging evidence indicates that heat shock proteins (HSPs) are critical regulators in
normal neural physiological function as well as in cell stress responses. The functions of …
normal neural physiological function as well as in cell stress responses. The functions of …
[HTML][HTML] Exosomal secretion of α-synuclein as protective mechanism after upstream blockage of macroautophagy
N Fussi, M Höllerhage, T Chakroun, NP Nykänen… - Cell death & …, 2018 - nature.com
Accumulation of pathological α-synuclein aggregates plays a major role in Parkinson's
disease. Macroautophagy is a mechanism to degrade intracellular protein aggregates by …
disease. Macroautophagy is a mechanism to degrade intracellular protein aggregates by …