[HTML][HTML] Small heat shock proteins: role in cellular functions and pathology

R Bakthisaran, R Tangirala, CM Rao - Biochimica et Biophysica Acta (BBA) …, 2015 - Elsevier
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 …

Walking the tightrope: proteostasis and neurodegenerative disease

JJ Yerbury, L Ooi, A Dillin, DN Saunders… - Journal of …, 2016 - Wiley Online Library
A characteristic of many neurodegenerative diseases, including Alzheimer's disease (AD),
Parkinson's disease (PD), Huntington's disease (HD), and amyotrophic lateral sclerosis …

Small heat-shock proteins: important players in regulating cellular proteostasis

TM Treweek, S Meehan, H Ecroyd… - Cellular and molecular life …, 2015 - Springer
Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone
proteins that play a critical role in mitigating and preventing protein aggregation under stress …

The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity

GKA Hochberg, H Ecroyd, C Liu… - Proceedings of the …, 2014 - National Acad Sciences
Mammalian small heat-shock proteins (sHSPs) are molecular chaperones that form
polydisperse and dynamic complexes with target proteins, serving as a first line of defense …

[HTML][HTML] The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity

D Cox, DR Whiten, JWP Brown, MH Horrocks… - Journal of Biological …, 2018 - ASBMB
Proteostasis, or protein homeostasis, encompasses the maintenance of the conformational
and functional integrity of the proteome and involves an integrated network of cellular …

[HTML][HTML] Small heat-shock proteins prevent α-synuclein aggregation via transient interactions and their efficacy is affected by the rate of aggregation

D Cox, E Selig, MDW Griffin, JA Carver… - Journal of Biological …, 2016 - ASBMB
The aggregation of α-synuclein (α-syn) into amyloid fibrils is associated with
neurodegenerative diseases, collectively referred to as the α-synucleinopathies. In vivo …

Advances in the characterization of RNA‐binding proteins

D Marchese, NS de Groot… - Wiley …, 2016 - Wiley Online Library
From transcription, to transport, storage, and translation, RNA depends on association with
different RNA‐binding proteins (RBPs). Methods based on next‐generation sequencing and …

Chaperones in neurodegeneration

I Lindberg, J Shorter, RL Wiseman, F Chiti… - Journal of …, 2015 - Soc Neuroscience
Cellular protein homeostasis (proteostasis) maintains the integrity of the proteome and
includes protein synthesis, folding, oligomerization, and turnover; chaperone proteins assist …

Neurodegenerative diseases: their onset, epidemiology, causes and treatment

S Zaib, H Javed, I Khan, F Jaber, A Sohail… - …, 2023 - Wiley Online Library
Neurodegenerative diseases are a group of diseases with several neuropathological
symptoms. Degenerative nerve diseases can be serious or life‐threatening. Because of the …

Gallic acid interacts with α-synuclein to prevent the structural collapse necessary for its aggregation

Y Liu, JA Carver, AN Calabrese, TL Pukala - Biochimica et Biophysica Acta …, 2014 - Elsevier
The accumulation of protein aggregates containing amyloid fibrils, with α-synuclein being
the main component, is a pathological hallmark of Parkinson's disease (PD). Molecules …