[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 …
Facing and overcoming sensitivity challenges in biomolecular NMR spectroscopy
In the Spring of 2013, NMR spectroscopists convened at the Weizmann Institute in Israel to
brainstorm on approaches to improve the sensitivity of NMR experiments, particularly when …
brainstorm on approaches to improve the sensitivity of NMR experiments, particularly when …
13C Direct Detected NMR for Challenging Systems
Thanks to recent improvements in NMR spectrometer hardware and pulse sequence design,
modern 13C NMR has become a useful tool for biomolecular applications. The complete …
modern 13C NMR has become a useful tool for biomolecular applications. The complete …
The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client
A Mainz, J Peschek, M Stavropoulou, KC Back… - Nature structural & …, 2015 - nature.com
Small heat-shock proteins, including αB-crystallin (αB), play an important part in protein
homeostasis, because their ATP-independent chaperone activity inhibits uncontrolled …
homeostasis, because their ATP-independent chaperone activity inhibits uncontrolled …
Mechanisms of small heat shock proteins
MK Janowska, HER Baughman… - Cold Spring …, 2019 - cshperspectives.cshlp.org
Small heat shock proteins (sHSPs) are ATP-independent chaperones that delay formation of
harmful protein aggregates. sHSPs' role in protein homeostasis has been appreciated for …
harmful protein aggregates. sHSPs' role in protein homeostasis has been appreciated for …
Local unfolding of the HSP27 monomer regulates chaperone activity
The small heat-shock protein HSP27 is a redox-sensitive molecular chaperone that is
expressed throughout the human body. Here, we describe redox-induced changes to the …
expressed throughout the human body. Here, we describe redox-induced changes to the …
Neuromuscular diseases due to chaperone mutations: a review and some new results
J Sarparanta, PH Jonson, S Kawan, B Udd - International journal of …, 2020 - mdpi.com
Skeletal muscle and the nervous system depend on efficient protein quality control, and they
express chaperones and cochaperones at high levels to maintain protein homeostasis …
express chaperones and cochaperones at high levels to maintain protein homeostasis …
Environmental factors modulating protein conformations and their role in protein aggregation diseases
The adverse physiological conditions have been long known to impact protein synthesis,
folding and functionality. Major physiological factors such as the effect of pH, temperature …
folding and functionality. Major physiological factors such as the effect of pH, temperature …
α-Crystallins in the vertebrate eye lens: Complex oligomers and molecular chaperones
MA Sprague-Piercy, MA Rocha… - Annual review of …, 2021 - annualreviews.org
α-Crystallins are small heat-shock proteins that act as holdase chaperones. In humans, αA-
crystallin is expressed only in the eye lens, while αB-crystallin is found in many tissues. α …
crystallin is expressed only in the eye lens, while αB-crystallin is found in many tissues. α …
Structure and function of α-crystallins: Traversing from in vitro to in vivo
Background The two α-crystallins (αA-and αB-crystallin) are major components of our eye
lenses. Their key function there is to preserve lens transparency which is a challenging task …
lenses. Their key function there is to preserve lens transparency which is a challenging task …