How do J-proteins get Hsp70 to do so many different things?

EA Craig, J Marszalek - Trends in biochemical sciences, 2017 - cell.com
Hsp70 chaperone machineries have pivotal roles in an array of fundamental biological
processes through their facilitation of protein folding, disaggregation, and remodeling. The …

Restricted access: spatial sequestration of damaged proteins during stress and aging

SM Hill, S Hanzén, T Nyström - EMBO reports, 2017 - embopress.org
The accumulation of damaged and aggregated proteins is a hallmark of aging and
increased proteotoxic stress. To limit the toxicity of damaged and aggregated proteins and to …

[HTML][HTML] Role of sHsps in organizing cytosolic protein aggregation and disaggregation

A Mogk, B Bukau - Cell Stress and Chaperones, 2017 - Elsevier
Small heat shock proteins (sHsps) exhibit an ATP-independent chaperone activity to prevent
the aggregation of misfolded proteins in vitro. The seemingly conflicting presence of sHsps …

ER stress causes widespread protein aggregation and prion formation

N Hamdan, P Kritsiligkou, CM Grant - Journal of Cell Biology, 2017 - rupress.org
Disturbances in endoplasmic reticulum (ER) homeostasis create a condition termed ER
stress. This activates the unfolded protein response (UPR), which alters the expression of …

Repair or destruction—an intimate liaison between ubiquitin ligases and molecular chaperones in proteostasis

É Kevei, W Pokrzywa, T Hoppe - Febs Letters, 2017 - Wiley Online Library
Cellular differentiation, developmental processes, and environmental factors challenge the
integrity of the proteome in every eukaryotic cell. The maintenance of protein homeostasis …

Kinetics of protein aggregates disposal by aggrephagy

S Tan, E Wong - Methods in enzymology, 2017 - Elsevier
Macroautophagy has generated considerable interest because of its ability to recognize and
target protein inclusions found prevalent in neurodegenerative diseases to lysosomes for …

Power provides protection: Genetic robustness in yeast depends on the capacity to generate energy

M Plech, K Tomala, H Tutaj, DE Piwcewicz… - PLoS …, 2017 - journals.plos.org
The functional basis of genetic robustness, the ability of organisms to suppress the effects of
mutations, remains incompletely understood. We exposed a set of 15 strains of …

On protein quality control, myofibrillar myopathies, and neurodegeneration

M Meister - 2017 - research.rug.nl
Proteins are the building blocks of cells and need to be folded into pre-determined 3-
dimensional shapes in order to fulfil their functions. In order to control the folding states of its …

20S proteasome assembly: alternative pathways and complexes

LJ Hammack - 2017 - search.proquest.com
The ubiquitin-proteasome system is responsible for the targeted degradation of proteins
within the cell. The 26S proteasome, which is the protease of this system, is a high molecular …

Aggrephagy

S Tan, E Wong - Autophagy and Signaling, 2017 - taylorfrancis.com
Formation of pathological protein inclusions involves aggregation of mutant or misfolded
proteins. Different types of aggregation-prone proteins are associated with different forms of …