[HTML][HTML] Degradation of proteins by PROTACs and other strategies

Y Wang, X Jiang, F Feng, W Liu, H Sun - Acta Pharmaceutica Sinica B, 2020 - Elsevier
Blocking the biological functions of scaffold proteins and aggregated proteins is a
challenging goal. PROTAC proteolysis-targeting chimaera (PROTAC) technology may be …

[PDF][PDF] Chaperone-mediated protein disaggregation triggers proteolytic clearance of intra-nuclear protein inclusions

F den Brave, LV Cairo, C Jagadeesan… - Cell reports, 2020 - cell.com
The formation of insoluble inclusions in the cytosol and nucleus is associated with impaired
protein homeostasis and is a hallmark of several neurodegenerative diseases. Due to the …

[HTML][HTML] Spatial organization of proteasome aggregates in the regulation of proteasome homeostasis

O Karmon, S Ben Aroya - Frontiers in Molecular Biosciences, 2020 - frontiersin.org
Misfolded proteins and insoluble aggregates are continuously produced in the cell and can
result in severe stress that threatens cellular fitness and viability if not managed effectively …

Hsp90 and its co-chaperone Sti1 control TDP-43 misfolding and toxicity

LTW Lin, A Razzaq, SE Di Gregorio, S Hong, B Charles… - bioRxiv, 2020 - biorxiv.org
Protein misfolding is a central feature of most neurodegenerative diseases. Molecular
chaperones can modulate the toxicity associated with protein misfolding, but it remains …

[HTML][HTML] Folliculin variants linked to Birt-Hogg-Dubé syndrome are targeted for proteasomal degradation

L Clausen, A Stein, M Grønbæk-Thygesen… - PLoS …, 2020 - journals.plos.org
Germline mutations in the folliculin (FLCN) tumor suppressor gene are linked to Birt-Hogg-
Dubé (BHD) syndrome, a dominantly inherited genetic disease characterized by …

The extent of Ssa1/Ssa2 Hsp70 chaperone involvement in nuclear protein quality control degradation varies with the substrate

RD Jones, C Enam, R Ibarra, HR Borror… - Molecular Biology of …, 2020 - Am Soc Cell Biol
Protein misfolding is a recurring phenomenon that cells must manage; otherwise misfolded
proteins can aggregate and become toxic should they persist. To counter this burden, cells …

[HTML][HTML] Releasing the lockdown: an emerging role for the ubiquitin-proteasome system in the breakdown of transient protein inclusions

Y Reiss, E Gur, T Ravid - Biomolecules, 2020 - mdpi.com
Intracellular protein inclusions are diverse cellular entities with distinct biological properties.
They vary in their protein content, sequestration sites, physiological function, conditions for …

Dual cooperation between HSP70 and the 26S proteasome in co-translational protein quality control

G Tian, C Hu, Y Yun, W Yang, W Dubiel, Y Cheng… - bioRxiv, 2020 - biorxiv.org
Co-translational degradation via the ubiquitin-proteasome system mediates quality control of
15–25% of nascent proteins, a proportion that is known to increase dramatically as a result …

[图书][B] Identifying Mechanisms of Regulation and Signal Integration of the Heat Shock Response

B Alford - 2020 - search.proquest.com
The heat shock response (HSR) is the cell's primary response to cytosolic misfolded protein.
It is conserved across eukaryotes and is essential for cell survival. How cells detect …

[图书][B] Redox regulation of mitochondrial responses in denervated and ageing skeletal muscle

M Scalabrin - 2020 - search.proquest.com
Sarcopenia is a characteristic of ageing where a substantial reduction of muscle tissue,
strength and function are seen (Baumann et al, 2016). Previous reports have suggested that …