Results 251 to 260 of about 1,426,666 (312)
A new glucocerebrosidase chaperone reduces α-synuclein and glycolipid levels in iPSC-derived dopaminergic neurons from patients with gaucher disease and parkinsonism [PDF]
et al, +3 more
core +1 more source
Pleiotropic Role of the RNA Chaperone Protein Hfq in the Human Pathogen Clostridium difficile
P. Boudry +12 more
semanticscholar +1 more source
Heat Stress Triggers Nuclear Invagination and Spatial Compartmentalization of Protein Metabolism
Cells adapt heat stress to shape a nuclear invagination region function as “protein metabolism hotspots”, where both protein production and degradation are enhanced. ABSTRACT Heat stress is a common challenge for cells, causing multiple types of cellular damage while triggering complex stress responses, including the highly conserved mechanism known as
Zhi‐Hao Zhang +11 more
wiley +1 more source
Dissection of Mitochondrial Function via Chemical Perturbation and Single‐Cell Profiling
We establish a systematic framework to dissect mitochondrial function at the module level by combining targeted chemical perturbations with scRNA‐seq. This approach reveals shared and module‐specific programs linking mitochondrial activity to mito‐nuclear communication, stress response, and cell cycle, highlighting the tight coupling between ...
Hao Luo +4 more
wiley +1 more source
RNA melting and RNA chaperone activities of plant cold shock domain proteins are not correlated. [PDF]
Zlobin N +4 more
europepmc +1 more source
The ALS‐associated E425K mutation uncouples DNAJC7 from the Hsp70 chaperone cycle
DNAJC7 is a J‐domain protein that plays a key role in protein quality control by regulating Hsp70 activity and preventing protein aggregation. We find that the ALS‐associated E425K mutation in DNAJC7 disrupts productive interaction and activation of Hsp70, thereby blocking the transfer and refolding of client proteins such as TDP‐43.
Bar Elmaleh +2 more
wiley +1 more source
Congenital dyserythropoietic anemia type I (CDA‐I) arises from mutations in Codanin1 and CDIN1. Using quantitative biophysical approaches, we show that disease‐associated mutations disrupt the CDIN1‐Codanin1 complex. Our findings provide critical insights into the molecular mechanism that links protein dysfunction to disturbing chromatin arrangement ...
Martin Stojaspal +8 more
wiley +1 more source
Proteostasis ensures proper protein folding, modification, and degradation, while its impairment triggers ER stress. Chronic ER stress and maladaptive UPR via the CHOP–ERO1 axis remodel ERMCs, altering calcium signaling and mitochondrial metabolism.
Giorgia Maria Renna +5 more
wiley +1 more source

