Results 41 to 50 of about 226,086 (342)
eLife, 2015 Eukaryotic cells possess a variety of signaling pathways that prevent accumulation of unfolded and misfolded proteins. Chief among these is the heat shock response (HSR), which is assumed to respond to unfolded proteins in the cytosol and nucleus alike ...
Yusuke Miyazaki +4 more
doaj +1 more source
The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases
Frontiers in Neuroscience, 2017 The accumulation of misfolded proteins in the human brain is one of the critical features of many neurodegenerative diseases, including Alzheimer's disease (AD). Assembles of beta-amyloid (Aβ) peptide—either soluble (oligomers) or insoluble (plaques) and
Rachel E. Lackie +7 more
semanticscholar +1 more source
Hematopoietic (stem) cells—The elixir of life?
FEBS Letters, EarlyView.The aging of HSCs (hematopoietic stem cells) and the blood system leads to the decline of other organs. Rejuvenating aged HSCs improves the function of the blood system, slowing the aging of the heart, kidney, brain, and liver, and the occurrence of age‐related diseases.
Emilie L. Cerezo +4 more
wiley +1 more source
eLife, 2015 RNA-protein (RNP) granules have been proposed to assemble by forming solid RNA/protein aggregates or through phase separation into a liquid RNA/protein phase. Which model describes RNP granules in living cells is still unclear.
Sonja Kroschwald +7 more
doaj +1 more source
Enzymes as chaperones and chaperones as enzymes
FEBS Letters, 1998 Chaperones and foldases are two groups of accessory proteins which assist maturation of nascent peptides into functional proteins in cells. Protein disulfide isomerase, a foldase, and ATP‐dependent proteases, responsible for degradation of misfolded proteins in cells, both have intrinsic chaperone activities.
Wang, Chih-Chen, Tsou, Chen-Lu
openaire +2 more sources
The role of histone modifications in transcription regulation upon DNA damage
FEBS Letters, EarlyView.This review discusses the critical role of histone modifications in regulating gene expression during the DNA damage response (DDR). By modulating chromatin structure and recruiting repair factors, these post‐translational modifications fine‐tune transcriptional programmes to maintain genomic stability.
Angelina Job Kolady, Siyao Wang
wiley +1 more source
Super Spy variants implicate flexibility in chaperone action
eLife, 2014 Experimental study of the role of disorder in protein function is challenging. It has been proposed that proteins utilize disordered regions in the adaptive recognition of their various binding partners.
Shu Quan +8 more
doaj +1 more source
Protein Aggregation in the ER: Calm behind the Storm
Cells, 2021 As one of the largest organelles in eukaryotic cells, the endoplasmic reticulum (ER) plays a vital role in the synthesis, folding, and assembly of secretory and membrane proteins.
Haisen Li, Shengyi Sun
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Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
Journal of Cell Biology, 2006 The voltage-dependent anion channel (VDAC) of the outer mitochondrial membrane mediates metabolic flow, Ca2+, and cell death signaling between the endoplasmic reticulum (ER) and mitochondrial networks.
G. Szabadkai +8 more
semanticscholar +1 more source
FEBS Letters, EarlyView.The Ile181Asn variant of human UDP‐xylose synthase (hUXS1), associated with a short‐stature genetic syndrome, has previously been reported as inactive. Our findings demonstrate that Ile181Asn‐hUXS1 retains catalytic activity similar to the wild‐type but exhibits reduced stability, a looser oligomeric state, and an increased tendency to precipitate ...
Tuo Li +2 more
wiley +1 more source