Results 91 to 100 of about 1,305,355 (298)
Differential Scales of Protein Quality Control [PDF]
Cell, 2014 Proteins are notorious for their unpleasant behavior-continually at risk of misfolding, collecting damage, aggregating, and causing toxicity and disease. To counter these challenges, cells have evolved elaborate chaperone and quality control networks that can resolve damage at the level of the protein, organelle, cell, or tissue. On the smallest scale,
Wolff, Suzanne +2 more
openaire +2 more sources
FEBS Letters, EarlyView.This study reveals how the mitochondrial protein Slm35 is regulated in Saccharomyces cerevisiae. The authors identify stress‐responsive DNA elements and two upstream open reading frames (uORFs) in the 5′ untranslated region of SLM35. One uORF restricts translation, and its mutation increases Slm35 protein levels and mitophagy.
Hernán Romo‐Casanueva +5 more
wiley +1 more source
Deceleration of fusion–fission cycles improves mitochondrial quality control during aging
, 2012 Mitochondrial dynamics and mitophagy play a key role in ensuring mitochondrial quality control. Impairment thereof was proposed to be causative to neurodegenerative diseases, diabetes, and cancer.
Michael Meyer-Hermann +18 more
core +1 more source
Defining the pathways involved in spatial protein quality control in Saccharomyces cerevisiae
, 2022 Proteins need to be folded into specific three-dimensional conformations to be functional. An extensive network of factors, the protein quality control (PQC) machinery, ensures that the cell maintains a healthy proteome by coordinating their synthesis ...
Schneider, Kara Linda
core +1 more source
FEBS Letters, EarlyView.We reconstituted Synechocystis glycogen synthesis in vitro from purified enzymes and showed that two GlgA isoenzymes produce glycogen with different architectures: GlgA1 yields denser, highly branched glycogen, whereas GlgA2 synthesizes longer, less‐branched chains.
Kenric Lee +3 more
wiley +1 more source
Endoplasmic Reticulum-Mediated Protein Quality Control in Arabidopsis
Frontiers in Plant Science, 2014 A correct three-dimensional structure is crucial for the physiological functions of a protein, yet the folding of proteins to acquire native conformation is a fundamentally error-prone process.
Jianming eLi, Yidan eLiu
doaj +1 more source
FEBS Letters, EarlyView.We identified a systemic, progressive loss of protein S‐glutathionylation—detected by nonreducing western blotting—alongside dysregulation of glutathione‐cycle enzymes in both neuronal and peripheral tissues of Taiwanese SMA mice. These alterations were partially rescued by SMN antisense oligonucleotide therapy, revealing persistent redox imbalance as ...
Sofia Vrettou, Brunhilde Wirth
wiley +1 more source
mBio, 2020 Chlamydia trachomatis is an obligate intracellular bacterium that undergoes a complex developmental cycle in which the bacterium differentiates between two functionally and morphologically distinct forms, the elementary body (EB) and reticulate body (RB),
Nicholas A. Wood +5 more
doaj +1 more source
Tau acetylation at K331 has limited impact on tau pathology in vivo
FEBS Letters, EarlyView.We mapped tau post‐translational modifications in humanized MAPT knock‐in mice and in amyloid‐bearing double knock‐in mice. Acetylation within the repeat domain, particularly around K331, showed modest increases under amyloid pathology. To test functional relevance, we generated MAPTK331Q knock‐in mice.
Shoko Hashimoto +3 more
wiley +1 more source
Calpain small subunit homodimerization is robust and calcium‐independent
FEBS Letters, EarlyView.Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy +4 more
wiley +1 more source