Results 61 to 70 of about 83,408 (297)
Functional Differences in Yeast Protein Disulfide Isomerases [PDF]
PDI1 is the essential gene encoding protein disulfide isomerase in yeast. The Saccharomyces cerevisiae genome, however, contains four other nonessential genes with homology to PDI1: MPD1, MPD2, EUG1, and EPS1. We have investigated the effects of simultaneous deletions of these genes. In several cases, we found that the ability of the PDI1 homologues to
Jakob R. Winther+5 more
openaire +3 more sources
The Interplay between Chemistry and Mechanics in the Transduction of a Mechanical Signal into a Biochemical Function [PDF]
There are many processes in biology in which mechanical forces are generated. Force-bearing networks can transduce locally developed mechanical signals very extensively over different parts of the cell or tissues.
Ainavarapu+152 more
core +1 more source
Due to their high biological activity, thiosemicarbazones have been developed for treatment of diverse diseases, including cancer, resulting in multiple clinical trials especially of the lead compound Triapine.
Sonja Hager+16 more
semanticscholar +1 more source
Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space [PDF]
Mitochondria are organelles that play a central role in cellular metabolism, as they are responsible for processes such as iron/sulfur cluster biogenesis, respiration and apoptosis.
MacPherson, Lisa+2 more
core +1 more source
Oxidative Protein-Folding Systems in Plant Cells
Plants are unique among eukaryotes in having evolved organelles: the protein storage vacuole, protein body, and chloroplast. Disulfide transfer pathways that function in the endoplasmic reticulum (ER) and chloroplasts of plants play critical roles in the
Yayoi Onda
doaj +1 more source
DsbG, a Protein Disulfide Isomerase with Chaperone Activity [PDF]
DsbG, a protein disulfide isomerase present in the periplasm of Escherichia coli, is shown to function as a molecular chaperone. Stoichiometric amounts of DsbG are sufficient to prevent the thermal aggregation of two classical chaperone substrate proteins, citrate synthase and luciferase.
James C.A. Bardwell+3 more
openaire +3 more sources
Background Disulfide bonds are one of the most common post-translational modifications found in proteins. The production of proteins that contain native disulfide bonds is challenging, especially on a large scale.
Enlund Eveliina+5 more
doaj +1 more source
The Unfolded Protein Response and the Role of Protein Disulfide Isomerase in Neurodegeneration
The maintenance and regulation of proteostasis is a critical function for post-mitotic neurons and its dysregulation is increasingly implicated in neurodegenerative diseases. Despite having different clinical manifestations, these disorders share similar
E. Perri+4 more
semanticscholar +1 more source
Identification of Protein-disulfide Isomerase Activity in Fibronectin [PDF]
Assembly and degradation of fibronectin-containing extracellular matrices are dynamic processes that are up-regulated during wound healing, embryogenesis, and metastasis. Although several of the early steps leading to fibronectin deposition have been identified, the mechanisms leading to the accumulation of fibronectin in disulfide-stabilized multimers
Kurt J. Langenbach, Jane Sottile
openaire +3 more sources
Orphan proteins of unknown function in the mitochondrial intermembrane space proteome: new pathways and metabolic cross-talk [PDF]
The mitochondrial intermembrane space (IMS) is involved in protein transport, lipid homeostasis and metal ion exchange, while further acting in signalling pathways such as apoptosis.
Manganas, Phanee+2 more
core +1 more source