Results 81 to 90 of about 21,311 (187)
Phylogenetic Relationship of Bombyx mori Protein Disulfide Isomerase
A cDNA that encodes protein disulfide isomerase was isolated from Bombyx mori (bPDI), in which an open reading frame of 494 amino acids contained two PDI-typical thioredoxin active sites of WCGHCK and an ER retention signal of the KDEL motif at its C-terminal. The bPDI protein shared less than 55% of the amino acid sequence homology with other reported
Tae Won, Goo +5 more
openaire +2 more sources
ABSTRACT In bread wheat (Triticum aestivum L.), cysteine (Cys) residues within the N‐ and C‐termini of high‐molecular‐weight glutenin subunits (HMW‐GSs) critically influence dough quality. However, the functional significance of Cys residue in their central repeat domain (CRD) remains unclear.
Bo Wei +16 more
wiley +1 more source
Protein disulfide isomerase (PDI) catalyzes the conversion of thiol-disulfide and plays an important role in various physiological events in animals. A PDI (OaPDI) from a tropical plant was detailed studied and it was found to be involved in response of ...
Zhengrong Zhang +5 more
doaj +1 more source
Stability and Conformational Resilience of Protein Disulfide Isomerase
Protein disulfide isomerase (PDI) is a redox-dependent protein with oxidoreductase and chaperone activities. It is a U-shaped protein with an abb'xa' structural organization in which the a and a' domains have CGHC active sites, the b and b' domains are involved with substrate binding, and x is a flexible linker. PDI exhibits substantial flexibility and
Jessica Guyette +3 more
openaire +3 more sources
ABSTRACT Over the past four decades, substantial research has investigated the regulation of ovarian maturation and spawning in the black tiger prawn (Penaeus monodon). In this species, female reproduction is strongly suppressed by gonad‐inhibiting hormone (GIH) released from the eyestalk, making eyestalk ablation (ESA) the most widely adopted spawning‐
Gourab Chowdhury +4 more
wiley +1 more source
Folding of peptides and proteins: role of disulfide bonds, recent developments
Disulfide-containing proteins are ideal models for studies of protein folding as the folding intermediates can be observed, trapped, and separated by HPLC during the folding reaction.
Hidaka Yuji, Shimamoto Shigeru
doaj +1 more source
Protein disulfide isomerases (PDIs), a family of thiol-disulfide oxidoreductases that are ubiquitous in all eukaryotes, are the principal catalysts for disulfide bond formation. Here, we investigated three rice (Oryza sativa) PDI family members (PDIL1;1,
Yayoi Onda, Yohei Kobori
doaj +1 more source
Role of Septin7 in mitochondrial dynamics and oxidative metabolism in C2C12 skeletal muscle cells
Abstract figure legend Knockdown of Septin7 alters the expression of markers responsible for mitochondrial dynamics. Members of the electron transport chain are also affected by diminished Septin7 level resulting in functional changes of mitochondrial respiration. Abstract Mitochondria are dynamic organelles that undergo fusion and fission.
Andrea Telek +13 more
wiley +1 more source
Thiol isomerases are a family of enzymes that participate in oxidative protein folding. They contain highly reactive vicinal thiols in a CXXC motif within their catalytic domains to mediate thiol-disulfide switching as part of their reductase, oxidase ...
Osamede C. Owegie +3 more
doaj +1 more source

