Results 81 to 90 of about 86,419 (320)
Nanoscale Mapping of the Subcellular Glycosylation Landscape
Using multiplexed super‐resolution imaging with fluorophore‐labeled lectins, this study reports intracellular glycosylation at the nanoscale across organelles and synaptic specializations. Extending glycan analysis beyond the cell surface, Glyco‐STORM reveals distinct glycosylation nanodomains in the ER, Golgi, lysosomes, and synaptic sites.
Helene Gregoria Schroeter +4 more
wiley +1 more source
High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility [PDF]
ERp27 (endoplasmic reticulum protein 27.7 kDa) is a homologue of PDI (protein disulfide-isomerase) localized to the endoplasmic reticulum. ERp27 is predicted to consist of two thioredoxinfold domains homologous with the non-catalytic b and b domains of ...
A. Katrine Wallis +52 more
core +4 more sources
Protein disulfide isomerase (PDI), secreted by platelets and endothelial cells on vascular injury, is required for thrombus formation. Using PDI variants that form mixed disulfide complexes with their substrates, we identify by kinetic trapping multiple ...
semanticscholar +1 more source
This study investigates the role of M2 macrophage‐derived extracellular vesicles (M2 EVs) in prostate cancer (PCa) metastasis. Mechanistically, M2 EVs horizontally transfer TXNDC5 mRNA to PCa cells, where the molecule induces the mesenchymal‐like state (MLS), enhancing PCa migration and invasion.
Cong Hu +14 more
wiley +1 more source
Summary: The mammalian endoplasmic reticulum (ER) harbors more than 20 members of the protein disulfide isomerase (PDI) family that act to maintain proteostasis.
Chihiro Hirayama +7 more
doaj +1 more source
Engineered Pathways for Correct Disulfide Bond Oxidation [PDF]
Correct formation of disulfide bonds is critical for protein folding. We find that cells lacking protein disulfide isomerases (PDIs) can use alternative mechanisms for correct disulfide bond formation.
Bardwell, James C. A., Ren, Guoping
core +2 more sources
Characterization of an A-Site Selective Protein Disulfide Isomerase A1 Inhibitor.
Protein disulfide isomerase A1 (PDIA1) is an endoplasmic reticulum (ER)-localized thiol-disulfide oxidoreductase that is an important folding catalyst for secretory pathway proteins.
Kyle S. Cole +7 more
semanticscholar +1 more source
Dual genetic strategies for improving wheat processing quality by regulating purothionin accumulation to modulate gluten quantity and quality. The first strategy involves targeting signal peptide (SP) cleavage sites (e.g., through mutation) to indirectly reduce gluten content, thereby disrupting gluten network formation.
Yijie Liu +16 more
wiley +1 more source
Biosynthesis and enzymology of the Caenorhabditis elegans cuticle: identification and characterization of a novel serine protease inhibitor. [PDF]
The nematode Caenorhabditis elegans represents an excellent model in which to examine nematode gene expression and function. A completed genome, straightforward transgenesis, available mutants and practical genome-wide RNAi approaches provide an ...
Andrew J. Birnie +42 more
core +1 more source
In this manuscript, protein disulfide isomerase A3 (PDIA3) is identified as a key factor mediating the susceptibility of ferroptosis in GBM. Inhibition of PDIA3 enhances IKE or cystine starvation‐induced ferroptosis in GBM cells by resulting in the accumulation of lipid peroxidation and a reduction in GSH level.
Jie Zhang +19 more
wiley +1 more source

