Results 121 to 130 of about 83,411 (273)
The flexibility and dynamics of protein disulfide isomerase
Proteins: Structure, Function, and Bioinformatics, 2016 We have studied the mobility of the multidomain folding catalyst, protein disulfide isomerase (PDI), by a coarse‐graining approach based on flexibility.
R. Römer +5 more
semanticscholar +1 more source
Prompting Fab Yeast Surface Display Efficiency by ER Retention and Molecular Chaperon Co-expression. [PDF]
, 2019 For antibody discovery and engineering, yeast surface display (YSD) of antigen-binding fragments (Fabs) and coupled fluorescence activated cell sorting (FACS) provide intact paratopic conformations and quantitative analysis at the monoclonal level, and ...
Ge, Xin +7 more
core
The MIA pathway: a key regulator of mitochondrial oxidative protein folding and biogenesis [PDF]
, 2015 Mitochondria are fundamental intracellular organelles with key roles in important cellular processes like energy production, Fe/S cluster biogenesis, and homeostasis of lipids and inorganic ions.
Mordas, Amelia, Tokatlidis, Konstantinos
core +2 more sources
Protein disulfide isomerase in thrombosis and vascular inflammation [PDF]
Journal of Thrombosis and Haemostasis, 2013 Protein disulfide isomerase (PDI) catalyzes disulfide bond oxidation, reduction and isomerization during protein synthesis in the endoplasmic reticulum (ER). In addition to its critical role in the ER, in vitro and in vivo studies with blocking antibodies and conditional knockout mice have demonstrated that cell surface PDI is required for thrombosis ...
openaire +3 more sources
Folding of peptides and proteins: role of disulfide bonds, recent developments
Biomolecular Concepts, 2013 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
Therapeutic implications of protein disulfide isomerase inhibition in thrombotic disease.
Arteriosclerosis, Thrombosis and Vascular Biology, 2015 The study of thrombus formation has increasingly applied in vivo tools such as genetically modified mice and intravital microscopy to the evaluation of molecular and cellular mechanisms of thrombosis.
R. Flaumenhaft, B. Furie, J. Zwicker
semanticscholar +1 more source
Impaired Cleavage of Preproinsulin Signal Peptide Linked to Autosomal-Dominant Diabetes [PDF]
, 2012 Recently, missense mutations upstream of preproinsulin’s signal peptide (SP) cleavage site were reported to cause mutant INS gene-induced diabetes of youth (MIDY).
Arvan, Peter +8 more
core +1 more source
FEBS Open Bio, 2014 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
Lack of an efficient endoplasmic reticulum-localized recycling system protects peroxiredoxin IV from hyperoxidation [PDF]
, 2014 Typical 2-cys peroxiredoxins are required to remove hydrogen peroxide from several different cellular compartments. Their activity can be regulated by hyperoxidation and consequent inactivation of the active site peroxidatic cysteine.
Bulleid, Neil J. +2 more
core +1 more source
iScience, 2021 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