Results 131 to 140 of about 3,418,558 (223)
The assembly of the beta-barrel proteins present in the outer membrane (OM) of Gram-negative bacteria is poorly characterized. After translocation across the inner membrane, unfolded beta-barrel proteins are escorted across the periplasm by chaperones ...
Denoncin, Katleen +7 more
core +1 more source
Cloning, expression, purification and characterization of Leishmania tropica PDI-2 protein
In Leishmania species, protein disulfide isomerase (PDI) is an essential enzyme that catalyzes thiol-disulfide interchange. The present work describes the isolation, cloning, sequencing and expression of the pdI-2 gene.
Ali Dina +3 more
doaj +1 more source
Estimation of Protein Disulfide-isomerase Activity : Based on Protein Refolding [PDF]
application/pdfProtein disulfide-isomerase (PDI) is associated with the refolding of proteins that have mis-matched disulfide bonds through the thiol-disulfide interchange reaction.
Taguchi, Hiroshi +7 more
core +1 more source
Disturbed flow regulates protein disulfide isomerase A1 expression via microRNA-204
Redox processes can modulate vascular pathophysiology. The endoplasmic reticulum redox chaperone protein disulfide isomerase A1 (PDIA1) is overexpressed during vascular proliferative diseases, regulating thrombus formation, endoplasmic reticulum stress ...
Leonardo Y. Tanaka +7 more
doaj +1 more source
Background Classic Philadelphia-negative myeloproliferative neoplasms (MPNs), such as polycythemia vera (PV), essential thrombocythemia (ET), and myelofibrosis (MF), are defined by the unregulated production of bone marrow components resulting from the ...
Marwa Salah Mohammed +7 more
doaj +1 more source
The isolation and purification to electrophoretical homogeneity and characterization of a protein disulfide isomerase from rat liver mitochondria is reported.
RIGOBELLO, MARIA PIA +3 more
core +1 more source
The smallest Protein Disulfide Isomerase-like protein from Arabidopsis thaliana
Thiol-disulfide oxidoreductases are the principal actors of oxidative protein folding in the endoplasmic reticulum (ER). Due to the presence of at least one thioredoxin (TRX) domain containing the catalytic active CXXC motif, these proteins belong to the
ALDO CERIOTTI +2 more
core
Molecular mechanisms of protein disulfide isomerase antagonism by punicalagin. [PDF]
Owegie OC +10 more
europepmc +1 more source
Protein Disulfide Isomerase and Assisted Protein Folding [PDF]
openaire +2 more sources
The protein disulfide isomerase P4HB/PDIA1 modulates cellular and misfolded forms of the prion protein. [PDF]
Amano G +4 more
europepmc +1 more source

