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Rotavirus-protein disulfide isomerase (zeige P4HB Proteine) interaction was demonstrated in vitro as well as inMA104 cells and intestinal villi from suckling mice.
Data show that diabetic mice had a worse postinfarction remodeling associated with (zeige DUT Proteine) an altered protein disulfide isomerase (PDI). redox state.
The absence of PDIp expression in pancreatic adenocarcinoma may serve as an additional biomarker for pancreatic cancer.
Elevated Pdi (zeige PDIA3 Proteine) expression is cis (zeige CISH Proteine) regulated and is not linked to diabetes susceptibility.
PDI (zeige PADI1 Proteine) overexpression is associated with Multiple Myeloma.
Tissue factor (zeige F3 Proteine)-regulated vascular smooth cell migration and microvessel formation is under the control of the ER-protein PDIA2.
It was found that PDI interacts with dengue virus nonstructural protein 1 (NS1) intracellularly as well as on the surface in the lipid raft domain.
Data show that cell surface disulfide isomerase (PDI (zeige P4HB Proteine)) expression and function regulate the capacity of natriuretic peptides to generate cyclic guanosine monophosphate (cGMP) through interaction with their receptors.
These results indicate that BPA (zeige DST Proteine), a widely distributed and potentially harmful chemical, inhibits Ero1-PDI (zeige PADI1 Proteine)-mediated disulfide bond formation.
PDI (zeige PADI1 Proteine) appears to regulate cytoskeletal reorganization by the thiol-disulfide exchange in beta-actin (zeige ACTB Proteine) via a redox-dependent mechanism.
Data indicate that protein disulfide isomerase (PDI (zeige P4HB Proteine)) and ERp44 (zeige ERP44 Proteine) dynamically localize Ero1alpha and peroxiredoxin 4 (zeige PRDX4 Proteine) in early secretory compartment (ESC).
GPx7 (zeige GPX7 Proteine) is an unusual CysGPx catalyzing the peroxidatic cycle by a one Cys (zeige DNAJC5 Proteine) mechanism in which GSH and PDI (zeige PADI1 Proteine) are alternative substrates.
Human major histocompatibility complex class 1 antigens (HLA-A,B,C) are potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation.
Data indicate that apoptosis induced by misfolded PrP (zeige C4BPA Proteine) proteins could be regulated by protein disulfide isomerase (PDI (zeige P4HB Proteine)) via mitochondrial dysfunction.
Protein disulfide isomerases (EC 22.214.171.124), such as PDIP, are endoplasmic reticulum (ER) resident proteins that catalyze protein folding and thiol-disulfide interchange reactions (Desilva et al., 1996
protein disulfide isomerase family A, member 2
, protein disulfide isomerase A2
, Protein disulfide-isomerase A2
, protein disulfide-isomerase A2-like
, protein disulfide isomerase (pancreas) like
, protein disulfide isomerase, pancreatic
, protein disulfide-isomerase A2
, Rho GDP dissociation inhibitor gamma
, pancreas-specific protein disulfide isomerase
, pancreatic protein disulfide isomerase
, protein disulfide isomerase-associated 2
, protein disulfide isomerase associated 2