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
Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast. [PDF]
MaryLynne LaMantia+5 more
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Extracellular pools of intracellular molecular chaperones are increasingly evident. The peri/epicellular(pec) pool of the endoplasmic reticulum redox chaperone protein disulfide isomerase-A1(PDI) is involved in thrombosis and vascular remodeling, while ...
Thaís L.S. Araujo+2 more
doaj
A Common Binding Site on the Microsomal Triglyceride Transfer Protein for Apolipoprotein B and Protein Disulfide Isomerase [PDF]
Paul Bradbury+12 more
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Glutaredoxin Accelerates Glutathione-dependent Folding of Reduced Ribonuclease A Together with Protein Disulfide-isomerase [PDF]
Johanna Lundström-Ljung, Arne Holmgren
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Kinetic Analysis of the Mechanism and Specificity of Protein-disulfide Isomerase Using Fluorescence-quenched Peptides [PDF]
Vibeke Westphal+4 more
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The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules [PDF]
Johan Kemmink+4 more
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nDsbD: a redox interaction hub in the Escherichia coli periplasm [PDF]
.: DsbD is a redox-active protein of the inner Escherichia coli membrane possessing an N-terminal (nDsbD) and a C-terminal (cDsbD) periplasmic domain. nDsbD interacts with four different redox proteins involved in the periplasmic disulfide isomerization ...
Capitani, G.+3 more
core
Two resident ER‐proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase [PDF]
Johanna Lundström-Ljung+4 more
openalex +1 more source