Results 141 to 150 of about 83,411 (273)

Protein disulfide isomerase in Philadelphia-negative myeloproliferative neoplasms: a case–control study

open access: yesThe Egyptian Journal of Internal Medicine
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]

open access: green, 1991
MaryLynne LaMantia   +5 more
openalex   +1 more source

Golgi-independent routes support protein disulfide isomerase externalization in vascular smooth muscle cells

open access: yesRedox Biology, 2017
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]

open access: hybrid, 1999
Paul Bradbury   +12 more
openalex   +1 more source

Kinetic Analysis of the Mechanism and Specificity of Protein-disulfide Isomerase Using Fluorescence-quenched Peptides [PDF]

open access: hybrid, 1998
Vibeke Westphal   +4 more
openalex   +1 more source

The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules [PDF]

open access: bronze, 1997
Johan Kemmink   +4 more
openalex   +1 more source

nDsbD: a redox interaction hub in the Escherichia coli periplasm [PDF]

open access: yes, 2018
.: 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  

A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase.

open access: hybrid, 1987
Juha Koivu   +5 more
openalex   +1 more source

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