R
Robert Noiva
Researcher at University of South Dakota
Publications - 9
Citations - 1460
Robert Noiva is an academic researcher from University of South Dakota. The author has contributed to research in topics: Protein disulfide-isomerase & Endoplasmic reticulum. The author has an hindex of 9, co-authored 9 publications receiving 1432 citations.
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Journal ArticleDOI
The Crystal Structure of Yeast Protein Disulfide Isomerase Suggests Cooperativity between Its Active Sites
TL;DR: Biochemical studies demonstrate that all domains of PDI, including the C-terminal tail, are required for full catalytic activity and defines a framework for rationalizing the differences between the two active sites and their respective roles in catalyzing the formation and rearrangement of disulfide bonds.
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Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum.
Robert Noiva,W J Lennarz +1 more
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Protein disulfide isomerase: the multifunctional redox chaperone of the endoplasmic reticulum.
TL;DR: Protein disulfide isomerase is a protein-thiol oxidoreductase that catalyzes the oxidation, reduction and isomerization of protein disulfides that has been demonstrated to participate in the regulation of reception function, cell-cell interaction, gene expression, and actin filament polymerization.
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Secretion, surface localization, turnover, and steady state expression of protein disulfide isomerase in rat hepatocytes.
Kunihiko Terada,Parthasarathi Manchikalapudi,Robert Noiva,Hugo O. Jauregui,Richard J. Stockert,Michael L. Schilsky +5 more
TL;DR: Though localized mainly in microsomal fractions of hepatocytes, direct immunofluorescence and cell surface radioiodination followed by immunoprecipitation revealed the presence of M 57,000 disulfide isomerase at the cell surface.
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Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites.
TL;DR: The peptide binding site is located in the COOH-terminal domain of the protein, and it is distinct from the two active sites for PDI-catalyzed disulfide isomerization and from the region of PDI that has estrogen receptor sequence similarity.