Search Results - "Noiva, Robert"

Protein disulfide isomerase: The multifunctional redox chaperone of the endoplasmic reticulum by Noiva, Robert

“…Protein disulfide isomerase (PDI) is a protein-thiol oxidoreductase that catalyzes the oxidation, reduction and isomerization of protein disulfides. In the…”
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The Crystal Structure of Yeast Protein Disulfide Isomerase Suggests Cooperativity between Its Active Sites by Tian, Geng, Xiang, Song, Noiva, Robert, Lennarz, William J., Schindelin, Hermann

“…Protein disulfide isomerase plays a key role in catalyzing the folding of secretory proteins. It features two catalytically inactive thioredoxin domains…”
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Conformational Remodeling of Proteasomal Substrates by PA700, the 19 S Regulatory Complex of the 26 S Proteasome by Liu, Chang-wei, Millen, Linda, Roman, Tracie B., Xiong, Hai, Gilbert, Hiram F., Noiva, Robert, DeMartino, George N., Thomas, Philip J.

“…PA700, the 19 S regulatory complex of the 26 S proteasome, plays a central role in the recognition and efficient degradation of misfolded proteins. PA700…”
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The Crystal Structure of Yeast Protein Disulfide Isomerase Suggests Cooperativity between Its Active Sites by Tian, Geng, Xiang, Song, Noiva, Robert, Lennarz, William J., Schindelin, Hermann

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An Atypical Protein Disulfide Isomerase from the Protozoan Parasite Leishmania Containing a Single Thioredoxin-like Domain by Padilla, Alejandro, Noiva, Robert, Lee, Nancy, Mohan, Ketha V. Krishna, Nakhasi, Hira L., Debrabant, Alain

“…In higher eukaryotes, secretory proteins are under the quality control of the endoplasmic reticulum for their proper folding and release into the secretory…”
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Secretion, Surface Localization, Turnover, and Steady State Expression of Protein Disulfide Isomerase in Rat Hepatocytes (∗) by Terada, Kunihiko, Manchikalapudi, Parthasarathi, Noiva, Robert, Jauregui, Hugo O., Stockert, Richard J., Schilsky, Michael L.

“…Protein disulfide isomerase in isolated rat hepatocytes was present at a concentration of 7 μg/mg cell protein, representing a ~2-fold enrichment compared to…”
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Novel Protein-disulfide Isomerases from the Early-diverging Protist Giardia lamblia by Knodler, Leigh A., Noiva, Robert, Mehta, Kapil, McCaffery, J. Michael, Aley, Stephen B., Svärd, Staffan G., Nystul, Todd G., Reiner, David S., Silberman, Jeffrey D., Gillin, Frances D.

“…Protein-disulfide isomerase is essential for formation and reshuffling of disulfide bonds during nascent protein folding in the endoplasmic reticulum. The two…”
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Oakland University William Beaumont School of Medicine by Ledford, Cynthia H., Pitts, Deirdre G., Thomas, David M., Taylor, Tracey A.H., Noiva, Robert, McAuley, Robert J., Mezwa, Duane G.

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Thyroid hormone binding protein contains glycosylation site binding protein activity by Kimura, H, Noiva, R, Mizunaga, T, Yamauchi, K, Horiuchi, R, Cheng, S Y, Lennarz, W J

“…Several lines of evidence provided by other workers indicate that within the same species thyroid hormone binding protein, the beta-subunit of prolyl…”
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Protein disulfide isomerase : a multifunctional protein resident in the lumen of the endoplasmic reticulum by NOIVA, R, LENNARZ, W. J

“…One subset of proteins resides in the lumen of the endoplasmic reticulum. The most abundant members of this subset are the glucose-regulated proteins, GRP-78…”
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Enzymatic catalysis of disulfide formation by Noiva, R

“…The formation of disulfide bridges in membrane and secretory proteins occurs during the protein folding process in the endoplasmic reticulum of eukaryotic…”
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Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kd luminal proteins of the ER by Geetha-Habib, M, Noiva, R, Kaplan, H A, Lennarz, W J

“…A 57 kd component of oligosaccharyl transferase, termed glycosylation site binding protein, specifically recognizes a photoaffinity probe containing the…”
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Novel protein-disulfide isomerases from the early-diverging protist giardia lamblia by Knodler, LA, Noiva, R, Mehta, K, McCaffery, JM, Aley, SB, Svard, SG, Nystul, TG, Reiner, DS, Silberman, JD, Gillin, FD

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Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites by NOIVA, R, FREEDMAN, R. B, LENNARZ, W. J

“…Protein disulfide isomerase (PDI) is a multifunctional protein resident in the lumen of the rough endoplasmic reticulum that facilitates protein folding via…”
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Peptide binding by protein disulfide isomerase, a resident protein of the endoplasmic reticulum lumen by Noiva, R, Kimura, H, Roos, J, Lennarz, W J

“…Previously we had demonstrated by photoaffinity labeling that a 57-kDa protein of the endoplasmic reticulum can bind and become covalently linked to…”
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Glycosylation Site-Binding Protein is Not Required for N-Linked Glycoprotein Synthesis by Noiva, Robert, Kaplan, Howard A., Lennarz, William J.

“…In prior studies we identified a 57-kDa protein in the lumen of the endoplasmic reticulum that, in addition to having both protein disulfide isomerase and…”
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Bovine serum hemopexin: properties of the protein from a single animal by Noiva, R, Pete, M J, Babin, D R

“…1. Hemopexin was isolated from bovine serum of a single animal in a yield of 0.5 mg/ml. 2. Bovine hemopexin was found to exist in two isoforms of mol. wt…”
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