Search Results - "Noiva, R"

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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Protein disulfide isomerase assisted protein folding in malaria parasites by Mahajan, B., Noiva, R., Yadava, A., Zheng, H., Majam, V., Mohan, K.V. Krishna, Moch, J.K., Haynes, J.D., Nakhasi, H., Kumar, S.

“…In eukaryotes, the formation of protein disulfide bonds among cysteine residues is mediated by protein disulfide isomerases and occurs in the highly oxidised…”
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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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The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase by PUIG, A, LYLES, M. M, NOIVA, R, GILBERT, H. F

“…The complexity of protein folding is often aggravated by the low solubility of the denatured state. The inefficiency of the oxidative refolding of reduced,…”
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Retrospective Study of Forensic Necropsies performed at the Faculty of Veterinary Medicine of the University of Lisbon between 2014 AND 2022 by Rafael, M.I., Noiva, R., Afonso, F., Ferreira da Silva, J., Peleteiro, M.C., Moreira, A., Correia, J., Pissarra, H.

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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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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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Cellular Immunophenotypic Characteristics in a Case of Extramedullary Haematopoiesis in a Goeldi's Monkey (Callimico goeldii) by Noiva, R., Pissarra, H., Fernandes, T., Bernardino, R., Peleteiro, C.

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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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Selenium concentrations in plasma of patients with arteriographically defined coronary atherosclerosis by Moore, J A, Noiva, R, Wells, I C

“…A prospective epidemiological study (Lancet ii: 175-179, 1982) implicates low concentrations of selenium in plasma in coronary atherogenesis. We examined this…”
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New Insights into the Importance of Rodent Populations in a Zoo Ecosystem in the Pathology and Spread of Calodium hepaticum in Primates by Correia, J., Crespo, A., Noiva, R., Pissarra, H., Fernandes, T., Bernardino, R., Afonso, F., Lapão, N., Vaz, Y., Carvalho, L., Peleteiro, C.

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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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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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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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