Protein Disulfide Isomerase
Mostrando 1-12 de 101 artigos, teses e dissertações.
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1. Papel da dissulfeto isomerase proteica (PDI) na migração de células musculares lisas vasculares: possível envolvimento de Nox1 NADPH oxidase e RhoGTPases / The role of protein disulfide isomerase (PDI) in vascular smooth muscle cell migration: possible interaction with Nox1 NADPH oxidase and RhoGTPases
A migração de células musculares lisas (VSMC) da camada média do vaso para a íntima é essencial para vasculogênese e contribui para o processo de aterosclerose e estenose após lesão por cateter-balão, caracterizando-se como um importante alvo terapêutico. Diversos trabalhos já demonstraram que fatores de crescimento (como PDGF e FGF) estimulam a
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 03/02/2012
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2. Participation of the endoplasmic reticulum protein chaperone thio-oxidoreductase in gonadotropin-releasing hormone receptor expression at the plasma membrane
Chaperone members of the protein disulfide isomerase family can catalyze the thiol-disulfide exchange reaction with pairs of cysteines. There are 14 protein disulfide isomerase family members, but the ability to catalyze a thiol disulfide exchange reaction has not been demonstrated for all of them. Human endoplasmic reticulum protein chaperone thio-oxidoredu
Brazilian Journal of Medical and Biological Research. Publicado em: 2009-02
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3. Mecanismo da interação entre a proteína dissulfeto isomerase e a NADPH oxidase: papel regulatório sobre a produção de espécies reativas de oxigênio em fagócitos profissionais / Mechanisms involved in the interaction of protein disulfide isomerase with NADPH oxidase: regulatory role on the reactive oxygen species generation by professional phagocytes
INTRODUÇÃO: A ativação da NADPH oxidase de neutrófilos requer o acoplamento das subunidades citosólicas p47phox, p67phox, p40phox e Rac2 ao componente de membrana citocromo b558. Em trabalhos anteriores, nós mostramos que as isoformas vasculares da oxidase são reguladas pela proteína dissulfeto isomerase (PDI), uma chaperona redox. Neste trabalho, n
Publicado em: 2009
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4. Inibição do proteasoma aumenta o estresse oxidativo e bloqueia a resposta da NADPH oxidase a estímulos em células musculares lisas vasculares / Proteasome Inhibiton increases oxidative stress and disrupts NADPH oxidase response to stimuli in vascular smooth muscle cells
Cellular processes governing vascular Nox family NADPH oxidases in disease conditions are unclear. Since redox processes are intrinsic to cell stress response, we asked whether oxidative stress merges with other types of stress via Nox(es). We focused on proteasome inhibition as a relevant stress condition. Vascular smooth muscle cells (VSMC) incubation with
Publicado em: 2009
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5. Peptidyl-prolyl cis-trans isomerase improves the efficiency of protein disulfide isomerase as a catalyst of protein folding.
The cis-trans isomerization of prolyl peptide bonds and the formation of disulfide bonds are both slow steps in protein folding. By using ribonuclease T1 as a model system, we show that these two processes can become linked in the oxidative folding of reduced proteins and that the formation of the correct disulfide bonds is facilitated in the presence of pep
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6. Carbohydrates Facilitate Correct Disulfide Bond Formation and Folding of Rotavirus VP7
It is well established that glycosylation is essential for assembly of enveloped viruses, but no information is yet available as to the function of carbohydrates on the nonenveloped but glycosylated rotavirus. We show that tunicamycin and, more pronouncedly, a combination of tunicamycin and brefeldin A treatment caused misfolding of the luminal VP7 protein,
American Society for Microbiology.
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7. Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity.
We identified and characterized an Erwinia chrysanthemi gene able to complement an Escherichia coli dsbA mutation that prevents disulfide bond formation in periplasmic proteins. This gene, dsbC, codes for a 24 kDa periplasmic protein that contains a characteristic active site sequence of disulfide isomerases, Phe-X-X-X-X-Cys-X-X-Cys. Besides the active site,
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8. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.
The Escherichia coli periplasmic protein DsbC is active both in vivo and in vitro as a protein disulfide isomerase. For DsbC to attack incorrectly formed disulfide bonds in substrate proteins, its two active-site cysteines should be in the reduced form. Here we present evidence that, in wild-type cells, these two cysteines are reduced. Further, we show that
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9. A Protein Disulfide Isomerase Gene Fusion Expression System That Increases the Extracellular Productivity of Bacillus brevis
We have developed a versatile Bacillus brevis expression and secretion system based on the use of fungal protein disulfide isomerase (PDI) as a gene fusion partner. Fusion with PDI increased the extracellular production of heterologous proteins (light chain of immunoglobulin G, 8-fold; geranylgeranyl pyrophosphate synthase, 12-fold). Linkage to PDI prevented
American Society for Microbiology.
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10. The Fusion-Controlling Disulfide Bond Isomerase in Retrovirus Env Is Triggered by Protein Destabilization
The membrane fusion function of murine leukemia virus (MLV) is carried by the Env protein. This protein is composed of three SU-TM subunit complexes. The fusion activity is loaded into the transmembrane TM subunit and controlled by the peripheral, receptor-binding SU subunit. It is assumed that TM adopts a metastable conformation in the native Env and that f
American Society for Microbiology.
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11. Roles of Protein-disulfide Isomerase-mediated Disulfide Bond Formation of Yeast Mnl1p in Endoplasmic Reticulum-associated DegradationS⃞
The endoplasmic reticulum (ER) has a strict protein quality control system. Misfolded proteins generated in the ER are degraded by the ER-associated degradation (ERAD). Yeast Mnl1p consists of an N-terminal mannosidase homology domain and a less conserved C-terminal domain and facilitates the ERAD of glycoproteins. We found that Mnl1p is an ER luminal pr
American Society for Biochemistry and Molecular Biology.
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12. Identification of a Disulfide Isomerase Protein of Leishmania major as a Putative Virulence Factor
Several approaches have been previously used to elucidate the genetic basis of Leishmania virulence. In general, they were based on laboratory Leishmania clones genetically modified or grown in the presence of selecting agents. In a previous study, we demonstrated that Leishmania major freshly isolated from human cutaneous lesions showed significant differen
American Society for Microbiology.