about
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulumERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin familySequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesisERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stressThiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44Stress Regulates Aquaporin-8 Permeability to Impact Cell Growth and Survival.Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tailCrystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDICrystal Structure of the ERp44-Peroxiredoxin 4 Complex Reveals the Molecular Mechanisms of Thiol-Mediated Protein RetentionGenomic organization and transcriptional analysis of the human genes coding for caveolin-1 and caveolin-2Expression of mutant or cytosolic PrP in transgenic mice and cells is not associated with endoplasmic reticulum stress or proteasome dysfunctionProgressively impaired proteasomal capacity during terminal plasma cell differentiation.Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein.Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum.Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum.Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44.Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum.Progressive quality control of secretory proteins in the early secretory compartment by ERp44A dynamic study of protein secretion and aggregation in the secretory pathway.The making of a professional secretory cell: architectural and functional changes in the ER during B lymphocyte plasma cell differentiation.Quality control in the endoplasmic reticulum protein factory.Entry of exogenous polypeptides into the nucleus of living cells: facts and speculations.Biochemical nature of Russell Bodies.Protein quality control in the early secretory pathwayManaging and exploiting stress in the antibody factory.Endoplasmic reticulum stress.Diseases originating from altered protein quality control in the endoplasmic reticulum.Iron increases the susceptibility of multiple myeloma cells to bortezomib.Building and operating an antibody factory: redox control during B to plasma cell terminal differentiation.Dynamic regulation of Ero1α and peroxiredoxin 4 localization in the secretory pathway.Assessing Heterogeneity of Osteolytic Lesions in Multiple Myeloma by ¹H HR-MAS NMR MetabolomicsGlutathione peroxidase 7 utilizes hydrogen peroxide generated by Ero1α to promote oxidative protein folding.Physiology and pathology of proteostasis in the early secretory compartment.Oxidative protein folding in the secretory pathway and redox signaling across compartments and cells.From antibodies to adiponectin: role of ERp44 in sizing and timing protein secretion.Proteostenosis and plasma cell pathophysiology.Protein degradation in the endoplasmic reticulum.Peroxides and peroxidases in the endoplasmic reticulum: integrating redox homeostasis and oxidative folding.On the redox control of B lymphocyte differentiation and function.Biogenesis and function of IgM: the role of the conserved mu-chain tailpiece glycans.
P50
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P50
description
hulumtues
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researcher
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wetenschapper
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հետազոտող
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name
Roberto Sitia
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Roberto Sitia
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Roberto Sitia
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Roberto Sitia
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Roberto Sitia
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type
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Roberto Sitia
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Roberto Sitia
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Roberto Sitia
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Roberto Sitia
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Roberto Sitia
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Roberto Sitia
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Roberto Sitia
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Roberto Sitia
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Roberto Sitia
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Roberto Sitia
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P21
P31
P496
0000-0001-7086-4152