Eszter Papp, Ph.D.
Affiliations: | 2006 | Semmelweis Egyetem, Hungary |
Area:
Molecular BiologyGoogle:
"Eszter Papp"Parents
Sign in to add mentor| Peter Csermely | grad student | 2006 | Semmelweis Egyetem | |
| (Az endoplazmatikus retikulum redox allapotanak valtozasai es ennek funkcionalis kovetkezmenyei stressz folyaman.) | ||||
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Publications
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| Papp E, Csermely P. (2006) Chemical chaperones: mechanisms of action and potential use. Handbook of Experimental Pharmacology. 405-16 |
| Papp E, Száraz P, Korcsmáros T, et al. (2006) Changes of endoplasmic reticulum chaperone complexes, redox state, and impaired protein disulfide reductase activity in misfolding alpha1-antitrypsin transgenic mice. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 20: 1018-20 |
| Piccirella S, Czegle I, Lizák B, et al. (2006) Uncoupled redox systems in the lumen of the endoplasmic reticulum. Pyridine nucleotides stay reduced in an oxidative environment. The Journal of Biological Chemistry. 281: 4671-7 |
| Papp E, Nardai G, Mandl J, et al. (2005) FAD oxidizes the ERO1-PDI electron transfer chain: the role of membrane integrity. Biochemical and Biophysical Research Communications. 338: 938-45 |
| Nardai G, Stadler K, Papp E, et al. (2005) Diabetic changes in the redox status of the microsomal protein folding machinery. Biochemical and Biophysical Research Communications. 334: 787-95 |
| Varsányi M, Szarka A, Papp E, et al. (2004) FAD transport and FAD-dependent protein thiol oxidation in rat liver microsomes. The Journal of Biological Chemistry. 279: 3370-4 |
| Nardai G, Korcsmáros T, Papp E, et al. (2003) Reduction of the endoplasmic reticulum accompanies the oxidative damage of diabetes mellitus. Biofactors (Oxford, England). 17: 259-67 |
| Papp E, Nardai G, Söti C, et al. (2003) Molecular chaperones, stress proteins and redox homeostasis. Biofactors (Oxford, England). 17: 249-57 |
| Csermely P, Soti C, Kalmar E, et al. (2003) Molecular chaperones, evolution and medicine Journal of Molecular Structure: Theochem. 666: 373-380 |