Typical 2-Cys peroxiredoxins - Modulation by covalent transformations and noncovalent interactions
2-Cys peroxiredoxins are peroxidases devoid of prosthetic groups that mediate in the defence against oxidative stress and the peroxide activation of signaling pathways. This dual capacity relies on the high reactivity of the conserved peroxidatic and resolving cysteines, whose modification embraces...
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| Formato: | Capítulo de libro |
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2009
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 28277caa a22021617a 4500 | ||
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| 001 | PAPER-8791 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230607131853.0 | ||
| 008 | 190411s2009 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-64149090868 | |
| 024 | 7 | |2 cas |a cysteine, 4371-52-2, 52-89-1, 52-90-4; disulfide, 16734-12-6; peroxidase, 9003-99-0; peroxide, 14915-07-2; Cysteine, 52-90-4; Molecular Chaperones; Peroxidases, 1.11.1.-; Peroxiredoxins, 1.11.1.15; Sulfenic Acids | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 100 | 1 | |a Aran, M. | |
| 245 | 1 | 0 | |a Typical 2-Cys peroxiredoxins - Modulation by covalent transformations and noncovalent interactions |
| 260 | |c 2009 | ||
| 270 | 1 | 0 | |m Wolosiuk, R. A.; Instituto Leloir, IIBBA-CONICET, Universidad de Buenos Aires, Patricias Argentinas 435, C1405BWE Buenos Aires, Argentina; email: rwolosiuk@leloir.org.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 504 | |a Poole, L.B., Nelson, K.J., Discovering mechanisms of signaling-mediated cysteine oxidation (2008) Curr Opin Chem Biol, 12, pp. 18-24 | ||
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| 504 | |a Jeong, W., Cha, M.K., Kim, I.H., Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)-alkyl hydroperoxide peroxidase C (AhpC) family (2000) J Biol Chem, 275, pp. 2924-2930 | ||
| 520 | 3 | |a 2-Cys peroxiredoxins are peroxidases devoid of prosthetic groups that mediate in the defence against oxidative stress and the peroxide activation of signaling pathways. This dual capacity relies on the high reactivity of the conserved peroxidatic and resolving cysteines, whose modification embraces not only the usual thiol-disulfide exchange but also higher oxidation states of the sulfur atom. These changes are part of a complex system wherein the cooperation with other post-translational modifications - phosphorylation, acetylation - may function as major regulatory mechanisms of the quaternary structure. More importantly, modern proteomic approaches have identified the oxyacids at cysteine residues as novel protein targets for unsuspected post-translational modifications, such as phosphorylation that yields the unusual sulfi(o)nic-phosphoryl anhydride. In this article, we review the biochemical attributes of 2-Cys peroxiredoxins that, in combination with complementary studies of forward and reverse genetics, have generated stimulating molecular models to explain how this enzyme integrates into cell signaling in vivo. © 2009 FEBS. |l eng | |
| 593 | |a Instituto Leloir, IIBBA-CONICET, Universidad de Buenos Aires, Patricias Argentinas 435, C1405BWE Buenos Aires, Argentina | ||
| 593 | |a Instituto Leloir, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina | ||
| 593 | |a Catedra de Bioquimica, Facultad de Agronomia, Universidad de Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a 2-CYS PEROXIREDOXIN |
| 690 | 1 | 0 | |a ATP BINDING |
| 690 | 1 | 0 | |a AUTOPHOSPHORYLATION |
| 690 | 1 | 0 | |a MOLECULAR CHAPERONE |
| 690 | 1 | 0 | |a OLIGOMERIZATION |
| 690 | 1 | 0 | |a OVEROXIDATION |
| 690 | 1 | 0 | |a OXIDATIVE STRESS |
| 690 | 1 | 0 | |a PEROXIDASE MECHANISM |
| 690 | 1 | 0 | |a SULFENIC ACID |
| 690 | 1 | 0 | |a SULFINIC-PHOSPHORYL ANHYDRIDE |
| 690 | 1 | 0 | |a CYSTEINE |
| 690 | 1 | 0 | |a DISULFIDE |
| 690 | 1 | 0 | |a PEROXIDASE |
| 690 | 1 | 0 | |a PEROXIDE |
| 690 | 1 | 0 | |a PEROXIREDOXIN |
| 690 | 1 | 0 | |a THIOL |
| 690 | 1 | 0 | |a ACETYLATION |
| 690 | 1 | 0 | |a COVALENT BOND |
| 690 | 1 | 0 | |a MOLECULAR INTERACTION |
| 690 | 1 | 0 | |a MOLECULAR MODEL |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a OLIGOMERIZATION |
| 690 | 1 | 0 | |a OXIDATION |
| 690 | 1 | 0 | |a OXIDATIVE STRESS |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN PHOSPHORYLATION |
| 690 | 1 | 0 | |a PROTEIN PROCESSING |
| 690 | 1 | 0 | |a PROTEIN QUATERNARY STRUCTURE |
| 690 | 1 | 0 | |a PROTEIN TARGETING |
| 690 | 1 | 0 | |a PROTEOMICS |
| 690 | 1 | 0 | |a REGULATORY MECHANISM |
| 690 | 1 | 0 | |a REVIEW |
| 690 | 1 | 0 | |a SIGNAL TRANSDUCTION |
| 690 | 1 | 0 | |a ANIMALS |
| 690 | 1 | 0 | |a CYSTEINE |
| 690 | 1 | 0 | |a HUMANS |
| 690 | 1 | 0 | |a MOLECULAR CHAPERONES |
| 690 | 1 | 0 | |a OXIDATION-REDUCTION |
| 690 | 1 | 0 | |a OXIDATIVE STRESS |
| 690 | 1 | 0 | |a PEROXIDASES |
| 690 | 1 | 0 | |a PEROXIREDOXINS |
| 690 | 1 | 0 | |a PHOSPHORYLATION |
| 690 | 1 | 0 | |a PROTEIN PROCESSING, POST-TRANSLATIONAL |
| 690 | 1 | 0 | |a SULFENIC ACIDS |
| 700 | 1 | |a Ferrero, D.S. | |
| 700 | 1 | |a Pagano, E. | |
| 700 | 1 | |a Wolosiuk, R.A. | |
| 773 | 0 | |d 2009 |g v. 276 |h pp. 2478-2493 |k n. 9 |p FEBS J. |x 1742464X |w (AR-BaUEN)CENRE-7262 |t FEBS Journal | |
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| 856 | 4 | 0 | |u https://doi.org/10.1111/j.1742-4658.2009.06984.x |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_1742464X_v276_n9_p2478_Aran |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1742464X_v276_n9_p2478_Aran |y Registro en la Biblioteca Digital |
| 961 | |a paper_1742464X_v276_n9_p2478_Aran |b paper |c PE | ||
| 962 | |a info:eu-repo/semantics/article |a info:ar-repo/semantics/artículo |b info:eu-repo/semantics/publishedVersion | ||
| 999 | |c 69744 | ||