Abstract
The study of redox processes has high potential to elucidate integrative mechanisms, due to the ubiquity and strength of their effects. Many studies involve the role of redox mechanisms in diseases. However, the complexity of this field has increased concerning structures, structure-function relations, methods, molecular and sub-cellular pathology of redox-regulated proteins, genomics, proteomics and metabolomics of oxidative stress. Thus, a multidisciplinary approach has become essential for meaningful advances in the field. Also, emerging groups have difficulty to address relevant points and sharpen educational skills. The main purpose of our Redoxome Network is to foster integrative collaborations, promote sustained development and assist emerging groups. Our goal is to perform studies that allow the design and assessment of novel antioxidant strategies with clinical applicability. We will address issues relevant toward overcoming Iimitations in knowledge of redox processes, as follows: 1) ROS generation and control in biological systems; 2) chemical reactivity of reactive oxygen species (ROS) in biological environments and consequent changes in structure and function of biomolecules; 3) Mechanisms and networks involved in redox signaling processes relevant to human disease; 4) diagnostic and therapeutic applications of redox processes. These strategies will enable, on a national basis, a concerted effort to attack key questions bridging meaningful gaps in the field. Our efforts will foster integration of multiple disciplines and institutions in our country and result in advances with educational, scientific, environmental and socioeconomic impact. (AU)
Scientific publications
(14)
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
SIMOES ONOFRE DE SANTI, MARIA EUGENIA;
PRATES, RENATO ARAUJO;
FRANCA, CRISTIANE MIRANDA;
LOPES, RUBIA GARCIA;
SOUSA, ALINE SILVA;
FERREIRA, LUIS RODOLFO;
BUSSADORI, SANDRA KALIL;
FERNANDES, ADJACI UCHOA;
DEANA, ALESSANDRO MELO.
Antimicrobial photodynamic therapy as a new approach for the treatment of vulvovaginal candidiasis: preliminary results.
Lasers in Medical Science,
v. 33,
n. 9,
p. 1925-1931,
DEC 2018.
Web of Science Citations: 1.
PEIXOTO, ALBERT SOUZA;
RYAN GEYER, R.;
IQBAL, ASIF;
TRUZZI, DANIELA R.;
SOARES MORETTI, ANA I.;
LAURINDO, FRANCISCO R. M.;
AUGUSTO, OHARA.
Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein-disulfide isomerase.
Journal of Biological Chemistry,
v. 293,
n. 4,
p. 1450-1465,
JAN 26 2018.
Web of Science Citations: 3.
MORI, MATEUS P.;
COSTA, RUTE A. P.;
SOLTYS, DANIELA T.;
FREIRE, THIAGO DE S.;
ROSSATO, FRANCO A.;
AMIGO, IGNACIO;
KOWALTOWSKI, ALICIA J.;
VERCESI, ANBAL E.;
DE SOUZA-PINTO, NADJA C.
Lack of XPC leads to a shift between respiratory complexes I and II but sensitizes cells to mitochondrial stress.
SCIENTIFIC REPORTS,
v. 7,
MAR 13 2017.
Web of Science Citations: 4.
SILVA-PORTELA, RITA C. B.;
CARVALHO, FABIOLA M.;
PEREIRA, CAROLINA P. M.;
DE SOUZA-PINTO, NADJA C.;
MODESTI, MAURO;
FUCHS, ROBERT P.;
AGNEZ-LIMA, LUCYMARA F.
ExoMeg1: a new exonuclease from metagenomic library.
SCIENTIFIC REPORTS,
v. 6,
JAN 27 2016.
Web of Science Citations: 4.
BAADER, WILHELM J.;
STEVANI, CASSIUS V.;
BECHARA, ETELVINO J. H.
``Photo{''} Chemistry Without Light?.
Journal of the Brazilian Chemical Society,
v. 26,
n. 12,
p. 2430-2447,
DEC 2015.
Web of Science Citations: 8.
GENARO-MATTOS, THIAGO C.;
QUEIROZ, RAPHAEL F.;
CUNHA, DANIELA;
APPOLINARIO, PATRICIA P.;
DI MASCIO, PAOLO;
NANTES, ISELI L.;
AUGUSTO, OHARA;
MIYAMOTO, SAYURI.
Cytochrome c Reacts with Cholesterol Hydroperoxides To Produce Lipid- and Protein-Derived Radicals.
BIOCHEMISTRY,
v. 54,
n. 18,
p. 2841-2850,
MAY 12 2015.
Web of Science Citations: 6.
COELHO, FERNANDO R.;
IQBAL, ASIF;
LINARES, EDLAINE;
SILVA, DANIEL F.;
LIMA, FILIPE S.;
CUCCOVIA, IOLANDA M.;
AUGUSTO, OHARA.
Oxidation of the Tryptophan 32 Residue of Human Superoxide Dismutase 1 Caused by Its Bicarbonate-dependent Peroxidase Activity Triggers the Non-amyloid Aggregation of the Enzyme.
Journal of Biological Chemistry,
v. 289,
n. 44,
p. 30690-30701,
OCT 31 2014.
Web of Science Citations: 15.
QUEIROZ, RAPHAEL F.;
PAVIANI, VERONICA;
COELHO, FERNANDO R.;
MARQUES, EMERSON E.;
DI MASCIO, PAOLO;
AUGUSTO, OHARA.
The carbonylation and covalent dimerization of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity is inhibited by the radical scavenger tempol.
Biochemical Journal,
v. 455,
n. 1,
p. 37-46,
OCT 1 2013.
Web of Science Citations: 11.