Detalhe da pesquisa
1.
Proteomic Characterization of Atherosclerotic Lesions In Situ Using Percutaneous Coronary Intervention Angioplasty Balloons-Brief Report.
Arterioscler Thromb Vasc Biol
; 42(7): 857-864, 2022 07.
Artigo
Inglês
| MEDLINE | ID: mdl-35443792
2.
Investigations of the Navß1b sodium channel subunit in human ventricle; functional characterization of the H162P Brugada syndrome mutant.
Am J Physiol Heart Circ Physiol
; 306(8): H1204-12, 2014 Apr 15.
Artigo
Inglês
| MEDLINE | ID: mdl-24561865
3.
Proteomic analysis of the extracellular matrix of human atherosclerotic plaques shows marked changes between plaque types.
Matrix Biol Plus
; 21: 100141, 2024 Feb.
Artigo
Inglês
| MEDLINE | ID: mdl-38292008
4.
The inflammatory oxidant peroxynitrous acid modulates the structure and function of the recombinant human V3 isoform of the extracellular matrix proteoglycan versican.
Redox Biol
; 64: 102794, 2023 08.
Artigo
Inglês
| MEDLINE | ID: mdl-37402332
5.
Identification of galectin-1 and other cellular targets of alpha,beta-unsaturated carbonyl compounds, including dimethylfumarate, by use of click-chemistry probes.
Redox Biol
; 59: 102560, 2023 02.
Artigo
Inglês
| MEDLINE | ID: mdl-36493513
6.
Peroxynitrous acid-modified extracellular matrix alters gene and protein expression in human coronary artery smooth muscle cells and induces a pro-inflammatory phenotype.
Free Radic Biol Med
; 186: 43-52, 2022 06.
Artigo
Inglês
| MEDLINE | ID: mdl-35526806
7.
Reaction of quinones with proteins: Kinetics of adduct formation, effects on enzymatic activity and protein structure, and potential reversibility of modifications.
Free Radic Biol Med
; 137: 169-180, 2019 06.
Artigo
Inglês
| MEDLINE | ID: mdl-31026584
8.
Identification and quantification of sites of nitration and oxidation in the key matrix protein laminin and the structural consequences of these modifications.
Redox Biol
; 24: 101226, 2019 06.
Artigo
Inglês
| MEDLINE | ID: mdl-31154162
9.
Aggregation of α- and ß- caseins induced by peroxyl radicals involves secondary reactions of carbonyl compounds as well as di-tyrosine and di-tryptophan formation.
Free Radic Biol Med
; 124: 176-188, 2018 08 20.
Artigo
Inglês
| MEDLINE | ID: mdl-29885785
10.
The peroxyl radical-induced oxidation of Escherichia coli FtsZ and its single tryptophan mutant (Y222W) modifies specific side-chains, generates protein cross-links and affects biological function.
Free Radic Biol Med
; 112: 60-68, 2017 11.
Artigo
Inglês
| MEDLINE | ID: mdl-28733212