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Structural and (Pseudo-)Enzymatic Properties of Neuroglobin: Its Possible Role in Neuroprotection.
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- Cells (2073-4409), 2021, v. 10, n. 12, p. 3366, doi. 10.3390/cells10123366
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Effects of Extracellular Osteoanabolic Agents on the Endogenous Response of Osteoblastic Cells.
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- Cells (2073-4409), 2021, v. 10, n. 9, p. 2383, doi. 10.3390/cells10092383
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Zymogen activation: Effect of peptides sequentially related to the bovine β-trypsin N-terminus on kazal inhibitor and benzamidine binding to bovine trypsinogen.
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- Journal of Molecular Recognition, 1988, v. 1, n. 3, p. 130, doi. 10.1002/jmr.300010306
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The enzymatic processing of α-dystroglycan by MMP-2 is controlled by two anchoring sites distinct from the active site.
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- PLoS ONE, 2018, v. 13, n. 2, p. 1, doi. 10.1371/journal.pone.0192651
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Copper(I) and Copper(II) Inhibit AB Peptides Proteolysis by Insulin-Degrading Enzyme Differently: Implications for Metallostasis Alteration in Alzheimer's Disease.
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- Chemistry - A European Journal, 2011, v. 17, n. 9, p. 2752, doi. 10.1002/chem.201002809
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Development of Potent Inhibitors of the <italic>Mycobacterium tuberculosis</italic> Virulence Factor Zmp1 and Evaluation of Their Effect on Mycobacterial Survival inside Macrophages.
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- ChemMedChem, 2018, v. 13, n. 5, p. 422, doi. 10.1002/cmdc.201700759
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- Article
Nitrite Reductase Activity of Ferrous Nitrobindins: A Comparative Study.
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- International Journal of Molecular Sciences, 2023, v. 24, n. 7, p. 6553, doi. 10.3390/ijms24076553
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Dexamethasone Downregulates Autophagy through Accelerated Turn-Over of the Ulk-1 Complex in a Trabecular Meshwork Cells Strain: Insights on Steroid-Induced Glaucoma Pathogenesis.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 11, p. 5891, doi. 10.3390/ijms22115891
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Mycobacterial and Human Ferrous Nitrobindins: Spectroscopic and Reactivity Properties.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 4, p. 1674, doi. 10.3390/ijms22041674
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NO Scavenging through Reductive Nitrosylation of Ferric Mycobacterium tuberculosis and Homo sapiens Nitrobindins.
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- International Journal of Molecular Sciences, 2020, v. 21, n. 24, p. 9395, doi. 10.3390/ijms21249395
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Cooperative Binding of the Cationic Porphyrin Tris-T4 Enhances Catalytic Activity of 20S Proteasome Unveiling a Complex Distribution of Functional States.
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- International Journal of Molecular Sciences, 2020, v. 21, n. 19, p. 7190, doi. 10.3390/ijms21197190
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Hydroxylamine-induced oxidation of ferrous nitrobindins.
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- Journal of Biological Inorganic Chemistry (JBIC), 2022, v. 27, n. 4/5, p. 443, doi. 10.1007/s00775-022-01940-9
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- Article
Kinetics of cyanide and carbon monoxide dissociation from ferrous human haptoglobin:hemoglobin(II) complexes.
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- Journal of Biological Inorganic Chemistry (JBIC), 2020, v. 25, n. 3, p. 351, doi. 10.1007/s00775-020-01766-3
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Fluoride and azide binding to ferric human hemoglobin:haptoglobin complexes highlights the ligand-dependent inequivalence of the α and β hemoglobin chains.
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- Journal of Biological Inorganic Chemistry (JBIC), 2019, v. 24, n. 2, p. 247, doi. 10.1007/s00775-019-01642-9
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- Article
Reductive nitrosylation of ferric microperoxidase-11.
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- Journal of Biological Inorganic Chemistry (JBIC), 2019, v. 24, n. 1, p. 21, doi. 10.1007/s00775-018-1623-z
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Reductive nitrosylation of ferric human hemoglobin bound to human haptoglobin 1-1 and 2-2.
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- Journal of Biological Inorganic Chemistry (JBIC), 2018, v. 23, n. 3, p. 437, doi. 10.1007/s00775-018-1551-y
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- Article
Hydroxylamine-induced oxidation of ferrous carbonylated truncated hemoglobins from Mycobacterium tuberculosis and Campylobacter jejuni is limited by carbon monoxide dissociation.
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- Journal of Biological Inorganic Chemistry (JBIC), 2017, v. 22, n. 6, p. 977, doi. 10.1007/s00775-017-1476-x
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The key role played by charge in the interaction of cytochrome c with cardiolipin.
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- Journal of Biological Inorganic Chemistry (JBIC), 2017, v. 22, n. 1, p. 19, doi. 10.1007/s00775-016-1404-5
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Cyanide binding to ferrous and ferric microperoxidase-11.
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- Journal of Biological Inorganic Chemistry (JBIC), 2016, v. 21, n. 4, p. 511, doi. 10.1007/s00775-016-1361-z
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- Article
The nitrite reductase activity of horse heart carboxymethylated-cytochrome c is modulated by cardiolipin.
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- Journal of Biological Inorganic Chemistry (JBIC), 2016, v. 21, n. 3, p. 421, doi. 10.1007/s00775-016-1351-1
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Novel Platinum(II) compounds modulate insulin-degrading enzyme activity and induce cell death in neuroblastoma cells.
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- Journal of Biological Inorganic Chemistry (JBIC), 2015, v. 20, n. 1, p. 101, doi. 10.1007/s00775-014-1217-3
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Cardiolipin modulates allosterically the nitrite reductase activity of horse heart cytochrome c.
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- Journal of Biological Inorganic Chemistry (JBIC), 2014, v. 19, n. 7, p. 1195, doi. 10.1007/s00775-014-1175-9
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Warfarin modulates the nitrite reductase activity of ferrous human serum heme–albumin.
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- Journal of Biological Inorganic Chemistry (JBIC), 2013, v. 18, n. 8, p. 939, doi. 10.1007/s00775-013-1040-2
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The collagenolytic action of MMP-1 is regulated by the interaction between the catalytic domain and the hinge region.
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- Journal of Biological Inorganic Chemistry (JBIC), 2012, v. 17, n. 4, p. 663, doi. 10.1007/s00775-012-0886-z
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Evidence for pH-dependent multiple conformers in iron(II) heme-human serum albumin: spectroscopic and kinetic investigation of carbon monoxide binding.
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- Journal of Biological Inorganic Chemistry (JBIC), 2012, v. 17, n. 1, p. 133, doi. 10.1007/s00775-011-0837-0
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- Article
The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125.
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- Journal of Biological Inorganic Chemistry (JBIC), 2011, v. 16, n. 2, p. 299, doi. 10.1007/s00775-010-0726-y
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Isoniazid and rifampicin inhibit allosterically heme binding to albumin and peroxynitrite isomerization by heme-albumin.
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- Journal of Biological Inorganic Chemistry (JBIC), 2011, v. 16, n. 1, p. 97, doi. 10.1007/s00775-010-0706-2
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- Article
pH dependence of the enzymatic processing of collagen I by MMP-1 (fibroblast collagenase), MMP-2 (gelatinase A), and MMP-14 ectodomain.
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- Journal of Biological Inorganic Chemistry (JBIC), 2010, v. 15, n. 8, p. 1219, doi. 10.1007/s00775-010-0680-8
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Extended cardiolipin anchorage to cytochrome c: a model for protein–mitochondrial membrane binding.
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- Journal of Biological Inorganic Chemistry (JBIC), 2010, v. 15, n. 5, p. 689, doi. 10.1007/s00775-010-0636-z
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Reversible two-step unfolding of heme–human serum albumin: a <sup>1</sup>H-NMR relaxometric and circular dichroism study.
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- Journal of Biological Inorganic Chemistry (JBIC), 2009, v. 14, n. 2, p. 209, doi. 10.1007/s00775-008-0439-7
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pH-dependent redox and CO binding properties of chelated protoheme- l-histidine and protoheme-glycyl- l-histidine complexes.
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- Journal of Biological Inorganic Chemistry (JBIC), 2006, v. 11, n. 2, p. 153, doi. 10.1007/s00775-005-0060-y
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Nitrosylation of rabbit ferrous heme-hemopexin.
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- Journal of Biological Inorganic Chemistry (JBIC), 2004, v. 9, n. 7, p. 800, doi. 10.1007/s00775-004-0598-0
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Anion concentration modulates the conformation and stability of the molten globule of cytochrome c.
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- Journal of Biological Inorganic Chemistry (JBIC), 2003, v. 8, n. 6, p. 663, doi. 10.1007/s00775-003-0462-7
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Enzymatic processing of collagen IV by MMP-2 (gelatinase A) affects neutrophil migration and it is modulated by extracatalytic domains.
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- Protein Science: A Publication of the Protein Society, 2006, v. 15, n. 12, p. 2805, doi. 10.1110/ps.062430706
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Oxygen exchange and energy metabolism in erythrocytes of Rett syndrome and their relationships with respiratory alterations.
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- Molecular & Cellular Biochemistry, 2017, v. 426, n. 1/2, p. 205, doi. 10.1007/s11010-016-2893-9
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Estimating the Cost of Equity Capital: Forecasting Accuracy for U.S. REIT Sector.
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- International Real Estate Review, 2019, v. 22, n. 3, p. 401
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Cardiolipin-cytochrome c complex: Switching cytochrome c from an electron-transfer shuttle to a myoglobin- and a peroxidase-like heme-protein.
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- IUBMB Life, 2015, v. 67, n. 2, p. 98, doi. 10.1002/iub.1350
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Reductive nitrosylation of the cardiolipin-ferric cytochrome c complex.
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- IUBMB Life, 2014, v. 66, n. 6, p. 438, doi. 10.1002/iub.1283
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- Article
Enzymatic processing by MMP-2 and MMP-9 of wild-type and mutated mouse β-dystroglycan.
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- IUBMB Life, 2012, v. 64, n. 12, p. 988, doi. 10.1002/iub.1095
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Ligand- and proton-linked conformational changes of the ferrous 2/2 hemoglobin of Pseudoalteromonas haloplanktis TAC125.
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- IUBMB Life, 2011, v. 63, n. 7, p. 566, doi. 10.1002/iub.492
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- Article
Structural heterogeneity and ligand gating in ferric methanosarcina acetivorans protoglobin mutants.
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- IUBMB Life, 2011, v. 63, n. 5, p. 287, doi. 10.1002/iub.484
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Cardiolipin drives cytochrome c proapoptotic and antiapoptotic actions.
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- IUBMB Life, 2011, v. 63, n. 3, p. 160, doi. 10.1002/iub.440
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- Article
Nitrosylation Mechanisms of <i>Mycobacterium tuberculosis</i> and <i>Campylobacter jejuni</i> Truncated Hemoglobins N, O, and P.
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- PLoS ONE, 2014, v. 9, n. 7, p. 1, doi. 10.1371/journal.pone.0102811
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Characterization of the Prostate-Specific Antigen (PSA) Catalytic Mechanism: A Pre-Steady-State and Steady-State Study.
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- PLoS ONE, 2014, v. 9, n. 7, p. 1, doi. 10.1371/journal.pone.0102470
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- Article
Nitrite-Reductase and Peroxynitrite Isomerization Activities of <i>Methanosarcina acetivorans</i> Protoglobin.
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- PLoS ONE, 2014, v. 9, n. 5, p. 1, doi. 10.1371/journal.pone.0095391
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- Article
Isoniazid Inhibits the Heme-Based Reactivity of <i>Mycobacterium tuberculosis</i> Truncated Hemoglobin N.
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- PLoS ONE, 2013, v. 8, n. 8, p. 1, doi. 10.1371/journal.pone.0069762
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- Article
Structure and Haem-Distal Site Plasticity in <i>Methanosarcina acetivorans</i> Protoglobin.
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- PLoS ONE, 2013, v. 8, n. 6, p. 1, doi. 10.1371/journal.pone.0066144
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- Article
Reciprocal Allosteric Modulation of Carbon Monoxide and Warfarin Binding to Ferrous Human Serum Heme-Albumin.
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- PLoS ONE, 2013, v. 8, n. 3, p. 1, doi. 10.1371/journal.pone.0058842
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- Article
Ligation Tunes Protein Reactivity in an Ancient Haemoglobin: Kinetic Evidence for an Allosteric Mechanism in Methanosarcina acetivorans Protoglobin.
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- PLoS ONE, 2012, v. 7, n. 3, p. 1, doi. 10.1371/journal.pone.0033614
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Design of a New Mimochrome with Unique Topology.
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- Chemistry - A European Journal, 2003, v. 9, n. 22, p. 5643, doi. 10.1002/chem.200304831
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- Article