Research Articles

“Bioinorganic chemistry of Parkinson disease: Affinity and structural features of Cu(I) binding to the full-length β-synuclein protein”

Miotto, M. C.; Pavese, M. D.; Quintanar, L.; Zweckstetter, M.; Griesinger, C.; Fernandez, C. O. “Bioinorganic chemistry of Parkinson disease: Affinity and structural features of Cu(I) binding to the full-length β-synuclein protein” Inorg. Chem. 2017, 56, 10387-10395. https://doi.org/10.1021/acs.inorgchem.7b0129

“Bioinorganic chemistry of Parkinson disease: Affinity and structural features of Cu(I) binding to the full-length β-synuclein protein” Read Post »

Research Articles

“Effect of ionic strength on the aggregation kinetics of the amidated amyloid beta peptide Aβ (1-40) in aqueous solutions”

Campos-Ramírez, A.; Márquez, M.; Quintanar, L.; Rojas-Ochoa, L.F. “Effect of ionic strength on the aggregation kinetics of the amidated amyloid beta peptide Aβ (1-40) in aqueous solutions” Biophys. Chem. 2017, 228, 98-107.  10.1016/j.bpc.2017.05.004

“Effect of ionic strength on the aggregation kinetics of the amidated amyloid beta peptide Aβ (1-40) in aqueous solutions” Read Post »

Research Articles

“Copper coordination features of human islet amyloid polypeptide: The type 2 diabetes peptide”

Sánchez-López, C.; Cortés-Mejía, R.; Miotto, M. C.; Binolfi, A.; Fernández, C.O.; M. del Campo, J.; Quintanar, L. “Copper coordination features of human islet amyloid polypeptide: The type 2 diabetes peptide” Inorg. Chem. 2016, 55, 10727-10740. https://doi.org/10.1021/acs.inorgchem.6b01963

“Copper coordination features of human islet amyloid polypeptide: The type 2 diabetes peptide” Read Post »

Research Articles

“Role of N-terminal methionine residues in the redox activity of copper bound to alpha-synuclein”

Rodríguez, E.; Arcos-López, T.; Trujano-Ortiz, L.; Fernández, C.O.; González, F.J.; Vela, A.; Quintanar, L. “Role of N-terminal methionine residues in the redox activity of copper bound to alpha-synuclein” J. Biol. Inorg. Chem. 2016, 21, 691-702.  10.1007/s00775-016-1376-5

“Role of N-terminal methionine residues in the redox activity of copper bound to alpha-synuclein” Read Post »

Research Articles

“Spectroscopic and theoretical study of Cu(I) binding to His111 in the human prion protein fragment 106-115”

Arcos-López, T.; Qayyum, M.; Rivillas-Acevedo, L.; Miotto, M.C.; Grande-Aztatzi, R.; Fernández, C.O.; Hedman, B.; Hodgson, K.O.; Vela, A.; Solomon, E.I.; Quintanar, L. “Spectroscopic and theoretical study of Cu(I) binding to His111 in the human prion protein fragment 106-115” Inorg. Chem. 2016, 55, 2909-2922. https://doi.org/10.1021/acs.inorgchem.5b02794

“Spectroscopic and theoretical study of Cu(I) binding to His111 in the human prion protein fragment 106-115” Read Post »

Research Articles

“Copper and zinc ions specifically promote nonamyloid aggregation of the highly stable human γ-D crystallin”

Quintanar, L.; Domìnguez-Calva, J.A.; Serebryany, E.; Rivillas-Acevedo, L.; Haase-Pettingell, C.; Amero, C.; King, J.A. “Copper and zinc ions specifically promote nonamyloid aggregation of the highly stable human γ-D crystallin” ACS Chem. Biol. 2016, 11, 263-272. Paper selected for the journal´s podcast:  http://pubs.acs.org/pb-assets/audio/acbcct/acbcctv11n01.mp3  https://doi.org/10.1021/acschembio.5b00919

“Copper and zinc ions specifically promote nonamyloid aggregation of the highly stable human γ-D crystallin” Read Post »

Research Articles

“Mercury reduces the enzymatic activity of neprilysin in differentiated SH-SY5Y cells”

Chin-Chan, M.; Segovia, J.; Quintanar, L.; Arcos-López, T.; Hersh, L. B.; Chow, K. M.; Rodgers, D.W.; Quintanilla-Vega, B. “Mercury reduces the enzymatic activity of neprilysin in differentiated SH-SY5Y cells” Toxicol. Sci. 2015, 145, 128-137. https://dx.doi.org/10.1093%2Ftoxsci%2Fkfv037

“Mercury reduces the enzymatic activity of neprilysin in differentiated SH-SY5Y cells” Read Post »

Research Articles

“Structural Basis for the Inhibition of Truncated Islet Amyloid Polypeptide Aggregation by Cu(II): Insights into the Bioinorganic Chemistry of Type II Diabetes”

Rivillas-Acevedo, L.; Sánchez-López, C.; Amero, C.; Quintanar, L. “Structural Basis for the Inhibition of Truncated Islet Amyloid Polypeptide Aggregation by Cu(II): Insights into the Bioinorganic Chemistry of Type II Diabetes” Inorg. Chem. 2015, 54, 3788-3796. https://doi.org/10.1021/ic502945k

“Structural Basis for the Inhibition of Truncated Islet Amyloid Polypeptide Aggregation by Cu(II): Insights into the Bioinorganic Chemistry of Type II Diabetes” Read Post »

Research Articles

“A bifunctional non-natural tetrapeptide modulates amyloid-beta peptide aggregation in the presence of Cu(II)”

Márquez, M.; Blancas-Mejía, L. M.; Campos, A.; Rojas, L.; Castañeda-Hernández, G.; Quintanar, L. “A bifunctional non-natural tetrapeptide modulates amyloid-beta peptide aggregation in the presence of Cu(II)” Metallomics. 2014, 6, 2189-2192. Artículo seleccionado para la portada de la revista. https://doi.org/10.1039/C4MT00257A

“A bifunctional non-natural tetrapeptide modulates amyloid-beta peptide aggregation in the presence of Cu(II)” Read Post »

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