Research Articles

“Thermodynamic stability of human γD-crystallin mutants using alchemical free-energy calculations”

Aguayo-Ortiz, R.; González-Navejas, A.; Palomino-Vizcaino, G.; Rodriguez-Meza, O.; Costas, M.;  Quintanar, L.; Dominguez, L. “Thermodynamic stability of human γD-crystallin mutants using alchemical free-energy calculations” J. Phys. Chem. B 2019, 123, 5671-5677.  https://doi.org/10.1021/acs.jpcb.9b01818

“Thermodynamic stability of human γD-crystallin mutants using alchemical free-energy calculations” Read Post »

Research Articles

“Interaction of Cu(I) with the Met-X3-Met motif of alpha-synuclein: binding ligands, affinity and structural features”

Gentile, I.; Garro, H.A.; Delgado-Ocaña, S.; Gonzalez, N.; Strohäker, T.; Schibich, D.; Quintanar, L.; Sambrotta, L.; Zweckstetter, M.; Griesinger, C.; Menacho-Márquez, M.; Fernandez, C. O. “Interaction of Cu(I) with the Met-X3-Met motif of alpha-synuclein: binding ligands, affinity and structural features” Metallomics 2018, 10, 1383.  https://DOI.org/10.1039/c8mt00232k

“Interaction of Cu(I) with the Met-X3-Met motif of alpha-synuclein: binding ligands, affinity and structural features” Read Post »

Research Articles

“Mercury-induced aggregation of human lens γ-crystallins reveals a potential role in cataract disease”

Domínguez-Calva, J.A.; Pérez-Vázquez, M.L.; Serebryany, E.; King, J.A.; Quintanar, L. “Mercury-induced aggregation of human lens γ-crystallins reveals a potential role in cataract disease” J. Biol. Inorg. Chem. 2018, 23, 1105-1118.  https://doi.org/10.1007/s00775-018-1607-z

“Mercury-induced aggregation of human lens γ-crystallins reveals a potential role in cataract disease” Read Post »

Research Articles

“A histidine switch for Zn-induced aggregation of γ-crystallins reveals a metal-bridging mechanism that is relevant to cataract disease”

Domínguez-Calva, J.A.; Haase-Pettingell, C.; Serebryany, E.; King, J.A.; Quintanar, L. “A histidine switch for Zn-induced aggregation of γ-crystallins reveals a metal-bridging mechanism that is relevant to cataract disease” Biochemistry 2018, 57, 4959-4962. https://doi.org/10.1021/acs.biochem.8b00436

“A histidine switch for Zn-induced aggregation of γ-crystallins reveals a metal-bridging mechanism that is relevant to cataract disease” Read Post »

Research Articles

“Neurotoxicity linked to dysfunctional metal ion homeostasis and xenobiotic metal exposure: Redox signaling and oxidative stress” 

Garza-Lombó, C.; Posadas, Y.; Quintanar, L.; Gonsebatt, M.E.; Franco, R. “Neurotoxicity linked to dysfunctional metal ion homeostasis and xenobiotic metal exposure: Redox signaling and oxidative stress” Antioxid Redox Signal 2018, 28, 1669-1703. https://doi.org/10.1089/ars.2017.7272

“Neurotoxicity linked to dysfunctional metal ion homeostasis and xenobiotic metal exposure: Redox signaling and oxidative stress”  Read Post »

Research Articles

“Neuroprotective alpha-cleavage of the human prion protein significantly impacts Cu(II) coordination at its His111 site”

Sánchez-López, C.; Fernández, C. O.; Quintanar, L. “Neuroprotective alpha-cleavage of the human prion protein significantly impacts Cu(II) coordination at its His111 site” Dalton Trans. 2018, 47, 9274-9282.  https://DOI.org/10.1039/C7DT03400H

“Neuroprotective alpha-cleavage of the human prion protein significantly impacts Cu(II) coordination at its His111 site” Read Post »

Research Articles

“Development of a Parenteral Formulation of NTS-Polyplex Nanoparticles for Clinical Purpose”

Aranda-Barradas, M. E.; Márquez, M.; Quintanar, L.; Santoyo-Salazar, J.; Espadas-Alvarez, A. J.; Martínez-Fong, D.; García-García, E. “Development of a Parenteral Formulation of NTS-Polyplex Nanoparticles for Clinical Purpose” Pharmaceutics 2018, 10, 5. https://doi.org/10.3390/pharmaceutics10010005

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Research Articles

“Methionine 109 plays a key role in Cu(II) binding to His111 in the 92-115 fragment of the human prion protein”

Sánchez-López, C.; Rivillas-Acevedo, L.; Cruz-Vásquez, O.; Quintanar, L. “Methionine 109 plays a key role in Cu(II) binding to His111 in the 92-115 fragment of the human prion protein” Inorg. Chim. Acta 2018, 481, 87-97.  https://doi.org/10.1016/j.ica.2017.09.046

“Methionine 109 plays a key role in Cu(II) binding to His111 in the 92-115 fragment of the human prion protein” Read Post »

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