Biología de Sistemas
Departamento
Federico
Gago Badenas
Catedrático/a de Universidad
Publicaciones en las que colabora con Federico Gago Badenas (27)
2022
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Identification of 1,2,3-triazolium salt-based inhibitors of Leishmania infantum trypanothione disulfide reductase with enhanced antileishmanial potency in cellulo and increased selectivity
European Journal of Medicinal Chemistry, Vol. 244
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Identification of L. infantum trypanothione synthetase inhibitors with leishmanicidal activity from a (non-biased) in-house chemical library
European Journal of Medicinal Chemistry, Vol. 243
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Pyridazino-pyrrolo-quinoxalinium salts as highly potent and selective leishmanicidal agents targeting trypanothione reductase
European Journal of Medicinal Chemistry, Vol. 227
2021
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Efficient Dimerization Disruption of Leishmania infantum Trypanothione Reductase by Triazole-phenyl-thiazoles
Journal of Medicinal Chemistry, Vol. 64, Núm. 9, pp. 6137-6160
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Small molecule–peptide conjugates as dimerization inhibitors of leishmania infantum trypanothione disulfide reductase
Pharmaceuticals, Vol. 14, Núm. 7
2020
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Generation of endoplasmic reticulum stress and inhibition of autophagy by plitidepsin induces proteotoxic apoptosis in cancer cells
Biochemical Pharmacology, Vol. 172
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Pseudoirreversible slow-binding inhibition of trypanothione reductase by a protein–protein interaction disruptor
British Journal of Pharmacology, Vol. 177, Núm. 22, pp. 5163-5176
2019
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Identification of NEK3 and MOK as novel targets for lithium
Chemical Biology and Drug Design
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Pyrrolopyrimidine vs Imidazole-Phenyl-Thiazole Scaffolds in Nonpeptidic Dimerization Inhibitors of Leishmania infantum Trypanothione Reductase
ACS Infectious Diseases, Vol. 5, Núm. 6, pp. 873-891
2018
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Trypanothione reductase inhibition and anti-leishmanial activity of all-hydrocarbon stapled α-helical peptides with improved proteolytic stability
European Journal of Medicinal Chemistry, Vol. 149, pp. 238-247
2017
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First example of peptides targeting the dimer interface of Leishmania infantum trypanothione reductase with potent in vitro antileishmanial activity#
European Journal of Medicinal Chemistry, Vol. 135, pp. 49-59
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Improved proteolytic stability and potent activity against Leishmania infantum trypanothione reductase of α/β-peptide foldamers conjugated to cell-penetrating peptides
European Journal of Medicinal Chemistry, Vol. 140, pp. 615-623
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Structure-based domain assignment in Leishmania infantum EndoG: Characterization of a pH-dependent regulatory switch and a C-Terminal extension that largely dictates DNA substrate preferences
Nucleic Acids Research, Vol. 45, Núm. 15, pp. 9030-9045
2016
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A functional BH3 domain in an aquaporin from Leishmania infantum
Cell Death Discovery, Vol. 2, Núm. 1
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Pro-death activity of a BH3 domain in an aquaporin from the protozoan parasite Leishmania
Cell Death and Disease
2015
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Comparison of hydrocarbon-and lactam-bridged cyclic peptides as dimerization inhibitors of Leishmania infantum trypanothione reductase
RSC Advances, Vol. 5, Núm. 69, pp. 55784-55794
2014
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Leishmania infantum EndoG is an endo/exo-nuclease essential for parasite survival
PLoS ONE, Vol. 9, Núm. 2
2013
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5′-trityl-substituted thymidine derivatives as a novel class of antileishmanial agents: Leishmania infantum EndoG as a potential target
ChemMedChem, Vol. 8, Núm. 7, pp. 1161-1174
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Probing the Dimerization Interface of Leishmania infantum Trypanothione Reductase with Site-Directed Mutagenesis and Short Peptides
ChemBioChem, Vol. 14, Núm. 10, pp. 1212-1217
2011
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Mechanistic insight into the catalytic activity of ββα-metallonucleases from computer simulations: Vibrio vulnificus periplasmic nuclease as a test case
ChemBioChem, Vol. 12, Núm. 17, pp. 2615-2622