Federico Gago Badenas-rekin lankidetzan egindako argitalpenak (22)

2022

  1. 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

  2. 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

  3. Pyridazino-pyrrolo-quinoxalinium salts as highly potent and selective leishmanicidal agents targeting trypanothione reductase

    European Journal of Medicinal Chemistry, Vol. 227

2021

  1. Efficient Dimerization Disruption of Leishmania infantum Trypanothione Reductase by Triazole-phenyl-thiazoles

    Journal of Medicinal Chemistry, Vol. 64, Núm. 9, pp. 6137-6160

  2. Small molecule–peptide conjugates as dimerization inhibitors of leishmania infantum trypanothione disulfide reductase

    Pharmaceuticals, Vol. 14, Núm. 7

2020

  1. Generation of endoplasmic reticulum stress and inhibition of autophagy by plitidepsin induces proteotoxic apoptosis in cancer cells

    Biochemical Pharmacology, Vol. 172

  2. 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

  1. Identification of NEK3 and MOK as novel targets for lithium

    Chemical Biology and Drug Design

  2. 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

  1. 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

  1. 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

  2. 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

  3. 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

  1. A functional BH3 domain in an aquaporin from Leishmania infantum

    Cell Death Discovery, Vol. 2, Núm. 1

  2. Pro-death activity of a BH3 domain in an aquaporin from the protozoan parasite Leishmania

    Cell Death and Disease

2015

  1. 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

  1. Leishmania infantum EndoG is an endo/exo-nuclease essential for parasite survival

    PLoS ONE, Vol. 9, Núm. 2

2013

  1. 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

  2. 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

  1. 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