BIOMOLECULAS
BIOMOLECULAS
José Luis
Neira Faleiro
Publicaciones en las que colabora con José Luis Neira Faleiro (23)
2022
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A single evolutionarily divergent mutation determines the different FAD-binding affinities of human and rat NQO1 due to site-specific phosphorylation
FEBS Letters, Vol. 596, Núm. 1, pp. 29-41
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Phosphorylation of Thr9 Affects the Folding Landscape of the N-Terminal Segment of Human AGT Enhancing Protein Aggregation of Disease-Causing Mutants
Molecules (Basel, Switzerland), Vol. 27, Núm. 24
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Structural insights into choline-O-sulfatase reveal the molecular determinants for ligand binding
Acta crystallographica. Section D, Structural biology, Vol. 78, pp. 669-682
2021
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Intrinsically disordered protein NUPR1 binds to the armadillo-repeat domain of Plakophilin 1
International Journal of Biological Macromolecules, Vol. 170, pp. 549-560
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The isolated GTPase-activating-protein-related domain of neurofibromin-1 has a low conformational stability in solution
Archives of Biochemistry and Biophysics, Vol. 700
2020
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The isolated armadillo-repeat domain of Plakophilin 1 is a monomer in solution with a low conformational stability
Journal of Structural Biology, Vol. 211, Núm. 3
2019
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Phosphorylation compromises FAD binding and intracellular stability of wild-type and cancer-associated NQO1: Insights into flavo-proteome stability
International Journal of Biological Macromolecules, Vol. 125, pp. 1275-1288
2017
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Enhanced vulnerability of human proteins towards disease-associated inactivation through divergent evolution
Human Molecular Genetics, Vol. 26, Núm. 18, pp. 3531-3544
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Intrinsically disordered chromatin protein NUPR1 binds to the C-terminal region of polycomb RING1B
Proceedings of the National Academy of Sciences of the United States of America, Vol. 114, Núm. 31, pp. E6332-E6341
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Site-to-site interdomain communication may mediate different loss-of-function mechanisms in a cancer-associated NQO1 polymorphism
Scientific Reports, Vol. 7
2016
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Human COA3 Is an Oligomeric Highly Flexible Protein in Solution
Biochemistry, Vol. 55, Núm. 45, pp. 6209-6220
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The chondroitin sulfate/dermatan sulfate 4-O-endosulfatase from marine bacterium Vibrio sp FC509 is a dimeric species: Biophysical characterization of an endosulfatase
Biochimie, Vol. 131, pp. 85-95
2014
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Biochemical and mutational studies of allantoinase from Bacillus licheniformis CECT 20T
Biochimie, Vol. 99, Núm. 1, pp. 178-188
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Electrostatic effects in the folding of the SH3 domain of the c-Src tyrosine kinase: PH-dependence in 3D-domain swapping and amyloid formation Julio Bacarizo1
PLoS ONE, Vol. 9, Núm. 12
2013
2012
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Peptides as inhibitors of the first phosphorylation step of the streptomyces coelicolor phosphoenolpyruvate: Sugar phosphotransferase system
Biochemistry, Vol. 51, Núm. 37, pp. 7393-7402
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Stability and binding of the phosphorylated species of the N-terminal domain of enzyme i and the histidine phosphocarrier protein from the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system
Archives of Biochemistry and Biophysics, Vol. 526, Núm. 1, pp. 44-53
2011
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Biochemical and mutational studies of the Bacillus cereus CECT 5050T formamidase support the existence of a C-E-E-K tetrad in several members of the nitrilase superfamily
Applied and Environmental Microbiology, Vol. 77, Núm. 16, pp. 5761-5769
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N-Carbamoyl-β-alanine amidohydrolase from Agrobacterium tumefaciens C58: A promiscuous enzyme for the production of amino acids
Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, Vol. 879, Núm. 29, pp. 3277-3282
2010
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The N-terminal domain of the enzyme I is a monomeric well-folded protein with a low conformational stability and residual structure in the unfolded state
Protein Engineering, Design and Selection, Vol. 23, Núm. 9, pp. 729-742