Publicaciones en las que colabora con José Luis Neira Faleiro (15)

2022

  1. 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

  1. 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

  1. 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

2016

  1. Human COA3 Is an Oligomeric Highly Flexible Protein in Solution

    Biochemistry, Vol. 55, Núm. 45, pp. 6209-6220

2014

  1. Biochemical and mutational studies of allantoinase from Bacillus licheniformis CECT 20T

    Biochimie, Vol. 99, Núm. 1, pp. 178-188

  2. 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

  1. The Histidine-Phosphocarrier Protein of the Phosphoenolpyruvate: Sugar Phosphotransferase System of Bacillus sphaericus Self-Associates

    PLoS ONE, Vol. 8, Núm. 7

2012

  1. Peptides as inhibitors of the first phosphorylation step of the streptomyces coelicolor phosphoenolpyruvate: Sugar phosphotransferase system

    Biochemistry, Vol. 51, Núm. 37, pp. 7393-7402

  2. 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

  1. 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

  2. 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

  1. 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

2009

  1. Metal-triggered changes in the stability and secondary structure of a tetrameric dihydropyrimidinase: A biophysical characterization

    Biophysical Chemistry, Vol. 139, Núm. 1, pp. 42-52

  2. Structure and conformational stability of a tetrameric thermostable N-succinylamino acid racemase

    Biopolymers, Vol. 91, Núm. 9, pp. 757-772

2006

  1. Site-directed mutagenesis indicates an important role of cysteines 76 and 181 in the catalysis of hydantoin racemase from Sinorhizobium meliloti

    Protein Science, Vol. 15, Núm. 12, pp. 2729-2738