Publicaciones en las que colabora con José M. Valpuesta (36)

2024

  1. Author Correction: The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70 (Nature Communications, (2023), 14, 1, (5436), 10.1038/s41467-023-41150-8)

    Nature Communications

2023

  1. The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70

    Nature communications, Vol. 14, Núm. 1, pp. 5436

2021

  1. Truncation‐driven lateral association of α‐synuclein hinders amyloid clearance by the Hsp70‐based disaggregase

    International Journal of Molecular Sciences, Vol. 22, Núm. 23

2019

  1. Structural insights into the ability of nucleoplasmin to assemble and chaperone histone octamers for DNA deposition

    Scientific Reports, Vol. 9, Núm. 1

2015

  1. Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE

    Journal of Biological Chemistry, Vol. 290, Núm. 16, pp. 10083-10092

2014

  1. The intrinsically disordered distal face of nucleoplasmin recognizes distinct oligomerization states of histones

    Nucleic Acids Research, Vol. 42, Núm. 2, pp. 1311-1325

2013

  1. Structural insights into the chaperone activity of the 40-kDa heat shock protein DnaJ: Binding and remodeling of a native substrate

    Journal of Biological Chemistry, Vol. 288, Núm. 21, pp. 15065-15074

2012

  1. Recognition of Membrane-Bound Fusion-Peptide/MPER Complexes by the HIV-1 Neutralizing 2F5 Antibody: Implications for Anti-2F5 Immunogenicity

    PLoS ONE, Vol. 7, Núm. 12

2010

  1. Nucleoplasmin binds histone H2A-H2B dimers through its distal face

    Journal of Biological Chemistry, Vol. 285, Núm. 44, pp. 33771-33778

2008

  1. The broadly neutralizing anti-human immunodeficiency virus type 1 4E10 monoclonal antibody is better adapted to membrane-bound epitope recognition and blocking than 2F5

    Journal of Virology, Vol. 82, Núm. 18, pp. 8986-8996

  2. The structure of CCT-Hsc70NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin

    Nature Structural and Molecular Biology, Vol. 15, Núm. 8, pp. 858-864

2005

  1. Ionic interactions at both inter-ring contact sites of GroEL are involved in transmission of the allosteric signal: A time-resolved infrared difference study

    Protein Science, Vol. 14, Núm. 9, pp. 2267-2274

2003

  1. GroEL stability and function. Contribution of the ionic interactions at the inter-ring contact sites

    Journal of Biological Chemistry, Vol. 278, Núm. 34, pp. 32083-32090

2002

  1. Purification and properties of TrwB, a hexameric, ATP-binding integral membrane protein essential for R388 plasmid conjugation

    Journal of Biological Chemistry, Vol. 277, Núm. 48, pp. 46456-46462

  2. Salt bridges at the inter-ring interface regulate the thermostat of GroEL

    Journal of Biological Chemistry, Vol. 277, Núm. 37, pp. 34024-34029

2000

  1. Interactions of the HIV-1 fusion peptide with large unilamellar vesicles and monolayers. A cryo-TEM and spectroscopic study

    Biochimica et Biophysica Acta - Biomembranes, Vol. 1467, Núm. 1, pp. 153-164

1999

  1. ATP hydrolysis induces an intermediate conformational state in GroEL

    European Journal of Biochemistry, Vol. 259, Núm. 1-2, pp. 347-355

  2. Characterization of ATP and DNA binding activities of TrwB, the coupling protein essential in plasmid R388 conjugation

    Journal of Biological Chemistry, Vol. 274, Núm. 51, pp. 36117-36124

  3. Conformational changes generated in GroEL during ATP hydrolysis as seen by time-resolved infrared spectroscopy

    Journal of Biological Chemistry, Vol. 274, Núm. 9, pp. 5508-5513

  4. Interbilayer lipid mixing induced by the human immunodeficiency virus type-1 fusion peptide on large unilamellar vesicles: The nature of the nonlamellar intermediates

    Chemistry and Physics of Lipids, Vol. 103, Núm. 1-2, pp. 11-20