Publicacions en què col·labora amb José M. Valpuesta (20)

2024

  1. A Targetable N-Terminal Motif Orchestrates α-Synuclein Oligomer-to-Fibril Conversion

    Journal of the American Chemical Society

  2. 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

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

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

1999

  1. ATP hydrolysis induces an intermediate conformational state in GroEL

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

  2. 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

1998

  1. GroEL under heat-shock: Switching from a folding to a storing function

    Journal of Biological Chemistry, Vol. 273, Núm. 49, pp. 32587-32594

1997

  1. Effects of the inter-ring communication in GroEL structural and functional asymmetry

    Journal of Biological Chemistry, Vol. 272, Núm. 52, pp. 32925-32932

1995

  1. Prediction of the structure of GroES and its interaction with GroEL

    Proteins: Structure, Function and Genetics, Vol. 22, Núm. 3, pp. 199-209

1990

  1. Infrared spectroscopic studies of detergent‐solubilized uncoupling protein from brown‐adipose‐tissue mitochondria

    European Journal of Biochemistry, Vol. 188, Núm. 1, pp. 83-89

1986

  1. Influence of temperature on the conformation of membrane proteins as seen by FT-IR

    Journal of Molecular Structure, Vol. 143, Núm. C, pp. 465-468