Publicaciones en colaboración con investigadoras/es de Instituto Biofisika (15)

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. All-or-none amyloid disassembly via chaperone-triggered fibril unzipping favors clearance of α-synuclein toxic species

    Proceedings of the National Academy of Sciences of the United States of America, Vol. 118, Núm. 36

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

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

  3. Unzipping the secrets of amyloid disassembly by the human disaggregase

    Cells, Vol. 10, Núm. 10

2017

  1. Label-Free, Multiplexed, Single-Molecule Analysis of Protein-DNA Complexes with Nanopores

    ACS Nano, Vol. 11, Núm. 6, pp. 5815-5825

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. DnaJ recruits DnaK to protein aggregates

    Journal of Biological Chemistry, Vol. 283, Núm. 3, pp. 1381-1390

2007

  1. GrpE N-terminal Domain Contributes to the Interaction with DnaK and Modulates the Dynamics of the Chaperone Substrate Binding Domain

    Journal of Molecular Biology, Vol. 374, Núm. 4, pp. 1054-1064

2006

  1. Crystal structure of the temperature-sensitive and allosteric-defective chaperonin GroELE461K

    Journal of Structural Biology, Vol. 155, Núm. 3, pp. 482-492

  2. Ionic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics

    Journal of Biological Chemistry, Vol. 281, Núm. 11, pp. 7479-7488

  3. Thermal Adaptation of the Yeast Mitochondrial Hsp70 System is Regulated by the Reversible Unfolding of its Nucleotide Exchange Factor

    Journal of Molecular Biology, Vol. 358, Núm. 5, pp. 1367-1377

2004

  1. Nucleoplasmin: A nuclear chaperone

    Biochemistry and Cell Biology

2003

  1. Activation mechanism of the nuclear chaperone nucleoplasmin: Role of the core domain

    Journal of Molecular Biology, Vol. 334, Núm. 3, pp. 585-593

2001

  1. Excluded volume effects on the refolding and assembly of an oligomeric protein. GroEL, a case study

    Journal of Biological Chemistry, Vol. 276, Núm. 2, pp. 957-964