Publicaciones en colaboración con investigadoras/es de Instituto Biofisika (22)

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. Oligonucleotide-directed protein threading through a rigid nanopore

    Methods in Molecular Biology (Humana Press Inc.), pp. 135-144

  3. Single-aminoacid discrimination in proteins with homogeneous nanopore sensors and neural networks

    Biosensors and Bioelectronics, Vol. 180

  4. The emerging landscape of single-molecule protein sequencing technologies

    Nature Methods, Vol. 18, Núm. 6, pp. 604-617

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

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

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

    Cells, Vol. 10, Núm. 10

  7. Use of pore-forming toxins to study co-translocational protein folding

    Methods in Enzymology (Academic Press Inc.), pp. 635-649

2020

  1. Free-energy landscapes of membrane co-translocational protein unfolding

    Communications Biology, Vol. 3, Núm. 1

  2. Transmembrane protein rotaxanes reveal kinetic traps in the refolding of translocated substrates

    Communications Biology, Vol. 3, Núm. 1

2018

  1. DNA-binding miniproteins based on zinc fingers. Assessment of the interaction using nanopores

    Chemical Science, Vol. 9, Núm. 17, pp. 4118-4123

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