Publicaciones en las que colabora con Arturo Muga Villate (51)

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

  3. Pseudophosphorylation of single residues of the J-domain of DNAJA2 regulates the holding/folding balance of the Hsc70 system

    Protein Science, Vol. 33, Núm. 8

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

2022

  1. Fine-tuning of the Hsc70-based Human Protein Disaggregase Machinery by the Distinctive C-terminal Extension of Apg2

    Journal of Molecular Biology, Vol. 434, Núm. 22

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. Inhibition of the human hsc70 system by small ligands as a potential anticancer approach

    Cancers, Vol. 13, Núm. 12

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

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

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

    Cells, Vol. 10, Núm. 10

2019

  1. Regulation of Human Hsc70 ATPase and Chaperone Activities by Apg2: Role of the Acidic Subdomain

    Journal of Molecular Biology, Vol. 431, Núm. 2, pp. 444-461

  2. The complex phosphorylation patterns that regulate the activity of Hsp70 and its cochaperones

    International Journal of Molecular Sciences, Vol. 20, Núm. 17

2018

  1. Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate

    Scientific Reports, Vol. 8, Núm. 1

2017

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

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

2016

  1. Crowding Modulates the Conformation, Affinity, and Activity of the Components of the Bacterial Disaggregase Machinery

    Journal of Molecular Biology, Vol. 428, Núm. 11, pp. 2474-2487

2015

  1. Chaperone-assisted protein aggregate reactivation: Different solutions for the same problem

    Archives of Biochemistry and Biophysics, Vol. 580, pp. 121-134

  2. ClpB dynamics is driven by its ATPase cycle and regulated by the DnaK system and substrate proteins

    Biochemical Journal, Vol. 466, Núm. 3, pp. 561-570

  3. 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. Crowding activates ClpB and enhances its association with DnaK for efficient protein aggregate reactivation

    Biophysical Journal, Vol. 106, Núm. 9, pp. 2017-2027

2013

  1. Screening and evaluation of small organic molecules as ClpB inhibitors and potential antimicrobials

    Journal of Medicinal Chemistry, Vol. 56, Núm. 18, pp. 7177-7189

  2. 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