Publicaciones en las que colabora con FERNANDO MORO PEREZ (33)

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

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

    Cancers, Vol. 13, Núm. 12

  2. 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

2011

  1. A quantitative analysis of the effect of nucleotides and the M Domain on the Association Equilibrium of ClpB

    Biochemistry, Vol. 50, Núm. 12, pp. 1991-2003

  2. Allosteric communication between the nucleotide binding domains of caseinolytic peptidase B

    Journal of Biological Chemistry, Vol. 286, Núm. 29, pp. 25547-25555

2010

  1. Energetics of nucleotide-induced DnaK conformational states

    Biochemistry, Vol. 49, Núm. 6, pp. 1338-1345

  2. Nucleotide utilization requirements that render ClpB active as a chaperone

    FEBS Letters, Vol. 584, Núm. 5, pp. 929-934