Publicaciones en las que colabora con JOSE ANGEL FERNANDEZ HIGUERO (13)

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

2020

  1. Extraction and Refolding Determinants of Chaperone-Driven Aggregated Protein Reactivation

    Journal of Molecular Biology, Vol. 432, Núm. 10, pp. 3239-3250

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. Structural and functional insights on the roles of molecular chaperones in the mistargeting and aggregation phenotypes associated with primary hyperoxaluria type I

    Advances in Protein Chemistry and Structural Biology (Academic Press Inc.), pp. 119-152

2018

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

    Scientific Reports, Vol. 8, Núm. 1

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

2011

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

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

2010

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

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