JOSE ANGEL
FERNANDEZ HIGUERO
Chercheur/Chercheuse/a dans le période 2016-2020
Publications dans lesquelles il/elle collabore avec JOSE ANGEL FERNANDEZ HIGUERO (13)
2024
2023
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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
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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
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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
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Extraction and Refolding Determinants of Chaperone-Driven Aggregated Protein Reactivation
Journal of Molecular Biology, Vol. 432, Núm. 10, pp. 3239-3250
2019
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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
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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
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Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate
Scientific Reports, Vol. 8, Núm. 1
2016
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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
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Chaperone-assisted protein aggregate reactivation: Different solutions for the same problem
Archives of Biochemistry and Biophysics, Vol. 580, pp. 121-134
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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
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Allosteric communication between the nucleotide binding domains of caseinolytic peptidase B
Journal of Biological Chemistry, Vol. 286, Núm. 29, pp. 25547-25555
2010
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Nucleotide utilization requirements that render ClpB active as a chaperone
FEBS Letters, Vol. 584, Núm. 5, pp. 929-934