![Foto de FERNANDO](/img/nophoto.png)
FERNANDO
MORO PEREZ
INVESTIGADOR/A DOCTOR/A PERMANENTE
Publications (42) FERNANDO MORO PEREZ publications
2024
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A Targetable N-Terminal Motif Orchestrates α-Synuclein Oligomer-to-Fibril Conversion
Journal of the American Chemical Society
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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
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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
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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
2022
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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
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Inhibition of the human hsc70 system by small ligands as a potential anticancer approach
Cancers, Vol. 13, Núm. 12
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Unzipping the secrets of amyloid disassembly by the human disaggregase
Cells, Vol. 10, Núm. 10
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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The complex phosphorylation patterns that regulate the activity of Hsp70 and its cochaperones
International Journal of Molecular Sciences, Vol. 20, Núm. 17
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
2017
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Label-Free, Multiplexed, Single-Molecule Analysis of Protein-DNA Complexes with Nanopores
ACS Nano, Vol. 11, Núm. 6, pp. 5815-5825
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
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Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE
Journal of Biological Chemistry, Vol. 290, Núm. 16, pp. 10083-10092
2014
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Crowding activates ClpB and enhances its association with DnaK for efficient protein aggregate reactivation
Biophysical Journal, Vol. 106, Núm. 9, pp. 2017-2027
2013
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Screening and evaluation of small organic molecules as ClpB inhibitors and potential antimicrobials
Journal of Medicinal Chemistry, Vol. 56, Núm. 18, pp. 7177-7189
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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
2012
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Regulation of the type IV secretion ATPase TrwD by magnesium: Implications for catalytic mechanism of the secretion ATPase superfamily
Journal of Biological Chemistry, Vol. 287, Núm. 21, pp. 17408-17414
2011
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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