Protein Folding and Chaperones Laboratory
Centro Nacional de Biotecnología
Madrid, EspañaPublicaciones en colaboración con investigadores/as de Centro Nacional de Biotecnología (9)
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
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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Truncation‐driven lateral association of α‐synuclein hinders amyloid clearance by the Hsp70‐based disaggregase
International Journal of Molecular Sciences, Vol. 22, Núm. 23
2015
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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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The intrinsically disordered distal face of nucleoplasmin recognizes distinct oligomerization states of histones
Nucleic Acids Research, Vol. 42, Núm. 2, pp. 1311-1325
2013
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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
2008
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The structure of CCT-Hsc70NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin
Nature Structural and Molecular Biology, Vol. 15, Núm. 8, pp. 858-864
2002
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Salt bridges at the inter-ring interface regulate the thermostat of GroEL
Journal of Biological Chemistry, Vol. 277, Núm. 37, pp. 34024-34029