ADELINA PRADO RUIZ-rekin lankidetzan egindako argitalpenak (16)

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

  3. Unzipping the secrets of amyloid disassembly by the human disaggregase

    Cells, Vol. 10, Núm. 10

2019

  1. Structural insights into the ability of nucleoplasmin to assemble and chaperone histone octamers for DNA deposition

    Scientific Reports, Vol. 9, Núm. 1

2016

  1. A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility

    Scientific Reports, Vol. 6

2014

  1. The intrinsically disordered distal face of nucleoplasmin recognizes distinct oligomerization states of histones

    Nucleic Acids Research, Vol. 42, Núm. 2, pp. 1311-1325

2010

  1. Nucleoplasmin binds histone H2A-H2B dimers through its distal face

    Journal of Biological Chemistry, Vol. 285, Núm. 44, pp. 33771-33778

2008

  1. Analysis of phosphorylation of the nuclear chaperona nucleoplasmin

    Proteómica: revista de la Sociedad Española de Proteómica, Núm. 1, pp. 50-50

2007

  1. Phosphorylation of both nucleoplasmin domains is required for activation of its chromatin decondensation activity

    Journal of Biological Chemistry, Vol. 282, Núm. 29, pp. 21213-21221

2005

  1. Nucleoplasmin-mediated unfolding of chromatin involves the displacement of linker-associated chromatin proteins

    Biochemistry, Vol. 44, Núm. 23, pp. 8274-8281

2004

  1. Nucleoplasmin: A nuclear chaperone

    Biochemistry and Cell Biology

2003

  1. Activation mechanism of the nuclear chaperone nucleoplasmin: Role of the core domain

    Journal of Molecular Biology, Vol. 334, Núm. 3, pp. 585-593

2002

  1. Electrostatic interactions at the C-terminal domain of nucleoplasmin modulate its chromatin decondensation activity

    Biochemistry, Vol. 41, Núm. 20, pp. 6408-6413

2001

  1. Structural and functional properties of Escherichia coli-derived nucleoplasmin: A comparative study of recombinant and natural proteins

    European Journal of Biochemistry, Vol. 268, Núm. 6, pp. 1739-1748

1990

  1. Solubilization of sarcoplasmic reticulum membranes by sodium dodecylsulphate. A Fourier-transform infrared spectroscopic study

    FEBS Letters, Vol. 269, Núm. 2, pp. 324-327

1988

  1. An FT-IR study of sarcoplasmic reticulum solubilization by triton X-100

    Mikrochimica Acta, Vol. 94, Núm. 1-6, pp. 385-388