Publicaciones en colaboración con investigadoras/es de Centro de Investigaciones Biológicas (11)

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. Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE

    Journal of Biological Chemistry, Vol. 290, Núm. 16, pp. 10083-10092

  2. Sedimentation Equilibrium Analysis of ClpB Self-Association in Diluted and Crowded Solutions

    Methods in Enzymology (Academic Press Inc.), pp. 135-160

2014

  1. Crowding activates ClpB and enhances its association with DnaK for efficient protein aggregate reactivation

    Biophysical Journal, Vol. 106, Núm. 9, pp. 2017-2027

2011

  1. 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

  2. Nuclear transporters in a multinucleated organism: Functional and localization analyses in Aspergillus nidulans

    Molecular Biology of the Cell, Vol. 22, Núm. 20, pp. 3874-3886

2008

  1. NapA and NapB are the Aspergillus nidulans Nap/SET family members and NapB is a nuclear protein specifically interacting with importin α

    Fungal Genetics and Biology, Vol. 45, Núm. 3, pp. 278-291

1999

  1. ATP hydrolysis induces an intermediate conformational state in GroEL

    European Journal of Biochemistry, Vol. 259, Núm. 1-2, pp. 347-355

1993

  1. Structural and Functional Studies on the Interaction of Sodium Dodecyl Sulfate with β-Galactosidase

    Archives of Biochemistry and Biophysics, Vol. 300, Núm. 1, pp. 451-457

1989

  1. An infrared spectroscopic study of β-galactosidase structure in aqueous solutions

    FEBS Letters, Vol. 252, Núm. 1-2, pp. 118-120

1988

  1. Interaction of SDS with β-galactosidase. A FT-IR study of the influence of detergent concentration and temperature.

    Journal of Molecular Structure, Vol. 175, Núm. C, pp. 67-72