Publicaciones en colaboración con investigadores/as de Brigham and Women's Hospital (11)

2017

  1. The FASTK family of proteins: Emerging regulators of mitochondrial RNA biology

    Nucleic Acids Research, Vol. 45, Núm. 19, pp. 10941-10947

2016

  1. Deletion of FAST (Fas-activated serine/threonine phosphoprotein) ameliorates immune complex arthritis in mice

    Modern Rheumatology, Vol. 26, Núm. 4, pp. 630-632

2015

  1. A Mitochondria-Specific Isoform of FASTK Is Present In Mitochondrial RNA Granules and Regulates Gene Expression and Function

    Cell Reports, Vol. 10, Núm. 7, pp. 1110-1121

2012

  1. The translational repressor T-cell intracellular antigen-1 (TIA-1) is a key modulator of Th2 and Th17 responses driving pulmonary inflammation induced by exposure to house dust mite

    Immunology Letters, Vol. 146, Núm. 1-2, pp. 8-14

2011

  1. Rapid IgE desensitization is antigen specific and impairs early and late mast cell responses targeting FcεRI internalization

    European Journal of Immunology, Vol. 41, Núm. 4, pp. 1004-1013

2010

  1. Fas-activated serine/threonine phosphoprotein promotes immune-mediated pulmonary inflammation

    Journal of Immunology, Vol. 184, Núm. 9, pp. 5325-5332

  2. Fast kinase domain-containing protein 3 is a mitochondrial protein essential for cellular respiration

    Biochemical and Biophysical Research Communications, Vol. 401, Núm. 3, pp. 440-446

2007

  1. Fas-activated serine/threonine phosphoprotein (FAST) is a regulator of alternative splicing

    Proceedings of the National Academy of Sciences of the United States of America, Vol. 104, Núm. 27, pp. 11370-11375

  2. T-cell intracellular antigen-1 (TIA-1)-induced translational silencing promotes the decay of selected mRNAs

    Journal of Biological Chemistry, Vol. 282, Núm. 41, pp. 30070-30077

2004

  1. FAST is a survival protein that senses mitochondrial stress and modulates TIA-1-regulated changes in protein expression

    Molecular and Cellular Biology, Vol. 24, Núm. 24, pp. 10718-10732

  2. SAP increases FynT kinase activity and is required for phosphorylation of SLAM and Ly9

    International Immunology, Vol. 16, Núm. 5, pp. 727-736