Maria J. Macias

    Research Group: 
    Structural characterization of macromolecular assemblies
    Unit: 
    STRUCTURAL & COMPUTATIONAL BIOLOGY
    Position: 
    Group Leader
    Office: 
    EM01B41-42
    Telephone: 
    +34 93 40 37189
    Email: 
    maria.macias@irbbarcelona.org

    ICREA Research Professor

     

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    Born in Zamora, Spain, in 1964. Degree in Chemistry from the University of Salamanca, Spain (1989). Currently working at the Department of Structural and Computational Biology at the Institute for Research in Biomedicine –IRB Barcelona.

    Ph.D. student in the group of Prof. Manuel Grande Benito, Dep. of Organic Chemistry Facultad de Ciencias Químicas, University of Salamanca (1989-1993). Postdoctoral Fellow in the group of Prof. Hartmut Oschkinat, department of structures and biocomputing EMBL, Heidelberg (Germany, 1993-98). Staff-Scientist l EMBL, department of structures and biocomputing EMBL, Heidelberg (Germany 1998-2002). ICREA researcher at the Institute for the Research in Biomedicine –IRB (Since 2002 till present).

    Research activity focus on the Structural characterization of biomolecules by Nuclear Magnetic resonance.

    Meet our scientists Videos

    Maria Macias: "Insights into the puzzle of life"

    Selected group publications

    Preventing fibril formation of a protein by selective mutation
    Maisuradze GG, Medina J, Kachlishvili K, Krupa P, Mozolewska MA, Martin-Malpartida P, Maisuradze L, Macias MJ and Scheraga HA.
    P Natl Acad Sci Usa, 112 (44), 13549-54 (2015)
    Structural Analysis of the Pin1-CPEB1 interaction and its potential role in CPEB1 degradation
    Schelhorn C, Martín-Malpartida P, Suñol D and Macias MJ.
    Sci Rep, 5 14990 (2015)
    Structural determinants of Smad function in TGF-β signaling
    Macias MJ, Martin-Malpartida P and Massagué J.
    Trends Biochem Sci, 40 (6), 296-308 (2015)
    Structure of the N-terminal domain of the protein Expansion: an `Expansion' to the Smad MH2 fold
    Beich-Frandsen M, Aragón E, Llimargas M, Benach J, Riera A, Pous J and Macias MJ.
    Acta Crystallogr D, 71 (Pt 4), 844-53 (2015)
    RNA recognition and self-association of CPEB4 is mediated by its tandem RRM domains
    Schelhorn C, Gordon JM, Ruiz L, Alguacil J, Pedroso E and Macias MJ.
    Nucleic Acids Res, 42 (15), 10185-95 (2014)
    Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways
    Aragón E, Goerner N, Xi Q, Gomes T, Gao S, Massagué J and Macias MJ.
    Structure, 20 (10), 1726-36 (2012)
    Fine-tuning the π-π aromatic interactions in peptides: somatostatin analogues containing mesityl alanine
    Martín-Gago P, Gomez-Caminals M, Ramón R, Verdaguer X, Martin-Malpartida P, Aragón E, Fernández-Carneado J, Ponsati B, López-Ruiz P, Cortes MA, Colás B, Macias MJ and Riera A.
    Angew Chem Int Edit, 51 (8), 1820-5 (2012)
    SSTR1- and SSTR3-Selective Somatostatin Analogues
    Ramón R, Martín-Gago P, Verdaguer X, Macias MJ, Martin-Malpartida P, Fernández-Carneado J, Gomez-Caminals M, Ponsati B, López-Ruiz P, Cortés MA, Colás B and Riera A.
    Chembiochem, 12 (4), 625-32 (2011)
    A Smad action turnover switch operated by WW domain readers of a phosphoserine code
    Aragón E, Goerner N, Zaromytidou AI, Xi Q, Escobedo A, Massagué J and Macias MJ.
    Gene Dev, 25 (12), 1275-88 (2011)
    Ubiquitin ligase Nedd4L targets activated Smad2/3 to limit TGF-beta signaling
    Gao S, Alarcón C, Sapkota G, Rahman S, Chen PY, Goerner N, Macias MJ, Erdjument-Bromage H, Tempst P and Massagué J.
    Mol Cell, 36 (3), 457-68 (2009)
    NMR structural studies on human p190-A RhoGAPFF1 revealed that domain phosphorylation by the PDGF-receptor alpha requires its previous unfolding
    Bonet R, Ruiz L, Aragón E, Martín-Malpartida P and Macias MJ.
    J Mol Biol, 389 (2), 230-7 (2009)
    Nuclear CDKs drive Smad transcriptional activation and turnover in BMP and TGF-beta pathways
    Alarcón C, Zaromytidou AI, Xi Q, Gao S, Yu J, Fujisawa S, Barlas A, Miller AN, Manova-Todorova K, Macias MJ, Sapkota G, Pan D and Massagué J.
    Cell, 139 (4), 757-69 (2009)
    NMR structural studies of the ItchWW3 domain reveal that phosphorylation at T30 inhibits the interaction with PPxY-containing ligands
    Morales B, Ramirez-Espain X, Shaw AZ, Martin-Malpartida P, Yraola F, Sánchez-Tilló E, Farrera C, Celada A, Royo M and Macias MJ
    Structure, 15 473-83 (2007)
    Full publication list