Search Results - (Author, Cooperation:M. Ribo)

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  1. 1
    J. Casares ; I. Negueruela ; M. Ribo ; I. Ribas ; J. M. Paredes ; A. Herrero ; S. Simon-Diaz
    Nature Publishing Group (NPG)
    Published 2014
    Staff View
    Publication Date:
    2014-01-17
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Published by:
    http://www.nature.com/

    Latest Papers from Table of Contents or Articles in Press
  2. 2
    J. Aleksic ; S. Ansoldi ; L. A. Antonelli ; P. Antoranz ; A. Babic ; P. Bangale ; J. A. Barrio ; J. Becerra Gonzalez ; W. Bednarek ; E. Bernardini ; B. Biasuzzi ; A. Biland ; O. Blanch ; S. Bonnefoy ; G. Bonnoli ; F. Borracci ; T. Bretz ; E. Carmona ; A. Carosi ; P. Colin ; E. Colombo ; J. L. Contreras ; J. Cortina ; S. Covino ; P. Da Vela ; F. Dazzi ; A. De Angelis ; G. De Caneva ; B. De Lotto ; E. de Ona Wilhelmi ; C. Delgado Mendez ; D. Dominis Prester ; D. Dorner ; M. Doro ; S. Einecke ; D. Eisenacher ; D. Elsaesser ; M. V. Fonseca ; L. Font ; K. Frantzen ; C. Fruck ; D. Galindo ; R. J. Garcia Lopez ; M. Garczarczyk ; D. Garrido Terrats ; M. Gaug ; N. Godinovic ; A. Gonzalez Munoz ; S. R. Gozzini ; D. Hadasch ; Y. Hanabata ; M. Hayashida ; J. Herrera ; D. Hildebrand ; J. Hose ; D. Hrupec ; W. Idec ; V. Kadenius ; H. Kellermann ; K. Kodani ; Y. Konno ; J. Krause ; H. Kubo ; J. Kushida ; A. La Barbera ; D. Lelas ; N. Lewandowska ; E. Lindfors ; S. Lombardi ; F. Longo ; M. Lopez ; R. Lopez-Coto ; A. Lopez-Oramas ; E. Lorenz ; I. Lozano ; M. Makariev ; K. Mallot ; G. Maneva ; N. Mankuzhiyil ; K. Mannheim ; L. Maraschi ; B. Marcote ; M. Mariotti ; M. Martinez ; D. Mazin ; U. Menzel ; J. M. Miranda ; R. Mirzoyan ; A. Moralejo ; P. Munar-Adrover ; D. Nakajima ; A. Niedzwiecki ; K. Nilsson ; K. Nishijima ; K. Noda ; R. Orito ; A. Overkemping ; S. Paiano ; M. Palatiello ; D. Paneque ; R. Paoletti ; J. M. Paredes ; X. Paredes-Fortuny ; M. Persic ; J. Poutanen ; P. G. Prada Moroni ; E. Prandini ; I. Puljak ; R. Reinthal ; W. Rhode ; M. Ribo ; J. Rico ; J. Rodriguez Garcia ; S. Rugamer ; T. Saito ; K. Saito ; K. Satalecka ; V. Scalzotto ; V. Scapin ; C. Schultz ; T. Schweizer ; S. N. Shore ; A. Sillanpaa ; J. Sitarek ; I. Snidaric ; D. Sobczynska ; F. Spanier ; V. Stamatescu ; A. Stamerra ; T. Steinbring ; J. Storz ; M. Strzys ; L. Takalo ; H. Takami ; F. Tavecchio ; P. Temnikov ; T. Terzic ; D. Tescaro ; M. Teshima ; J. Thaele ; O. Tibolla ; D. F. Torres ; T. Toyama ; A. Treves ; M. Uellenbeck ; P. Vogler ; R. Zanin ; M. Kadler ; R. Schulz ; E. Ros ; U. Bach ; F. Krauss ; J. Wilms
    American Association for the Advancement of Science (AAAS)
    Published 2014
    Staff View
    Publication Date:
    2014-11-08
    Publisher:
    American Association for the Advancement of Science (AAAS)
    Print ISSN:
    0036-8075
    Electronic ISSN:
    1095-9203
    Topics:
    Biology
    Chemistry and Pharmacology
    Computer Science
    Medicine
    Natural Sciences in General
    Physics
    Published by:
    http://www.aaas.org/

    Latest Papers from Table of Contents or Articles in Press
  3. 3
    Staff View
    ISSN:
    0003-2697
    Source:
    Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics:
    Biology
    Chemistry and Pharmacology
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1006/abio.1994.1234

    Articles: DFG German National Licenses
  4. 4
    Staff View
    ISSN:
    1420-9071
    Keywords:
    Key words. Ribonuclease; binding sites; RNA; catalysis; enzyme kinetics.
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Biology
    Medicine
    Notes:
    Abstract. The enzymatic catalysis of polymeric substrates such as proteins, polysaccharides or nucleic acids requires precise alignment between the enzyme and the substrate regions flanking the region occupying the active site. In the case of ribonucleases, enzyme-substrate binding may be directed by electrostatic interactions between the phosphate groups of the RNA molecule and basic amino acid residues on the enzyme. Specific interactions between the nitrogenated bases and particular amino acids in the active site or adjacent positions may also take place. The substrate-binding subsites of ribonuclease A have been characterized by structural and kinetic studies. In addition to the active site (p1 ), the role of other noncatalytic phosphate-binding subsites in the correct alignment of the polymeric substrate has been proposed. p2 and p0 have been described as phosphate-binding subsites that bind the phosphate group adjacent to the 3′ side and 5′ side, respectively, of the phosphate in the active site. In both cases, basic amino acids (Lys-7 and Arg-10 in p2 , and Lys-66 in p0 ) are involved in binding. However, these binding sites play different roles in the catalytic process of ribonuclease A. The electrostatic interactions in p2 are important both in catalysis and in the endonuclease activity of the enzyme, whilst the p0 electrostatic interaction contributes only to binding of the RNA.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/s000180050205

    Articles: DFG German National Licenses