Showing Publication Results for :

MINT - a Molecular INTeractions database
Resource Category : Webserver -> Protein -> Interactions, Pathways, Enzymes

  1. Title of the Paper : MINT, the molecular interaction database: 2009 update (View at PubMed)
    Contributors : Ceol, A.; Chatr Aryamontri, A.; Licata, L.; Peluso, D.; Briganti, L.; Perfetto, L.; Castagnoli, L.; Cesareni, G.
    Address : Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica, 00133 Rome. arnaud.ceol@uniroma2.it
    Publication Name : Nucleic Acids Res
    Volume : 38
    Issue : Database issue
    Pages : D532-9
    Publication Year : 2010
    ISSN : 1362-4962 (Electronic) 0305-1048 (Linking)
    Language : English
    Abstract : MINT (http://mint.bio.uniroma2.it/mint) is a public repository for molecular interactions reported in peer-reviewed journals. Since its last report, MINT has grown considerably in size and evolved in scope to meet the requirements of its users. The main changes include a more precise definition of the curation policy and the development of an enhanced and user-friendly interface to facilitate the analysis of the ever-growing interaction dataset. MINT has adopted the PSI-MI standards for the annotation and for the representation of molecular interactions and is a member of the IMEx consortium.



  2. Title of the Paper : MINT: a Molecular INTeraction database (View at PubMed)
    Contributors : Zanzoni, A.; Montecchi-Palazzi, L.; Quondam, M.; Ausiello, G.; Helmer-Citterich, M.; Cesareni, G.
    Address : Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica, 00133 Rome, Italy.
    Publication Name : FEBS Lett
    Volume : 513
    Issue : 1
    Pages : 135-40
    Publication Year : 2002
    ISSN : 0014-5793 (Print) 0014-5793 (Linking)
    Language : English
    Abstract : Protein interaction databases represent unique tools to store, in a computer readable form, the protein interaction information disseminated in the scientific literature. Well organized and easily accessible databases permit the easy retrieval and analysis of large interaction data sets. Here we present MINT, a database (http://cbm.bio.uniroma2.it/mint/index.html) designed to store data on functional interactions between proteins. Beyond cataloguing binary complexes, MINT was conceived to store other types of functional interactions, including enzymatic modifications of one of the partners. Release 1.0 of MINT focuses on experimentally verified protein-protein interactions. Both direct and indirect relationships are considered. Furthermore, MINT aims at being exhaustive in the description of the interaction and, whenever available, information about kinetic and binding constants and about the domains participating in the interaction is included in the entry. MINT consists of entries extracted from the scientific literature by expert curators assisted by \'MINT Assistant\', a software that targets abstracts containing interaction information and presents them to the curator in a user-friendly format. The interaction data can be easily extracted and viewed graphically through \'MINT Viewer\'. Presently MINT contains 4568 interactions, 782 of which are indirect or genetic interactions.