Many protein interactions are mediated by small protein modules binding to short linear peptides. DOMINO (http://mint.bio.uniroma2.it/domino/) is an open-access database comprising more than 3900 annotated experiments describing interactions mediated by protein-interaction domains. DOMINO can be searched with a versatile search tool and the interaction networks can be visualized with a convenient graphic display applet that explicitly identifies the domains/sites involved in the interactions.

Ceol, A., Chatr_aryamontri, A., Santonico, E., Sacco, R., Castagnoli, L., Cesareni, G. (2007). DOMINO: a database of domain-peptide interactions. NUCLEIC ACIDS RESEARCH, 35, D557-D560 [10.1093/nar/gkl961].

DOMINO: a database of domain-peptide interactions

SANTONICO, ELENA;CASTAGNOLI, LUISA;CESARENI, GIOVANNI
2007-01-01

Abstract

Many protein interactions are mediated by small protein modules binding to short linear peptides. DOMINO (http://mint.bio.uniroma2.it/domino/) is an open-access database comprising more than 3900 annotated experiments describing interactions mediated by protein-interaction domains. DOMINO can be searched with a versatile search tool and the interaction networks can be visualized with a convenient graphic display applet that explicitly identifies the domains/sites involved in the interactions.
2007
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/18 - GENETICA
English
Con Impact Factor ISI
peptide; access to information; article; computer interface; DOMINO database; Internet; priority journal; protein database; protein domain; protein interaction; proteomics; Binding Sites; Databases, Protein; Internet; Ligands; Peptides; Protein Interaction Mapping; Protein Structure, Tertiary; User-Computer Interface
Ceol, A., Chatr_aryamontri, A., Santonico, E., Sacco, R., Castagnoli, L., Cesareni, G. (2007). DOMINO: a database of domain-peptide interactions. NUCLEIC ACIDS RESEARCH, 35, D557-D560 [10.1093/nar/gkl961].
Ceol, A; Chatr_aryamontri, A; Santonico, E; Sacco, R; Castagnoli, L; Cesareni, G
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/35165
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