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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2003

Contributo in rivista

Tipo: Articolo in rivista

Titolo: (Active Sequences Collection) database: a new tool to assign functions to protein sequences.

Anno di pubblicazione: 2003

Autori: Facchiano A, Facchiano A, Facchiano F.

Affiliazioni autori: Angelo Facchiano: Istituto di Scienze dell'Alimentazione, CNR, Avellino Antonio Facchiano e Francesco Facchiano: Istituto Dermopatico dell'Immacolata, IDI IRCCS, Roma

Autori CNR:

  • ANGELO FACCHIANO

Lingua: inglese

Abstract: Active Sequences Collection (ASC) is a collection of amino acid sequences, with an unique feature: only short sequences are collected, with a demonstrated biological activity. The current version of ASC consists of three sections: DORRS, a collection of active RGD-containing peptides; TRANSIT, a collection of protein regions active as substrates of transglutaminase enzyme (TGase), and BAC, a collection of short peptides with demonstrated biological activity. Literature references for each entry are reported, as well as cross references to other databases, when available. The current version of ASC includes more than 800 different entries. The main scope of this collection is to offer a new tool to investigate the structural features of protein active sites, additionally to similarity searches against large protein databases or searching for known functional patterns. ASC database is available at the web address http://crisceb.unina2.it/ASC/ which also offers a dedicated query interface to compare user-defined protein sequences with the database, as well as an updating interface to allow contribution of new referenced active sequences.

Pagine da: 379

Pagine a: 382

Rivista:

Nucleic acids research Oxford University Press
Paese di pubblicazione: Regno Unito
Lingua: inglese
ISSN: 0305-1048

Numero volume: 31

DOI: 10.1093/nar/gkg042

Referee: Sė: Internazionale

Indicizzato da: PubMed [12520027]

Parole chiave:

  • database
  • sequenze proteiche
  • attivita' biologica
  • transglutaminasi
  • peptide RGD

Strutture CNR:

 
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