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Cited by 1,562

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

New and continuing developments at PROSITE

Open access
Sigrist, Christian J. A., de Castro, Edouard, Cerutti, Lorenzo, Cuche, Béatrice A., Hulo, Nicolas, Bridge, Alan, Bougueleret, Lydie, Xenarios, Ioannis·2012·Nucleic Acids Research
DOI 10.1093/nar/gks1067
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Abstract

PROSITE (http://prosite.expasy.org/) consists of documentation entries describing protein domains, families and functional sites, as well as associated patterns and profiles to identify them. It is complemented by ProRule a collection of rules, which increases the discriminatory power of these profiles and patterns by providing additional information about functionally and/or structurally critical amino acids. PROSITE signatures, together with ProRule, are used for the annotation of domains and features of UniProtKB/Swiss-Prot entries. Here, we describe recent developments that allow users to perform whole-proteome annotation as well as a number of filtering options that can be combined to perform powerful targeted searches for biological discovery. The latest version of PROSITE (release 20.85, of 30 August 2012) contains 1308 patterns, 1039 profiles and 1041 ProRules.

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Cites

  • PROSITE: a documented database using patterns and profiles as motif descriptors

    Sigrist, C. J. A. (2002) · Briefings in Bioinformatics · doi:10.1093/bib/3.3.265 · Cited by 913 · cited 2×

    “These regions are identified using two types of signatures: generalized profiles (weight matrices) that describe protein families and modular protein domains and patterns (regular expressions) that describe short sequence motifs often corresponding to functionally or structurally important residues (1).”
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Show all 1 references

Research works printed but not linked: 13

  1. Sigrist, 2005, ProRule: a new database containing functional and structural information on PROSITE profiles, Bioinformatics, 21, 4060, 10.1093/bioinformatics/bti614 · DOI
  2. The UniProt Consortium, 2012, Reorganizing the protein space at the Universal Protein Resource (UniProt), Nucleic Acids Res., 40, D71, 10.1093/nar/gkr981 · DOI · Paper page
  3. de Castro, 2006, ScanProsite: detection of PROSITE signature matches and ProRule-associated functional and structural residues in proteins, Nucleic Acids Res., 34, W362, 10.1093/nar/gkl124 · DOI · Paper page
  4. Hunter, 2012, InterPro in 2011: new developments in the family and domain prediction database, Nucleic Acids Res., 40, D306, 10.1093/nar/gkr948 · DOI · Paper page
  5. Sigrist, 2010, PROSITE, a protein domain database for functional characterization and annotation, Nucleic Acids Res., 38, D161, 10.1093/nar/gkp885 · DOI
  6. Wurm, 2011, The genome of the fire ant Solenopsis invicta, Proc. Natl Acad. Sci. USA, 108, 5679, 10.1073/pnas.1009690108 · DOI · Paper page
  7. Hulo, 2008, The 20 years of PROSITE, Nucleic Acids Res., 36, D245, 10.1093/nar/gkm977 · DOI · Paper page
  8. Levitt, 2009, Nature of the protein universe, Proc. Natl Acad. Sci. USA, 106, 11079, 10.1073/pnas.0905029106 · DOI · Paper page
  9. Buljan, 2009, The evolution of protein domain families, Biochem. Soc. Trans., 37, 751, 10.1042/BST0370751 · DOI
  10. Bastian, 2008, Bgee: integrating and comparing heterogeneous transcriptome data among species, 124, 10.1007/978-3-540-69828-9_12 · DOI
  11. Watschinger, 2010, Identification of the gene encoding alkylglycerol monooxygenase defines a third class of tetrahydrobiopterin-dependent enzymes, Proc. Natl Acad. Sci. USA, 107, 13672, 10.1073/pnas.1002404107 · DOI
  12. Watschinger, 2009, Glyceryl ether monooxygenase resembles aromatic amino acid hydroxylases in metal ion and tetrahydrobiopterin dependence, Biol. Chem., 390, 3, 10.1515/BC.2009.010 · DOI
  13. Soodsma, 1972, Partial characterization of the alkylglycerol cleavage enzyme system of rat liver, J. Biol. Chem., 247, 3923, 10.1016/S0021-9258(19)45123-5 · DOI

Cited by

Metadata

Authors
Sigrist, C. J. A., de Castro, E., Cerutti, L., Cuche, B. A., Hulo, N., Bridge, A., Bougueleret, L., & Xenarios, I.
Venue
Nucleic Acids Research
Publisher
Oxford University Press (OUP)
Published
2012-11-17
Volume
41
Issue
D1
Pages
D344-D347
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
DOI
10.1093/nar/gks1067
OpenAlex
W2107158607
Cited by
1,562
References
1
FWCI
22.54
Type
journal article
Language
en
Open access
gold
Licence
creativecommons.org/licenses/by-nc/3.0 (vor, 1417 d)

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