The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
PROSITE, a protein domain database for functional characterization and annotation
Open accessAbstract
PROSITE 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 based on profiles and patterns, which increases the discriminatory power of these profiles and patterns by providing additional information about functionally and/or structurally critical amino acids. PROSITE is largely used for the annotation of domain features of UniProtKB/Swiss-Prot entries. Among the 983 (DNA-binding) domains, repeats and zinc fingers present in Swiss-Prot (release 57.8 of 22 September 2009), 696 ( approximately 70%) are annotated with PROSITE descriptors using information from ProRule. In order to allow better functional characterization of domains, PROSITE developments focus on subfamily specific profiles and a new profile building method giving more weight to functionally important residues. Here, we describe AMSA, an annotated multiple sequence alignment format used to build a new generation of generalized profiles, the migration of ScanProsite to Vital-IT, a cluster of 633 CPUs, and the adoption of the Distributed Annotation System (DAS) to facilitate PROSITE data integration and interchange with other sources. The latest version of PROSITE (release 20.54, of 22 September 2009) contains 1308 patterns, 863 profiles and 869 ProRules. PROSITE is accessible at: http://www.expasy.org/prosite/.
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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302
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×
“Each PROSITE signature is linked to an annotation document where the user can find information on the protein family or domain detected by the signature, such as the origin of its name, taxonomic occurrence, domain architecture, function, 3D structure, main characteristics of the sequence, domain size and literature r…”
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Cited by
MAFFT Multiple Sequence Alignment Software Version 7: Improvements in Performance and Usability
Katoh, K., & Standley, D. M. (2013) · Molecular Biology and Evolution · doi:10.1093/molbev/mst010 · Cited by 46,209
The Pfam protein families database
Punta, M., Coggill, P. C., Eberhardt, R. Y., Mistry, J., Tate, J., Boursnell, C., Pang, N., Forslund, K., Ceric, G., Clements, J., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gkr1065 · Cited by 3,719
Detecting differential usage of exons from RNA-seq data
Anders, S., Reyes, A., & Huber, W. (2012) · Genome Research · doi:10.1101/gr.133744.111 · Cited by 1,545
Claudins and the Modulation of Tight Junction Permeability
Günzel, D., & Yu, A. S. L. (2013) · Physiological Reviews · doi:10.1152/physrev.00019.2012 · Cited by 1,456
MuSiC: Identifying mutational significance in cancer genomes
Dees, N. D., Zhang, Q., Kandoth, C., Wendl, M. C., Schierding, W., Koboldt, D. C., Mooney, T. B., Callaway, M. B., Dooling, D., Mardis, E. R., et al. (2012) · Genome Research · doi:10.1101/gr.134635.111 · Cited by 677
Metadata
- Authors
- Sigrist, C. J. A., Cerutti, L., de Castro, E., Langendijk-Genevaux, P. S., Bulliard, V., Bairoch, A., & Hulo, N.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2009-10-24
- Volume
- 38
- Issue
- suppl_1
- Pages
- D161-D166
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2155744824
- Cited by
- 858
- References
- 2
- FWCI
- 32.77
- Type
- journal article
- Language
- en
- Open access
- gold
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