ArticleNucleic acids research2004
DSDBASE: a consortium of native and modelled disulphide bonds in proteins.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
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- Rational Design of Disulfide Bridges inMolecules (Basel, Switzerland) · 2023Article
- Disulfide Bond Engineering for Enhancing the Thermostability of the Maltotetraose-Forming Amylase fromFoods (Basel, Switzerland) · 2022Article
- DSDBASE 2.0: updated version of DiSulphide dataBASE, a database on disulphide bonds in proteins.Database : the journal of biological databases and curation · 2022Article
- The Activity of Escherichia coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain.Journal of bacteriology · 2016Article
- Article
- The RdgC protein employs a novel mechanism involving a finger domain to bind to circular DNA.Nucleic acids research · 2010Article
- Binding mode prediction of conformationally restricted anandamide analogs within the CB1 receptor.Journal of molecular signaling · 2008Article
- IWS: integrated web server for protein sequence and structure analysis.Bioinformation · 2007Article
- Posttranslational protein modification in Archaea.Microbiology and molecular biology reviews : MMBR · 2005Review
- HCA and HML isolated from the red marine algae Hypnea cervicornis and Hypnea musciformis define a novel lectin family.Protein science : a publication of the Protein Society · 2005Article
- CysView: protein classification based on cysteine pairing patterns.Nucleic acids research · 2004Article
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Authors and funding
4 authors.
Funding
Abstract
DSDBASE is a database of disulphide bonds in proteins, which provides information on native disulphides and those that are stereochemically possible between pairs of residues for all known protein structural entries. The modelling of disulphides has been performed, using MODIP, by the identification of residue pairs that can strainlessly accommodate a covalent cross-link. We also assess the stereochemical quality of the covalent cross-link and grade them appropriately. One of the potential uses of the database is to design site-directed mutants in order to enhance the thermal stability of a protein. The proposed sites of mutations can be viewed specifically with respect to active sites of enzymes and across physiological dimers. The occurrence of native and modelled disulphides increases the dimensions of the database enormously. This database can also be employed for proposing three-dimensional models of disulphide-rich short polypeptides. The database can be accessed from http://www.ncbs.res.in/ approximately faculty/mini/dsdbase/dsdbase.html. Supplementary information can be accessed from http://www.ncbs.res.in/ approximately faculty/mini/dsdbase/nar/suppl.htm.
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