DISULFIND: a disulfide bonding state and cysteine connectivity prediction server
Top Cited Papers
Open Access
- 1 July 2006
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 34 (Web Server), W177-W181
- https://doi.org/10.1093/nar/gkl266
Abstract
DISULFIND is a server for predicting the disulfide bonding state of cysteines and their disulfide connectivity starting from sequence alone. Optionally, disulfide connectivity can be predicted from sequence and a bonding state assignment given as input. The output is a simple visualization of the assigned bonding state (with confidence degrees) and the most likely connectivity patterns. The server is available at http://disulfind.dsi.unifi.it/.Keywords
This publication has 16 references indexed in Scilit:
- Large‐scale prediction of disulphide bridges using kernel methods, two‐dimensional recursive neural networks, and weighted graph matchingProteins-Structure Function and Bioinformatics, 2005
- SCRATCH: a protein structure and structural feature prediction serverNucleic Acids Research, 2005
- Disulfide connectivity prediction using secondary structure information and diresidue frequenciesBioinformatics, 2005
- Prediction of disulfide‐bonded cysteines in proteomes with a hidden neural networkProteomics, 2004
- Prediction of the disulfide-bonding state of cysteines in proteins based on dipeptide compositionBiochemical and Biophysical Research Communications, 2004
- Disulfide connectivity prediction using recursive neural networks and evolutionary informationBioinformatics, 2004
- Predicting the disulfide bonding state of cysteines using protein descriptorsProteins-Structure Function and Bioinformatics, 2002
- Prediction of disulfide connectivity in proteinsBioinformatics, 2001
- Predicting the oxidation state of cysteines by multiple sequence alignmentBioinformatics, 2000
- Role of evolutionary information in predicting the disulfide-bonding state of cysteine in proteins.1999