Literature DB >> 15044227

The DISOPRED server for the prediction of protein disorder.

Jonathan J Ward1, Liam J McGuffin, Kevin Bryson, Bernard F Buxton, David T Jones.   

Abstract

UNLABELLED: Dynamically disordered regions appear to be relatively abundant in eukaryotic proteomes. The DISOPRED server allows users to submit a protein sequence, and returns a probability estimate of each residue in the sequence being disordered. The results are sent in both plain text and graphical formats, and the server can also supply predictions of secondary structure to provide further structural information. AVAILABILITY: The server can be accessed by non-commercial users at http://bioinf.cs.ucl.ac.uk/disopred/

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Year:  2004        PMID： 15044227     DOI： 10.1093/bioinformatics/bth195

Source DB:  PubMed          Journal:  Bioinformatics        ISSN： 1367-4803            Impact factor:   6.937


  312 in total

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Journal:  Bioinformatics       Date:  2012-06-15       Impact factor: 6.937

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9.  Multiple proteolytic events in caspase-6 self-activation impact conformations of discrete structural regions.

Authors:  Kevin B Dagbay; Jeanne A Hardy
Journal:  Proc Natl Acad Sci U S A       Date:  2017-09-01       Impact factor: 11.205

10.  Understanding the physical properties that control protein crystallization by analysis of large-scale experimental data.

Authors:  W Nicholson Price; Yang Chen; Samuel K Handelman; Helen Neely; Philip Manor; Richard Karlin; Rajesh Nair; Jinfeng Liu; Michael Baran; John Everett; Saichiu N Tong; Farhad Forouhar; Swarup S Swaminathan; Thomas Acton; Rong Xiao; Joseph R Luft; Angela Lauricella; George T DeTitta; Burkhard Rost; Gaetano T Montelione; John F Hunt
Journal:  Nat Biotechnol       Date:  2009-01       Impact factor: 54.908
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