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Kevin Bryson

University of Glasgow

ORCID: 0000-0002-1163-6368

Publishes on Bioinformatics and Genomic Networks, Mitochondrial Function and Pathology, Cancer, Hypoxia, and Metabolism. 111 papers and 10.8k citations.

111Publications
10.8kTotal Citations

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Top publicationsby citations

The PSIPRED protein structure prediction server
Cited by 3.9k

SUMMARY: The PSIPRED protein structure prediction server allows users to submit a protein sequence, perform a prediction of their choice and receive the results of the prediction both textually via e-mail and graphically via the web. The user may select one of three prediction methods to apply to their sequence: PSIPRED, a highly accurate secondary structure prediction method; MEMSAT 2, a new version of a widely used transmembrane topology prediction method; or GenTHREADER, a sequence profile based fold recognition method. AVAILABILITY: Freely available to non-commercial users at http://globin.bio.warwick.ac.uk/psipred/

Scalable web services for the PSIPRED Protein Analysis Workbench
Daniel Buchan, Federico Minneci, Tim C. O. Nugent et al.|Nucleic Acids Research|2013
Cited by 1.3kOpen Access

Here, we present the new UCL Bioinformatics Group's PSIPRED Protein Analysis Workbench. The Workbench unites all of our previously available analysis methods into a single web-based framework. The new web portal provides a greatly streamlined user interface with a number of new features to allow users to better explore their results. We offer a number of additional services to enable computationally scalable execution of our prediction methods; these include SOAP and XML-RPC web server access and new HADOOP packages. All software and services are available via the UCL Bioinformatics Group website at http://bioinf.cs.ucl.ac.uk/.

A large-scale evaluation of computational protein function prediction
Predrag Radivojac, Wyatt T. Clark, Tal Oron et al.|Nature Methods|2013
Cited by 1.1kOpen Access

Automated annotation of protein function is challenging. As the number of sequenced genomes rapidly grows, the overwhelming majority of protein products can only be annotated computationally. If computational predictions are to be relied upon, it is crucial that the accuracy of these methods be high. Here we report the results from the first large-scale community-based critical assessment of protein function annotation (CAFA) experiment. Fifty-four methods representing the state of the art for protein function prediction were evaluated on a target set of 866 proteins from 11 organisms. Two findings stand out: (i) today's best protein function prediction algorithms substantially outperform widely used first-generation methods, with large gains on all types of targets; and (ii) although the top methods perform well enough to guide experiments, there is considerable need for improvement of currently available tools.

Protein structure prediction servers at University College London
Kevin Bryson, Liam J. McGuffin, R. L. Marsden et al.|Nucleic Acids Research|2005
Cited by 729Open Access

A number of state-of-the-art protein structure prediction servers have been developed by researchers working in the Bioinformatics Unit at University College London. The popular PSIPRED server allows users to perform secondary structure prediction, transmembrane topology prediction and protein fold recognition. More recent servers include DISOPRED for the prediction of protein dynamic disorder and DomPred for domain boundary prediction. These servers are available from our software home page at http://bioinf.cs.ucl.ac.uk/software.html.

The DISOPRED server for the prediction of protein disorder
Jonathan J. Ward, Liam J. McGuffin, Kevin Bryson et al.|Bioinformatics|2004
Cited by 706Open Access

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/