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dc.contributor.authorOfoegbu, Tochukwu C.
dc.contributor.authorDavid, Alessia
dc.contributor.authorKelley, Lawrence A.
dc.contributor.authorMezulis, Stefans
dc.contributor.authorIslam, Suhail A.
dc.contributor.authorMersmann, Sophia F.
dc.contributor.authorStrömich, Léonie
dc.contributor.authorVakser, Ilya A.
dc.contributor.authorHoulston, Richard S.
dc.contributor.authorSternberg, Michael J.E.
dc.identifier.citationOfoegbu, T. C., David, A., Kelley, L. A., Mezulis, S., Islam, S. A., Mersmann, S. F., Strömich, L., Vakser, I. A., Houlston, R. S., & Sternberg, M. (2019). PhyreRisk: A Dynamic Web Application to Bridge Genomics, Proteomics and 3D Structural Data to Guide Interpretation of Human Genetic Variants. Journal of molecular biology, 431(13), 2460–2466.
dc.descriptionThis work is licensed under a Creative Commons Attribution 4.0 International License.en_US
dc.description.abstractPhyreRisk is an open-access, publicly accessible web application for interactively bridging genomic, proteomic and structural data facilitating the mapping of human variants onto protein structures. A major advance over other tools for sequence-structure variant mapping is that PhyreRisk provides information on 20,214 human canonical proteins and an additional 22,271 alternative protein sequences (isoforms). Specifically, PhyreRisk provides structural coverage (partial or complete) for 70% (14,035 of 20,214 canonical proteins) of the human proteome, by storing 18,874 experimental structures and 84,818 pre-built models of canonical proteins and their isoforms generated using our in house Phyre2. PhyreRisk reports 55,732 experimentally, multi-validated protein interactions from IntAct and 24,260 experimental structures of protein complexes.

Another major feature of PhyreRisk is that, rather than presenting a limited set of precomputed variant-structure mapping of known genetic variants, it allows the user to explore novel variants using, as input, genomic coordinates formats (Ensembl, VCF, reference SNP ID and HGVS notations) and Human Build GRCh37 and GRCh38. PhyreRisk also supports mapping variants using amino acid coordinates and searching for genes or proteins of interest.

PhyreRisk is designed to empower researchers to translate genetic data into protein structural information, thereby providing a more comprehensive appreciation of the functional impact of variants. PhyreRisk is freely available at
dc.description.sponsorshipWellcome Trust 104955/Z/14/Zen_US
dc.description.sponsorshipWellcome Trust PhD studentship 108908/B/15/Zen_US
dc.description.sponsorshipBBSRC BB/M011526/1en_US
dc.description.sponsorshipBBSRC BB/P011705/1en_US
dc.description.sponsorshipNSF DBI1565107en_US
dc.description.sponsorshipNIH R01GM074255en_US
dc.rights© 2019 The Authors. Published by Elsevier Ltd.en_US
dc.subjectWeb resourceen_US
dc.subjectSequence-structure mappingen_US
dc.subjectHuman proteomeen_US
dc.subjectGenetic variantsen_US
dc.titlePhyreRisk: A Dynamic Web Application to Bridge Genomics, Proteomics and 3D Structural Data to Guide Interpretation of Human Genetic Variantsen_US
kusw.kuauthorVakser, Ilya A.
kusw.kudepartmentMolecular Biosciencesen_US
kusw.oaversionScholarly/refereed, publisher versionen_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US

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© 2019 The Authors. Published by Elsevier Ltd.
Except where otherwise noted, this item's license is described as: © 2019 The Authors. Published by Elsevier Ltd.