{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,21]],"date-time":"2025-11-21T12:38:55Z","timestamp":1763728735190,"version":"3.41.2"},"reference-count":52,"publisher":"Oxford University Press (OUP)","issue":"5","license":[{"start":{"date-parts":[[2024,4,25]],"date-time":"2024-04-25T00:00:00Z","timestamp":1714003200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004727","name":"Flanders Institute for Biotechnology","doi-asserted-by":"publisher","award":["G0C2818N","G0C0320N","G053420N","G0C3522N"],"award-info":[{"award-number":["G0C2818N","G0C0320N","G053420N","G0C3522N"]}],"id":[{"id":"10.13039\/501100004727","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,5,2]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:sec>\n                  <jats:title>Motivation<\/jats:title>\n                  <jats:p>Proteins, the molecular workhorses of biological systems, execute a multitude of critical functions dictated by their precise three-dimensional structures. In a complex and dynamic cellular environment, proteins can undergo misfolding, leading to the formation of aggregates that take up various forms, including amorphous and ordered aggregation in the shape of amyloid fibrils. This phenomenon is closely linked to a spectrum of widespread debilitating pathologies, such as Alzheimer\u2019s disease, Parkinson\u2019s disease, type-II diabetes, and several other proteinopathies, but also hampers the engineering of soluble agents, as in the case of antibody development. As such, the accurate prediction of aggregation propensity within protein sequences has become pivotal due to profound implications in understanding disease mechanisms, as well as in improving biotechnological and therapeutic applications.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Results<\/jats:title>\n                  <jats:p>We previously developed Cordax, a structure-based predictor that utilizes logistic regression to detect aggregation motifs in protein sequences based on their structural complementarity to the amyloid cross-beta architecture. Here, we present a dedicated web server interface for Cordax. This online platform combines several features including detailed scoring of sequence aggregation propensity, as well as 3D visualization with several customization options for topology models of the structural cores formed by predicted aggregation motifs. In addition, information is provided on experimentally determined aggregation-prone regions that exhibit sequence similarity to predicted motifs, scores, and links to other predictor outputs, as well as simultaneous predictions of relevant sequence propensities, such as solubility, hydrophobicity, and secondary structure propensity.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Availability and implementation<\/jats:title>\n                  <jats:p>The Cordax webserver is freely accessible at https:\/\/cordax.switchlab.org\/.<\/jats:p>\n               <\/jats:sec>","DOI":"10.1093\/bioinformatics\/btae279","type":"journal-article","created":{"date-parts":[[2024,4,25]],"date-time":"2024-04-25T16:36:25Z","timestamp":1714062985000},"source":"Crossref","is-referenced-by-count":5,"title":["CORDAX web server: an online platform for the prediction and 3D visualization of aggregation motifs in protein sequences"],"prefix":"10.1093","volume":"40","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4030-1022","authenticated-orcid":false,"given":"Nikolaos","family":"Louros","sequence":"first","affiliation":[{"name":"Switch Laboratory, VIB Center for Brain and Disease Research, VIB , 3000 Leuven, Belgium"},{"name":"Department of Cellular and Molecular Medicine, Switch Laboratory, KU Leuven , 3000 Leuven, Belgium"},{"name":"Switch Laboratory, VIB Center for AI & Computational Biology, VIB , 3000 Leuven, Belgium"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9189-7399","authenticated-orcid":false,"given":"Frederic","family":"Rousseau","sequence":"additional","affiliation":[{"name":"Switch Laboratory, VIB Center for Brain and Disease Research, VIB , 3000 Leuven, Belgium"},{"name":"Department of Cellular and Molecular Medicine, Switch Laboratory, KU Leuven , 3000 Leuven, Belgium"},{"name":"Switch Laboratory, VIB Center for AI & Computational Biology, VIB , 3000 Leuven, Belgium"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2020-0168","authenticated-orcid":false,"given":"Joost","family":"Schymkowitz","sequence":"additional","affiliation":[{"name":"Switch Laboratory, VIB Center for Brain and Disease Research, VIB , 3000 Leuven, Belgium"},{"name":"Department of Cellular and Molecular Medicine, Switch Laboratory, KU Leuven , 3000 Leuven, Belgium"},{"name":"Switch Laboratory, VIB Center for AI & Computational Biology, VIB , 3000 Leuven, Belgium"}]}],"member":"286","published-online":{"date-parts":[[2024,4,25]]},"reference":[{"key":"2024050903005733700_btae279-B1","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.semcdb.2018.05.004","article-title":"RHIM-based protein:protein interactions in microbial defence against programmed cell death by necroptosis","volume":"99","author":"Baker","year":"2020","journal-title":"Semin Cell Dev 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