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Title:           A3D Model Organism Database A3D-MODB: a database for proteome aggregation predictions in model organisms
Subject:         DOI: 10.1093/nar/gkad942 , 52, Database issue, 28-10-2023. Abstract: Protein aggregation has been associated with aging and different pathologies and represents a bottleneck in the industrial production of biotherapeutics. Numerous past studies performed in Escherichia coli and other model organisms have allowed to dissect the biophysical principles underlying this process. This knowledge fuelled the development of computational tools, such as Aggrescan 3D (A3D) to forecast and re-design protein aggregation. Here, we present the A3D Model Organism Database (A3D-MODB) http://biocomp.chem.uw.edu.pl/A3D2/MODB, a comprehensive resource for the study of structural protein aggregation in the proteomes of 12 key model species spanning distant biological clades. In addition to A3D predictions, this resource incorporates information useful for contextualizing protein aggregation, including membrane protein topology and structural model confidence, as an indirect reporter of protein disorder. The database is openly accessible without any need for registration. We foresee A3D-MOBD evolving into a central hub for conducting comprehensive, multi-species analyses of protein aggregation, fostering the development of protein-based solutions for medical, biotechnological, agricultural and industrial applications.
Keywords:        
Author:          Badaczewska-Dawid Aleksandra E., Kuriata Aleksander, Pintado-Grima Carlos, Garcia-Pardo Javier, Burdukiewicz Micha, Iglesias Valentn, Kmiecik Sebastian, Ventura Salvador
Creator:         OUP
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    Author: Badaczewska-Dawid Aleksandra E., Kuriata Aleksander, Pintado-Grima Carlos, Garcia-Pardo Javier, Burdukiewicz Micha, Iglesias Valentn, Kmiecik Sebastian, Ventura Salvador
    Subject: DOI: 10.1093/nar/gkad942 , 52, Database issue, 28-10-2023. Abstract: Protein aggregation has been associated with aging and different pathologies and represents a bottleneck in the industrial production of biotherapeutics. Numerous past studies performed in Escherichia coli and other model organisms have allowed to dissect the biophysical principles underlying this process. This knowledge fuelled the development of computational tools, such as Aggrescan 3D (A3D) to forecast and re-design protein aggregation. Here, we present the A3D Model Organism Database (A3D-MODB) http://biocomp.chem.uw.edu.pl/A3D2/MODB, a comprehensive resource for the study of structural protein aggregation in the proteomes of 12 key model species spanning distant biological clades. In addition to A3D predictions, this resource incorporates information useful for contextualizing protein aggregation, including membrane protein topology and structural model confidence, as an indirect reporter of protein disorder. The database is openly accessible without any need for registration. We foresee A3D-MOBD evolving into a central hub for conducting comprehensive, multi-species analyses of protein aggregation, fostering the development of protein-based solutions for medical, biotechnological, agricultural and industrial applications.
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   Type: CRC32
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