TY - JOUR
T1 - A3D Model Organism Database (A3D-MODB)
T2 - a database for proteome aggregation predictions in model organisms
AU - Badaczewska-Dawid, Aleksandra E.
AU - Kuriata, Aleksander
AU - Pintado-Grima, Carlos
AU - Garcia-Pardo, Javier
AU - Burdukiewicz, Michał
AU - Iglesias, Valentín
AU - Kmiecik, Sebastian
AU - Ventura, Salvador
N1 - Publisher Copyright:
© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.
PY - 2023/10/28
Y1 - 2023/10/28
N2 - 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.
AB - 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.
KW - Animals
KW - Databases, Protein
KW - Humans
KW - Protein Aggregates
KW - Proteome
KW - Aggrescan3d
KW - Yeast
KW - Force
KW - Propensities
KW - Sequence
KW - Topology
KW - Design
KW - Proteins
KW - Alpha
KW - Web server
UR - https://www.scopus.com/pages/publications/85181852600
UR - https://www.mendeley.com/catalogue/fb45e047-5599-302c-b2bc-53ac91b71ad1/
U2 - 10.1093/nar/gkad942
DO - 10.1093/nar/gkad942
M3 - Article
C2 - 37897355
AN - SCOPUS:85181852600
SN - 0305-1048
VL - 52
SP - D360-D367
JO - Nucleic acids research
JF - Nucleic acids research
IS - D1
ER -