TY - JOUR
T1 - Aggregating amyloid resources
T2 - A comprehensive review of databases on amyloid-like aggregation
AU - Iglesias, Valentín
AU - Chilimoniuk, Jarosław
AU - Pintado-Grima, Carlos
AU - Bárcenas, Oriol
AU - Ventura, Salvador
AU - Burdukiewicz, Michał
N1 - Publisher Copyright:
© 2024 The Authors
PY - 2024/12
Y1 - 2024/12
N2 - Protein aggregation is responsible for several degenerative conditions in humans, and it is also a bottleneck in industrial protein production and storage of biotherapeutics. Bioinformatics tools have been developed to predict and redesign protein solubility more efficiently by understanding the underlying principles behind aggregation. As more experimental data become available, dedicated resources for storing, indexing, classifying and consolidating experimental results have emerged. These resources vary in focus, including aggregation-prone regions, 3D patches or protein stretches capable of forming amyloid fibrils. Some of these resources also consider the experimental conditions that cause protein aggregation and how they affect the process. This review article explores how protein aggregation databases have evolved and surveys state-of-the-art resources. We highlight their applications, complementarity and existing limitations. Moreover, we showcase the existing symbiosis between amyloid-related databases and predictive tools. To increase the usefulness of our review, we supplement it with a comprehensive list of present and past amyloid databases: https://biogenies.info/amyloid-database-list/.
AB - Protein aggregation is responsible for several degenerative conditions in humans, and it is also a bottleneck in industrial protein production and storage of biotherapeutics. Bioinformatics tools have been developed to predict and redesign protein solubility more efficiently by understanding the underlying principles behind aggregation. As more experimental data become available, dedicated resources for storing, indexing, classifying and consolidating experimental results have emerged. These resources vary in focus, including aggregation-prone regions, 3D patches or protein stretches capable of forming amyloid fibrils. Some of these resources also consider the experimental conditions that cause protein aggregation and how they affect the process. This review article explores how protein aggregation databases have evolved and surveys state-of-the-art resources. We highlight their applications, complementarity and existing limitations. Moreover, we showcase the existing symbiosis between amyloid-related databases and predictive tools. To increase the usefulness of our review, we supplement it with a comprehensive list of present and past amyloid databases: https://biogenies.info/amyloid-database-list/.
KW - Amyloid
KW - Bioinformatics
KW - Biotherapeutics
KW - Database
KW - Prion
KW - Protein aggregation
KW - Protein solubility
UR - http://www.scopus.com/inward/record.url?scp=85208481285&partnerID=8YFLogxK
U2 - 10.1016/j.csbj.2024.10.047
DO - 10.1016/j.csbj.2024.10.047
M3 - Article
C2 - 39582896
AN - SCOPUS:85208481285
SN - 2001-0370
VL - 23
SP - 4011
EP - 4018
JO - Computational and Structural Biotechnology Journal
JF - Computational and Structural Biotechnology Journal
ER -