CPAD 2.0: a repository of curated experimental data on aggregating proteins and peptides.
Protein aggregation
aggregation-prone regions
amyloid
database
fibrils
Journal
Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis
ISSN: 1744-2818
Titre abrégé: Amyloid
Pays: England
ID NLM: 9433802
Informations de publication
Date de publication:
Jun 2020
Jun 2020
Historique:
pubmed:
26
1
2020
medline:
30
1
2021
entrez:
26
1
2020
Statut:
ppublish
Résumé
The Curated Protein Aggregation Database (CPAD) is a manually curated and open-access database dedicated to providing comprehensive information related to mechanistic, kinetic and structural aspects of protein and peptide aggregation. The database has been updated to CPAD 2.0 by significantly expanding datasets and improving the user-interface. Key features of CPAD 2.0 are (i) 83,098 data points on aggregation kinetics experiments, (ii) 565 structures related to aggregation, which are classified into proteins, fibrils, and protein-ligand complexes, (iii) 2031 aggregating/non-aggregating peptides with pre-calculated aggregation properties, and (iv) 912 aggregation-prone regions in amyloidogenic proteins. This database will help the scientific community (a) by facilitating research leading to improved understanding of protein aggregation, (b) by helping develop, validate and benchmark mechanistic and kinetic models of protein aggregation, and (c) by assisting experimentalists with design of their investigations and dissemination of data generated by their studies. CPAD 2.0 can be accessed at https://web.iitm.ac.in/bioinfo2/cpad2/index.html.
Identifiants
pubmed: 31979981
doi: 10.1080/13506129.2020.1715363
doi:
Substances chimiques
Amyloid
0
Peptides
0
Protein Aggregates
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM