SoDCoD: a comprehensive database of Cu/Zn superoxide dismutase conformational diversity caused by ALS-linked gene mutations and other perturbations.
Riko TabuchiYurika MomozawaYuki HayashiHisashi NomaHidenori IchijoTakao FujisawaPublished in: Database : the journal of biological databases and curation (2024)
A structural alteration in copper/zinc superoxide dismutase (SOD1) is one of the common features caused by amyotrophic lateral sclerosis (ALS)-linked mutations. Although a large number of SOD1 variants have been reported in ALS patients, the detailed structural properties of each variant are not well summarized. We present SoDCoD, a database of superoxide dismutase conformational diversity, collecting our comprehensive biochemical analyses of the structural changes in SOD1 caused by ALS-linked gene mutations and other perturbations. SoDCoD version 1.0 contains information about the properties of 188 types of SOD1 mutants, including structural changes and their binding to Derlin-1, as well as a set of genes contributing to the proteostasis of mutant-like wild-type SOD1. This database provides valuable insights into the diagnosis and treatment of ALS, particularly by targeting conformational alterations in SOD1. Database URL: https://fujisawagroup.github.io/SoDCoDweb/.
Keyphrases
- amyotrophic lateral sclerosis
- wild type
- molecular dynamics
- molecular dynamics simulations
- adverse drug
- single molecule
- hydrogen peroxide
- end stage renal disease
- ejection fraction
- newly diagnosed
- emergency department
- dna methylation
- prognostic factors
- heavy metals
- gene expression
- peritoneal dialysis
- genome wide
- social media
- risk assessment
- patient reported
- aqueous solution