fALSdb is a unique resource providing comprehensive data on ALS causing SOD1 mutants. It analyzes the effect of each mutation on SOD1 in order to identify what such effect of mutation causes ALS. Development of fALSdb turns to be a new approach to understand the disease causing mechanism with respect to each mutation.

ALS

Amyotrophic lateral sclerosis (ALS) also referred to as motor neuron disease or Lou Gehrig's disease is a fatal neuromuscular disease that causes damage to the nerve cells controlling the voluntary muscle movement. The onset of the disease is observed to be 55 and above. It is caused when there occurs a mutation in the SOD1enzyme. The mutation causes the SOD1 protein to misfold. These misfolded SOD1 form aggregates and deposit over the healthy motor neurons. This makes the healthy motor neurons to shrink, thereby making them inefficient to perform its muscle movement.
There are two types of ALS:
Sporadic ALS - Cause is unknown.
Familial ALS - There is a hereditary factor where the condition is known to run in families.
The rate of familial ALS is found to be between 1.5 and 5%. The remaining 95% of cases do not have an obvious family history of ALS and appear to occur sporadically throughout the community.

SOD

SOD is responsible for destroying free superoxide radicals in the body by converting these harmful superoxide radicals to molecular oxygen and hydrogen peroxide. Thus, they are an important antioxidant defense in nearly all cells exposed to oxygen. Oxidation reactions can produce free radicals which in turn can start chain reactions. When chain reactions occur in a cell, it can cause cell damage or cell death. Antioxidants terminate these chain reactions by removing free radicals.

SOD1

Cu/Zn Superoxide dismutase(SOD1) is an enzyme encoded by SOD1 gene located on chromosome 21. SOD1 is commonly used by eukaryotes. The Cu-Zn SOD1 is a homo dimer of molecular weight 32,500 Da. It is an 8-stranded Greek key beta-barrel. The two subunits are tightly joined back-to-back by hydrophobic and electrostatic interactions. Length of a subunit is 153 amino acids.

List of collected SOD1 mutations