Abstract:The Cu/Zn Human Superoxide Dismutase (SOD1) is a dimeric
metalloenzyme
whose genetic mutations are directly related to amyotrophic lateral
sclerosis (ALS), so understanding its folding mechanism is of fundamental
importance. Currently, the SOD1 dimer formation is studied via molecular
dynamics simulations using a simplified structure-based model and
an all-atom model. Results from the simplified model reveal a mechanism
dependent on distances between monomers, which are limited by constraints
to mimic concentr… Show more
“…Which particular documented morphological, biochemical, or genetic abnormalities of astrocytes are the primary causes of disease progression is yet unknown. 30 To the best of our knowledge, this is the first work to show how the thrombin PAR1 pathway is involved in the pathology of the brain in SOD1 mice. Inhibiting the PAR1 pathway is a unique technique to treat ALS.…”
Superoxide dismutase (SOD) is an important metalloenzyme that catalyzes the dismutation of superoxide radicals (O2˙−) into hydrogen peroxide (H2O2) and oxygen (O2).
“…Which particular documented morphological, biochemical, or genetic abnormalities of astrocytes are the primary causes of disease progression is yet unknown. 30 To the best of our knowledge, this is the first work to show how the thrombin PAR1 pathway is involved in the pathology of the brain in SOD1 mice. Inhibiting the PAR1 pathway is a unique technique to treat ALS.…”
Superoxide dismutase (SOD) is an important metalloenzyme that catalyzes the dismutation of superoxide radicals (O2˙−) into hydrogen peroxide (H2O2) and oxygen (O2).
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