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Article

Changes in hydrophobicity mainly promotes the aggregation tendency of ALS associated SOD1 mutants.

International journal of biological macromolecules - 15 Feb 2020

Tompa Dharma Rao, Kadhirvel Saraboji

Abstract excerpt

Protein misfolding and aggregation due to mutations, are associated with fatal neurodegenerative disorders. The mutations in Cu/Zn superoxide dismutase (SOD1) causing its misfolding and aggregation are found linked to the motor neuron disorder, amyotrophic lateral sclerosis. Since the mutations are scattered throughout SOD1 structure, determining the exact molecular mechanism underlying the ALS pathology remains...

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Identifiers

PMID: 31669277
DOI: 10.1016/j.ijbiomac.2019.09.181

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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