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Article

A Zn-dependent structural transition of SOD1 modulates its ability to undergo phase separation.

The EMBO journal - 16 Jan 2023

Das Bidisha, Roychowdhury Sumangal, Mohanty Priyesh, Rizuan Azamat, Chakraborty Joy, Mittal Jeetain, Chattopadhyay Krishnananda

Abstract excerpt

The misfolding and mutation of Cu/Zn superoxide dismutase (SOD1) is commonly associated with amyotrophic lateral sclerosis (ALS). SOD1 can accumulate within stress granules (SGs), a type of membraneless organelle, which is believed to form via liquid-liquid phase separation (LLPS). Using wild-type, metal-deficient, and different ALS disease mutants of SOD1 and computer simulations, we report here that the absence...

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Identifiers

PMID: 36416085
DOI: 10.15252/embj.2022111185
PMCID: PMC9841336

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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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