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Article

Engineering a monobody specific to monomeric Cu/Zn-superoxide dismutase associated with amyotrophic lateral sclerosis.

Protein science : a publication of the Protein Society - 1 Apr 2024

Amesaka Hiroshi, Hara Mizuho, Sakai Yuki, Shintani Atsuko, Sue Kaori, Yamanaka Tomoyuki, Tanaka Shun-Ichi, Furukawa Yoshiaki

Abstract excerpt

Misfolding of mutant Cu/Zn-superoxide dismutase (SOD1) has been implicated in familial form of amyotrophic lateral sclerosis (ALS). A natively folded SOD1 forms a tight homodimer, and the dimer dissociation has been proposed to trigger the oligomerization/aggregation of SOD1. Besides increasing demand for probes allowing the detection of monomerized forms of SOD1 in various applications, the development of probes...

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Identifiers

PMID: 38511674
DOI: 10.1002/pro.4961
PMCID: PMC10955725

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SOD1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

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