Evidence map›Paper›PMID 38511674›Full record

ArticleProtein science : a publication of the Protein Society2024

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

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

Abstract read
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In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Hiroshi AmesakaDepartment of Biomolecular Chemistry, Kyoto Prefectural University, Kyoto, Japan.
Mizuho HaraDepartment of Biomolecular Chemistry, Kyoto Prefectural University, Kyoto, Japan.
Yuki SakaiDepartment of Biomolecular Chemistry, Kyoto Prefectural University, Kyoto, Japan.
Atsuko ShintaniDepartment of Chemistry, Keio University, Yokohama, Japan.
Kaori SueDepartment of Chemistry, Keio University, Yokohama, Japan.
Tomoyuki YamanakaDepartment of Neuroscience of Disease, Brain Research Institute, Niigata University, Niigata, Japan.
Shun-Ichi TanakaDepartment of Biomolecular Chemistry, Kyoto Prefectural University, Kyoto, Japan.ORCID 0000-0003-4270-0374
Yoshiaki FurukawaDepartment of Chemistry, Keio University, Yokohama, Japan.ORCID 0000-0002-1918-372X

Funding

Grants-in-Aid for Scientific Research on Innovative Areas 19H05765Grants-in-Aid for Scientific Research on Innovative Areas 20H05516Ministry of Education, Culture, Sports, Science and Technology of Japan 22K19389Scientific Research (B) 22H02768Scientific Research (C) 21K05386
6 · The paper itself

Abstract

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 has been limited to conventional antibodies. Here, we have developed Mb(S4) monobody, a small synthetic binding protein based on the fibronectin type III scaffold, that recognizes a monomeric but not dimeric form of SOD1 by performing combinatorial library selections using phage and yeast-surface display methods. Although Mb(S4) was characterized by its excellent selectivity to the monomeric conformation of SOD1, the monomeric SOD1/Mb(S4) complex was not so stable (apparent K

Indexed as

Amyotrophic Lateral SclerosisHumansMutationProtein FoldingSaccharomyces cerevisiaeSuperoxide DismutaseSuperoxide Dismutase-1ZincSuperoxide DismutaseSuperoxide Dismutase-1Zincamyotrophic lateral sclerosisbiolayer interferometrychemical crosslinkingCu/Zn‐superoxide dismutasemonobodyphage display

Identifiers

PMID38511674
PMCPMC10955725

What OpenQuestion holds

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LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.