Evidence map›Paper›PMID 36316570›Full record

ArticleNature chemical biology2023

cIAP1-based degraders induce degradation via branched ubiquitin architectures.

Yoshino Akizuki, Mai Morita, Yuki Mori, Ai Kaiho-Soma, Shivani Dixit, Akinori Endo, Marie Shimogawa, Gosuke Hayashi, Mikihiko Naito, Akimitsu Okamoto and 3 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.3field-weighted citation impact, top 6% of its field
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

25 citing papers in PubMed, 39 citations in OpenAlex.

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  13. Tau degradation in Alzheimer's disease: Mechanisms and therapeutic opportunities.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
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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

13 authors at 3 institutions in 1 country.

Yoshino AkizukiSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Tokyo, Japan.
Mai MoritaSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Tokyo, Japan.
Yuki MoriSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Tokyo, Japan.
Ai Kaiho-SomaInstitute for Advanced Life Sciences, Hoshi University, Tokyo, Japan.
Shivani DixitDepartment of Advanced Interdisciplinary Studies, Graduate School of Engineering, University of Tokyo, Tokyo, Japan.
Akinori EndoProtein Metabolism Project, Tokyo Metropolitan Institute of Medical Sciences, Tokyo, Japan.
Marie ShimogawaDepartment of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, Tokyo, Japan.
Gosuke HayashiDepartment of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, Tokyo, Japan.
Mikihiko NaitoSocial Cooperation Program of Targeted Protein Degradation, Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan.ORCID http://orcid.org/0000-0003-0451-1337
Akimitsu OkamotoDepartment of Advanced Interdisciplinary Studies, Graduate School of Engineering, University of Tokyo, Tokyo, Japan.ORCID http://orcid.org/0000-0002-7418-6237
Keiji TanakaProtein Metabolism Project, Tokyo Metropolitan Institute of Medical Sciences, Tokyo, Japan.
Yasushi SaekiProtein Metabolism Project, Tokyo Metropolitan Institute of Medical Sciences, Tokyo, Japan.
Fumiaki OhtakeSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Tokyo, Japan. f-ohtake@hoshi.ac.jp.ORCID http://orcid.org/0000-0002-8590-6172
Hoshi University · JPThe University of Tokyo · JPTokyo Metropolitan Institute of Medical Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Targeted protein degradation through chemical hijacking of E3 ubiquitin ligases is an emerging concept in precision medicine. The ubiquitin code is a critical determinant of the fate of substrates. Although two E3s, CRL2

Indexed as

UbiquitinUbiquitin-Protein LigasesProteasome Endopeptidase ComplexProteolysisUbiquitinationProteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID36316570
OpenAlexW4307715788

What OpenQuestion holds

Textmetadata
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.