Evidence map›Paper›PMID 36743654›Full record

ArticleFrontiers in bioengineering and biotechnology2022

A nanobody-based molecular toolkit for ubiquitin-proteasome system explores the main role of survivin subcellular localization.

Hui Miao, Chang Liu, Hao Ouyang, Peiwen Zhang, Yuping Liu, Chen Zhang, Changping Deng, Yunhui Fu, Jinping Niu, Wenyun Zheng and 3 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in bioengineering and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 15 citations in OpenAlex.

  1. Emerging biologic modalities for targeted protein degradation.The Journal of biological chemistry · 2026
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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 2 countries.

Hui MiaoState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.
Chang LiuState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.
Hao OuyangDepartment of Hepatology, Yueyang Hospital of Integrated Traditional Chinese and Western Medicine, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Peiwen ZhangShanghai Key Laboratory of New Drug Design, School of Pharmacy, East China University of Science and Technology, Shanghai, China.
Yuping LiuShanghai Key Laboratory of New Drug Design, School of Pharmacy, East China University of Science and Technology, Shanghai, China.
Chen ZhangState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.
Changping DengState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.
Yunhui FuState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.
Jinping NiuState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.
Wenyun ZhengShanghai Key Laboratory of New Drug Design, School of Pharmacy, East China University of Science and Technology, Shanghai, China.
Fang YouDepartment of Chemical and Biomolecular Engineering, National University of Singapore, Singapore, Singapore.
Yi YangDepartment of Chemical and Biomolecular Engineering, National University of Singapore, Singapore, Singapore.
Xingyuan MaState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.
East China University of Science and Technology · CNNational University of Singapore · SGShanghai University of Traditional Chinese Medicine · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Targeted protein degradation is a powerful tool for determining the function of specific proteins nowadays. Survivin is the smallest member of the inhibitor of the apoptosis protein (IAP) family. It exists in the cytoplasm and nucleus of cells, but the exact function of survivin in different subcellular locations retained unclear updates due to the lack of effective and simple technical means. In this study, we created a novel nanoantibody-based molecular toolkit, namely, the ubiquitin-proteasome system (Nb4A-Fc-T2A-TRIM21), that can target to degrade survivin localized in cytoplasmic and cell nuclear by ubiquitinating, and by which to verify the potential roles of survivin subcellular localization. Also, the results showed that the cytoplasmic survivin mainly plays an anti-apoptotic function by directly or indirectly inhibiting the caspase pathway, and the nuclear survivin mainly promotes cell proliferation and participates in the regulation of the cell cycle. In addition, the Nb4A-Fc-T2A-TRIM21 system can degrade the endogenous survivin protein in a large amount by the ubiquitin-proteasome pathway, and the system can provide theoretical support for ubiquitination degradation targeting other endogenous proteins.

Indexed as

anti-cancerapoptosis and cell cyclenanobody targetedsurvivin subcellular functionTRIM21

Identifiers

PMID36743654
PMCPMC9895104
OpenAlexW4317631252

What OpenQuestion holds

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LicenceCC BY
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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.