Evidence map›Paper›PMID 40382329›Full record

ArticleNature communications2025

A generalizable approach for programming protease-responsive conformationally inhibited artificial transcriptional factors.

Yinxia Liu, Lingyun Zhao, Jinshan Long, Zhenye Huang, Ying Long, Jianjun He, Jian-Hui Jiang

Erratum issuedAbstract read
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Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Yinxia LiuAffiliated XiangTan Central Hospital of Hunan University, College of Chemistry and Chemical Engineering, School of Biomedical Sciences, Hunan University, Changsha, 410082, China.
Lingyun ZhaoAffiliated XiangTan Central Hospital of Hunan University, College of Chemistry and Chemical Engineering, School of Biomedical Sciences, Hunan University, Changsha, 410082, China.
Jinshan LongAffiliated XiangTan Central Hospital of Hunan University, College of Chemistry and Chemical Engineering, School of Biomedical Sciences, Hunan University, Changsha, 410082, China.
Zhenye HuangAffiliated XiangTan Central Hospital of Hunan University, College of Chemistry and Chemical Engineering, School of Biomedical Sciences, Hunan University, Changsha, 410082, China.
Ying LongAffiliated XiangTan Central Hospital of Hunan University, College of Chemistry and Chemical Engineering, School of Biomedical Sciences, Hunan University, Changsha, 410082, China.
Jianjun HeAffiliated XiangTan Central Hospital of Hunan University, College of Chemistry and Chemical Engineering, School of Biomedical Sciences, Hunan University, Changsha, 410082, China. jianjunh@hnu.edu.cn.ORCID http://orcid.org/0000-0001-9779-2662
Jian-Hui JiangAffiliated XiangTan Central Hospital of Hunan University, College of Chemistry and Chemical Engineering, School of Biomedical Sciences, Hunan University, Changsha, 410082, China. jianhuijiang@hnu.edu.cn.ORCID http://orcid.org/0000-0003-1594-4023

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synthetic genetic circuits that harness programmable protein modules and artificial transcription factors (ATF) to devise event-triggerable cascaded pathways represent an essential class of tools for studying cell biology. Fine-tuning the general structural functionality of ATFs is important for constructing orthogonal and composable transcriptional regulators. Here, we report the design of a protease-responsive conformationally inhibited system (PRCIS). By intramolecularly linking the free DNA-binding domains of ATF to confined dimerized regions, the transcriptional binding is conformationally inactivated. The function of DNA binding is reinstated upon proteolytic cleavage of linkages, activating the downstream gene expressions. The versatility of PRCIS design is demonstrated through its adaptability to various ATFs and proteases, showcasing high activation ratios and specificity. Furthermore, the development of PRCIS-based triple-orthogonal protease-responsive and dual-orthogonal chemical-inducible platforms and Boolean logic operations are elaborated in this paper, providing a generalizable design for synthetic biology.

Indexed as

Peptide HydrolasesSynthetic BiologyTranscription FactorsDNAProtein BindingProtein ConformationProtein EngineeringDNAPeptide HydrolasesTranscription Factors

Identifiers

PMID40382329
PMCPMC12085601

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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.