Evidence map›Paper›PMID 40770049›Full record

ArticleCommunications biology2025

Facile expression of proteins with desired N-terminal amino acid via an engineered cysteine protease domain.

Xiangman Zou, Zhi Liu, Fengnan Song, Wei Zhou, Jiaying Hang, Chenchen Feng, Tianhong Yuan, Jinhua Dong, Wei Shi, Feng Tang and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Xiangman Zou *Key Laboratory of Structure-Based Drug Design and Discovery (Ministry of Education), Shenyang Pharmaceutical University, Shenyang, China.
Zhi Liu *State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.ORCID http://orcid.org/0000-0002-1417-9852
Fengnan SongState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Wei ZhouState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Jiaying HangState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Chenchen FengState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
Tianhong YuanSchool of Basic Medicine, Guizhou Medical University, Guizhou, China.
Jinhua DongKey Laboratory of Structure-Based Drug Design and Discovery (Ministry of Education), Shenyang Pharmaceutical University, Shenyang, China. jhdong@syphu.edu.cn.ORCID http://orcid.org/0000-0003-2951-0939
Wei ShiState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China. hsw201204@163.com.ORCID http://orcid.org/0000-0002-9924-8756
Feng TangKey Laboratory of Structure-Based Drug Design and Discovery (Ministry of Education), Shenyang Pharmaceutical University, Shenyang, China. tangfeng2013@simm.ac.cn.ORCID http://orcid.org/0000-0002-2156-7271
Wei HuangKey Laboratory of Structure-Based Drug Design and Discovery (Ministry of Education), Shenyang Pharmaceutical University, Shenyang, China. huangwei@simm.ac.cn.ORCID http://orcid.org/0000-0001-6432-1848

Funding

National Natural Science Foundation of China (National Science Foundation of China) 22422705, 82325045, 92478204, 22337003, 22277126, and 82204183
6 · The paper itself

Abstract

The removal of N-terminal methionine (Met) or fused N-terminal purification tags to expose the first amino acid of the target protein is critically important for studying the potential regulatory role of the N-terminal residue. However, current tag-removal approaches typically rely on enzymatic cleavage or require harsh reaction conditions. Here, we report a strategy for expressing proteins of interest (POI) with custom N-terminal amino acids by introducing an engineered cysteine protease domain (CPD) tag at the N-terminus. The cleavable tag is chemically triggered by inositol hexakisphosphate (InsP

Indexed as

Amino AcidsCysteine EndopeptidasesCysteine ProteasesProtein EngineeringHumansPhytic AcidProtein DomainsAmino AcidsCysteine EndopeptidasesCysteine ProteasesPhytic Acid

Identifiers

PMID40770049
PMCPMC12329031

What Socratic holds

Textmetadata
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 Socratic graph.