Evidence map›Paper›PMID 40525527›Full record

ArticleFEBS letters2025

Purification tags markedly affect self-aggregation of CPEB3.

Harunobu Saito, Yujin Lee, Motoharu Ueno, Naotaka Sekiyama, Masatomo So, Ayako Furukawa, Kenji Sugase

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

7 authors.

Harunobu SaitoDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Japan.ORCID https://orcid.org/0009-0004-4771-5086
Yujin LeeDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Japan.
Motoharu UenoDepartment of Biophysics, Graduate School of Science, Kyoto University, Japan.
Naotaka SekiyamaDepartment of Biophysics, Graduate School of Science, Kyoto University, Japan.ORCID https://orcid.org/0000-0003-4537-6565
Masatomo SoDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Japan.ORCID https://orcid.org/0000-0002-4815-4995
Ayako FurukawaDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Japan.ORCID https://orcid.org/0000-0001-9310-9918
Kenji SugaseDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Japan.ORCID https://orcid.org/0000-0001-8623-7743

Funding

Japan Society for the Promotion of Science 22H05088Japan Society for the Promotion of Science 22KK0098
6 · The paper itself

Abstract

Since protein aggregation-including liquid-liquid phase separation (LLPS) and amyloid fibril formation-plays a critical role in both diseases and biological functions, understanding the mechanisms underlying protein aggregation is essential. Recombinant proteins are commonly used in vitro to investigate protein aggregation processes. However, if the purification tags remain uncleaved, they may affect the results and hinder accurate interpretation. Our findings demonstrate that the His

Indexed as

Protein AggregatesRNA-Binding ProteinsAmyloidAnimalsGreen Fluorescent ProteinsHistidineIntrinsically Disordered ProteinsMiceRecombinant ProteinsAmyloidGreen Fluorescent ProteinsHistidineIntrinsically Disordered ProteinsProtein AggregatesRecombinant ProteinsRNA-Binding Proteinsamyloid fibrilCPEB3His tagIDRLLPSprotein aggregation

Identifiers

PMID40525527
PMCPMC12519062

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.