Evidence map›Paper›PMID 35550603›Full record

ArticleExperimental & molecular medicine2022

The optimized core peptide derived from CABIN1 efficiently inhibits calcineurin-mediated T-cell activation.

Sangho Lee, Han-Teo Lee, Young Ah Kim, Il-Hwan Lee, Seong-Jun Kang, Kyeongpyo Sim, Chung-Gyu Park, Kyungho Choi, Hong-Duk Youn

Open access · goldAbstract read
In one paragraph

Article in Experimental & molecular medicine, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 45% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
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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

9 authors at 1 institution in 2 countries.

Sangho LeeNational Creative Research Center for Epigenome Reprogramming Network, Department of Biomedical Sciences, Ischemic/Hypoxic Disease Institute, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea.
Han-Teo LeeDepartment of Molecular Medicine & Biopharmaceutical Sciences, Graduate School of Convergence Science, Seoul National University, Seoul, 03080, Republic of Korea.
Young Ah KimDepartment of Molecular Medicine & Biopharmaceutical Sciences, Graduate School of Convergence Science, Seoul National University, Seoul, 03080, Republic of Korea.
Il-Hwan LeeDepartment of Biomedical Science, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea.
Seong-Jun KangDepartment of Biomedical Science, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea.
Kyeongpyo SimDepartment of Biomedical Science, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea.
Chung-Gyu ParkDepartment of Biomedical Science, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea.ORCID http://orcid.org/0000-0003-4083-8791
Kyungho ChoiDepartment of Biomedical Science, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea.
Hong-Duk YounNational Creative Research Center for Epigenome Reprogramming Network, Department of Biomedical Sciences, Ischemic/Hypoxic Disease Institute, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea. hdyoun@snu.ac.kr.ORCID http://orcid.org/0000-0001-9741-8566
Seoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The C-terminal fragment of CABIN1 interacts with calcineurin and represses the transcriptional activity of the nuclear factor of activated T cells (NFAT). However, the specific sequences and mechanisms through which it binds to calcineurin are unclear. This study determined that decameric peptide (CABIN1 residues 2146-2155) is minimally required for binding to calcineurin. This peptide contains a unique "PPTP" C-terminal sequence and a "PxIxIT" N-terminal motif. Furthermore, p38MAPK phosphorylated the threonine residue of the "PPTP" sequence under physiological conditions, dramatically enhancing the peptide's binding affinity to calcineurin. Therefore, the CABIN1 peptide inhibited the calcineurin-NFAT pathway and the activation of T cells more efficiently than the VIVIT peptide without affecting calcineurin's phosphatase activity. The CABIN1 peptide could thus be a more potent calcineurin inhibitor and provide therapeutic opportunities for various diseases caused by the calcineurin-NFAT pathway.

Indexed as

CalcineurinNFATC Transcription FactorsLymphocyte ActivationPeptidesT-LymphocytesCalcineurinNFATC Transcription FactorsPeptides

Identifiers

PMID35550603
PMCPMC9166766
OpenAlexW4280550947

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.