Evidence map›Paper›PMID 30108178›Full record

ArticleThe Journal of biological chemistry2018

Highly efficient cellular uptake of a cell-penetrating peptide (CPP) derived from the capsid protein of porcine circovirus type 2.

Wanting Yu, Yang Zhan, Boxin Xue, Yanpeng Dong, Yanfeng Wang, Ping Jiang, Aibing Wang, Yujie Sun, Yi Yang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

23 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  6. MeCP2 is a naturally supercharged protein with cell membrane transduction capabilities.Protein science : a publication of the Protein Society · 2024
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  12. Review
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  17. Decoding the proteome of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) for cell-penetrating peptides involved in pathogenesis or applicable as drug delivery vectors.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2020
    Article
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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 4 institutions in 1 country.

Wanting YuFrom the Key Laboratory of Animal Vaccine and Protein Engineering and.
Yang ZhanFrom the Key Laboratory of Animal Vaccine and Protein Engineering and.
Boxin XueState Key Laboratory of Membrane Biology, Biodynamic Optical Imaging Center (BIOPIC), School of Life Sciences, Peking University, Beijing 100871, China.
Yanpeng DongCollege of Veterinary Medicine, Nanjing Agricultural University, Nanjing 210095, China, and.
Yanfeng WangTsinghua-Peking Joint Center for Life Science, Tsinghua University, Beijing 100084, China.
Ping JiangCollege of Veterinary Medicine, Nanjing Agricultural University, Nanjing 210095, China, and.
Aibing WangFrom the Key Laboratory of Animal Vaccine and Protein Engineering and.
Yujie SunState Key Laboratory of Membrane Biology, Biodynamic Optical Imaging Center (BIOPIC), School of Life Sciences, Peking University, Beijing 100871, China, sun_yujie@pku.edu.cn.
Yi YangFrom the Key Laboratory of Animal Vaccine and Protein Engineering and yiyang@hunau.edu.cn.ORCID 0000-0003-2502-1011
Hunan Agricultural University · CNNanjing Agricultural University · CNPeking University · CNTsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Porcine circovirus type 2 (PCV2) is one of the smallest, nonenveloped, single-stranded DNA viruses. The PCV2 capsid protein (Cap) is the sole viral structural protein and main antigenic determinant. Previous sequence analysis has revealed that the N terminus of the PCV2 Cap contains a nuclear localization signal (NLS) enriched in positively charged residues. Here, we report that PCV2's NLS can function as a cell-penetrating peptide (CPP). We observed that this NLS can carry macromolecules,

Indexed as

AnimalsAntibodies, ViralCapsid ProteinsCell-Penetrating PeptidesCircovirusDNA, Single-StrandedDNA, ViralEpitopesHumansNuclear Localization Signalsrev Gene Products, Human Immunodeficiency VirusSwineAntibodies, ViralCapsid ProteinsCell-Penetrating PeptidesDNA, Single-StrandedDNA, ViralEpitopesNuclear Localization Signalsrev Gene Products, Human Immunodeficiency Viruscapsid proteincell-penetrating peptide (CPP)cellular uptakeCircoviridaeendocytosisintracellular traffickingmembranemembrane permeabilitynuclear localization signal (NLS)permeabilityporcine circovirus virus (PCV)protein deliverytransport vector

Identifiers

PMID30108178
PMCPMC6166719
OpenAlexW2885808213

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.