Evidence map›Paper›PMID 35720466›Full record

ArticleFood science and biotechnology2022

Prediction and identification of new type holin protein of

Do-Won Park, Jong Hun Lee, Jong-Hyun Park

Open access · greenAbstract read
In one paragraph

Article in Food science and biotechnology, 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
0.7field-weighted citation impact, top 29% 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, 5 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Do-Won ParkDepartment of Food Science and Biotechnology, College of Bionano Technology, Gachon University, Seongnam, 13120 Republic of Korea.
Jong Hun LeeDepartment of Food Science and Biotechnology, College of Bionano Technology, Gachon University, Seongnam, 13120 Republic of Korea.
Jong-Hyun ParkDepartment of Food Science and Biotechnology, College of Bionano Technology, Gachon University, Seongnam, 13120 Republic of Korea.ORCID 0000-0002-0291-6579
Gachon University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteriophages (phages) infecting specifically target bacteria utilize a unique lysis module known as the holin-endolysin cassette to release progeny. Studies on the phage lytic proteins could contribute to the development of alternatives to antibiotics. Here, we predicted and identified the holin protein of rV5-like phage ECP26 for increasing lytic activity of the phage endolysin. In silico analysis revealed that open reading frame 151 (ORF151) of ECP26 contained two transmembrane domains. Co-expression of endolysin with ORF151 resulted in the cell lysis of Supplementary information: The online version contains supplementary material available at 10.1007/s10068-022-01089-w.

Indexed as

BacteriophageEscherichia coliHolinrV5-like phage

Identifiers

PMID35720466
PMCPMC9203637
OpenAlexW4281830018

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.