Evidence map›Paper›PMID 28050849›Full record

ArticleAMB Express2017

Glycin-rich antimicrobial peptide YD1 from B. amyloliquefaciens, induced morphological alteration in and showed affinity for plasmid DNA of E. coli.

Md Saifur Rahman, Yun Hee Choi, Yoon Seok Choi, Jin Cheol Yoo

Open access · goldAbstract read
In one paragraph

Article in AMB Express, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.2field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 36 citations in OpenAlex.

  1. A One Health Perspective onMicroorganisms · 2026
    Review
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  12. Article
  13. The antimicrobial peptide YD attenuates inflammationActa pharmaceutica Sinica. B · 2021
    Article
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  16. 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

4 authors at 1 institution in 1 country.

Md Saifur RahmanDepartment of Pharmacy, College of Pharmacy, Chosun University, Gwangju, 501-759, Republic of Korea.
Yun Hee ChoiDepartment of Pharmacy, College of Pharmacy, Chosun University, Gwangju, 501-759, Republic of Korea.
Yoon Seok ChoiDepartment of Pharmacy, College of Pharmacy, Chosun University, Gwangju, 501-759, Republic of Korea.
Jin Cheol YooDepartment of Pharmacy, College of Pharmacy, Chosun University, Gwangju, 501-759, Republic of Korea. jcyu@chosun.ac.kr.
Chosun University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antimicrobial peptides (AMPs), low-molecular-weight proteins with broad-spectrum antimicrobial activity, are the most promising candidates for the development of novel antimicrobials. A powerful cationic glycine-rich AMP YD1 (MW ~ 1.0 kDa) was purified from Bacillus amyloliquefaciens CBSYD1 isolated from traditional Korean fermented food kimchi, for the treatment of multidrug-resistant (MDR) bacteria. Strain CBSYD1 was identified 99.79% similar to Bacillus amyloliquefaciens subsp. plantarum FZB42(T) by 16S rRNA sequence analysis. The amino acid sequence residues of YD1 were determined to be Ala-Pro-Lys-Gly-Val-Gln-Gly-Pro-Asn-Gly by Edman degradation method. After the analysis and comparison of YD1 peptide sequence using several bioinformatic servers, peptide sequence has been considered to be unique. YD1 displayed antimicrobial activity against gram-positive and gram-negative bacteria. The minimal inhibitory concentrations (MIC) of YD1 for Escherichia coli KCTC1923 (E. coli), methicillin-resistant Staphylococcus aureus B15 (MRSA), and vancomycin-resistant enterococci (VRE) ranged from 8 to 64 µg/mL, representing greater potency than commercial reference antibiotics. The antimicrobial mechanism of YD1 was determined to involve cell-penetrating translocation inside the cell and interaction with the DNA leading ultimately to bacterial cell death. Analogously, Gly-Pro-Asn-Gly is the likely expected cell-penetrating motif for YD1. YD1 could be a promising antimicrobial agent for the clinical application.

Indexed as

Antimicrobial peptideBacillus amyloliquefaciens CBSYD1Mechanism of actionPurification

Identifiers

PMID28050849
PMCPMC5209312
OpenAlexW2564078335

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.