Evidence map›Paper›PMID 29614844›Full record

ReviewMolecules (Basel, Switzerland)2018

Tryptophan-Rich and Proline-Rich Antimicrobial Peptides.

Awdhesh Kumar Mishra, Jaehyuk Choi, Eunpyo Moon, Kwang-Hyun Baek

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
9.9field-weighted citation impact, top 1% 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

85 citing papers in PubMed, 192 citations in OpenAlex.

  1. Novel Peptide-Triazole Conjugates: Strategic Synthesis, Antimicrobial Properties, and Molecular Docking Study.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Review

25 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Awdhesh Kumar MishraDepartment of Biotechnology, Yeungnam University, Gyeongsan, Gyeongbuk 38541, Korea. awadhesh.biotech07@gmail.com.ORCID 0000-0002-3312-3264
Jaehyuk ChoiDepartment of Biotechnology, Yeungnam University, Gyeongsan, Gyeongbuk 38541, Korea. stanza15@naver.com.
Eunpyo MoonDepartment of Biological Science, Ajou University, Suwon 442-749, Korea. emoon@ajou.ac.kr.
Kwang-Hyun BaekDepartment of Biotechnology, Yeungnam University, Gyeongsan, Gyeongbuk 38541, Korea. khbaek@ynu.ac.kr.
Yeungnam University · KRAjou University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Due to the increasing emergence of drug-resistant pathogenic microorganisms, there is a world-wide quest to develop new-generation antibiotics. Antimicrobial peptides (AMPs) are small peptides with a broad spectrum of antibiotic activities against bacteria, fungi, protozoa, viruses and sometimes exhibit cytotoxic activity toward cancer cells. As a part of the native host defense system, most AMPs target the membrane integrity of the microorganism, leading to cell death by lysis. These membrane lytic effects are often toxic to mammalian cells and restrict their systemic application. However, AMPs containing predominantly either tryptophan or proline can kill microorganisms by targeting intracellular pathways and are therefore a promising source of next-generation antibiotics. A minimum length of six amino acids is required for high antimicrobial activity in tryptophan-rich AMPs and the position of these residues also affects their antimicrobial activity. The aromatic side chain of tryptophan is able to rapidly form hydrogen bonds with membrane bilayer components. Proline-rich AMPs interact with the 70S ribosome and disrupt protein synthesis. In addition, they can also target the heat shock protein in target pathogens, and consequently lead to protein misfolding. In this review, we will focus on describing the structures, sources, and mechanisms of action of the aforementioned AMPs.

Indexed as

AnimalsAnti-Infective AgentsBacteriaFungiHumansPeptidesProlineTryptophanAnti-Infective AgentsPeptidesProlineTryptophanantimicrobial peptidemembrane lysisproline-rich antimicrobial peptidessynthetic combinatorial librariestryptophan-rich antimicrobial peptides

Identifiers

PMID29614844
PMCPMC6017362
OpenAlexW2794817296

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.