Evidence map›Paper›PMID 35615024›Full record

ReviewComputational and structural biotechnology journal2022

Evolving and assembling to pierce through: Evolutionary and structural aspects of antimicrobial peptides.

Sukriyo Chakraborty, Ritika Chatterjee, Dipshikha Chakravortty

Open access · goldAbstract readReview
In one paragraph

Review in Computational and structural biotechnology journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

10 citing papers in PubMed, 23 citations in OpenAlex.

  1. Potential of isoquinoline-alkaloid-richFrontiers in pharmacology · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. Graphene-Oxide Peptide-Containing Materials for Biomedical Applications.International journal of molecular sciences · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
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.

Sukriyo ChakrabortyDepartment of Undergraduate Studies, Indian Institute of Science, Bengaluru, India.
Ritika ChatterjeeDepartment of Microbiology and Cell Biology, Division of Biological Science, Indian Institute of Science, Bengaluru, India.
Dipshikha ChakravorttyDepartment of Microbiology and Cell Biology, Division of Biological Science, Indian Institute of Science, Bengaluru, India.
Indian Institute of Science Bangalore · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The burgeoning menace of antimicrobial resistance across the globe has necessitated investigations into other chemotherapeutic strategies to combat infections. Antimicrobial peptides, or host defense peptides, are a set of promising therapeutic candidates in this regard. Most of them cause membrane permeabilization and are a key component of the innate immune response to pathogenic invasion. It has also been reported that peptide self-assembly is a driving factor governing the microbicidal activity of these peptide candidates. While efforts have been made to develop novel synthetic peptides against various microbes, many clinical trials of such peptides have failed due to toxicity and hemolytic activity to the host. A function-guided rational peptide engineering, based on evolutionary principles, physicochemical properties and activity determinants of AMP activity, is expected to help in targeting specific microbes. Furthermore, it is important to develop a unified understanding of the evolution of AMPs in order to fully appreciate their importance in host defense. This review seeks to explore the evolution of AMPs and the physicochemical determinants of AMP activity. The specific interactions driving AMP self-assembly have also been reviewed, emphasizing implications of this self-assembly on microbicidal and immunomodulatory activity.

Indexed as

AMP evolutionAMPs, Antimicrobial peptidesAntimicrobial peptidesHD6, Human-α-defensin 6HDPs, Host defense peptidesMRSA, Methicillin-resistant Staphylococcus aureusMUV, Multilamellar VesiclePeptide self-assemblyPhysicochemical determinantsStructural motifsSUV, Single Unilamellar Vesicle

Identifiers

PMID35615024
PMCPMC9117813
OpenAlexW4280610651

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.