Evidence map›Paper›PMID 30637367›Full record

ArticlePeptide science (Hoboken, N.J.)2018

Antimicrobial activity of a porphyrin binding peptide.

David J Shirley, Christina L Chrom, Elizabeth A Richards, Benjamin R Carone, Gregory A Caputo

Abstract read
In one paragraph

Article in Peptide science (Hoboken, N.J.), 2018. 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
–field-weighted citation impact
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.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Activity and characterization of a pH-sensitive antimicrobial peptide.Biochimica et biophysica acta. Biomembranes · 2019
    Article
  9. Article
  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

5 authors.

David J ShirleyDepartment of Chemistry and Biochemistry, Rowan University, 201 Mullica Hill Road Glassboro, NJ 08028.
Christina L ChromDepartment of Chemistry and Biochemistry, Rowan University, 201 Mullica Hill Road Glassboro, NJ 08028.
Elizabeth A RichardsDepartment of Chemistry and Biochemistry, Rowan University, 201 Mullica Hill Road Glassboro, NJ 08028.
Benjamin R CaroneDepartment of Molecular and Cellular Biosciences, Rowan University, 201 Mullica Hill Road Glassboro, NJ 08028.
Gregory A CaputoDepartment of Chemistry and Biochemistry, Rowan University, 201 Mullica Hill Road Glassboro, NJ 08028.

Funding

Structure-Activity Relationship in Host Defense PeptidesR15GM094330 · NIGMS · ROWAN UNIVERSITY · PI CAPUTO, GREGORY ALEXANDER · 2010 to 2010
$292k
NIGMS NIH HHS R15 GM094330
6 · The paper itself

Abstract

Amphiphilic alpha-helices are common motifs used in numerous biological systems including membrane channels/pores and antimicrobial peptides (AMPs), and binding proteins, and a variety of synthetic biomaterials. Previously, an amphiphilic peptide with lysine-containing motifs was shown to reversibly bind the anionic porphyrin meso-Tetra(4-sulfonatophenyl)porphyrin (TPPS

Indexed as

Antimicrobial peptidesfluorescencelipid bindingmembrane permeabilizationporphyrin binding

Identifiers

PMID30637367
PMCPMC6324581

What OpenQuestion holds

Textmetadata
LicenceTDM
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.