Evidence map›Paper›PMID 10075974›Full record

ArticleThe Journal of experimental medicine1999

An inflammatory polypeptide complex from Staphylococcus epidermidis: isolation and characterization.

C Mehlin, C M Headley, S J Klebanoff

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

97 citing papers in PubMed, 205 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. The Pathogenicity Mechanisms ofInternational journal of molecular sciences · 2025
    Review
  5. Journal of bacteriology · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Molecular Characteristics and Pathogenicity ofInternational journal of molecular sciences · 2023
    Review
  10. Review
  11. Two transporters cooperate to secrete amphipathic peptides from the cytoplasmic and membranous milieus.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Phenol-Soluble Modulins FromFrontiers in cellular and infection microbiology · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

37 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

3 authors at 1 institution in 1 country.

C MehlinDepartment of Pathobiology, University of Washington, Seattle, Washington 98195, USA.
C M Headley
S J Klebanoff
University of Washington · US

Funding

ANTIMICROBIAL EFFECT OF PEROXIDASE - ROLE IN LEUKOCYTESR01AI007763 · NIAID · UNIVERSITY OF WASHINGTON · PI KLEBANOFF, SEYMOUR J · 1985 to 1987
–
ANTIMICROBIAL EFFECT OF PEROXIDASE--ROLE IN LEUKOCYTESR37AI007763 · NIAID · UNIVERSITY OF WASHINGTON · PI KLEBANOFF, SEYMOUR J · 1988 to 1999
–
NIAID NIH HHS AI07763
6 · The paper itself

Abstract

Staphylococcus epidermidis releases factors that activate the HIV-1 long terminal repeat, induce cytokine release, and activate nuclear factor B in cells of macrophage lineage. The active material had a mass of 34,500 daltons, was inactivated by proteases and partitioned into the phenol layer on hot aqueous phenol extraction, and thus was termed phenol-soluble modulin (PSM). High performance liquid chromatography (HPLC) of crude PSM yielded two peaks of activity designated PSM peak 1 and peak 2. MALDI-TOF (matrix-assisted laser desorption ionization-time of flight) mass spectroscopy indicated the presence of two components in peak 1, which were designated PSM and PSM. Peak 2 contained a single component, designated PSM. Separation of PSM and PSM in peak 1 could be achieved by a second HPLC procedure. The structure of each component was determined by amino acid sequence analysis and identification and sequencing of their genes. PSM, PSM, and PSM were 22-, 44-, and 25-amino acid, respectively, strongly hydrophobic polypeptides. PSM was identified as Staphylococcus epidermidis delta toxin, whereas PSM and PSM exhibited more distant homology to previously described staphylococcal toxins. They appeared to exist as a complex or aggregate with activity greater than the component parts. The properties of the S. epidermidis PSMs suggest that they may contribute to the systemic manifestations of Gram-positive sepsis.

Indexed as

Amino Acid SequenceBacterial ProteinsBase SequenceCell LineCytokinesHIV Long Terminal RepeatHumansLipopolysaccharidesMolecular Sequence DataMolecular WeightNF-kappa BStaphylococcus epidermidisTeichoic AcidsBacterial ProteinsCytokinesLipopolysaccharideslipoteichoic acidNF-kappa BTeichoic Acids

Identifiers

PMID10075974
PMCPMC2193041
OpenAlexW2167872449

What OpenQuestion holds

Texttitle and abstract
LicenceCC BY-NC-SA
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.