Evidence map›Paper›PMID 15504869›Full record

ArticleAntimicrobial agents and chemotherapy2004

Platelet microbicidal protein 1: structural themes of a multifunctional antimicrobial peptide.

Nannette Y Yount, Kimberly D Gank, Yan Qiong Xiong, Arnold S Bayer, Thomas Pender, William H Welch, Michael R Yeaman

Open access · greenAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
6.0field-weighted citation impact, top 4% 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

35 citing papers in PubMed, 67 citations in OpenAlex.

  1. Beyond hemostasis, the immunomodulatory nature of platelets.Research and practice in thrombosis and haemostasis · 2025
    Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Modulation of toll-like receptor signaling by antimicrobial peptides.Seminars in cell & developmental biology · 2019
    Review
  11. Review
  12. Amyloid Beta Peptide Is Released during Thrombosis in the Skin.International journal of molecular sciences · 2018
    Article
  13. Article
  14. Review
  15. Review
  16. Chemokine-Derived Peptides: Novel Antimicrobial and Antineoplasic Agents.International journal of molecular sciences · 2015
    Review
  17. Article
  18. Platelets: at the nexus of antimicrobial defence.Nature reviews. Microbiology · 2014
    Review
  19. Article
  20. 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

7 authors at 3 institutions in 1 country.

Nannette Y YountDavid Geffen School of Medicine at UCLA, Division of Infectious Diseases, St. John's Cardiovascular Research Center, Research & Education Institute at Harbor-UCLA Medical Center, Torrance, CA 90502, USA.
Kimberly D Gank
Yan Qiong Xiong
Arnold S Bayer
Thomas Pender
William H Welch
Michael R Yeaman
University of California, Los Angeles · USOffice of Infectious Diseases · USUniversity of Nevada, Reno · US

Funding

DETERMINANTS IN PLATELET MICROBICIDAL PROTEINSR01AI048031 · NIAID · LA BIOMED RES INST/ HARBOR UCLA MED CTR · PI YEAMAN, MICHAEL R · 2000 to 2004
$1.6M
NIAID NIH HHS AI-48031NIAID NIH HHS R01 AI048031
6 · The paper itself

Abstract

Mammalian platelets release platelet microbicidal proteins (PMPs) as components of their antimicrobial armamentarium. The present studies defined the structure of PMP-1 and examined its structure-activity relationships. Amino acid sequencing and mass spectroscopy demonstrated that distinct N-terminal polymorphism variants of PMP-1 isolated from nonstimulated or thrombin-stimulated platelets arise from a single PMP-1 propeptide. Sequence data (NH(2)-[S]D(1)DPKE(5)SEGDL(10)HCVCV(15)KTTSL(20) . . .) enabled cloning of PMP-1 from bone marrow and characterization of its full-length cDNA. PMP-1 is translated as a 106-amino-acid precursor and is processed to yield 73-residue (8,053 Da) and 72-residue (7,951-Da) variants. Searches with the BLAST program and sequence alignments demonstrated the homology of PMP-1 to members of the mammalian platelet factor 4 (PF-4) family of proteins. On the basis of phylogenetic relatedness, congruent sequence motifs, and predicted three-dimensional structures, PMP-1 shares the greatest homology with human PF-4 (hPF-4). By integration of its structural and antimicrobial properties, these results establish the identity of PMP-1 as a novel rabbit analogue of the microbicidal chemokine (kinocidin) hPF-4. These findings advance the hypothesis that stimuli in the setting of infection prompt platelets to release PF-4-class or related kinocidins, which have structures consistent with their likely multiple roles that bridge molecular and cellular mechanisms of antimicrobial host defense.

Indexed as

Amino Acid SequenceAnimalsAnti-Bacterial AgentsArtificial IntelligenceBlood ProteinsChemical PhenomenaChemistry, PhysicalCloning, MolecularDNA, ComplementaryElectrochemistryElectrophoresis, Polyacrylamide GelHumansIn Vitro TechniquesKruppel-Like Transcription FactorsMass SpectrometryModels, MolecularAnti-Bacterial AgentsBlood ProteinsDNA, ComplementaryKruppel-Like Transcription Factorsplatelet microbicidal protein, Oryctolagus cuniculusRepressor ProteinsThrombinZNF85 protein, human

Identifiers

PMID15504869
PMCPMC525416
OpenAlexW2137093661

What OpenQuestion holds

Textmetadata
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.