Evidence map›Paper›PMID 17217910›Full record

ArticleBiochimica et biophysica acta2007

Modular determinants of antimicrobial activity in platelet factor-4 family kinocidins.

Michael R Yeaman, Nannette Y Yount, Alan J Waring, Kimberly D Gank, Deborah Kupferwasser, Robert Wiese, Arnold S Bayer, William H Welch

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
1.9field-weighted citation impact, top 17% 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

40 citing papers in PubMed, 83 citations in OpenAlex.

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  13. Dual actions of group BProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Unifying structural signature of eukaryotic α-helical host defense peptides.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Review
  16. Modulation of toll-like receptor signaling by antimicrobial peptides.Seminars in cell & developmental biology · 2019
    Review
  17. Review
  18. Article
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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

8 authors at 3 institutions in 1 country.

Michael R YeamanDivision of Infectious Diseases, LAC-Harbor UCLA Medical Center, Torrance, CA 90509, USA. MRYeaman@ucla.edu
Nannette Y Yount
Alan J Waring
Kimberly D Gank
Deborah Kupferwasser
Robert Wiese
Arnold S Bayer
William H Welch
UCLA Medical Center · USUniversity of California, Los Angeles · USUniversity of Nevada, Reno · US

Funding

Staphylococcal Adaptations to Platelet Microbicidal ProteinR01AI039108 · NIAID · LUNDQUIST INSTITUTE FOR BIOMEDICAL INNOVATION AT HARBOR-UCLA MEDICAL CENTER · PI BAYER, ARNOLD S · 1997 to 2016
$5.1M
Microbicidal Proteins from PlateletsR01AI039001 · NIAID · LUNDQUIST INSTITUTE FOR BIOMEDICAL INNOVATION AT HARBOR-UCLA MEDICAL CENTER · PI YEAMAN, MICHAEL R · 2006 to 2010
$1.7M
DETERMINANTS IN PLATELET MICROBICIDAL PROTEINSR01AI048031 · NIAID · LA BIOMED RES INST/ HARBOR UCLA MED CTR · PI YEAMAN, MICHAEL R · 2000 to 2004
$1.6M
CORE FACILITY RESEARCH PEPTIDE SYNTHESIZERS10RR014857 · NCRR · LA BIOMED RES INST/ HARBOR UCLA MED CTR · PI YEAMAN, MICHAEL R · 2001 to 2001
$132k
MICROBICIDAL PROTEINS FROM PLATELETSR29AI039001 · NIAID · LA BIOMED RES INST/ HARBOR UCLA MED CTR · PI YEAMAN, MICHAEL R · 1996 to 2000
$99k
NCRR NIH HHS RR-14857NCRR NIH HHS S10 RR014857NIAID NIH HHS AI-39001NIAID NIH HHS AI-39108NIAID NIH HHS AI-48031NIAID NIH HHS R01 AI039001NIAID NIH HHS R01 AI039108NIAID NIH HHS R01 AI048031NIAID NIH HHS R29 AI039001
6 · The paper itself

Abstract

Mammalian platelets contain an array of antimicrobial peptides, termed platelet microbicidal proteins (PMPs). Human and rabbit PMPs include known chemokines, such as platelet factor-4 (hPF-4); PMP-1 is the rabbit orthologue of hPF-4. Chemokines that also exert direct antimicrobial activity have been termed kinocidins. A consensus peptide domain library representing mammalian PF-4 family members was analyzed to define structural domains contributing to antimicrobial activity against a panel of human pathogens. Secondary conformations were assessed by circular dichroism spectrometry, and molecular modeling was employed to investigate structural correlates of antimicrobial efficacy. Antimicrobial activity against isogenic peptide-susceptible or -resistant Staphylococcus aureus, Salmonella typhimurium, and Candida albicans strain pairs mapped to the C-terminal hemimer (38-74) and modular domains thereof (49-63 and 60-74). Increasing electrostatic charge and steric bulk were general correlates of efficacy. Structural data corroborated spatial distribution of charge, steric bulk and putative secondary structure with organism-specific efficacy. Microbicidal efficacies of the cPMP antimicrobial hemimer and C-terminal peptide (60-74) were retained in a complex human-blood biomatrix assay. Collectively, these results suggest that modular determinants arising from structural components acting independently and cooperatively govern the antimicrobial functions of PF-4 family kinocidins against specific target pathogens.

Indexed as

Amino Acid SequenceAnti-Bacterial AgentsBlood PlateletsCandida albicansChemokinesCircular DichroismColony Count, MicrobialDose-Response Relationship, DrugHumansMass SpectrometryMicrobial Sensitivity TestsModels, MolecularMolecular Sequence DataPlatelet Factor 4Protein ConformationProtein Structure, SecondaryAnti-Bacterial AgentsChemokinesPlatelet Factor 4

Identifiers

PMID17217910
PMCPMC2827485
OpenAlexW2001422402

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.