Evidence map›Paper›PMID 32723923›Full record

ArticlemBio2020

Lipoprotein

John H Gardiner, Gloria Komazin, Miki Matsuo, Kaitlin Cole, Friedrich Götz, Timothy C Meredith

Open access · goldAbstract read
In one paragraph

Article in mBio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

26 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Mutation of lipoprotein processing pathway geneAntimicrobial agents and chemotherapy · 2026
    Article
  6. Article
  7. Article
  8. LipoproteinmBio · 2025
    Article
  9. SpbR controls lipoteichoic acid length by directly inhibiting signal peptidase SpsB inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Identification and characterization of the lipoproteinProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Identification and Characterization of the LipoproteinbioRxiv : the preprint server for biology · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Frontiers in microbiology · 2022
    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

6 authors at 2 institutions in 2 countries.

John H GardinerThe Huck Institutes of the Life Sciences, The Pennsylvania State University, University Park, Pennsylvania, USA.
Gloria KomazinDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania, USA.
Miki MatsuoMicrobial Genetics, Interfaculty Institute of Microbiology and Infection Medicine Tübingen, University of Tübingen, Tübingen, Germany.
Kaitlin ColeDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania, USA.
Friedrich GötzMicrobial Genetics, Interfaculty Institute of Microbiology and Infection Medicine Tübingen, University of Tübingen, Tübingen, Germany.
Timothy C MeredithThe Huck Institutes of the Life Sciences, The Pennsylvania State University, University Park, Pennsylvania, USA txm50@psu.edu.ORCID 0000-0002-1901-6841
Pennsylvania State University · USUniversity of Tübingen · DE

Funding

N-terminal acylation of Lipoproteins in FirmicutesR01GM127482 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI Timothy C. Meredith · 2018 to 2026
$3.0M
NIGMS NIH HHS R01 GM127482
6 · The paper itself

Abstract

Bacterial lipoproteins (Lpps) are a class of membrane-associated proteins universally distributed among all bacteria. A characteristic N-terminal cysteine residue that is variably acylated anchors C-terminal globular domains to the extracellular surface, where they serve numerous roles, including in the capture and transport of essential nutrients. Lpps are also ligands for the Toll-like receptor 2 (TLR2) family, a key component of the innate immune system tasked with bacterial recognition. While Lpp function is conserved in all prokaryotes, structural heterogeneity in the N-terminal acylation state is widespread among

Indexed as

Signal TransductionAcylationAcyltransferasesBacterial ProteinsBiocatalysisHEK293 CellsHumansLipoproteinsStaphylococcus aureusToll-Like Receptor 2AcyltransferasesBacterial ProteinsLipoproteinsTLR2 protein, humanToll-Like Receptor 2acyl transferasesimmune responselipoproteinsStaphylococcusStaphylococcus aureusTLR2Toll-like receptors

Identifiers

PMID32723923
PMCPMC7387801
OpenAlexW3045785510

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.