Evidence map›Paper›PMID 24915020›Full record

ArticleBiochimica et biophysica acta2015

Peptidoglycan architecture of Gram-positive bacteria by solid-state NMR.

Sung Joon Kim, James Chang, Manmilan Singh

Abstract read
In one paragraph

Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing 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

73 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Raman signatures ofFrontiers in microbiology · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. International journal of molecular sciences · 2024
    Article
  13. Review
  14. Article
  15. The BioCascade Impactor: A novel device for direct collection of size-fractionated bioaerosols into liquid medium.Aerosol science and technology : the journal of the American Association for Aerosol Research · 2024
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Solid-state NMR molecular snapshots ofProceedings of the National Academy of Sciences of the United States of America · 2023
    Article

13 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.

Sung Joon KimDepartment of Chemistry and Biochemistry, Baylor University, Waco, TX 76706, USA. Electronic address: Sung_J_Kim@baylor.edu.
James ChangDepartment of Chemistry and Biochemistry, Baylor University, Waco, TX 76706, USA.
Manmilan SinghDepartment of Chemistry, Washington University, St. Louis, MO 63130, USA.

Funding

Structure of Proteins in Cell Walls by REDOR NMRR01EB002058 · NIBIB · WASHINGTON UNIVERSITY · PI SCHAEFER, JACOB · 2003 to 2013
$3.2M
NIBIB NIH HHS EB002058NIBIB NIH HHS R01 EB002058
6 · The paper itself

Abstract

Peptidoglycan is an essential component of cell wall in Gram-positive bacteria with unknown architecture. In this review, we summarize solid-state NMR approaches to address some of the unknowns in the Gram-positive bacteria peptidoglycan architecture: 1) peptidoglycan backbone conformation, 2) PG-lattice structure, 3) variations in the peptidoglycan architecture and composition, 4) the effects of peptidoglycan bridge-length on the peptidoglycan architecture in Fem mutants, 5) the orientation of glycan strands with respect to the membrane, and 6) the relationship between the peptidoglycan structure and the glycopeptide antibiotic mode of action. Solid-state NMR analyses of Staphylococcus aureus cell wall show that peptidoglycan chains are surprisingly ordered and densely packed. The peptidoglycan disaccharide backbone adopts 4-fold screw helical symmetry with the disaccharide unit periodicity of 40Å. Peptidoglycan lattice in the S. aureus cell wall is formed by cross-linked PG stems that have parallel orientations. The structural characterization of Fem-mutants of S. aureus with varying lengths of bridge structures suggests that the PG-bridge length is an important determining factor for the PG architecture.

Indexed as

Anti-Bacterial AgentsCell WallGram-Positive BacteriaMagnetic Resonance SpectroscopyMolecular ConformationPeptidoglycanStaphylococcus aureusAnti-Bacterial AgentsPeptidoglycanArchitectureCell wallOritavancinPeptidoglycanREDORStaphylococcus aureus

Identifiers

PMID24915020
PMCPMC4258515

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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.