Evidence map›Paper›PMID 33558391›Full record

ArticleJournal of bacteriology2021

Identification of potential regulatory domains within the MreC and MreD components of the cell elongation machinery.

Patricia D A Rohs, Jeanna M Qiu, Grasiela Torres, Mandy D Smith, Elayne M Fivenson, Thomas G Bernhardt

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. A broadly conserved gram-positive lipoprotein regulates cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Conformational regulation of two essential activators of bacterial cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Elongasome core proteins and class A PBP1a display zonal, processive movement at the midcell ofProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. A role for the Gram-negative outer membrane in bacterial shape determination.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Article
  18. Article
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  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 1 country.

Patricia D A RohsDepartment of Microbiology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Jeanna M QiuDepartment of Microbiology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Grasiela TorresDepartment of Microbiology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Mandy D SmithDepartment of Microbiology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Elayne M FivensonDepartment of Microbiology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Thomas G BernhardtDepartment of Microbiology, Harvard Medical School, Boston, Massachusetts 02115, USA thomas_bernhardt@hms.harvard.edu.
Harvard University · USHoward Hughes Medical Institute · US

Funding

Peptidoglycan Biogenesis in Escherichia ColiR01AI083365 · NIAID · HARVARD MEDICAL SCHOOL · PI Thomas G Bernhardt · 2010 to 2026
$8.3M
Bacteriology PhD Training ProgramT32AI132120 · NIAID · HARVARD MEDICAL SCHOOL · PI RUDNER, DAVID Z · 2017 to 2021
$1.7M
NIAID NIH HHS R01 AI083365NIAID NIH HHS T32 AI132120
6 · The paper itself

Abstract

The bacterial peptidoglycan (PG) cell wall maintains cell shape and prevents osmotic lysis. During growth of rod-shaped cells, PG is incorporated along the cell cylinder by the RodA-PBP2 synthase of the multi-protein Rod system (elongasome). Filaments of the actin-like MreB protein orient synthesis of the new PG material. They are connected to the RodA-PBP2 synthase in part through the RodZ component. MreC and MreD are other conserved components of the system, but their function is not well understood. Amino acid changes in RodA-PBP2 were recently identified that bypass a requirement for MreC and MreD function, suggesting the Mre proteins act as activators of the synthase. To further investigate their function, we developed a genetic strategy to identify dominant-negative alleles of

Identifiers

PMID33558391
PMCPMC8092158
OpenAlexW3128057403

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.