Evidence map›Paper›PMID 41183199›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

Conformational regulation of two essential activators of bacterial cell elongation.

Morgan S A Gilman, Irina Shlosman, Daniel D Samé Guerra, Masy Domecillo, Elayne M Fivenson, Claire Bourett, Thomas G Bernhardt, Nicholas F Polizzi, Joseph J Loparo, Andrew C Kruse

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  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 · 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

10 authors.

Morgan S A Gilman *Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.ORCID 0000-0001-6746-6284
Irina Shlosman *Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.
Daniel D Samé Guerra *Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.
Masy DomecilloDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.
Elayne M FivensonDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.
Claire BourettDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.
Thomas G BernhardtDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.ORCID 0000-0003-3566-7756
Nicholas F PolizziDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.
Joseph J LoparoDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.ORCID 0000-0003-4941-4696
Andrew C KruseDepartment of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.ORCID 0000-0002-1467-1222

Funding

Project 3: Defining and defeating the mechanisms of outer membrane biogenesis in Gram-negative bacteriaU19AI158028 · NIAID · HARVARD MEDICAL SCHOOL · PI WALKER, SUZANNE · 2022 to 2025
$10.1M
Peptidoglycan Biogenesis in Escherichia ColiR01AI083365 · NIAID · HARVARD MEDICAL SCHOOL · PI Thomas G Bernhardt · 2010 to 2026
$8.3M
Structure and dynamics of bacterial cell wall synthasesR01AI187524 · NIAID · HARVARD MEDICAL SCHOOL · PI Andrew Kruse, Joseph J. Loparo · 2025 to 2026
$1.4M
De novo design of small-molecule-binding proteinsR00GM135519 · NIGMS · DANA-FARBER CANCER INST · PI POLIZZI, NICHOLAS · 2022 to 2024
$747k
HHMI (HHMI) N/AHHS | NIH (NIH) R01 AI87524NIAID NIH HHS R01 AI083365NIAID NIH HHS R01 AI187524NIAID NIH HHS U19 AI158028NIGMS NIH HHS R00 GM135519NSF | NSF Graduate Research Fellowship Program (GRFP) N/A
6 · The paper itself

Abstract

The peptidoglycan (PG) cell wall is critical for bacterial growth and survival and is a primary antibiotic target. MreD is an essential accessory factor of the Rod complex, which carries out PG synthesis during elongation, yet little is known about how MreD facilitates this process. Here, we present the cryoelectron microscopy structure of

Indexed as

Bacterial ProteinsThermus thermophilusCell WallCryoelectron MicroscopyEscherichia coliModels, MolecularPeptidoglycanProtein ConformationBacterial ProteinsPeptidoglycanbacterial elongationcryo-EMpeptidoglycansingle-molecule FRETstructural biology

Identifiers

PMID41183199
PMCPMC12625996

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.