Evidence map›Paper›PMID 31772021›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Probing transient excited states of the bacterial cell division regulator MinE by relaxation dispersion NMR spectroscopy.

Mengli Cai, Ying Huang, Yang Shen, Min Li, Michiyo Mizuuchi, Rodolfo Ghirlando, Kiyoshi Mizuuchi, G Marius Clore

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Metamorphic proteins and how to find them.Current opinion in structural biology · 2024
    Review
  4. Article
  5. Intrinsic structural dynamics dictate enzymatic activity and inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Fluid protein fold space and its implications.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  7. Distinguishing features of fold-switching proteins.Protein science : a publication of the Protein Society · 2023
    Review
  8. Three-dimensional chiral morphodynamics of chemomechanical active shells.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. AlphaFold2 fails to predict protein fold switching.Protein science : a publication of the Protein Society · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Functional and Regulatory Roles of Fold-Switching Proteins.Structure (London, England : 1993) · 2021
    Review
  14. 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

8 authors at 2 institutions in 1 country.

Mengli CaiLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.
Ying HuangLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0540.
Yang ShenLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.
Min LiLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0540.
Michiyo MizuuchiLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0540.
Rodolfo GhirlandoLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0540.
Kiyoshi MizuuchiLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0540 mariusc@mail.nih.gov kiyoshimi@niddk.nih.gov.
G Marius CloreLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520; mariusc@mail.nih.gov kiyoshimi@niddk.nih.gov.
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial MinD and MinE form a standing oscillatory wave which positions the cell division inhibitor MinC, that binds MinD, everywhere on the membrane except at the midpoint of the cell, ensuring midcell positioning of the cytokinetic septum. During this process MinE undergoes fold switching as it interacts with different partners. We explore the exchange dynamics between major and excited states of the MinE dimer in 3 forms using

Indexed as

Nuclear Magnetic Resonance, BiomolecularCell Cycle ProteinsEscherichia coli ProteinsModels, MolecularProtein ConformationProtein FoldingCell Cycle ProteinsEscherichia coli ProteinsMinE protein, E coliexcited statesfold switchingmillisecond exchange dynamicsprotein conformational dynamicsself-organizing standing wave

Identifiers

PMID31772021
PMCPMC6925984
OpenAlexW2989906483

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.