Evidence map›Paper›PMID 31142644›Full record

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

Torque-dependent remodeling of the bacterial flagellar motor.

Navish Wadhwa, Rob Phillips, Howard C Berg

Abstract 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 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

  1. Journal of bacteriology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Osmotic stress triggers fast and reversible PMF collapse inbioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Review
  9. Review
  10. A dynamic compositional equilibrium governs mRNA recognition by eIF3.bioRxiv : the preprint server for biology · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  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

3 authors.

Navish WadhwaDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138; navish_wadhwa@fas.harvard.edu.ORCID 0000-0002-3514-5256
Rob PhillipsDepartment of Physics, California Institute of Technology, Pasadena, CA 91125.ORCID 0000-0003-3082-2809
Howard C BergDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138.

Funding

SENSORY TRANSDUCTION IN BACTERIAL CHEMOTAXISR01AI016478 · NIAID · HARVARD UNIVERSITY · PI BERG, HOWARD C · 1985 to 2019
$14.1M
The Principles of Regulatory, Conformational and Evolutionary AdaptationR35GM118043 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI ROB PHILLIPS · 2016 to 2026
$7.9M
NIAID NIH HHS R01 AI016478NIGMS NIH HHS R35 GM118043
6 · The paper itself

Abstract

Multisubunit protein complexes are ubiquitous in biology and perform a plethora of essential functions. Most of the scientific literature treats such assemblies as static: their function is assumed to be independent of their manner of assembly, and their structure is assumed to remain intact until they are degraded. Recent observations of the bacterial flagellar motor, among others, bring these notions into question. The torque-generating stator units of the motor assemble and disassemble in response to changes in load. Here, we used electrorotation to drive tethered cells forward, which decreases motor load, and measured the resulting stator dynamics. No disassembly occurred while the torque remained high, but all of the stator units were released when the motor was spun near the zero-torque speed. When the electrorotation was turned off, so that the load was again high, stator units were recruited, increasing motor speed in a stepwise fashion. A model in which speed affects the binding rate and torque affects the free energy of bound stator units captures the observed torque-dependent stator assembly dynamics, providing a quantitative framework for the environmentally regulated self-assembly of a major macromolecular machine.

Indexed as

BacteriaBacterial ProteinsFlagellaMacromolecular SubstancesMolecular Motor ProteinsTorqueBacterial ProteinsMacromolecular SubstancesMolecular Motor Proteinsbacterial flagellar motormolecular motormultisubunit complexregulated self-assembly

Identifiers

PMID31142644
PMCPMC6576217

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.