Evidence map›Paper›PMID 17873883›Full record

ArticleNature structural & molecular biology2007

The structure of bacterial ParM filaments.

Albina Orlova, Ethan C Garner, Vitold E Galkin, John Heuser, R Dyche Mullins, Edward H Egelman

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
25.9field-weighted citation impact, top 1% 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

47 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. The evolution of archaeal flagellar filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Archaeal actin from a hyperthermophile forms a single-stranded filament.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  11. Review
  12. Article
  13. Article
  14. Structure of the ParM filament at 8.5Å resolution.Journal of structural biology · 2013
    Article
  15. Article
  16. Article
  17. The bacterial cytoskeleton: more than twisted filaments.Current opinion in cell biology · 2013
    Review
  18. Article
  19. Are ParM filaments polar or bipolar?Journal of molecular biology · 2012
    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

6 authors at 3 institutions in 1 country.

Albina OrlovaDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia 22908-0733, USA.
Ethan C Garner
Vitold E Galkin
John Heuser
R Dyche Mullins
Edward H Egelman
University of Virginia · USUniversity of California, San Francisco · USWashington University in St. Louis · US

Funding

MECHANISMS OF ARP2/3 ACTIVATION AND FUNCTIONR01GM061010 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MULLINS, R DYCHE · 2000 to 2015
$3.8M
Structural Studies of ActinR01GM081303 · NIGMS · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H. · 2007 to 2016
$3.6M
Mechanism and function of a novel actin nucleatorR01GM075287 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MULLINS, R DYCHE · 2006 to 2009
$1.0M
NIGMS NIH HHS GM061010NIGMS NIH HHS GM081303NIGMS NIH HHS GM675287NIGMS NIH HHS R01 GM061010NIGMS NIH HHS R01 GM075287NIGMS NIH HHS R01 GM081303
6 · The paper itself

Abstract

Bacterial ParM is a homolog of eukaryotic actin and is involved in moving plasmids so that they segregate properly during cell division. Using cryo-EM and three-dimensional reconstruction, we show that ParM filaments have a different structure from F-actin, with very different subunit-subunit interfaces. These interfaces result in the helical handedness of the ParM filament being opposite to that of F-actin. Like F-actin, ParM filaments have a variable twist, and we show that this involves domain-domain rotations within the ParM subunit. The present results yield new insights into polymorphisms within F-actin, as well as the evolution of polymer families.

Indexed as

Protein Structure, QuaternaryActinsCryoelectron MicroscopyEscherichia coliEscherichia coli ProteinsModels, MolecularMolecular Sequence DataProtein SubunitsActinsEscherichia coli ProteinsParM protein, E coliProtein Subunits

Identifiers

PMID17873883
PMCPMC3541950
OpenAlexW1972945264

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.