Evidence map›Paper›PMID 21339292›Full record

ArticleThe Journal of biological chemistry2011

Architecture and assembly of a divergent member of the ParM family of bacterial actin-like proteins.

Christopher R Rivera, Justin M Kollman, Jessica K Polka, David A Agard, R Dyche Mullins

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Effects of polymerization and nucleotide identity on the conformational dynamics of the bacterial actin homolog MreB.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  9. Accessory factors promote AlfA-dependent plasmid segregation by regulating filament nucleation, disassembly, and bundling.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  10. Article
  11. Review
  12. Structure of the ParM filament at 8.5Å resolution.Journal of structural biology · 2013
    Article
  13. Article
  14. The bacterial cytoskeleton: more than twisted filaments.Current opinion in cell biology · 2013
    Review
  15. Review
  16. Article
  17. Article
  18. 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

5 authors at 1 institution in 1 country.

Christopher R RiveraDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, California 94158, USA.
Justin M Kollman
Jessica K Polka
David A Agard
R Dyche Mullins
University of California, San Francisco · US

Funding

Microtubule Nucleation: Structure & MechanismR01GM031627 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI AGARD, DAVID A. · 1985 to 2016
$6.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM031627
6 · The paper itself

Abstract

Eubacteria and archaea contain a variety of actin-like proteins (ALPs) that form filaments with surprisingly diverse architectures, assembly dynamics, and cellular functions. Although there is much data supporting differences between ALP families, there is little data regarding conservation of structure and function within these families. We asked whether the filament architecture and biochemical properties of the best-understood prokaryotic actin, ParM from plasmid R1, are conserved in a divergent member of the ParM family from plasmid pB171. Previous work demonstrated that R1 ParM assembles into filaments that are structurally distinct from actin and the other characterized ALPs. They also display three biophysical properties thought to be essential for DNA segregation: 1) rapid spontaneous nucleation, 2) symmetrical elongation, and 3) dynamic instability. We used microscopic and biophysical techniques to compare and contrast the architecture and assembly of these related proteins. Despite being only 41% identical, R1 and pB171 ParMs polymerize into nearly identical filaments with similar assembly dynamics. Conservation of the core assembly properties argues for their importance in ParM-mediated DNA segregation and suggests that divergent DNA-segregating ALPs with different assembly properties operate via different mechanisms.

Indexed as

Actin CytoskeletonActinsAdenosine TriphosphateCloning, MolecularDNAEscherichia coli ProteinsImage Processing, Computer-AssistedKineticsModels, BiologicalPhosphatesPlasmidsPolymersProtein ConformationProteinsScattering, RadiationActinsAdenosine TriphosphateDNAEscherichia coli ProteinsParM protein, E coliPhosphatesPolymersProteins

Identifiers

PMID21339292
PMCPMC3077629
OpenAlexW2107957377

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.