Evidence map›Paper›PMID 19478069›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Modeling the physics of FtsZ assembly and force generation.

Harold P Erickson

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing 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

57 citing papers in PubMed.

  1. Article
  2. Extensile Active Hydrogels Driven by Living FtsZ Polymers.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Cleavage-furrow formation without F-actin inProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Z-ring Structure and Constriction Dynamics inFrontiers in microbiology · 2017
    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

1 author.

Harold P EricksonDepartment of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA. h.erickson@cellbio.duke.edu

Funding

Structure and Assembly Dynamics of FtsZR01GM066014 · NIGMS · DUKE UNIVERSITY · PI ERICKSON, HAROLD P · 2002 to 2018
$7.5M
NIGMS NIH HHS GM66014NIGMS NIH HHS R01 GM066014
6 · The paper itself

Abstract

The tubulin homolog FtsZ is the major cytoskeletal protein in bacterial cytokinesis. It can generate a constriction force on the bacterial membrane or inside tubular liposomes. Several models have recently been proposed for how this force might be generated. These fall into 2 categories. The first is based on a conformational change from a straight to a curved protofilament. The simplest "hydrolyze and bend" model proposes a 22 degrees bend at every interface containing a GDP. New evidence suggests another curved conformation with a 2.5 degrees bend at every interface and that the relation of curvature to GTP hydrolysis is more complicated than previously thought. However, FtsZ protofilaments do appear to be mechanically rigid enough to bend membranes. A second category of models is based on lateral bonding between protofilaments, postulating that a contraction could be generated when protofilaments slide to increase the number of lateral bonds. Unfortunately these lateral bond models have ignored the contribution of subunit entropy when adding bond energies; if included, the mechanism is seen to be invalid. Finally, I address recent models that try to explain how protofilaments 1-subunit-thick show a cooperative assembly.

Indexed as

Bacterial ProteinsCytoskeletal ProteinsEscherichia coliGuanosine TriphosphateModels, BiologicalTubulinBacterial ProteinsCytoskeletal ProteinsFtsZ protein, BacteriaGuanosine TriphosphateTubulin

Identifiers

PMID19478069
PMCPMC2695047

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.