Evidence map›Paper›PMID 22262316›Full record

ArticleChemphyschem : a European journal of chemical physics and physical chemistry2012

Three-dimensional super-resolution imaging of the midplane protein FtsZ in live Caulobacter crescentus cells using astigmatism.

Julie S Biteen, Erin D Goley, Lucy Shapiro, W E Moerner

Abstract read
In one paragraph

Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2012. 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. Article
  3. Article
  4. Review
  5. Article
  6. From single bacterial cell imaging towardsEssays in biochemistry · 2019
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Beyond force generation: Why is a dynamic ring of FtsZ polymers essential for bacterial cytokinesis?BioEssays : news and reviews in molecular, cellular and developmental biology · 2017
    Review
  15. Z-ring Structure and Constriction Dynamics inFrontiers in microbiology · 2017
    Article
  16. Article
  17. Shedding light on biology of bacterial cells.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016
    Review
  18. Review
  19. Addressing the Requirements of High-Sensitivity Single-Molecule Imaging of Low-Copy-Number Proteins in Bacteria.Chemphyschem : a European journal of chemical physics and physical chemistry · 2016
    Article
  20. Structures of the nucleoid occlusion protein SlmA bound to DNA and the C-terminal domain of the cytoskeletal protein FtsZ.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

4 authors.

Julie S BiteenDepartment of Chemistry, Stanford University, Stanford, CA 94305, USA.
Erin D Goley
Lucy Shapiro
W E Moerner

Funding

REGULATION OF DIFFERENTIATION IN CAULOBACTERR01GM032506 · NIGMS · YESHIVA UNIVERSITY · PI SHAPIRO, LUCILLE · 1985 to 2014
$7.1M
Subcellular architecture of regulatory protein complexes at the bacterial poleR01GM086196 · NIGMS · STANFORD UNIVERSITY · PI MOERNER, WILLIAM E, SHAPIRO, LUCILLE · 2008 to 2015
$4.7M
NIGMS NIH HHS R01 GM032506NIGMS NIH HHS R01 GM086196NIGMS NIH HHS R01GM086196
6 · The paper itself

Abstract

Single-molecule super-resolution imaging provides a non-invasive method for nanometer-scale imaging and is ideally suited to investigations of quasi-static structures within live cells. Here, we extend the ability to image subcellular features within bacteria cells to three dimensions based on the introduction of a cylindrical lens in the imaging pathway. We investigate the midplane protein FtsZ in Caulobacter crescentus with super-resolution imaging based on fluorescent-protein photoswitching and the natural polymerization/depolymerization dynamics of FtsZ associated with the Z-ring. We quantify these dynamics and determine the FtsZ depolymerization time to be <100 ms. We image the Z-ring in live and fixed C. crescentus cells at different stages of the cell cycle and find that the FtsZ superstructure is dynamic with the cell cycle, forming an open shape during the stalked stage and a dense focus during the pre-divisional stage.

Indexed as

AstigmatismBacterial ProteinsCaulobacter crescentusCytoskeletal ProteinsImaging, Three-DimensionalLuminescent ProteinsPolymerizationBacterial ProteinsCytoskeletal ProteinsFtsZ protein, BacteriaLuminescent Proteins

Identifiers

PMID22262316
PMCPMC3712621

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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.