Evidence map›Paper›PMID 25997350›Full record

ArticleMethods in cell biology2015

Using supported bilayers to study the spatiotemporal organization of membrane-bound proteins.

Phuong A Nguyen, Christine M Field, Aaron C Groen, Timothy J Mitchison, Martin Loose

Abstract read
In one paragraph

Article in Methods in cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

8 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  3. Article
  4. STAR protocols · 2020
    Article
  5. Stochastic activation and bistability in a Rab GTPase regulatory network.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. Article
  7. Article
  8. Review
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 2 institutions in 2 countries.

Phuong A Nguyen *Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
Christine M FieldDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
Aaron C GroenDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
Timothy J MitchisonDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
Martin Loose *Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
Marine Biological Laboratory · USHarvard University · US

Funding

Resource CoreP40OD010997 · OD · MARINE BIOLOGICAL LABORATORY · PI Marko E Horb · 2012 to 2026
$13.1M
MICROTUBULE DYNAMICS AND MITOTIC MECHANISMR01GM039565 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1988 to 2018
$6.2M
MICROTUBULE DYNAMICS AND MITOTIC MECHANISMR37GM039565 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1997 to 2006
$3.2M
NIGMS NIH HHS GM39565NIGMS NIH HHS R01 GM039565NIGMS NIH HHS R37 GM039565NIH HHS P40 OD010997
6 · The paper itself

Abstract

Cell division in prokaryotes and eukaryotes is commonly initiated by the well-controlled binding of proteins to the cytoplasmic side of the cell membrane. However, a precise characterization of the spatiotemporal dynamics of membrane-bound proteins is often difficult to achieve in vivo. Here, we present protocols for the use of supported lipid bilayers to rebuild the cytokinetic machineries of cells with greatly different dimensions: the bacterium Escherichia coli and eggs of the vertebrate Xenopus laevis. Combined with total internal reflection fluorescence microscopy, these experimental setups allow for precise quantitative analyses of membrane-bound proteins. The protocols described to obtain glass-supported membranes from bacterial and vertebrate lipids can be used as starting points for other reconstitution experiments. We believe that similar biochemical assays will be instrumental to study the biochemistry and biophysics underlying a variety of complex cellular tasks, such as signaling, vesicle trafficking, and cell motility.

Indexed as

AnimalsAurora Kinase AAurora Kinase BBacterial ProteinsCarrier ProteinsCell Cycle ProteinsCell DivisionCell MembraneCell MovementCytoskeletal ProteinsEscherichia coliEscherichia coli ProteinsLipid BilayersMembrane ProteinsMicroscopy, FluorescenceOvumaurkb protein, XenopusAurora Kinase AAurora Kinase BBacterial ProteinsCarrier ProteinsCell Cycle ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsA protein, E coliFtsZ protein, BacteriaLipid BilayersMembrane ProteinsTissue ExtractsXenopus ProteinsZipA protein, E coliCell divisionCytokinesis signalingE. coliFtsAFtsZIn vitro reconstitutionLipidsMicrotubulesSupported bilayerXenopus

Identifiers

PMID25997350
PMCPMC4578691
OpenAlexW2339521790

What OpenQuestion holds

Textmetadata
LicenceTDM
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.