Evidence map›Paper›PMID 25997355›Full record

ArticleMethods in cell biology2015

Reconstitution of proteins on electroformed giant unilamellar vesicles.

Eva M Schmid, David L Richmond, Daniel A Fletcher

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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
9.3field-weighted citation impact, top 2% 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

22 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Frontiers in cell and developmental biology · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. A synergy between mechanosensitive calcium- and membrane-binding mediates tension-sensing by C2-like domains.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Review
  12. Chloroplast Sec14-like 1 (CPSFL1) is essential for normal chloroplast development and affects carotenoid accumulation inProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Interplay between α-synuclein amyloid formation and membrane structure.Biochimica et biophysica acta. Proteins and proteomics · 2019
    Review
  15. Article
  16. Article
  17. Article
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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

3 authors at 2 institutions in 2 countries.

Eva M SchmidDepartment of Bioengineering & Biophysics Program, University of California, Berkeley, CA, USA.
David L RichmondMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Daniel A FletcherDepartment of Bioengineering & Biophysics Program, University of California, Berkeley, CA, USA; Physical Biosciences, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
University of California, Berkeley · USMax Planck Institute of Molecular Cell Biology and Genetics · DE

Funding

A membrane encapsulation system for cellular reconstitutionR01GM114344 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI FLETCHER, DANIEL A · 2015 to 2018
$1.2M
NIGMS NIH HHS R01 GM114344
6 · The paper itself

Abstract

In vitro reconstitution of simplified biological systems from molecular parts has proven to be a powerful method for investigating the biochemical and biophysical principles underlying cellular processes. In recent years, there has been a growing interest in reconstitution of protein-membrane interactions to understand the critical role played by membranes in organizing molecular-scale events into micron-scale patterns and protrusions. However, while all reconstitution experiments depend on identifying and isolating an essential set of soluble biomolecules, such as proteins, DNA, and RNA, reconstitution of membrane-based processes involves the additional challenge of forming and working with lipid bilayer membranes with composition, fluidity, and mechanical properties appropriate for the process at hand. Here we discuss a selection of methods for forming synthetic lipid bilayer membranes and present a versatile electroformation protocol that our lab uses for reconstituting proteins on giant unilamellar vesicles. This synthetic membrane-based approach to reconstitution offers the ability to study protein organization and activity at membranes under more cell-like conditions, addressing a central challenge to accomplishing the grand goal of "building the cell."

Indexed as

Cell MembraneDNALipid BilayersMicroscopy, ConfocalProtein BindingProteinsUnilamellar LiposomesDNALipid BilayersProteinsUnilamellar LiposomesElectroformationLipid bilayerLiposomeMembrane proteinMembrane reconstitutionProtein–membrane interactionVesicleVideo protocol

Identifiers

PMID25997355
PMCPMC5564371
OpenAlexW2400405804

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.