Evidence map›Paper›PMID 26470917›Full record

ArticleMicroscopy (Oxford, England)2016

Single-particle electron microscopy in the study of membrane protein structure.

Rita De Zorzi, Wei Mi, Maofu Liao, Thomas Walz

Abstract read
In one paragraph

Article in Microscopy (Oxford, England), 2016. 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
–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

18 citing papers in PubMed.

  1. Optimized bacterial expression of a synthetic BRIL antibody.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  2. Article
  3. Article
  4. Cell-derived nanomaterials for biomedical applications.Science and technology of advanced materials · 2024
    Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Selection of Biophysical Methods for Characterisation of Membrane Proteins.International journal of molecular sciences · 2019
    Review
  14. Article
  15. Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017
    Review
  16. Article
  17. Article
  18. 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

4 authors.

Rita De ZorziDepartment of Cell Biology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA Howard Hughes Medical Institute, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
Wei MiDepartment of Cell Biology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
Maofu LiaoDepartment of Cell Biology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
Thomas WalzDepartment of Cell Biology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA Howard Hughes Medical Institute, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA twalz@rockefeller.edu.

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Single-particle electron microscopy (EM) provides the great advantage that protein structure can be studied without the need to grow crystals. However, due to technical limitations, this approach played only a minor role in the study of membrane protein structure. This situation has recently changed dramatically with the introduction of direct electron detection device cameras, which allow images of unprecedented quality to be recorded, also making software algorithms, such as three-dimensional classification and structure refinement, much more powerful. The enhanced potential of single-particle EM was impressively demonstrated by delivering the first long-sought atomic model of a member of the biomedically important transient receptor potential channel family. Structures of several more membrane proteins followed in short order. This review recounts the history of single-particle EM in the study of membrane proteins, describes the technical advances that now allow this approach to generate atomic models of membrane proteins and provides a brief overview of some of the membrane protein structures that have been studied by single-particle EM to date.

Indexed as

Cell MembraneCryoelectron MicroscopyImaging, Three-DimensionalMembrane ProteinsMembrane Proteinscryo-electron microscopymembrane proteinssingle-particle electron microscopystructure determination

Identifiers

PMID26470917
PMCPMC4749050

What OpenQuestion holds

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Registered trials

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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.