Evidence map›Paper›PMID 26355100›Full record

ReviewMolecular & cellular proteomics : MCP2015

Protein Neighbors and Proximity Proteomics.

Johanna S Rees, Xue-Wen Li, Sarah Perrett, Kathryn S Lilley, Antony P Jackson

Abstract readReview
In one paragraph

Review in Molecular & cellular proteomics : MCP, 2015. 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. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Proximity Labeling in Plants.Annual review of plant biology · 2023
    Review
  9. Article
  10. Review
  11. Bio-protocol · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Frontiers in molecular biosciences · 2022
    Article
  18. Article
  19. Review
  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

5 authors.

Johanna S ReesFrom the ‡Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, United Kingdom CB2 1QW, the §Cambridge Centre for Proteomics, University of Cambridge, Tennis Court Road, Cambridge, United Kingdom CB2 1QR, and jsr31@cam.ac.uk.ORCID http://orcid.org/0000-0003-2066-8617
Xue-Wen Lithe ‖National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China.
Sarah Perrettthe ‖National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China sarah.perrett@cantab.net.ORCID http://orcid.org/0000-0003-0137-0997
Kathryn S Lilleythe §Cambridge Centre for Proteomics, University of Cambridge, Tennis Court Road, Cambridge, United Kingdom CB2 1QR, and k.s.lilley@bioc.cam.ac.uk.ORCID http://orcid.org/0000-0003-0594-6543
Antony P JacksonFrom the ‡Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, United Kingdom CB2 1QW, apj10@cam.ac.uk.ORCID http://orcid.org/0000-0002-2895-7387

Funding

Biotechnology and Biological Sciences Research Council BB/D001242/1Biotechnology and Biological Sciences Research Council BB/H024085/1Biotechnology and Biological Sciences Research Council BB/J021091/1
6 · The paper itself

Abstract

Within cells, proteins can co-assemble into functionally integrated and spatially restricted multicomponent complexes. Often, the affinities between individual proteins are relatively weak, and proteins within such clusters may interact only indirectly with many of their other protein neighbors. This makes proteomic characterization difficult using methods such as immunoprecipitation or cross-linking. Recently, several groups have described the use of enzyme-catalyzed proximity labeling reagents that covalently tag the neighbors of a targeted protein with a small molecule such as fluorescein or biotin. The modified proteins can then be isolated by standard pulldown methods and identified by mass spectrometry. Here we will describe the techniques as well as their similarities and differences. We discuss their applications both to study protein assemblies and to provide a new way for characterizing organelle proteomes. We stress the importance of proteomic quantitation and independent target validation in such experiments. Furthermore, we suggest that there are biophysical and cell-biological principles that dictate the appropriateness of enzyme-catalyzed proximity labeling methods to address particular biological questions of interest.

Indexed as

BiotinCarbon-Nitrogen LigasesDNA-(Apurinic or Apyrimidinic Site) LyaseEscherichia coliEscherichia coli ProteinsFluoresceinHorseradish PeroxidaseIsotope LabelingMass SpectrometryProteomeProteomicsRepressor ProteinsStaining and LabelingTyramineBiotinbirA protein, E coliCarbon-Nitrogen LigasesDNA-(Apurinic or Apyrimidinic Site) LyaseEscherichia coli ProteinsFluoresceinHorseradish PeroxidaseProteomeRepressor ProteinsTyramine

Identifiers

PMID26355100
PMCPMC4638030

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.