Evidence map›Paper›PMID 32127388›Full record

ReviewMolecular & cellular proteomics : MCP2020

Proximity Dependent Biotinylation: Key Enzymes and Adaptation to Proteomics Approaches.

Payman Samavarchi-Tehrani, Reuben Samson, Anne-Claude Gingras

Open access · hybridAbstract readReview
In one paragraph

Review in Molecular & cellular proteomics : MCP, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed
15.9field-weighted citation impact, top 1% 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

123 citing papers in PubMed, 201 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. A Spatiotemporal Atlas of the Androgen Receptor Proximal Interactome.bioRxiv : the preprint server for biology · 2026
    Article
  5. Review
  6. Article
  7. Mass spectrometry proteomics for studying mitostasis.Protein science : a publication of the Protein Society · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Mapping Trypanosoma Protein Interactome by Proximity-Dependent Biotinylation.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

63 more citing papers are in PubMed but not listed here.

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 1 country.

Payman Samavarchi-TehraniLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Canada.
Reuben SamsonLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Canada; Department of Molecular Genetics, University of Toronto, Toronto, Canada.
Anne-Claude GingrasLunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Canada; Department of Molecular Genetics, University of Toronto, Toronto, Canada. Electronic address: gingras@lunenfeld.ca.
University of Toronto · CALunenfeld-Tanenbaum Research Institute · CA

Funding

CIHR FDN 143301
6 · The paper itself

Abstract

The study of protein subcellular distribution, their assembly into complexes and the set of proteins with which they interact with is essential to our understanding of fundamental biological processes. Complementary to traditional assays, proximity-dependent biotinylation (PDB) approaches coupled with mass spectrometry (such as BioID or APEX) have emerged as powerful techniques to study proximal protein interactions and the subcellular proteome in the context of living cells and organisms. Since their introduction in 2012, PDB approaches have been used in an increasing number of studies and the enzymes themselves have been subjected to intensive optimization. How these enzymes have been optimized and considerations for their use in proteomics experiments are important questions. Here, we review the structural diversity and mechanisms of the two main classes of PDB enzymes: the biotin protein ligases (BioID) and the peroxidases (APEX). We describe the engineering of these enzymes for PDB and review emerging applications, including the development of PDB for coincidence detection (split-PDB). Lastly, we briefly review enzyme selection and experimental design guidelines and reflect on the labeling chemistries and their implication for data interpretation.

Indexed as

ProteomicsAnimalsBiotinylationEnzymesHumansStaining and LabelingSubstrate SpecificityEnzymesAPEXBioIDbiotin ligasecellular organellesenzymesmass spectrometrymolecular biologyperoxidaseprotein engineeringProtein-protein interactionsproximity-dependent biotinylation

Identifiers

PMID32127388
PMCPMC7196579
OpenAlexW3010256122

What Socratic holds

Textmetadata
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 Socratic graph.