Evidence map›Paper›PMID 32909689›Full record

ReviewWiley interdisciplinary reviews. Developmental biology2021

Proximity-dependent labeling methods for proteomic profiling in living cells: An update.

Justin A Bosch, Chiao-Lin Chen, Norbert Perrimon

Abstract readReview
In one paragraph

Review in Wiley interdisciplinary reviews. Developmental biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing 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

85 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Probing direct interactions between nuclear proteins in cells with nxReLo.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

25 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.

Justin A BoschDepartment of Genetics, Blavatnik Institute, Harvard Medical School, Boston, Massachusetts, USA.ORCID 0000-0001-8499-1566
Chiao-Lin ChenDepartment of Genetics, Blavatnik Institute, Harvard Medical School, Boston, Massachusetts, USA.ORCID 0000-0003-3118-0502
Norbert PerrimonDepartment of Genetics, Blavatnik Institute, Harvard Medical School, Boston, Massachusetts, USA.ORCID 0000-0001-7542-472X

Funding

Mapping protein communication between organs in homeostasis and diseaseR01DK121409 · NIDDK · HARVARD MEDICAL SCHOOL · PI CARR, STEVEN A, MCMAHON, ANDREW P. · 2018 to 2022
$8.3M
Characterization of the Insulin to Autophagy Pathway in MusclesR01AR057352 · NIAMS · HARVARD MEDICAL SCHOOL · PI NORBERT PERRIMON · 2010 to 2026
$8.2M
NIAMS NIH HHS R01 AR057352NIDDK NIH HHS R01 DK121409
6 · The paper itself

Abstract

Characterizing the proteome composition of organelles and subcellular regions of living cells can facilitate the understanding of cellular organization as well as protein interactome networks. Proximity labeling-based methods coupled with mass spectrometry (MS) offer a high-throughput approach for systematic analysis of spatially restricted proteomes. Proximity labeling utilizes enzymes that generate reactive radicals to covalently tag neighboring proteins. The tagged endogenous proteins can then be isolated for further analysis by MS. To analyze protein-protein interactions or identify components that localize to discrete subcellular compartments, spatial expression is achieved by fusing the enzyme to specific proteins or signal peptides that target to particular subcellular regions. Although these technologies have only been introduced recently, they have already provided deep insights into a wide range of biological processes. Here, we provide an updated description and comparison of proximity labeling methods, as well as their applications and improvements. As each method has its own unique features, the goal of this review is to describe how different proximity labeling methods can be used to answer different biological questions. This article is categorized under: Technologies > Analysis of Proteins.

Indexed as

Protein Interaction Domains and MotifsAnimalsHumansProteinsProteomeStaining and LabelingProteinsProteomeAPEXBioIDHRPproximity labeling PUP-IT

Identifiers

PMID32909689
PMCPMC8142282

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.