Evidence map›Paper›PMID 31969649›Full record

ArticleCommunications biology2020

Biotin proximity tagging favours unfolded proteins and enables the study of intrinsically disordered regions.

David-Paul Minde, Manasa Ramakrishna, Kathryn S Lilley

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 43 citations in OpenAlex.

  1. A unified photosensitizer platform forbioRxiv : the preprint server for biology · 2026
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  10. Molecular Spatiomics by Proximity Labeling.Accounts of chemical research · 2022
    Article
  11. Review
  12. Article
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  14. Frontiers in molecular biosciences · 2022
    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 1 institution in 1 country.

David-Paul Minde *Department of Biochemistry, Cambridge Centre for Proteomics, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QR, UK. dpm43@cam.ac.uk.ORCID http://orcid.org/0000-0002-2985-622X
Manasa Ramakrishna *Medical Research Council Toxicology Unit, University of Cambridge, Lancaster Road, Leicester, LE1 9HN, UK.ORCID http://orcid.org/0000-0002-5736-8311
Kathryn S LilleyDepartment of Biochemistry, Cambridge Centre for Proteomics, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QR, UK. k.s.lilley@bioc.cam.ac.uk.ORCID http://orcid.org/0000-0003-0594-6543
University of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/N010493/1
6 · The paper itself

Abstract

Intrinsically Disordered Regions (IDRs) are enriched in disease-linked proteins known to have multiple post-translational modifications, but there is limited in vivo information about how locally unfolded protein regions contribute to biological functions. We reasoned that IDRs should be more accessible to targeted in vivo biotinylation than ordered protein regions, if they retain their flexibility in human cells. Indeed, we observed increased biotinylation density in predicted IDRs in several cellular compartments >20,000 biotin sites from four proximity proteomics studies. We show that in a biotin 'painting' time course experiment, biotinylation events in Escherichia coli ribosomes progress from unfolded and exposed regions at 10 s, to structured and less accessible regions after five minutes. We conclude that biotin proximity tagging favours sites of local disorder in proteins and suggest the possibility of using biotin painting as a method to gain unique insights into in vivo condition-dependent subcellular plasticity of proteins.

Indexed as

Protein Interaction Domains and MotifsProtein UnfoldingAmino Acid SequenceBiotinBiotinylationHumansIntrinsically Disordered ProteinsLysineModels, MolecularProtein BindingProtein ConformationProtein Processing, Post-TranslationalProtein TransportProteomicsRibosomesStructure-Activity RelationshipBiotinIntrinsically Disordered ProteinsLysineTyrosine

Identifiers

PMID31969649
PMCPMC6976632
OpenAlexW3002324816

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.