Evidence map›Paper›PMID 33616531›Full record

ArticleeLife2021

Identifying molecular features that are associated with biological function of intrinsically disordered protein regions.

Taraneh Zarin, Bob Strome, Gang Peng, Iva Pritišanac, Julie D Forman-Kay, Alan M Moses

Abstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed.

  1. Article
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  6. Review
  7. The Disordered Region of ASXL1 Acts as an Auto-Regulator Through Condensation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  14. Evolution of a fuzzy ribonucleoprotein complex in viral assembly.bioRxiv : the preprint server for biology · 2025
    Article
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  19. Evolutionarily conserved grammar rules viral factories of amoeba-infecting members of the hyperdiverseProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Article

3 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

6 authors.

Taraneh ZarinDepartment of Cell and Systems Biology, University of Toronto, Toronto, Canada.ORCID 0000-0003-1253-3843
Bob StromeDepartment of Cell and Systems Biology, University of Toronto, Toronto, Canada.
Gang PengDepartment of Cell and Systems Biology, University of Toronto, Toronto, Canada.
Iva PritišanacDepartment of Cell and Systems Biology, University of Toronto, Toronto, Canada.
Julie D Forman-KayProgram in Molecular Medicine, Hospital for Sick Children, Toronto, Canada.ORCID 0000-0001-8265-972X
Alan M MosesDepartment of Cell and Systems Biology, University of Toronto, Toronto, Canada.ORCID 0000-0003-3118-3121

Funding

CIHR FDN-148375CIHR PJT-148532
6 · The paper itself

Abstract

In previous work, we showed that intrinsically disordered regions (IDRs) of proteins contain sequence-distributed molecular features that are conserved over evolution, despite little sequence similarity that can be detected in alignments (Zarin et al., 2019). Here, we aim to use these molecular features to predict specific biological functions for individual IDRs and identify the molecular features within them that are associated with these functions. We find that the predictable functions are diverse. Examining the associated molecular features, we note some that are consistent with previous reports and identify others that were previously unknown. We experimentally confirm that elevated isoelectric point and hydrophobicity, features that are positively associated with mitochondrial localization, are necessary for mitochondrial targeting function. Remarkably, increasing isoelectric point in a synthetic IDR restores weak mitochondrial targeting. We believe feature analysis represents a new systematic approach to understand how biological functions of IDRs are specified by their protein sequences.

Indexed as

Amino Acid SequenceHydrophobic and Hydrophilic InteractionsIntrinsically Disordered ProteinsIsoelectric PointMitochondriaModels, StatisticalProteomeSaccharomyces cerevisiaeIntrinsically Disordered ProteinsProteomecell biologycomputational biologyevolutionary signaturesExpectation-MaximizationIDRsIRLSlassologistic regressionS. cerevisiaesystems biology

Identifiers

PMID33616531
PMCPMC7932695

What OpenQuestion holds

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LicenceCC BY
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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.