Evidence map›Paper›PMID 28597295›Full record

ReviewCellular and molecular life sciences : CMLS2017

Evolution of intrinsic disorder in eukaryotic proteins.

Joseph B Ahrens, Janelle Nunez-Castilla, Jessica Siltberg-Liberles

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. SIRT1 Exon 2-Encoded IDR Gates CREB-Dependent Transcriptional Timing During Fasting.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
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  9. Review
  10. Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024
    Article
  11. Multisubstrate specificity shaped the complex evolution of the aminotransferase family across the tree of life.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Intrinsically Disordered Proteins: An Overview.International journal of molecular sciences · 2022
    Review
  19. Article
  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

3 authors.

Joseph B AhrensDepartment of Biological Sciences, Biomolecular Sciences Institute, Florida International University, 11200 SW 8th St, Miami, FL, 33199, USA.
Janelle Nunez-CastillaDepartment of Biological Sciences, Biomolecular Sciences Institute, Florida International University, 11200 SW 8th St, Miami, FL, 33199, USA.
Jessica Siltberg-LiberlesDepartment of Biological Sciences, Biomolecular Sciences Institute, Florida International University, 11200 SW 8th St, Miami, FL, 33199, USA. jliberle@fiu.edu.

Funding

MBRS RESEARCH INITIATIVE FOR SCIENTIFIC ENHANCEMENTR25GM061347 · NIGMS · FLORIDA INTERNATIONAL UNIVERSITY · PI LICKLITER, ROBERT E · 2000 to 2016
$14.7M
NIGMS NIH HHS R25 GM061347
6 · The paper itself

Abstract

Conformational flexibility conferred though regions of intrinsic structural disorder allows proteins to behave as dynamic molecules. While it is well-known that intrinsically disordered regions can undergo disorder-to-order transitions in real-time as part of their function, we also are beginning to learn more about the dynamics of disorder-to-order transitions along evolutionary time-scales. Intrinsically disordered regions endow proteins with functional promiscuity, which is further enhanced by the ability of some of these regions to undergo real-time disorder-to-order transitions. Disorder content affects gene retention after whole genome duplication, but it is not necessarily conserved. Altered patterns of disorder resulting from evolutionary disorder-to-order transitions indicate that disorder evolves to modify function through refining stability, regulation, and interactions. Here, we review the evolution of intrinsically disordered regions in eukaryotic proteins. We discuss the interplay between secondary structure and disorder on evolutionary time-scales, the importance of disorder for eukaryotic proteome expansion and functional divergence, and the evolutionary dynamics of disorder.

Indexed as

Evolution, MolecularBiodiversityEukaryotaIntrinsically Disordered ProteinsProtein Structure, TertiaryProteomeIntrinsically Disordered ProteinsProteomeDisorder-to-order transitionDosageEvolutionary dynamicsFunctional divergenceGene duplicationIntrinsic disorderNeutralityProtein evolution

Identifiers

PMID28597295
PMCPMC11107722

What OpenQuestion holds

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Registered trials

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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.