Evidence map›Paper›PMID 30733475›Full record

ArticleScientific reports2019

Evolutionary Approach of Intrinsically Disordered CIP/KIP Proteins.

Muhamad Fahmi, Masahiro Ito

Abstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

17 citing papers in PubMed.

  1. Article
  2. Exploring Disordered Regions of Human Spliceosome Proteins.The journal of physical chemistry letters · 2026
    Article
  3. Article
  4. Review
  5. Intrinsically Disordered Proteins: An Overview.International journal of molecular sciences · 2022
    Review
  6. Article
  7. ATP regulates RNA-driven cold inducible RNA binding protein phase separation.Protein science : a publication of the Protein Society · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Regulation of p27Biomolecules · 2020
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. In Silico Study of Rett Syndrome Treatment-Related Genes,International journal of molecular sciences · 2019
    Article
  17. 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

2 authors.

Muhamad FahmiAdvanced Life Sciences Program, Graduate School of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga, 525-8577, Japan.ORCID 0000-0003-4359-1405
Masahiro ItoAdvanced Life Sciences Program, Graduate School of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga, 525-8577, Japan. maito@sk.ritsumei.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mammalian CIP/KIP family proteins are intrinsically disordered proteins (IDPs) that can regulate various cellular processes. However, many reports have shown that IDPs generally evolve more rapidly than ordered proteins. Here, to elucidate the functional adaptability of CIP/KIP proteins in vertebrate, we analysed the rates of evolution in relation to their structural and sequence properties and predicted the post-translational modification based on the sequence data. The results showed that CIP/KIP proteins generally could maintain their function through evolution in the vertebrate. Basically, the disordered region that acts as a flexible linker or spacer has a conserved propensity for structural disorder and a persistent, fast rate of amino acid substitution, which could result in a significantly faster rate of evolution compared to the ordered proteins. Describing the pattern of structural order-disorder evolution, this study may give an insight into the well-known characteristics of IDPs in the evolution of CIP/KIP proteins.

Indexed as

Amino Acid SequenceCalcium-Binding ProteinsCyclin-Dependent Kinase Inhibitor ProteinsEvolution, MolecularHumansIntrinsically Disordered ProteinsModels, MolecularPhosphorylationPhylogenyProtein ConformationStructure-Activity RelationshipCalcium-Binding ProteinsCIB1 protein, humanCyclin-Dependent Kinase Inhibitor ProteinsIntrinsically Disordered Proteins

Identifiers

PMID30733475
PMCPMC6367352

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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.