Evidence map›Paper›PMID 33542394›Full record

ArticleScientific reports2021

Intrinsic disorder in protein domains contributes to both organism complexity and clade-specific functions.

Chao Gao, Chong Ma, Huqiang Wang, Haolin Zhong, Jiayin Zang, Rugang Zhong, Fuchu He, Dong Yang

Abstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

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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

23 citing papers in PubMed.

  1. Article
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  10. Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Review
  13. Article
  14. Approaches for the Identification of Intrinsically Disordered Protein Domains.Methods in molecular biology (Clifton, N.J.) · 2023
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  15. Review
  16. 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

8 authors.

Chao Gao *State Key Laboratory of Proteomics, National Center for Protein Sciences (Beijing), Beijing Proteome Research Center, Beijing Institute of Lifeomics, 38 Science Park Road, Changping District, Beijing, 102206, China.
Chong Ma *State Key Laboratory of Proteomics, National Center for Protein Sciences (Beijing), Beijing Proteome Research Center, Beijing Institute of Lifeomics, 38 Science Park Road, Changping District, Beijing, 102206, China.
Huqiang WangState Key Laboratory of Proteomics, National Center for Protein Sciences (Beijing), Beijing Proteome Research Center, Beijing Institute of Lifeomics, 38 Science Park Road, Changping District, Beijing, 102206, China.
Haolin ZhongState Key Laboratory of Proteomics, National Center for Protein Sciences (Beijing), Beijing Proteome Research Center, Beijing Institute of Lifeomics, 38 Science Park Road, Changping District, Beijing, 102206, China.
Jiayin ZangState Key Laboratory of Proteomics, National Center for Protein Sciences (Beijing), Beijing Proteome Research Center, Beijing Institute of Lifeomics, 38 Science Park Road, Changping District, Beijing, 102206, China.
Rugang ZhongBeijing Key Laboratory of Environmental and Viral Oncology, College of Life Science and Bioengineering, Beijing University of Technology, Beijing, 100124, China.
Fuchu HeState Key Laboratory of Proteomics, National Center for Protein Sciences (Beijing), Beijing Proteome Research Center, Beijing Institute of Lifeomics, 38 Science Park Road, Changping District, Beijing, 102206, China. hefc@nic.bmi.ac.cn.
Dong Yang *State Key Laboratory of Proteomics, National Center for Protein Sciences (Beijing), Beijing Proteome Research Center, Beijing Institute of Lifeomics, 38 Science Park Road, Changping District, Beijing, 102206, China. yangdongbprc@163.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interestingly, some protein domains are intrinsically disordered (abbreviated as IDD), and the disorder degree of same domains may differ in different contexts. However, the evolutionary causes and biological significance of these phenomena are unclear. Here, we address these issues by genome-wide analyses of the evolutionary and functional features of IDDs in 1,870 species across the three superkingdoms. As the result, there is a significant positive correlation between the proportion of IDDs and organism complexity with some interesting exceptions. These phenomena may be due to the high disorder of clade-specific domains and the different disorder degrees of the domains shared in different clades. The functions of IDDs are clade-specific and the higher proportion of post-translational modification sites may contribute to their complex functions. Compared with metazoans, fungi have more IDDs with a consecutive disorder region but a low disorder ratio, which reflects their different functional requirements. As for disorder variation, it's greater for domains among different proteins than those within the same proteins. Some clade-specific 'no-variation' or 'high-variation' domains are involved in clade-specific functions. In sum, intrinsic domain disorder is related to both the organism complexity and clade-specific functions. These results deepen the understanding of the evolution and function of IDDs.

Indexed as

Protein ConformationAmino Acid SequenceAnimalsComputational BiologyEvolution, MolecularFungiGenomeIntrinsically Disordered ProteinsProtein DomainsProteinsIntrinsically Disordered ProteinsProteins

Identifiers

PMID33542394
PMCPMC7862400

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