Evidence map›Paper›PMID 25752799›Full record

ReviewProtein science : a publication of the Protein Society2015

How do disordered regions achieve comparable functions to structured domains?

Natasha S Latysheva, Tilman Flock, Robert J Weatheritt, Sreenivas Chavali, M Madan Babu

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
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  12. Generation of the configurational ensemble of an intrinsically disordered protein from unbiased molecular dynamics simulation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
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  14. Review
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  17. Control of mRNA decapping by autoinhibition.Nucleic acids research · 2018
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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

5 authors.

Natasha S LatyshevaMRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, United Kingdom.
Tilman FlockMRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, United Kingdom.
Robert J WeatherittMRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, United Kingdom.
Sreenivas ChavaliMRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, United Kingdom.
M Madan BabuMRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, United Kingdom.

Funding

Medical Research Council MC_U105185859
6 · The paper itself

Abstract

The traditional structure to function paradigm conceives of a protein's function as emerging from its structure. In recent years, it has been established that unstructured, intrinsically disordered regions (IDRs) in proteins are equally crucial elements for protein function, regulation and homeostasis. In this review, we provide a brief overview of how IDRs can perform similar functions to structured proteins, focusing especially on the formation of protein complexes and assemblies and the mediation of regulated conformational changes. In addition to highlighting instances of such functional equivalence, we explain how differences in the biological and physicochemical properties of IDRs allow them to expand the functional and regulatory repertoire of proteins. We also discuss studies that provide insights into how mutations within functional regions of IDRs can lead to human diseases.

Indexed as

Intrinsically Disordered ProteinsProtein Structure, TertiaryAnimalsHumansMiceModels, MolecularProtein ConformationProteomeIntrinsically Disordered ProteinsProteomedisordered proteinsdisorder-to-order transitionsIDRs in protein complexesmacromolecular protein assemblies

Identifiers

PMID25752799
PMCPMC4456105

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.