Evidence map›Paper›PMID 33243935›Full record

ReviewMolecules and cells2020

Mechanisms of Macromolecular Interactions Mediated by Protein Intrinsic Disorder.

Sunghyun Hong, Sangmin Choi, Ryeonghyeon Kim, Junseock Koh

Open access · diamondAbstract readReview
In one paragraph

Review in Molecules and cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 25% of its field
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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
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  4. The Proteomic Analysis of Cancer-Related Alterations in the Human Unfoldome.International journal of molecular sciences · 2024
    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

4 authors at 1 institution in 1 country.

Sunghyun HongSchool of Biological Sciences, Seoul National University, Seoul 08826, Korea.ORCID https://orcid.org/0000-0003-4676-3313
Sangmin ChoiSchool of Biological Sciences, Seoul National University, Seoul 08826, Korea.ORCID https://orcid.org/0000-0002-8061-6336
Ryeonghyeon KimSchool of Biological Sciences, Seoul National University, Seoul 08826, Korea.ORCID https://orcid.org/0000-0003-4542-5339
Junseock KohSchool of Biological Sciences, Seoul National University, Seoul 08826, Korea.ORCID https://orcid.org/0000-0002-2920-2656
Seoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intrinsically disordered proteins or regions (IDPs or IDRs) are widespread in the eukaryotic proteome. Although lacking stable three-dimensional structures in the free forms, IDRs perform critical functions in various cellular processes. Accordingly, mutations and altered expression of IDRs are associated with many pathological conditions. Hence, it is of great importance to understand at the molecular level how IDRs interact with their binding partners. In particular, discovering the unique interaction features of IDRs originating from their dynamic nature may reveal uncharted regulatory mechanisms of specific biological processes. Here we discuss the mechanisms of the macromolecular interactions mediated by IDRs and present the relevant cellular processes including transcription, cell cycle progression, signaling, and nucleocytoplasmic transport. Of special interest is the multivalent binding nature of IDRs driving assembly of multicomponent macromolecular complexes. Integrating the previous theoretical and experimental investigations, we suggest that such IDR-driven multiprotein complexes can function as versatile allosteric switches to process diverse cellular signals. Finally, we discuss the future challenges and potential medical applications of the IDR research.

Indexed as

HumansIntrinsically Disordered ProteinsMacromolecular SubstancesSignal TransductionIntrinsically Disordered ProteinsMacromolecular Substancesallosterycoupled folding and bindingdynamic bindingintrinsically disordered proteins or regionsmacromolecular complexmultivalent binding

Identifiers

PMID33243935
PMCPMC7700844
OpenAlexW3107501523

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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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.