Evidence map›Paper›PMID 36430530›Full record

ReviewInternational journal of molecular sciences2022

Intrinsically Disordered Proteins: An Overview.

Rakesh Trivedi, Hampapathalu Adimurthy Nagarajaram

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.

0numbers the graph read from it
0cells of the map it votes in
118citing 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

118 citing papers in PubMed.

  1. Article
  2. Exchange dynamics and kinetic control of gene regulation complexes.Nature reviews. Molecular cell biology · 2026
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58 more citing papers are in PubMed but not listed here.

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.

Rakesh TrivediDepartment of Translational Molecular Pathology, The University of Texas MD Anderson Cancer Center, Houston, TX 77054, USA.ORCID 0000-0003-4835-1814
Hampapathalu Adimurthy NagarajaramLaboratory of Computational Biology, Department of Systems and Computational Biology, School of Life Sciences, University of Hyderabad, Hyderabad 500046, Telangana, India.ORCID 0000-0001-8568-0620

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many proteins and protein segments cannot attain a single stable three-dimensional structure under physiological conditions; instead, they adopt multiple interconverting conformational states. Such intrinsically disordered proteins or protein segments are highly abundant across proteomes, and are involved in various effector functions. This review focuses on different aspects of disordered proteins and disordered protein regions, which form the basis of the so-called "Disorder-function paradigm" of proteins. Additionally, various experimental approaches and computational tools used for characterizing disordered regions in proteins are discussed. Finally, the role of disordered proteins in diseases and their utility as potential drug targets are explored.

Indexed as

Intrinsically Disordered ProteinsProteomeIntrinsically Disordered ProteinsProteomeintrinsically disordered proteinsintrinsically disordered regionsprotein functionprotein structure

Identifiers

PMID36430530
PMCPMC9693201

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.