Evidence map›Paper›PMID 26287166›Full record

ReviewInternational journal of molecular sciences2015

Disorder Prediction Methods, Their Applicability to Different Protein Targets and Their Usefulness for Guiding Experimental Studies.

Jennifer D Atkins, Samuel Y Boateng, Thomas Sorensen, Liam J McGuffin

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

42 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Prediction of Intrinsic Disorder Functions with DEPICTER2.Methods in molecular biology (Clifton, N.J.) · 2025
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  8. Review
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  10. Computational prediction of disordered binding regions.Computational and structural biotechnology journal · 2023
    Review
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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 2 institutions in 1 country.

Jennifer D AtkinsSchool of Biological Sciences, University of Reading, Whiteknights, Reading RG6 6AS, UK. j.atkins@pgr.reading.ac.uk.
Samuel Y BoatengSchool of Biological Sciences, University of Reading, Whiteknights, Reading RG6 6AS, UK. s.boateng@reading.ac.uk.
Thomas SorensenDiamond Light Source Ltd., Diamond House, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK. thomas.sorensen@diamond.ac.uk.
Liam J McGuffinSchool of Biological Sciences, University of Reading, Whiteknights, Reading RG6 6AS, UK. l.j.mcguffin@reading.ac.uk.
University of Reading · GBDiamond Light Source · GB

Funding

British Heart Foundation PG/10/64/28520
6 · The paper itself

Abstract

The role and function of a given protein is dependent on its structure. In recent years, however, numerous studies have highlighted the importance of unstructured, or disordered regions in governing a protein's function. Disordered proteins have been found to play important roles in pivotal cellular functions, such as DNA binding and signalling cascades. Studying proteins with extended disordered regions is often problematic as they can be challenging to express, purify and crystallise. This means that interpretable experimental data on protein disorder is hard to generate. As a result, predictive computational tools have been developed with the aim of predicting the level and location of disorder within a protein. Currently, over 60 prediction servers exist, utilizing different methods for classifying disorder and different training sets. Here we review several good performing, publicly available prediction methods, comparing their application and discussing how disorder prediction servers can be used to aid the experimental solution of protein structure. The use of disorder prediction methods allows us to adopt a more targeted approach to experimental studies by accurately identifying the boundaries of ordered protein domains so that they may be investigated separately, thereby increasing the likelihood of their successful experimental solution.

Indexed as

AnimalsComputational BiologyHumansIntrinsically Disordered ProteinsModels, MolecularProtein ConformationProtein FoldingSoftwareIntrinsically Disordered Proteinsdisorder prediction methodsintrinsic disorderstructural bioinformaticstypes of disorder

Identifiers

PMID26287166
PMCPMC4581285
OpenAlexW2165324573

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.