Evidence map›Paper›PMID 28003858›Full record

ReviewBiophysical reviews2016

Analytical methods for structural ensembles and dynamics of intrinsically disordered proteins.

Marieke Schor, Antonia S J S Mey, Cait E MacPhee

Abstract readReview
In one paragraph

Review in Biophysical reviews, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Monitoring α-synuclein aggregation.Neurobiology of disease · 2023
    Review
  5. The Two-Step Clustering Approach for Metastable States Learning.International journal of molecular sciences · 2021
    Review
  6. Article
  7. Article
  8. Review
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

3 authors.

Marieke SchorSchool of Physics and Astronomy, University of Edinburgh, Edinburgh, UK.
Antonia S J S MeySchool of Chemistry, University of Edinburgh, Edinburgh, UK.
Cait E MacPheeSchool of Physics and Astronomy, University of Edinburgh, Edinburgh, UK. cait.macphee@ed.ac.uk.ORCID http://orcid.org/0000-0001-8313-8387

Funding

European Research Council 336289
6 · The paper itself

Abstract

Intrinsically disordered proteins, proteins that do not have a well-defined three-dimensional structure, make up a significant proportion of our proteome and are particularly prevalent in signaling and regulation. Although their importance has been realized for two decades, there is a lack of high-resolution experimental data. Molecular dynamics simulations have been crucial in reaching our current understanding of the dynamical structural ensemble sampled by intrinsically disordered proteins. In this review, we discuss enhanced sampling simulation methods that are particularly suitable to characterize the structural ensemble, along with examples of applications and limitations. The dynamics within the ensemble can be rigorously analyzed using Markov state models. We discuss recent developments that make Markov state modeling a viable approach for studying intrinsically disordered proteins. Finally, we briefly discuss challenges and future directions when applying molecular dynamics simulations to study intrinsically disordered proteins.

Indexed as

Conformational ensemblesEnhanced sampling simulationsIntrinsically disordered proteinsMarkov state modeling

Identifiers

PMID28003858
PMCPMC5135723

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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.