Evidence map›Paper›PMID 29805999›Full record

ReviewACS central science2018

Looking at the Disordered Proteins through the Computational Microscope.

Payel Das, Silvina Matysiak, Jeetain Mittal

Abstract readReview
In one paragraph

Review in ACS central science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
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  9. Multiscale Modeling of Protein-RNA Condensation in and Out of Equilibrium.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  10. Review
  11. Article
  12. Review
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  14. Review
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  18. Assessing the Role of Calmodulin's Linker Flexibility in Target Binding.International journal of molecular sciences · 2021
    Article
  19. Article
  20. Article
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.

Payel DasIBM Thomas J. Watson Research Center, Yorktown Heights, New York 10598, United States.
Silvina MatysiakFischell Department of Bioengineering, University of Maryland, College Park, Maryland 20742, United States.
Jeetain MittalDepartment of Chemical and Biomolecular Engineering, Lehigh University, Bethlehem, Pennsylvania 18015, United States.

Funding

Turning off the molecular switch for pathological self-assembly of FUSR01GM118530 · NIGMS · BROWN UNIVERSITY · PI FAWZI, NICOLAS LUX · 2016 to 2020
$1.6M
NIGMS NIH HHS R01 GM118530
6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) have attracted wide interest over the past decade due to their surprising prevalence in the proteome and versatile roles in cell physiology and pathology. A large selection of IDPs has been identified as potential targets for therapeutic intervention. Characterizing the structure-function relationship of disordered proteins is therefore an essential but daunting task, as these proteins can adapt transient structure, necessitating a new paradigm for connecting structural disorder to function. Molecular simulation has emerged as a natural complement to experiments for atomic-level characterizations and mechanistic investigations of this intriguing class of proteins. The diverse range of length and time scales involved in IDP function requires performing simulations at multiple levels of resolution. In this Outlook, we focus on summarizing available simulation methods, along with a few interesting example applications. We also provide an outlook on how these simulation methods can be further improved in order to provide a more accurate description of IDP structure, binding, and assembly.

Identifiers

PMID29805999
PMCPMC5968442

What OpenQuestion holds

Textmetadata
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.