Evidence map›Paper›PMID 32525675›Full record

ArticleThe journal of physical chemistry. B2020

A Unified De Novo Approach for Predicting the Structures of Ordered and Disordered Proteins.

John J Ferrie, E James Petersson

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. HumanResearch square · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Recent Advances in NMR Protein Structure Prediction with ROSETTA.International journal of molecular sciences · 2023
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

2 authors.

John J FerrieDepartment of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, United States.
E James PeterssonDepartment of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, United States.ORCID 0000-0003-3854-9210

Funding

Studying Aggregation in Neurodegenerative Disease Using Synthetic ProteinsR01NS103873 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI Ernest James Petersson · 2019 to 2026
$2.1M
Semi-synthetic a-Synuclein for Tracking Aggregation and Cell-to-Cell TransmissionR01NS081033 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI PETERSSON, ERNEST JAMES · 2012 to 2015
$1.3M
Semi-synthetic a-Synuclein for Tracking Aggregation and Cell-to-Cell TransmissionR56NS081033 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI PETERSSON, ERNEST JAMES · 2017 to 2017
$357k
NINDS NIH HHS R01 NS081033NINDS NIH HHS R01 NS103873NINDS NIH HHS R56 NS081033
6 · The paper itself

Abstract

As recognition of the abundance and relevance of intrinsically disordered proteins (IDPs) continues to grow, demand increases for methods that can rapidly predict the conformational ensembles populated by these proteins. To date, IDP simulations have largely been dominated by molecular dynamics (MD) simulations, which require significant compute times and/or complex hardware. Recent developments in MD have afforded methods capable of simulating both ordered and disordered proteins, yet to date, accurate fold prediction from a sequence has been dominated by Monte Carlo (MC)-based methods such as Rosetta. To overcome the limitations of current approaches in IDP simulation using Rosetta while maintaining its utility for modeling folded domains, we developed PyRosetta-based algorithms that allow for the accurate de novo prediction of proteins across all degrees of foldedness along with structural ensembles of disordered proteins. Our simulations have accuracy comparable to state-of-the-art MD with vastly reduced computational demands.

Indexed as

Intrinsically Disordered ProteinsAlgorithmsMolecular Dynamics SimulationMonte Carlo MethodProtein ConformationIntrinsically Disordered Proteins

Identifiers

PMID32525675
PMCPMC7725001

What OpenQuestion holds

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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.