Evidence map›Paper›PMID 20399180›Full record

ArticleStructure (London, England : 1993)2010

Dynameomics: a comprehensive database of protein dynamics.

Marc W van der Kamp, R Dustin Schaeffer, Amanda L Jonsson, Alexander D Scouras, Andrew M Simms, Rudesh D Toofanny, Noah C Benson, Peter C Anderson, Eric D Merkley, Steven Rysavy and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

76 citing papers in PubMed, 158 citations in OpenAlex.

  1. AI-Physics-Experiment Trinity for Integrated Protein Dynamics Modeling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  2. Fast prediction of protein flexibility.Bioinformatics (Oxford, England) · 2026
    Article
  3. Article
  4. A FAIR-Compliant Management Solution for Molecular Simulation Trajectories.Journal of chemical information and modeling · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Building protein structure-specific rotamer libraries.Bioinformatics (Oxford, England) · 2023
    Article
  15. Article
  16. Review
  17. Article
  18. Pre-exascale HPC approaches for molecular dynamics simulations. Covid-19 research: A use case.Wiley interdisciplinary reviews. Computational molecular science · 2022
    Article
  19. Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021
    Review
  20. Article

16 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 1 institution in 1 country.

Marc W van der KampDepartment of Bioengineering, University of Washington, Seattle, WA 98195-5013, USA.
R Dustin Schaeffer
Amanda L Jonsson
Alexander D Scouras
Andrew M Simms
Rudesh D Toofanny
Noah C Benson
Peter C Anderson
Eric D Merkley
Steven Rysavy
Dennis Bromley
David A C Beck
Valerie Daggett
University of Washington · US

Funding

University of Washington Biomedical Informatics and Data Science Research Training ProgramT15LM007442 · NLM · UNIVERSITY OF WASHINGTON · PI JOHN H. GENNARI, Andrea L. Hartzler · 2002 to 2026
$19.6M
MOLECULAR DYNAMICS SIMULATIONS OF PROTEIN UNFOLDINGR01GM050789 · NIGMS · UNIVERSITY OF WASHINGTON · PI DAGGETT, VALERIE D · 2000 to 2014
$3.9M
MOLECULAR DYNAMICS SIMULATIONS OF PROTEIN UNFOLDINGR29GM050789 · NIGMS · UNIVERSITY OF WASHINGTON · PI DAGGETT, VALERIE D · 1995 to 1999
–
NIGMS NIH HHS GM50789NIGMS NIH HHS R01 GM050789NIGMS NIH HHS R29 GM050789NLM NIH HHS T15 LM007442NLM NIH HHS TG 3 T15 LM007442-04S1
6 · The paper itself

Abstract

The dynamic behavior of proteins is important for an understanding of their function and folding. We have performed molecular dynamics simulations of the native state and unfolding pathways of over 2000 protein/peptide systems (approximately 11,000 independent simulations) representing the majority of folds in globular proteins. These data are stored and organized using an innovative database approach, which can be mined to obtain both general and specific information about the dynamics and folding/unfolding of proteins, relevant subsets thereof, and individual proteins. Here we describe the project in general terms and the type of information contained in the database. Then we provide examples of mining the database for information relevant to protein folding, structure building, the effect of single-nucleotide polymorphisms, and drug design. The native state simulation data and corresponding analyses for the 100 most populated metafolds, together with related resources, are publicly accessible through http://www.dynameomics.org.

Indexed as

AlgorithmsAnimalsComputational BiologyDatabases, ProteinHumansModels, MolecularMolecular ConformationPolymorphism, Single NucleotideProtein DenaturationProtein FoldingProteinsProteomicsProteins

Identifiers

PMID20399180
PMCPMC2892689
OpenAlexW1984493861

What OpenQuestion holds

Textmetadata
LicenceTDM
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.