Evidence map›Paper›PMID 20827723›Full record

ArticleProteins2010

Determining macromolecular assembly structures by molecular docking and fitting into an electron density map.

Keren Lasker, Andrej Sali, Haim J Wolfson

Abstract read
In one paragraph

Article in Proteins, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Mapping the native organization of the yeast nuclear pore complex using nuclear radial intensity measurements.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  5. Article
  6. Review
  7. Article
  8. Stoichiometry and compositional plasticity of the yeast nuclear pore complex revealed by quantitative fluorescence microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Integrative structure modeling with the Integrative Modeling Platform.Protein science : a publication of the Protein Society · 2018
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Challenges in structural approaches to cell modeling.Journal of molecular biology · 2016
    Review
  15. The Evolving Contribution of Mass Spectrometry to Integrative Structural Biology.Journal of the American Society for Mass Spectrometry · 2016
    Review
  16. Article
  17. Article
  18. Article
  19. Journal of applied crystallography · 2015
    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.

Keren LaskerRaymond and Beverly Sackler Faculty of Exact Sciences, Blavatnik School of Computer Science, Tel Aviv University, Tel Aviv 69978, Israel.
Andrej Sali
Haim J Wolfson

Funding

Center for Protein Folding Machinery (RMI)PN2EY016525 · NEI · BAYLOR COLLEGE OF MEDICINE · PI CHIU, WAH · 2005 to 2015
$33.6M
NEW TOOLS FOR EXPLORING THE DYNAMIC INTERACTOME(RMI)U54RR022220 · NCRR · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2005 to 2011
$19.3M
IMP: Software for Hybrid Determination of Macromolecular Assembly StructuresR01GM083960 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2008 to 2024
$5.2M
Protein Modeling by Satisfaction of Spatial RestraintsR01GM054762 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2001 to 2008
$2.1M
NCRR NIH HHS U54 RR022220NEI NIH HHS PN2 EY016525NIGMS NIH HHS R01 GM054762NIGMS NIH HHS R01 GM083960NIGMS NIH HHS R01 GM54762
6 · The paper itself

Abstract

Structural models of macromolecular assemblies are instrumental for gaining a mechanistic understanding of cellular processes. Determining these structures is a major challenge for experimental techniques, such as X-ray crystallography, NMR spectroscopy and electron microscopy (EM). Thus, computational modeling techniques, including molecular docking, are required. The development of most molecular docking methods has so far been focused on modeling of binary complexes. We have recently introduced the MultiFit method for modeling the structure of a multisubunit complex by simultaneously optimizing the fit of the model into an EM density map of the entire complex and the shape complementarity between interacting subunits. Here, we report algorithmic advances of the MultiFit method that result in an efficient and accurate assembly of the input subunits into their density map. The successful predictions and the increasing number of complexes being characterized by EM suggests that the CAPRI challenge could be extended to include docking-based modeling of macromolecular assemblies guided by EM.

Indexed as

AlgorithmsMolecular Dynamics SimulationBacterial ProteinsComputational BiologyElectronsInternetMolecular ConformationMultiprotein ComplexesPrincipal Component AnalysisProtein BindingBacterial ProteinsMultiprotein Complexes

Identifiers

PMID20827723
PMCPMC2952722

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.