Evidence map›Paper›PMID 16738133›Full record

ArticleNucleic acids research2006

Protein complex compositions predicted by structural similarity.

Fred P Davis, Hannes Braberg, Min-Yi Shen, Ursula Pieper, Andrej Sali, M S Madhusudhan

Abstract readValidation Study
In one paragraph

Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. HOMCOS: an updated server to search and model complex 3D structures.Journal of structural and functional genomics · 2016
    Article
  7. Article
  8. Review
  9. Article
  10. Toward a "structural BLAST": using structural relationships to infer function.Protein science : a publication of the Protein Society · 2013
    Review
  11. Article
  12. Article
  13. Expanding the conformational selection paradigm in protein-ligand docking.Methods in molecular biology (Clifton, N.J.) · 2012
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Protein interface conservation across structure space.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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

6 authors.

Fred P DavisDepartment of Biopharmaceutical Sciences, California Institute for Quantitative Biomedical Research, University of California San Francisco, 1700 4th Street, Byers Hall, San Francisco, CA 94143-2552, USA.
Hannes Braberg
Min-Yi Shen
Ursula Pieper
Andrej Sali
M S Madhusudhan

Funding

NEW TOOLS FOR EXPLORING THE DYNAMIC INTERACTOME(RMI)U54RR022220 · NCRR · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2005 to 2011
$19.3M
X-RAY CRYSTALLOGRAPHYP01AI035707 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ROUSH, WILLIAM R · 1995 to 2008
$7.8M
NCRR NIH HHS U54 RR022220NIAID NIH HHS AI035707NIAID NIH HHS P01 AI035707
6 · The paper itself

Abstract

Proteins function through interactions with other molecules. Thus, the network of physical interactions among proteins is of great interest to both experimental and computational biologists. Here we present structure-based predictions of 3387 binary and 1234 higher order protein complexes in Saccharomyces cerevisiae involving 924 and 195 proteins, respectively. To generate candidate complexes, comparative models of individual proteins were built and combined together using complexes of known structure as templates. These candidate complexes were then assessed using a statistical potential, derived from binary domain interfaces in PIBASE (http://salilab.org/pibase). The statistical potential discriminated a benchmark set of 100 interface structures from a set of sequence-randomized negative examples with a false positive rate of 3% and a true positive rate of 97%. Moreover, the predicted complexes were also filtered using functional annotation and sub-cellular localization data. The ability of the method to select the correct binding mode among alternates is demonstrated for three camelid VHH domain-porcine alpha-amylase interactions. We also highlight the prediction of co-complexed domain superfamilies that are not present in template complexes. Through integration with MODBASE, the application of the method to proteomes that are less well characterized than that of S.cerevisiae will contribute to expansion of the structural and functional coverage of protein interaction space. The predicted complexes are deposited in MODBASE (http://salilab.org/modbase).

Indexed as

Algorithmsalpha-AmylasesComputational BiologyModels, MolecularMultiprotein ComplexesProtein BindingProtein Interaction MappingProtein Structure, TertiaryROC CurveSaccharomyces cerevisiae Proteinsalpha-AmylasesMultiprotein ComplexesSaccharomyces cerevisiae Proteins

Identifiers

PMID16738133
PMCPMC1474056

What OpenQuestion holds

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LicenceCC BY-NC
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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.