Evidence map›Paper›PMID 25139910›Full record

ArticleMolecular & cellular proteomics : MCP2014

Determining protein complex structures based on a Bayesian model of in vivo Förster resonance energy transfer (FRET) data.

Massimiliano Bonomi, Riccardo Pellarin, Seung Joong Kim, Daniel Russel, Bryan A Sundin, Michael Riffle, Daniel Jaschob, Richard Ramsden, Trisha N Davis, Eric G D Muller and 1 more

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. 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. Tutorial on integrative spatiotemporal modeling by integrative modeling platform.Protein science : a publication of the Protein Society · 2025
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  13. Integrative structure modeling with the Integrative Modeling Platform.Protein science : a publication of the Protein Society · 2018
    Article
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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

11 authors.

Massimiliano BonomiFrom the ‡Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California, San Francisco, California 94158; §Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom; sali@salilab.org mb2006@cam.ac.uk emuller@u.washington.edu.
Riccardo PellarinFrom the ‡Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California, San Francisco, California 94158;
Seung Joong KimFrom the ‡Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California, San Francisco, California 94158;
Daniel RusselFrom the ‡Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California, San Francisco, California 94158;
Bryan A Sundin‖Department of Biochemistry, University of Washington, Seattle, Washington 98195.
Michael Riffle‖Department of Biochemistry, University of Washington, Seattle, Washington 98195.
Daniel Jaschob‖Department of Biochemistry, University of Washington, Seattle, Washington 98195.
Richard Ramsden‖Department of Biochemistry, University of Washington, Seattle, Washington 98195.
Trisha N Davis‖Department of Biochemistry, University of Washington, Seattle, Washington 98195.
Eric G D Muller‖Department of Biochemistry, University of Washington, Seattle, Washington 98195 sali@salilab.org mb2006@cam.ac.uk emuller@u.washington.edu.
Andrej SaliFrom the ‡Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, University of California, San Francisco, California 94158; sali@salilab.org mb2006@cam.ac.uk emuller@u.washington.edu.

Funding

VIRAL DEGENERATIVE DEMENTING DISEASE IN AGING (SUPP)P01AG002132 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 1985 to 2024
$51.7M
TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
NEW TOOLS FOR EXPLORING THE DYNAMIC INTERACTOME(RMI)U54RR022220 · NCRR · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2005 to 2011
$19.3M
TR&D Project 4. The Imaging Stage: Multiscale Spatiotemporal Modeling of Macromolecular Systems in Cellular NeighborhoodsP41GM109824 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2014 to 2023
$18.8M
IMP: Software for Hybrid Determination of Macromolecular Assembly StructuresR01GM083960 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2008 to 2024
$5.2M
NCRR NIH HHS U54 RR022220NIA NIH HHS P01 AG002132NIGMS NIH HHS P41 GM103533NIGMS NIH HHS P41 GM109824NIGMS NIH HHS R01 GM083960
6 · The paper itself

Abstract

The use of in vivo Förster resonance energy transfer (FRET) data to determine the molecular architecture of a protein complex in living cells is challenging due to data sparseness, sample heterogeneity, signal contributions from multiple donors and acceptors, unequal fluorophore brightness, photobleaching, flexibility of the linker connecting the fluorophore to the tagged protein, and spectral cross-talk. We addressed these challenges by using a Bayesian approach that produces the posterior probability of a model, given the input data. The posterior probability is defined as a function of the dependence of our FRET metric FRETR on a structure (forward model), a model of noise in the data, as well as prior information about the structure, relative populations of distinct states in the sample, forward model parameters, and data noise. The forward model was validated against kinetic Monte Carlo simulations and in vivo experimental data collected on nine systems of known structure. In addition, our Bayesian approach was validated by a benchmark of 16 protein complexes of known structure. Given the structures of each subunit of the complexes, models were computed from synthetic FRETR data with a distance root-mean-squared deviation error of 14 to 17 Å. The approach is implemented in the open-source Integrative Modeling Platform, allowing us to determine macromolecular structures through a combination of in vivo FRETR data and data from other sources, such as electron microscopy and chemical cross-linking.

Indexed as

Fluorescence Resonance Energy TransferAlgorithmsBacterial ProteinsBayes TheoremComputer SimulationLuminescent ProteinsMolecular StructureMonte Carlo MethodProtein Interaction MappingProtein Structure, QuaternarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsBacterial ProteinsLuminescent ProteinsSaccharomyces cerevisiae Proteinsyellow fluorescent protein, Bacteria

Identifiers

PMID25139910
PMCPMC4223474

What OpenQuestion holds

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Registered trials

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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.