Evidence map›Paper›PMID 27387657›Full record

ArticleJournal of the American Chemical Society2016

Finding Our Way in the Dark Proteome.

Asmit Bhowmick, David H Brookes, Shane R Yost, H Jane Dyson, Julie D Forman-Kay, Daniel Gunter, Martin Head-Gordon, Gregory L Hura, Vijay S Pande, David E Wemmer and 2 more

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing 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

71 citing papers in PubMed.

  1. Review
  2. Shining light on the dark proteome with unstructural biology.Current research in structural biology · 2026
    Article
  3. Article
  4. Accurate conformational ensembles of intrinsically disordered proteins using reweighting based on NMR chemical shifts.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Prediction of Disordered Linkers Using APOD.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. Article

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

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

12 authors.

Asmit Bhowmick
David H Brookes
Shane R Yost
H Jane DysonDepartment of Integrative Structural and Computational Biology, Scripps Research Institute , La Jolla, California 92037, United States.
Julie D Forman-KayMolecular Structure and Function Program, Hospital for Sick Children , Toronto, Ontario M5G 0A4, Canada.
Daniel Gunter
Martin Head-Gordon
Gregory L Hura
Vijay S PandeDepartment of Chemistry, Stanford University , Stanford, California 94305, United States.
David E Wemmer
Peter E WrightDepartment of Biochemistry, University of Toronto , Toronto, Ontario M5S 1A8, Canada.
Teresa Head-Gordon

Funding

Structural basis for CBP/p300 transcriptional regulationR01CA096865 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI WRIGHT, PETER EDWIN · 2002 to 2016
$6.2M
Interactions between Hsp90, Co-chaperones and Client ProteinsR01GM113251 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DYSON, HELEN JANE · 2015 to 2018
$1.5M
High Accuracy Computational Methods for Biomolecular Nuclear Magnetic Resonance SpectroscopyU01GM121667 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HEAD-GORDON, MARTIN PAUL, HEAD-GORDON, TERESA L. · 2017 to 2020
$1.3M
NCI NIH HHS R01 CA096865NIGMS NIH HHS R01 GM113251NIGMS NIH HHS U01 GM121667
6 · The paper itself

Abstract

The traditional structure-function paradigm has provided significant insights for well-folded proteins in which structures can be easily and rapidly revealed by X-ray crystallography beamlines. However, approximately one-third of the human proteome is comprised of intrinsically disordered proteins and regions (IDPs/IDRs) that do not adopt a dominant well-folded structure, and therefore remain "unseen" by traditional structural biology methods. This Perspective considers the challenges raised by the "Dark Proteome", in which determining the diverse conformational substates of IDPs in their free states, in encounter complexes of bound states, and in complexes retaining significant disorder requires an unprecedented level of integration of multiple and complementary solution-based experiments that are analyzed with state-of-the art molecular simulation, Bayesian probabilistic models, and high-throughput computation. We envision how these diverse experimental and computational tools can work together through formation of a "computational beamline" that will allow key functional features to be identified in IDP structural ensembles.

Indexed as

Computational BiologyProteomeBayes TheoremChromatography, GelCrystallography, X-RayGenome, HumanHumansIntrinsically Disordered ProteinsKineticsMagnetic Resonance SpectroscopyMolecular Dynamics SimulationProbabilityProtein ConformationProtein FoldingProteomicsSoftwareIntrinsically Disordered ProteinsProteome

Identifiers

PMID27387657
PMCPMC5051545

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.