Evidence map›Paper›PMID 27693355›Full record

ArticleCell2016

Intrinsically Disordered Proteins Drive Emergence and Inheritance of Biological Traits.

Sohini Chakrabortee, James S Byers, Sandra Jones, David M Garcia, Bhupinder Bhullar, Amelia Chang, Richard She, Laura Lee, Brayon Fremin, Susan Lindquist and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.

0numbers the graph read from it
0cells of the map it votes in
120citing papers in PubMed
12.9field-weighted citation impact, top 1% 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

120 citing papers in PubMed, 207 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Protein structure shapes natural genetic variation andbioRxiv : the preprint server for biology · 2025
    Article
  8. When life began with fully acquired heredity: a non-standard hypothesis of evolutionary origins.Theory in biosciences = Theorie in den Biowissenschaften · 2025
    Article
  9. Review
  10. Evolution of cross-tolerance to metals in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025
    Review
  16. Article
  17. Prion-like Properties of Short Isoforms of Human Chromatin Modifier PHC3.International journal of molecular sciences · 2025
    Article
  18. Review
  19. Article
  20. Article

60 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

11 authors at 3 institutions in 1 country.

Sohini ChakraborteeWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
James S ByersDepartment of Developmental Biology, Stanford University, Stanford, CA 94305, USA.
Sandra JonesWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
David M GarciaDepartment of Chemical and Systems Biology, Stanford University, Stanford, CA 94305, USA.
Bhupinder BhullarWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA.
Amelia ChangDepartment of Biology, Stanford University, Stanford, CA 94305, USA.
Richard SheDepartment of Chemical and Systems Biology, Stanford University, Stanford, CA 94305, USA.
Laura LeeDepartment of Biology, Stanford University, Stanford, CA 94305, USA.
Brayon FreminDepartment of Chemical and Systems Biology, Stanford University, Stanford, CA 94305, USA.
Susan LindquistWhitehead Institute for Biomedical Research, Cambridge, MA 02142, USA; HHMI and Department of Biology, MIT, Cambridge, MA 02139, USA. Electronic address: lindquist_admin@wi.mit.edu.
Daniel F JaroszDepartment of Developmental Biology, Stanford University, Stanford, CA 94305, USA; Department of Chemical and Systems Biology, Stanford University, Stanford, CA 94305, USA. Electronic address: jarosz@stanford.edu.
Stanford University · USWhitehead Institute for Biomedical Research · USIIT@MIT · US

Funding

INSTITUTIONAL TRAINING GRANT IN GENOME SCIENCET32HG000044 · NHGRI · STANFORD UNIVERSITY · PI MICHAEL P. SNYDER · 1995 to 2026
$32.2M
GENETICS TRAINING PROGRAM FOR PHD CANDIDATEST32GM007790 · NIGMS · STANFORD UNIVERSITY · PI BRUNET, ANNE, KINGSLEY, DAVID M · 1985 to 2020
$12.8M
Protein-based Molecular Memories in Gene Regulation, Disease, and DevelopmentDP2GM119140 · NIGMS · STANFORD UNIVERSITY · PI JAROSZ, DANIEL · 2015 to 2015
$2.4M
Quantitative analysis of the evolving genotype-to-phenotype mapR00GM098600 · NIGMS · STANFORD UNIVERSITY · PI JAROSZ, DANIEL · 2013 to 2015
$728k
Heritable protein aggregation affecting genome preservation and RNA regulationF32GM109680 · NIGMS · STANFORD UNIVERSITY · PI GARCIA, DAVID M. · 2014 to 2016
$111k
HHMINHGRI NIH HHS T32 HG000044NIGMS NIH HHS DP2 GM119140NIGMS NIH HHS F32 GM109680NIGMS NIH HHS R00 GM098600NIGMS NIH HHS T32 GM007790
6 · The paper itself

Abstract

Prions are a paradigm-shifting mechanism of inheritance in which phenotypes are encoded by self-templating protein conformations rather than nucleic acids. Here, we examine the breadth of protein-based inheritance across the yeast proteome by assessing the ability of nearly every open reading frame (ORF; ∼5,300 ORFs) to induce heritable traits. Transient overexpression of nearly 50 proteins created traits that remained heritable long after their expression returned to normal. These traits were beneficial, had prion-like patterns of inheritance, were common in wild yeasts, and could be transmitted to naive cells with protein alone. Most inducing proteins were not known prions and did not form amyloid. Instead, they are highly enriched in nucleic acid binding proteins with large intrinsically disordered domains that have been widely conserved across evolution. Thus, our data establish a common type of protein-based inheritance through which intrinsically disordered proteins can drive the emergence of new traits and adaptive opportunities.

Indexed as

Quantitative Trait, HeritableAmyloidEvolution, MolecularHeat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsIntrinsically Disordered ProteinsOpen Reading FramesPrionsProteomeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmyloidHeat-Shock ProteinsHsP104 protein, S cerevisiaeHSP70 Heat-Shock ProteinsHSP82 protein, S cerevisiaeHSP90 Heat-Shock ProteinsIntrinsically Disordered ProteinsPrionsProteomeSaccharomyces cerevisiae Proteinsepigeneticsintrinsic disorderprionsprotein folding

Identifiers

PMID27693355
PMCPMC5066306
OpenAlexW2524788592

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.