Evidence map›Paper›PMID 29424691›Full record

ArticleeLife2018

Pi-Pi contacts are an overlooked protein feature relevant to phase separation.

Robert McCoy Vernon, Paul Andrew Chong, Brian Tsang, Tae Hun Kim, Alaji Bah, Patrick Farber, Hong Lin, Julie Deborah Forman-Kay

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 495 papers.

0numbers the graph read from it
0cells of the map it votes in
495citing papers in PubMed
33.2field-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

495 citing papers in PubMed, 949 citations in OpenAlex.

  1. Article
  2. Engineering a protein homodimer from a heterodimer: A chimeric DBHS protein.Protein science : a publication of the Protein Society · 2026
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435 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

8 authors at 2 institutions in 1 country.

Robert McCoy VernonProgram in Molecular Medicine, Hospital for Sick Children, Toronto, Canada.
Paul Andrew ChongProgram in Molecular Medicine, Hospital for Sick Children, Toronto, Canada.
Brian TsangProgram in Molecular Medicine, Hospital for Sick Children, Toronto, Canada.
Tae Hun KimProgram in Molecular Medicine, Hospital for Sick Children, Toronto, Canada.
Alaji BahProgram in Molecular Medicine, Hospital for Sick Children, Toronto, Canada.
Patrick FarberProgram in Molecular Medicine, Hospital for Sick Children, Toronto, Canada.
Hong LinProgram in Molecular Medicine, Hospital for Sick Children, Toronto, Canada.
Julie Deborah Forman-KayProgram in Molecular Medicine, Hospital for Sick Children, Toronto, Canada.ORCID http://orcid.org/0000-0001-8265-972X
Hospital for Sick Children · CAUniversity of Toronto · CA

Funding

CIHR 114985
6 · The paper itself

Abstract

Protein phase separation is implicated in formation of membraneless organelles, signaling puncta and the nuclear pore. Multivalent interactions of modular binding domains and their target motifs can drive phase separation. However, forces promoting the more common phase separation of intrinsically disordered regions are less understood, with suggested roles for multivalent cation-pi, pi-pi, and charge interactions and the hydrophobic effect. Known phase-separating proteins are enriched in pi-orbital containing residues and thus we analyzed pi-interactions in folded proteins. We found that pi-pi interactions involving non-aromatic groups are widespread, underestimated by force-fields used in structure calculations and correlated with solvation and lack of regular secondary structure, properties associated with disordered regions. We present a phase separation predictive algorithm based on pi interaction frequency, highlighting proteins involved in biomaterials and RNA processing.

Indexed as

Protein FoldingHydrophobic and Hydrophilic InteractionsIntrinsically Disordered ProteinsOrganellesProtein BindingStatic ElectricityIntrinsically Disordered Proteinsbioinformaticscomputational biologyhumanmolecular biophysicspi interactionspredictionprotein interactionsprotein phase separationprotein structurestructural biologysystems biology

Identifiers

PMID29424691
PMCPMC5847340
OpenAlexW2786469974

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.