Evidence map›Paper›PMID 27836835›Full record

ReviewCold Spring Harbor perspectives in biology2017

Cross-β Polymerization of Low Complexity Sequence Domains.

Masato Kato, Steven L McKnight

Abstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Phase separation of the oncogenic fusion protein EWS::FLI1 is modulated by its DNA-binding domain.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  10. The Impact of Space and Time on the Functional Output of the Genome.Cold Spring Harbor perspectives in biology · 2022
    Review
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  19. Altered Phase Separation and Cellular Impact inFrontiers in cellular neuroscience · 2021
    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

2 authors.

Masato KatoDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390-9152.
Steven L McKnightDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390-9152.

Funding

Reversible Polymerization of Low Complexity Polypeptide Sequences as a FrameworkU01GM107623 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MCKNIGHT, STEVEN L · 2014 to 2017
$2.0M
NIGMS NIH HHS U01 GM107623
6 · The paper itself

Abstract

Most transcription factors and RNA regulatory proteins encoded by eukaryotic genomes ranging from yeast to humans contain polypeptide domains variously described as intrinsically disordered, prion-like, or of low complexity (LC). These LC domains exist in an unfolded state when DNA and RNA regulatory proteins are studied in biochemical isolation from cells. Upon incubation in the purified state, many of these LC domains polymerize into homogeneous, labile amyloid-like fibers. Here, we consider several lines of evidence that may favor biologic utility for LC domain polymers.

Indexed as

ArtifactsHumansOpen Reading FramesPolymerizationPrionsTranscription FactorsPrionsTranscription Factors

Identifiers

PMID27836835
PMCPMC5334260

What OpenQuestion holds

Textmetadata
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.