Evidence map›Paper›PMID 31048495›Full record

ArticleRNA (New York, N.Y.)2019

C9orf72 and triplet repeat disorder RNAs: G-quadruplex formation, binding to PRC2 and implications for disease mechanisms.

Xueyin Wang, Karen J Goodrich, Erin G Conlon, Jianchao Gao, Annette H Erbse, James L Manley, Thomas R Cech

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2019. 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
2.1field-weighted citation impact, top 12% 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

34 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
  3. Microprotein Regulates G-quadruplex Driven RNA Aggregation.bioRxiv : the preprint server for biology · 2026
    Article
  4. TDP-43 controls RNA structure through high affinity lattice interactions.bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. TDP-43 Epigenetic Facets and Their Neurodegenerative Implications.International journal of molecular sciences · 2023
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
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

7 authors at 3 institutions in 1 country.

Xueyin Wang *Department of Biochemistry, University of Colorado Boulder, Boulder, Colorado 80309, USA.
Karen J Goodrich *Department of Biochemistry, University of Colorado Boulder, Boulder, Colorado 80309, USA.
Erin G Conlon *Department of Biological Sciences, Columbia University, New York, New York 10027, USA.
Jianchao GaoDepartment of Biological Sciences, Columbia University, New York, New York 10027, USA.
Annette H ErbseDepartment of Biochemistry, University of Colorado Boulder, Boulder, Colorado 80309, USA.
James L ManleyDepartment of Biological Sciences, Columbia University, New York, New York 10027, USA.
Thomas R CechDepartment of Biochemistry, University of Colorado Boulder, Boulder, Colorado 80309, USA.
Columbia University · USHoward Hughes Medical Institute · USUniversity of Colorado Boulder · US

Funding

Regulation of RNA processing: Mechanisms and ConsequencesR35GM118136 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI James L. Manley · 2016 to 2026
$8.9M
Howard Hughes Medical InstituteNIGMS NIH HHS R35 GM118136
6 · The paper itself

Abstract

Some neurological disorders, including amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), fragile X syndrome, Huntington's disease, myotonic dystrophy, and various ataxias, can be caused by expansions of short nucleic acid sequence repeats in specific genes. A possible disease mechanism involves the transcribed repeat RNA binding an RNA-binding protein (RBP), resulting in its sequestration and thus dysfunction. Polycomb repressive complex 2 (PRC2), the histone methyltransferase that deposits the H3K27me3 mark of epigenetically silenced chromatin, binds G-rich RNAs and has especially high affinity for G-quadruplex (G-Q) structures. Here, we find that PRC2 target genes are derepressed and the RNA binding subunit EZH2 largely insoluble in postmortem brain samples from ALS/FTD patients with

Indexed as

Trinucleotide RepeatsAmyotrophic Lateral SclerosisAutopsyC9orf72 ProteinCircular DichroismEnhancer of Zeste Homolog 2 ProteinEpigenesis, GeneticFrontotemporal DementiaG-QuadruplexesHumansPolycomb Repressive Complex 2SolubilityC9orf72 ProteinEnhancer of Zeste Homolog 2 ProteinEZH2 protein, humanPolycomb Repressive Complex 2ALSepigeneticsG-quadruplexneurological disordersRNA–protein interactions

Identifiers

PMID31048495
PMCPMC6633194
OpenAlexW2943624515

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.