Evidence map›Paper›PMID 29625167›Full record

ReviewSeminars in cell & developmental biology2019

Idiosyncrasies of hnRNP A1-RNA recognition: Can binding mode influence function.

Jeffrey D Levengood, Blanton S Tolbert

Open access · greenAbstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

22 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Novel roles for RNA binding proteins squid, hephaesteus, and Hrb27C in Drosophila oogenesis.Developmental dynamics : an official publication of the American Association of Anatomists · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Effects of NFrontiers in oncology · 2022
    Review
  15. Article
  16. Article
  17. Article
  18. hnRNP A1B, a Splice Variant ofFrontiers in neuroscience · 2021
    Article
  19. Review
  20. Article
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 at 1 institution in 1 country.

Jeffrey D LevengoodDepartment of Chemistry, Case Western Reserve University, Cleveland, OH, United States.
Blanton S TolbertDepartment of Chemistry, Case Western Reserve University, Cleveland, OH, United States. Electronic address: bst18@case.edu.
Case Western Reserve University · US

Funding

The Center for HIV RNA Studies (CRNA)P50GM103297 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DAYIE, KWAKU · 2012 to 2016
$21.7M
The Center for HIV RNA Studies (CRNA)U54GM103297 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TELESNITSKY, ALICE · 2017 to 2018
$10.2M
Quantum Helium Recovery SystemR01GM126833 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI BREWER, GARY A., TOLBERT, BLANTON SMITH · 2018 to 2021
$1.9M
STRUCTURAL BIOPHYSICS OF HIV ALTERNATIVE SPLICINGR01GM101979 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI TOLBERT, BLANTON SMITH · 2012 to 2016
$1.6M
NIGMS NIH HHS P50 GM103297NIGMS NIH HHS R01 GM101979NIGMS NIH HHS R01 GM126833NIGMS NIH HHS U54 GM103297
6 · The paper itself

Abstract

The heterogeneous nuclear ribonucleoproteins (hnRNPs) are a diverse family of RNA binding proteins that function in most stages of RNA metabolism. The prototypical member, hnRNP A1, is composed of three major domains; tandem N-terminal RNA Recognition Motifs (RRMs) and a C-terminal mostly intrinsically disordered region. HnRNP A1 is broadly implicated in basic cellular RNA processing events such as splicing, stability, nuclear export and translation. Due to its ubiquity and abundance, hnRNP A1 is also frequently usurped to control viral gene expression. Deregulation of the RNA metabolism functions of hnRNP A1 in neuronal cells contributes to several neurodegenerative disorders. Because of these roles in human pathologies, the study of hnRNP A1 provides opportunities for the development of novel therapeutics, with disruption of its RNA binding capabilities being the most promising target. The functional diversity of hnRNP A1 is reflected in the complex nature by which it interacts with various RNA targets. Indeed, hnRNP A1 binds both structured and unstructured RNAs with binding affinities that span several magnitudes. Available structures of hnRNP A1-RNA complexes also suggest a degree of plasticity in molecular recognition. Given the reinvigoration in hnRNP A1, the goal of this review is to use the available structural biochemical developments as a framework to interpret its wide-range of RNA functions.

Indexed as

Binding SitesHeterogeneous Nuclear Ribonucleoprotein A1HumansRNASubstrate SpecificityHeterogeneous Nuclear Ribonucleoprotein A1RNAAlternative splicingHnRNP A1Intrinsically disordered protein (IDP)Protein-RNA interactionsRNA binding protein (RBP)RNA recognition motif (RRM)

Identifiers

PMID29625167
PMCPMC6177329
OpenAlexW2797890309

What OpenQuestion holds

Textmetadata
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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.