Evidence map›Paper›PMID 32656996›Full record

ReviewWiley interdisciplinary reviews. RNA2021

The multifaceted role of PARP1 in RNA biogenesis.

Rebekah Eleazer, Yvonne N Fondufe-Mittendorf

Open access · hybridAbstract readReview
In one paragraph

Review in Wiley interdisciplinary reviews. RNA, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.7field-weighted citation impact, top 8% 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

36 citing papers in PubMed, 49 citations in OpenAlex.

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  20. PARP1 and OGG1 in Medicated Patients With Depression and the Response to ECT.The international journal of neuropsychopharmacology · 2023
    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.

Rebekah EleazerDepartment of Molecular and Cellular Biochemistry and Markey Cancer Center, University of Kentucky, Lexington, Kentucky, USA.
Yvonne N Fondufe-MittendorfDepartment of Molecular and Cellular Biochemistry and Markey Cancer Center, University of Kentucky, Lexington, Kentucky, USA.ORCID 0000-0002-2551-9920
University of Kentucky · US

Funding

University of Kentucky Markey Cancer Center Support Grant ECIA SupplementP30CA177558 · NCI · UNIVERSITY OF KENTUCKY · PI Jennifer F Rogers · 2013 to 2026
$38.3M
Molecular mechanisms of iAs-mediated carcinogenesis through the lens of histone H2B variantsR01ES034253 · NIEHS · VAN ANDEL RESEARCH INSTITUTE · PI Yvonne Nsokika Fondufe-Mittendorf · 2022 to 2026
$3.3M
Molecular Underpinnings in the Establishment of an Oncogenic 3D Genome inResponse to Environmental Arsenic ExposureR01ES031846 · NIEHS · VAN ANDEL RESEARCH INSTITUTE · PI FONDUFE-MITTENDORF, YVONNE NSOKIKA · 2020 to 2024
$2.7M
The role of chromatin structural and epigenetic changes in arsenic-induced gene expressionR01ES024478 · NIEHS · UNIVERSITY OF KENTUCKY · PI FONDUFE-MITTENDORF, YVONNE NSOKIKA · 2015 to 2019
$1.8M
NCI NIH HHS P30 CA177558NIEHS NIH HHS R01 ES024478NIEHS NIH HHS R01 ES031846NIEHS NIH HHS R01 ES034253
6 · The paper itself

Abstract

Poly(ADP-ribose) polymerases (PARPs) are abundant nuclear proteins that synthesize ADP ribose polymers (pADPr) and catalyze the addition of (p)ADPr to target biomolecules. PARP1, the most abundant and well-studied PARP, is a multifunctional enzyme that participates in numerous critical cellular processes. A considerable amount of PARP research has focused on PARP1's role in DNA damage. However, an increasing body of evidence outlines more routine roles for PARP and PARylation in nearly every step of RNA biogenesis and metabolism. PARP1's involvement in these RNA processes is pleiotropic and has been ascribed to PARP1's unique flexible domain structures. PARP1 domains are modular self-arranged enabling it to recognize structurally diverse substrates and to act simultaneously through multiple discrete mechanisms. These mechanisms include direct PARP1-protein binding, PARP1-nucleic acid binding, covalent PARylation of target molecules, covalent autoPARylation, and induction of noncovalent interactions with PAR molecules. A combination of these mechanisms has been implicated in PARP1's context-specific regulation of RNA biogenesis and metabolism. We examine the mechanisms of PARP1 regulation in transcription initiation, elongation and termination, co-transcriptional splicing, RNA export, and post-transcriptional RNA processing. Finally, we consider promising new investigative avenues for PARP1 involvement in these processes with an emphasis on PARP1 regulation of subcellular condensates. This article is categorized under: RNA Processing > Splicing Regulation/Alternative Splicing.

Indexed as

Poly(ADP-ribose) PolymerasesRNANuclear ProteinsRNA SplicingNuclear ProteinsPoly(ADP-ribose) PolymerasesRNAchromatinPARP1RNA biogenesissplicing

Identifiers

PMID32656996
PMCPMC7856298
OpenAlexW3042068060

What Socratic 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 Socratic graph.