Evidence map›Paper›PMID 36368907›Full record

ArticleLife science alliance2023

Protein and RNA ADP-ribosylation detection is influenced by sample preparation and reagents used.

Lisa Weixler, Nonso Josephat Ikenga, Jim Voorneveld, Gülcan Aydin, Timo Mhr Bolte, Jeffrey Momoh, Mareike Bütepage, Alexandra Golzmann, Bernhard Lüscher, Dmitri V Filippov and 2 more

Open access · goldAbstract read
In one paragraph

Article in Life science alliance, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.2field-weighted citation impact, top 6% 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

21 citing papers in PubMed, 31 citations in OpenAlex.

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  14. Poly-ADP-ribosylation dynamics, signaling, and analysis.Environmental and molecular mutagenesis · 2024
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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

12 authors at 2 institutions in 2 countries.

Lisa WeixlerInstitute of Biochemistry and Molecular Biology, RWTH Aachen University, Aachen, Germany.ORCID 0000-0003-4453-017X
Nonso Josephat IkengaInstitute of Biochemistry and Molecular Biology, RWTH Aachen University, Aachen, Germany.ORCID 0000-0002-2206-7121
Jim VoorneveldLeiden Institute of Chemistry, Leiden University Department of Bioorganic Synthesis, Leiden, Netherlands.
Gülcan AydinInstitute of Biochemistry and Molecular Biology, RWTH Aachen University, Aachen, Germany.
Timo Mhr BolteInstitute of Biochemistry and Molecular Biology, RWTH Aachen University, Aachen, Germany.
Jeffrey MomohInstitute of Biochemistry and Molecular Biology, RWTH Aachen University, Aachen, Germany.
Mareike BütepageInstitute of Biochemistry and Molecular Biology, RWTH Aachen University, Aachen, Germany.
Alexandra GolzmannInstitute of Biochemistry and Molecular Biology, RWTH Aachen University, Aachen, Germany.
Bernhard LüscherInstitute of Biochemistry and Molecular Biology, RWTH Aachen University, Aachen, Germany.ORCID 0000-0002-9622-8709
Dmitri V FilippovLeiden Institute of Chemistry, Leiden University Department of Bioorganic Synthesis, Leiden, Netherlands.
Roko ŽajaInstitute of Biochemistry and Molecular Biology, RWTH Aachen University, Aachen, Germany rzaja@ukaachen.de kfeijs@ukaachen.de.ORCID 0000-0003-3944-0153
Karla Lh FeijsInstitute of Biochemistry and Molecular Biology, RWTH Aachen University, Aachen, Germany rzaja@ukaachen.de kfeijs@ukaachen.de.ORCID 0000-0002-8074-2180
RWTH Aachen University · DELeiden University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The modification of substrates with ADP-ribose (ADPr) is important in, for example, antiviral immunity and cancer. Recently, several reagents were developed to detect ADP-ribosylation; however, it is unknown whether they recognise ADPr, specific amino acid-ADPr linkages, or ADPr with the surrounding protein backbone. We first optimised methods to prepare extracts containing ADPr-proteins and observe that depending on the amino acid modified, the modification is heatlabile. We tested the reactivity of available reagents with diverse ADP-ribosylated protein and RNA substrates and observed that not all reagents are equally suited for all substrates. Next, we determined cross-reactivity with adenylylated RNA, AMPylated proteins, and metabolites, including NADH, which are detected by some reagents. Lastly, we analysed ADP-ribosylation using confocal microscopy, where depending on the fixation method, either mitochondrion, nucleus, or nucleolus is stained. This study allows future work dissecting the function of ADP-ribosylation in cells, both on protein and on RNA substrates, as we optimised sample preparation methods and have defined the reagents suitable for specific methods and substrates.

Indexed as

ADP-RibosylationRNAAdenosine Diphosphate RiboseAmino AcidsIndicators and ReagentsProteinsAdenosine Diphosphate RiboseAmino AcidsIndicators and ReagentsProteinsRNA

Identifiers

PMID36368907
PMCPMC9652768
OpenAlexW4308790721

What Socratic holds

Textmetadata
LicenceCC BY
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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.