Evidence map›Paper›PMID 32282108›Full record

ArticleChembiochem : a European journal of chemical biology2020

Olaparib-Based Photoaffinity Probes for PARP-1 Detection in Living Cells.

Jim Voorneveld, Bogdan I Florea, Thomas Bakkum, Rafal J Mendowicz, Miriam S van der Veer, Berend Gagestein, Sander I van Kasteren, Mario van der Stelt, Herman S Overkleeft, Dmitri V Filippov

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Proteome-Wide Profiling of Olaparib Interactors Using a Biotinylated Photoaffinity Probe.Chembiochem : a European journal of chemical biology · 2025
    Article
  2. Article
  3. Review
  4. Olaparib-Based Photoaffinity Probes for PARP-1 Detection in Living Cells.Chembiochem : a European journal of chemical biology · 2020
    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

10 authors at 1 institution in 1 country.

Jim VoorneveldBio-organic Synthesis Group Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC, Leiden, The Netherlands.
Bogdan I FloreaBio-organic Synthesis Group Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC, Leiden, The Netherlands.
Thomas BakkumBio-organic Synthesis Group Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC, Leiden, The Netherlands.
Rafal J MendowiczBio-organic Synthesis Group Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC, Leiden, The Netherlands.
Miriam S van der VeerBio-organic Synthesis Group Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC, Leiden, The Netherlands.
Berend GagesteinBio-organic Synthesis Group Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC, Leiden, The Netherlands.
Sander I van KasterenBio-organic Synthesis Group Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC, Leiden, The Netherlands.
Mario van der SteltBio-organic Synthesis Group Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC, Leiden, The Netherlands.
Herman S OverkleeftBio-organic Synthesis Group Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC, Leiden, The Netherlands.
Dmitri V FilippovBio-organic Synthesis Group Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC, Leiden, The Netherlands.ORCID 0000-0002-6978-7425
Leiden University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The poly-ADP-ribose polymerase (PARP) is a protein from the family of ADP-ribosyltransferases that catalyzes polyadenosine diphosphate ribose (ADPR) formation in order to attract the DNA repair machinery to sites of DNA damage. The inhibition of PARP activity by olaparib can cause cell death, which is of clinical relevance in some tumor types. This demonstrates that quantification of PARP activity in the context of living cells is of great importance. In this work, we present the design, synthesis and biological evaluation of photo-activatable affinity probes inspired by the olaparib molecule that are equipped with a diazirine for covalent attachment upon activation by UV light and a ligation handle for the addition of a reporter group of choice. SDS-PAGE, western blotting and label-free LC-MS/MS quantification analysis show that the probes target the PARP-1 protein and are selectively outcompeted by olaparib; this suggests that they bind in the same enzymatic pocket. Proteomics data are available via ProteomeXchange with identifier PXD018661.

Indexed as

Cells, CulturedHumansMolecular StructurePhotoaffinity LabelsPhotochemical ProcessesPhthalazinesPiperazinesPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) Polymerase InhibitorsUltraviolet RaysolaparibPARP1 protein, humanPhotoaffinity LabelsPhthalazinesPiperazinesPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) Polymerase Inhibitorsbioorthogonal chemistrychemical proteomicsolaparibPARP-1photoaffinity probes

Identifiers

PMID32282108
PMCPMC7496120
OpenAlexW3015849070

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.