Evidence map›Paper›PMID 18977144›Full record

ArticleBioorganic & medicinal chemistry2008

Poly(ADP-ribose) polymerase-1 activity facilitates the dissociation of nuclear proteins from platinum-modified DNA.

Evan R Guggenheim, Alison E Ondrus, Mohammad Movassaghi, Stephen J Lippard

Open access · greenAbstract read
In one paragraph

Article in Bioorganic & medicinal chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 48 citations in OpenAlex.

  1. Sequence-Specific Pharmacokinetic and Pharmacodynamic Phase I/Ib Study of Olaparib Tablets and Carboplatin in Women's Cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2017
    Trial
  2. Transcriptomics revealsOncotarget · 2022
    Article
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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

4 authors at 1 institution in 1 country.

Evan R GuggenheimDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Alison E Ondrus
Mohammad Movassaghi
Stephen J Lippard
Massachusetts Institute of Technology · US

Funding

Understanding and Improving Platinum Anticancer DrugsR01CA034992 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI YILMAZ, OMER · 1985 to 2018
$6.8M
CHEMISTRY AND BIOLOGY OF PLATINUM ANTICANCER DRUGSR37CA034992 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LIPPARD, STEPHEN J. · 1990 to 2008
$5.7M
Synthesis and Study of Complex Natural ProductsR01GM074825 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI MOVASSAGHI, MOHAMMAD · 2005 to 2019
$4.6M
NCI NIH HHS CA34992NCI NIH HHS R37 CA034992NIGMS NIH HHS GM074825
6 · The paper itself

Abstract

The affinity of the poly(ADP-ribose) polymerase-1 (PARP-1) for platinum-damaged DNA was first discovered during photo-cross-linking experiments using the photoactive compound Pt-BP6 [J. Am. Chem. Soc.2004, 126, 6536-6537], an analogue of the anticancer drug cis-diamminedichloroplatinum(II), cisplatin. Although PARP inhibitors sensitize cancer cells to cisplatin, there are conflicting reports in the literature about their efficacy. In order to improve our understanding of the mechanism by which PARP inhibition might potentiate the cell-killing ability of cisplatin, and to shed light on the source of the discrepancy among different laboratories, we have in the present study probed the influence of three PARP inhibitors in four types of cancer cells, cervical (HeLa), testicular (NTera2), pancreatic (BxPC3), and osteosarcoma (U2OS), on the results of Pt-BP6 photo-cross-linking experiments and cytotoxicity assays. We find that the activity of PARP proteins following exposure to platinum-modified DNA results in the dissociation of DNA-bound proteins. PARP inhibitors were able to sensitize some, but not all, of the cell lines to cisplatin. This cell line-dependence and the potential consequences of PARP-initiated protein removal from platinum-DNA lesions are discussed. Control experiments revealed that NTera2 cells are especially sensitive to PARP inhibition.

Indexed as

DNA DamagePoly(ADP-ribose) Polymerase InhibitorsAntineoplastic AgentsCell ExtractsCisplatinCross-Linking ReagentsDNAEnzyme InhibitorsHeLa CellsHeterocyclic Compounds, 4 or More RingsHumansNuclear ProteinsPoly(ADP-ribose) PolymerasesTumor Cells, CulturedAntineoplastic AgentsCell ExtractsCEP-6800CisplatinCross-Linking ReagentsDNAEnzyme InhibitorsHeterocyclic Compounds, 4 or More RingsNuclear ProteinsPoly(ADP-ribose) Polymerase InhibitorsPoly(ADP-ribose) Polymerases

Identifiers

PMID18977144
PMCPMC2662712
OpenAlexW2010168200

What OpenQuestion holds

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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 OpenQuestion graph.