Evidence map›Paper›PMID 15647511›Full record

ArticleNucleic acids research2005

Deficiency in 3'-phosphoglycolate processing in human cells with a hereditary mutation in tyrosyl-DNA phosphodiesterase (TDP1).

Tong Zhou, Jae Wan Lee, Haritha Tatavarthi, James R Lupski, Kristoffer Valerie, Lawrence F Povirk

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
4.0field-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

78 citing papers in PubMed, 150 citations in OpenAlex.

  1. Review
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  6. Critical DNA damaging pathways in tumorigenesis.Seminars in cancer biology · 2022
    Review
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18 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Tong ZhouDepartment of Pharmacology and Toxicology, Virginia Commonwealth University, Richmond, VA 23298-0230, USA.
Jae Wan Lee
Haritha Tatavarthi
James R Lupski
Kristoffer Valerie
Lawrence F Povirk
Virginia Commonwealth University · US

Funding

Repair of DNA double-strand breaks with damaged endsR01CA040615 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI POVIRK, LAWRENCE F · 1985 to 2014
$3.2M
Tyrosyl-DNA phosphodiesterase and oxidative DNA damageR01AG023783 · NIA · VIRGINIA COMMONWEALTH UNIVERSITY · PI POVIRK, LAWRENCE F · 2004 to 2008
$1.3M
NCI NIH HHS CA40615NCI NIH HHS R01 CA040615NIA NIH HHS AG023783NIA NIH HHS R01 AG023783
6 · The paper itself

Abstract

Tyrosyl-DNA phosphodiesterase (TDP1) is a DNA repair enzyme that removes peptide fragments linked through tyrosine to the 3' end of DNA, and can also remove 3'-phosphoglycolates (PGs) formed by free radical-mediated DNA cleavage. To assess whether TDP1 is primarily responsible for PG removal during in vitro end joining of DNA double-strand breaks (DSBs), whole-cell extracts were prepared from lymphoblastoid cells derived either from spinocerebellar ataxia with axonal neuropathy (SCAN1) patients, who have an inactivating mutation in the active site of TDP1, or from closely matched normal controls. Whereas extracts from normal cells catalyzed conversion of 3'-PG termini, both on single-strand oligomers and on 3' overhangs of DSBs, to 3'-phosphate termini, extracts of SCAN1 cells did not process either substrate. Addition of recombinant TDP1 to SCAN1 extracts restored 3'-PG removal, allowing subsequent gap filling on the aligned DSB ends. Two of three SCAN1 lines examined were slightly more radiosensitive than normal cells, but only for fractionated radiation in plateau phase. The results suggest that the TDP1 mutation in SCAN1 abolishes the 3'-PG processing activity of the enzyme, and that there are no other enzymes in cell extracts capable of processing protruding 3'-PG termini. However, the lack of severe radiosensitivity suggests that there must be alternative, TDP1-independent pathways for repair of 3'-PG DSBs.

Indexed as

DNA DamageMutationCell LineGlycolatesHumansPhosphoric Diester HydrolasesPhosphorylationRadiation, IonizingSpinocerebellar AtaxiasGlycolatesphosphoglycolatePhosphoric Diester HydrolasesTDP1 protein, humantyrosyl-DNA phosphodiesterase

Identifiers

PMID15647511
PMCPMC546157
OpenAlexW2026233878

What OpenQuestion holds

Textmetadata
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.