Evidence map›Paper›PMID 11972036›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Human XPA and RPA DNA repair proteins participate in specific recognition of triplex-induced helical distortions.

Karen M Vasquez, Jesper Christensen, Lei Li, Rick A Finch, Peter M Glazer

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

59 citing papers in PubMed, 112 citations in OpenAlex.

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  14. Nanotechnology for delivery of peptide nucleic acids (PNAs).Journal of controlled release : official journal of the Controlled Release Society · 2016
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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

5 authors at 1 institution in 1 country.

Karen M VasquezDepartment of Carcinogenesis, University of Texas M. D. Anderson Cancer Center, Science Park-Research Division, Park Road 1-C, Smithville, TX 78957, USA. kvasquez@sprd1.mdacc.tmc.edu
Jesper Christensen
Lei Li
Rick A Finch
Peter M Glazer
The University of Texas MD Anderson Cancer Center · US

Funding

REPAIR OF GENOME DESTABILIZING DNA STRUCTURESR01CA093729 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Karen M Vasquez · 2002 to 2026
$8.2M
Molecular Genetics of Parvoviral DNA ReplicationR37AI026109 · NIAID · YALE UNIVERSITY · PI TATTERSALL, PETER J. · 2009 to 2018
$5.4M
MOLECULAR GENETICS OF PARVOVIRAL DNA REPLICATIONR01AI026109 · NIAID · YALE UNIVERSITY · PI TATTERSALL, PETER J. · 1988 to 2009
$3.0M
TARGETED MUTAGENESIS OF DNA VIA TRIPLE HELIX FORMATIONR01CA064186 · NCI · YALE UNIVERSITY · PI GLAZER, PETER M · 1995 to 2008
$2.6M
UNUSUAL DNA STRUCTURES AND GENOMIC INSTABILITYF32CA075723 · NCI · YALE UNIVERSITY · PI VASQUEZ, KAREN M · 1997 to 2000
$27k
NCI NIH HHS CA64186NCI NIH HHS CA75723NCI NIH HHS CA93729NCI NIH HHS F32 CA075723NCI NIH HHS R01 CA064186NCI NIH HHS R01 CA093729NIAID NIH HHS AI26109NIAID NIH HHS R01 AI026109NIAID NIH HHS R37 AI026109
6 · The paper itself

Abstract

Nucleotide excision repair (NER) plays a central role in maintaining genomic integrity by detecting and repairing a wide variety of DNA lesions. Xeroderma pigmentosum complementation group A protein (XPA) is an essential component of the repair machinery, and it is thought to be involved in the initial step as a DNA damage recognition and/or confirmation factor. Human replication protein A (RPA) and XPA have been reported to interact to form a DNA damage recognition complex with greater specificity for damaged DNA than XPA alone. The mechanism by which these two proteins recognize such a wide array of structures resulting from different types of DNA damage is not known. One possibility is that they recognize a common feature of the lesions, such as distortions of the helical backbone. We have tested this idea by determining whether human XPA and RPA proteins can recognize the helical distortions induced by a DNA triple helix, a noncanonical DNA structure that has been shown to induce DNA repair, mutagenesis, and recombination. We measured binding of XPA and RPA, together or separately, to substrates containing triplexes with three, two, or no strands covalently linked by psoralen conjugation and photoaddition. We found that RPA alone recognizes all covalent triplex structures, but also forms multivalent nonspecific DNA aggregates at higher concentrations. XPA by itself does not recognize the substrates, but it binds them in the presence of RPA. Addition of XPA decreases the nonspecific DNA aggregate formation. These results support the hypothesis that the NER machinery is targeted to helical distortions and demonstrate that RPA can recognize damaged DNA even without XPA.

Indexed as

DNADNA DamageBase SequenceBinding SitesDNA-Binding ProteinsDNA PrimersDNA RepairDose-Response Relationship, DrugEnzyme-Linked Immunosorbent AssayFicusinHumansIntronsMolecular Sequence DataMutagenesis, Site-DirectedProtein BindingRecombination, GeneticDNADNA-Binding ProteinsDNA PrimersFicusinReplication Protein ARPA1 protein, humantriplex DNAXeroderma Pigmentosum Group A ProteinXPA protein, human

Identifiers

PMID11972036
PMCPMC122865
OpenAlexW1984694497

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.