Evidence map›Paper›PMID 20577208›Full record

ArticleNature2010

Structure and mechanism of human DNA polymerase eta.

Christian Biertümpfel, Ye Zhao, Yuji Kondo, Santiago Ramón-Maiques, Mark Gregory, Jae Young Lee, Chikahide Masutani, Alan R Lehmann, Fumio Hanaoka, Wei Yang

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 224 papers.

0numbers the graph read from it
0cells of the map it votes in
224citing papers in PubMed
13.4field-weighted citation impact, top 1% 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

224 citing papers in PubMed, 335 citations in OpenAlex.

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164 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 5 institutions in 5 countries.

Christian BiertümpfelLaboratory of Molecular Biology, NIDDK, NIH, 9000 Rockville Pike, Building 5, Room B103, Bethesda, Maryland 20892, USA.
Ye Zhao
Yuji Kondo
Santiago Ramón-Maiques
Mark Gregory
Jae Young Lee
Chikahide Masutani
Alan R Lehmann
Fumio Hanaoka
Wei Yang
Dongguk University · KROsaka University · JPUbe Frontier University · JPUniversity of Sussex · GBZhejiang University · CN

Funding

Structural and mechanistic studies of translesion DNA synthesisZIADK036146 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YANG, WEI · 2009 to 2025
$7.7M
Structural and mechanistic studies Of DNA mismatch repairZIADK036119 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YANG, WEI · 2009 to 2025
$6.6M
Structural and mechanistic studies of translesion DNA synthesisZ01DK036146 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YANG, WEI · 2007 to 2008
$601k
Intramural NIH HHS Z01 DK036146Intramural NIH HHS ZIA DK036146Medical Research Council G0501450
6 · The paper itself

Abstract

The variant form of the human syndrome xeroderma pigmentosum (XPV) is caused by a deficiency in DNA polymerase eta (Poleta), a DNA polymerase that enables replication through ultraviolet-induced pyrimidine dimers. Here we report high-resolution crystal structures of human Poleta at four consecutive steps during DNA synthesis through cis-syn cyclobutane thymine dimers. Poleta acts like a 'molecular splint' to stabilize damaged DNA in a normal B-form conformation. An enlarged active site accommodates the thymine dimer with excellent stereochemistry for two-metal ion catalysis. Two residues conserved among Poleta orthologues form specific hydrogen bonds with the lesion and the incoming nucleotide to assist translesion synthesis. On the basis of the structures, eight Poleta missense mutations causing XPV can be rationalized as undermining the molecular splint or perturbing the active-site alignment. The structures also provide an insight into the role of Poleta in replicating through D loop and DNA fragile sites.

Indexed as

Adenosine TriphosphateBase SequenceBiocatalysisCatalytic DomainCrystallography, X-RayDNADNA DamageDNA-Directed DNA PolymeraseHumansKineticsModels, MolecularMutation, MissensePyrimidine DimersStructure-Activity RelationshipXeroderma PigmentosumY-Family DNA PolymerasesAdenosine TriphosphateDNADNA-Directed DNA PolymerasePyrimidine DimersRad30 proteinY-Family DNA Polymerases

Identifiers

PMID20577208
PMCPMC2899710
OpenAlexW2042344660

What OpenQuestion holds

Textmetadata
LicenceTDM
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.