Evidence map›Paper›PMID 24458997›Full record

ArticleProtein science : a publication of the Protein Society2014

Mispairs with Watson-Crick base-pair geometry observed in ternary complexes of an RB69 DNA polymerase variant.

Shuangluo Xia, William H Konigsberg

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

17 citing papers in PubMed.

  1. Article
  2. Article
  3. The proofreading mechanism of the human leading-strand DNA polymerase ε holoenzyme.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  6. Structural and functional insight into mismatch extension by human DNA polymerase α.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Article
  9. Crystallographic evidence of Watson-Crick connectivity in the base pair of anionic adenine with thymine.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

2 authors.

Shuangluo XiaDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, 06520-8114.
William H Konigsberg

Funding

Molecular Biology and Structure of a DNA ReplicaseR01GM063276 · NIGMS · YALE UNIVERSITY · PI KONIGSBERG, WILLIAM H · 2001 to 2013
$4.2M
NIGMS NIH HHS GM063276-09
6 · The paper itself

Abstract

Recent structures of DNA polymerase complexes with dGMPCPP/dT and dCTP/dA mispairs at the insertion site have shown that they adopt Watson-Crick geometry in the presence of Mn(2+) indicating that the tautomeric or ionization state of the base has changed. To see whether the tautomeric or ionization state of base-pair could be affected by its microenvironment, we determined 10 structures of an RB69 DNA polymerase quadruple mutant with dG/dT or dT/dG mispairs at position n-1 to n-5 of the Primer/Template duplex. Different shapes of the mispairs, including Watson-Crick geometry, have been observed, strongly suggesting that the local environment of base-pairs plays an important role in their tautomeric or ionization states.

Indexed as

Base PairingBase Pair MismatchDNA-Directed DNA PolymeraseGenetic VariationModels, MolecularMolecular ConformationMutationProtein EngineeringViral Proteinsbacteriophage RB69 DNA polymeraseDNA-Directed DNA PolymeraseViral ProteinsRB69 DNA polymerasetautomerizationthymine-guanine mispairsWatson-Crick base-pairs

Identifiers

PMID24458997
PMCPMC3970900

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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.