Evidence map›Paper›PMID 30698796›Full record

ArticleNucleic acids research2019

Structural and functional analysis of the nucleotide and DNA binding activities of the human PIF1 helicase.

Saba Dehghani-Tafti, Vladimir Levdikov, Alfred A Antson, Ben Bax, Cyril M Sanders

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

31 citing papers in PubMed, 43 citations in OpenAlex.

  1. Regulation of Pfh1 helicase activity by nucleic acid interactions and mitochondrial SSB.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  15. Role and Regulation of Pif1 Family Helicases at the Replication Fork.International journal of molecular sciences · 2022
    Review
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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 3 institutions in 1 country.

Saba Dehghani-TaftiDepartment of Oncology and Metabolism, Academic Unit of Molecular Oncology, University of Sheffield, Beech Hill Rd., Sheffield S10 2RX, UK.
Vladimir LevdikovYork Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, UK.
Alfred A AntsonYork Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, UK.
Ben BaxYork Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, UK.
Cyril M SandersDepartment of Oncology and Metabolism, Academic Unit of Molecular Oncology, University of Sheffield, Beech Hill Rd., Sheffield S10 2RX, UK.
University of Sheffield · GBUniversity of York · GBCardiff University · GB

Funding

Biotechnology and Biological Sciences Research Council BB/R001685/1Wellcome Trust 206377/Z/17/ZWellcome Trust WT098230Wellcome Trust WT101528Wellcome Trust WT206377
6 · The paper itself

Abstract

Pif1 is a multifunctional helicase and DNA processing enzyme that has roles in genome stability. The enzyme is conserved in eukaryotes and also found in some prokaryotes. The functions of human PIF1 (hPIF1) are also critical for survival of certain tumour cell lines during replication stress, making it an important target for cancer therapy. Crystal structures of hPIF1 presented here explore structural events along the chemical reaction coordinate of ATP hydrolysis at an unprecedented level of detail. The structures for the apo as well as the ground and transition states reveal conformational adjustments in defined protein segments that can trigger larger domain movements required for helicase action. Comparisons with the structures of yeast and bacterial Pif1 reveal a conserved ssDNA binding channel in hPIF1 that we show is critical for single-stranded DNA binding during unwinding, but not the binding of G quadruplex DNA. Mutational analysis suggests that while the ssDNA-binding channel is important for helicase activity, it is not used in DNA annealing. Structural differences, in particular in the DNA strand separation wedge region, highlight significant evolutionary divergence of the human PIF1 protein from bacterial and yeast orthologues.

Indexed as

Adenosine TriphosphateCrystallography, X-RayDNA-Binding ProteinsDNA HelicasesDNA, Single-StrandedGenomic InstabilityHumansHydrolysisNucleotidesProtein ConformationSaccharomyces cerevisiae ProteinsAdenosine TriphosphateDNA-Binding ProteinsDNA HelicasesDNA, Single-StrandedNucleotidesPIF1 protein, humanPIF1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID30698796
PMCPMC6451128
OpenAlexW2914556220

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.