Evidence map›Paper›PMID 31744872›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Branched unwinding mechanism of the Pif1 family of DNA helicases.

Saurabh P Singh, Andrea Soranno, Melanie A Sparks, Roberto Galletto

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

14 citing papers in PubMed, 21 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
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. "Helicase" Activity promoted through dynamic interactions between a ssDNA translocase and a diffusing SSB protein.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Role and Regulation of Pif1 Family Helicases at the Replication Fork.International journal of molecular sciences · 2022
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Lysine acetylation regulates the activity of nuclear Pif1.The Journal of biological chemistry · 2020
    Article
  13. Review
  14. Article
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

4 authors at 2 institutions in 1 country.

Saurabh P SinghDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110.
Andrea SorannoDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110.
Melanie A SparksDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110.
Roberto GallettoDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110 galletto@wustl.edu.
Washington University in St. Louis · USLiving Systems (United States) · US

Funding

HELICASE ACTIVITY AND ITS ROLE IN TELOMERE AND TELOMERASE REGULATIONR01GM098509 · NIGMS · WASHINGTON UNIVERSITY · PI GALLETTO, ROBERTO · 2011 to 2020
$2.7M
Conformational and functional analysis of Apolipoprotein ER01AG062837 · NIA · WASHINGTON UNIVERSITY · PI SORANNO, ANDREA · 2019 to 2023
$2.2M
NIA NIH HHS R01 AG062837NIGMS NIH HHS R01 GM098509
6 · The paper itself

Abstract

Members of the Pif1 family of helicases function in multiple pathways that involve DNA synthesis: DNA replication across G-quadruplexes; break-induced replication; and processing of long flaps during Okazaki fragment maturation. Furthermore, Pif1 increases strand-displacement DNA synthesis by DNA polymerase δ and allows DNA replication across arrays of proteins tightly bound to DNA. This is a surprising feat since DNA rewinding or annealing activities limit the amount of single-stranded DNA product that Pif1 can generate, leading to an apparently poorly processive helicase. In this work, using single-molecule Förster resonance energy transfer approaches, we show that 2 members of the Pif1 family of helicases, Pif1 from

Indexed as

Adenosine TriphosphateDNADNA HelicasesFluorescence Resonance Energy TransferKineticsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsAdenosine TriphosphateDNADNA HelicasesPfh1 protein, S pombePIF1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsDNA replicationDNA unwindinghelicasesingle molecule

Identifiers

PMID31744872
PMCPMC6900637
OpenAlexW2989742364

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.