Evidence map›Paper›PMID 30239884›Full record

ArticleNucleic acids research2018

The signature motif of the Saccharomyces cerevisiae Pif1 DNA helicase is essential in vivo for mitochondrial and nuclear functions and in vitro for ATPase activity.

Carly L Geronimo, Saurabh P Singh, Roberto Galletto, Virginia A Zakian

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

13 citing papers in PubMed, 13 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. G-quadruplexes as a source of vulnerability in BRCA2Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  7. Role and Regulation of Pif1 Family Helicases at the Replication Fork.International journal of molecular sciences · 2022
    Review
  8. Article
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  10. 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

4 authors at 2 institutions in 1 country.

Carly L GeronimoDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544-1014, USA.
Saurabh P SinghDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO 63110, USA.
Roberto GallettoDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO 63110, USA.
Virginia A ZakianDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544-1014, USA.
Princeton University · USWashington University in St. Louis · US

Funding

Telomere maintenance and replication fork progression in yeast and human cellsR35GM118279 · NIGMS · PRINCETON UNIVERSITY · PI ZAKIAN, VIRGINIA A. · 2016 to 2020
$4.5M
HELICASE ACTIVITY AND ITS ROLE IN TELOMERE AND TELOMERASE REGULATIONR01GM098509 · NIGMS · WASHINGTON UNIVERSITY · PI GALLETTO, ROBERTO · 2011 to 2020
$2.7M
National Science Foundation DGE1656466NIGMS NIH HHS R01 GM098509NIGMS NIH HHS R35 GM118279
6 · The paper itself

Abstract

Pif1 family DNA helicases are conserved from bacteria to humans and have critical and diverse functions in vivo that promote genome integrity. Pif1 family helicases share a 23 amino acid region, called the Pif1 signature motif (SM) that is unique to this family. To determine the importance of the SM, we did mutational and functional analysis of the SM from the Saccharomyces cerevisiae Pif1 (ScPif1). The mutations deleted portions of the SM, made one or multiple single amino acid changes in the SM, replaced the SM with its counterpart from a bacterial Pif1 family helicase and substituted an α-helical domain from another helicase for the part of the SM that forms an α helix. Mutants were tested for maintenance of mitochondrial DNA, inhibition of telomerase at telomeres and double strand breaks, and promotion of Okazaki fragment maturation. Although certain single amino acid changes in the SM can be tolerated, the presence and sequence of the ScPif1 SM were essential for all tested in vivo functions. Consistent with the in vivo analyses, in vitro studies showed that the presence and sequence of the ScPif1 SM were critical for ATPase activity but not substrate binding.

Indexed as

Adenosine TriphosphatasesAmino Acid MotifsCell NucleusDNA HelicasesDNA ReplicationHumansMitochondriaProtein StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionTelomeraseTelomereAdenosine TriphosphatasesDNA HelicasesPIF1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTelomerase

Identifiers

PMID30239884
PMCPMC6144861
OpenAlexW2883778967

What OpenQuestion holds

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LicenceCC BY-NC
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.