Evidence map›Paper›PMID 35934473›Full record

ArticleMethods in enzymology2022

Biochemical methods to monitor loading and activation of hexameric helicases.

Amy J Fernandez, James M Berger

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods in enzymology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Amy J FernandezDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, MD, United States.
James M BergerDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, MD, United States. Electronic address: jmberger@jhmi.edu.

Funding

PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
Program of Molecular BiophysicsT32GM135131 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Karen G. Fleming · 2020 to 2026
$5.4M
Mechanistic Studies of Replication Initiation in ProkaryotesR37GM071747 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI James M. Berger · 2017 to 2026
$4.4M
NIGMS NIH HHS R37 GM071747NIGMS NIH HHS T32 GM008403NIGMS NIH HHS T32 GM135131
6 · The paper itself

Abstract

Ring-shaped hexameric helicases are an essential class of enzymes that unwind duplex nucleic acids to support a variety of cellular processes. Because of their critical roles in cells, hexameric helicase dysfunction has been linked to DNA damage and genomic instability. Biochemical characterization of hexameric helicase activity and regulation in vitro is necessary for understanding enzyme function and aiding drug discovery efforts. In this chapter, we describe protocols for characterizing mechanisms of helicase loading, activation, and unwinding using the model replicative hexameric DnaB helicase and its cognate DnaC loading factor from E. coli.

Indexed as

Escherichia coliEscherichia coli ProteinsBacterial ProteinsDnaB HelicasesDNA HelicasesDNA ReplicationBacterial ProteinsDnaB HelicasesDNA HelicasesEscherichia coli ProteinsDNA unwindingHelicase loadingHexameric helicase

Identifiers

PMID35934473
PMCPMC13166123

What OpenQuestion holds

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Registered trials

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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.