Evidence map›Paper›PMID 24931273›Full record

ArticleBioorganic & medicinal chemistry2014

Chemical modifications of DNA for study of helicase mechanisms.

Kevin D Raney

Open access · bronzeAbstract read
In one paragraph

Article in Bioorganic & medicinal chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
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

1 author at 1 institution in 1 country.

Kevin D RaneyDepartment of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, 4301 W. Markham St., Slot 516, Little Rock, AR 72205, USA. Electronic address: raneykevind@uams.edu.
University of Arkansas for Medical Sciences · US

Funding

DNA Helicases: Mechanisms and FunctionsR01GM098922 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI RANEY, KEVIN DOUGLAS · 2011 to 2017
$1.7M
NIGMS NIH HHS R01 GM098922NIGMS NIH HHS R01GM098922
6 · The paper itself

Abstract

Helicases are ubiquitous enzymes that are required for virtually all processes in DNA and RNA metabolism including replication, repair, recombination, transcription, and translation. The mechanisms for helicase-catalyzed unwinding of double-stranded DNA or remodeling of RNA have been the subject of intense investigation for more than two decades. The central function of these enzymes is to transduce the energy available from ATP binding and hydrolysis to alter the conformation of nucleic acids. Specific interactions between helicases and nucleic acids have been investigated by chemical approaches in which the nucleic acid substrate has been modified in order to provide specific insight into the enzymatic mechanism.

Indexed as

BiocatalysisDNADNA HelicasesDNADNA HelicasesAbasic siteBiotinylated DNADNA unwindingFRETMethylphosphonatePeptide nucleic acid

Identifiers

PMID24931273
PMCPMC4135034
OpenAlexW2046411079

What OpenQuestion holds

Textmetadata
LicenceTDM
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.