Evidence map›Paper›PMID 26209133›Full record

ArticleNucleic acids research2015

Transcription yield of fully 2'-modified RNA can be increased by the addition of thermostabilizing mutations to T7 RNA polymerase mutants.

Adam J Meyer, Daniel J Garry, Bradley Hall, Michelle M Byrom, Hannah G McDonald, Xu Yang, Y Whitney Yin, Andrew D Ellington

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

49 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
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  3. Computational redesign of a thermostable T7 RNA polymerase.Protein engineering, design & selection : PEDS · 2026
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  9. Computational redesign of a thermostable T7 RNA polymerase.bioRxiv : the preprint server for biology · 2025
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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

8 authors at 2 institutions in 1 country.

Adam J MeyerInstitute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA andy.ellington@mail.utexas.edu.
Daniel J GarryInstitute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.
Bradley HallAltermune Technologies, LLC, Irvine, CA 92606, USA.
Michelle M ByromInstitute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.
Hannah G McDonaldInstitute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.
Xu YangDepartment of Pharmacology and Toxicology, Sealy Center for Structural Biology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Y Whitney YinDepartment of Pharmacology and Toxicology, Sealy Center for Structural Biology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Andrew D EllingtonInstitute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, TX 78712, USA Center for Systems & Synthetic Biology, University of Texas at Austin, Austin, TX 78712, USA.
The University of Texas at Austin · USThe University of Texas Medical Branch at Galveston · US

Funding

Center for Innovation in Point of Care Technologies for the Future of Cancer CareU54EB015403 · NIBIB · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI KLAPPERICH, CATHERINE M. · 2012 to 2016
$8.9M
Dissecting Dual Function of Pol gamma in mtDNA Replication and Oxidative Damage RepairR01GM110591 · NIGMS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI YIN, YUHUI · 2014 to 2018
$1.3M
Studies of toxicities of HIV RT inhibitors to human mitochondrial DNA polymeraseR01GM083703 · NIGMS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI YIN, YUHUI · 2008 to 2012
$1.3M
NIBIB NIH HHS 5U54EB015403-02NIGMS NIH HHS GM083703NIGMS NIH HHS R01 GM110591
6 · The paper itself

Abstract

On average, mutations are deleterious to proteins. Mutations conferring new function to a protein often come at the expense of protein folding or stability, reducing overall activity. Over the years, a panel of T7 RNA polymerases have been designed or evolved to accept nucleotides with modified ribose moieties. These modified RNAs have proven useful, especially in vivo, but the transcriptional yields tend to be quite low. Here we show that mutations previously shown to increase the thermal tolerance of T7 RNA polymerase can increase the activity of mutants with expanded substrate range. The resulting polymerase mutants can be used to generate 2'-O-methyl modified RNA with yields much higher than enzymes currently employed.

Indexed as

MutationTranscription, GeneticDNA-Directed RNA PolymerasesEnzyme StabilityRNASubstrate SpecificityTemperatureViral Proteinsbacteriophage T7 RNA polymeraseDNA-Directed RNA PolymerasesRNAViral Proteins

Identifiers

PMID26209133
PMCPMC4551944
OpenAlexW2139188291

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.