Evidence map›Paper›PMID 27794454›Full record

ReviewMethods (San Diego, Calif.)2017

Characterization of aminoacyl-tRNA synthetase stability and substrate interaction by differential scanning fluorimetry.

Jamie A Abbott, Nathan M Livingston, Shawn B Egri, Ethan Guth, Christopher S Francklyn

Open access · greenAbstract readReview
In one paragraph

Review in Methods (San Diego, Calif.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Tyrosine Supplementation Rescues a Growth Defect in a HumanizedInternational journal of molecular sciences · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Thermostability Improvement of L-Asparaginase fromMolecules (Basel, Switzerland) · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Aminoacyl-tRNA synthetases.Methods (San Diego, Calif.) · 2017
    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

5 authors at 2 institutions in 1 country.

Jamie A AbbottDepartment of Biochemistry, University of Vermont, Burlington, VT 05405, USA. Electronic address: Jamie.Abbott@uvm.edu.
Nathan M LivingstonDepartment of Biochemistry, University of Vermont, Burlington, VT 05405, USA.
Shawn B EgriDepartment of Biochemistry, University of Vermont, Burlington, VT 05405, USA.
Ethan GuthChemistry & Biochemistry Department, Norwich University, Northfield, VT 05663, USA.
Christopher S FrancklynDepartment of Biochemistry, University of Vermont, Burlington, VT 05405, USA. Electronic address: Christopher.Francklyn@uvm.edu.
University of Vermont · USNorwich University · US

Funding

Structure and Mechanism of Class II tRNA SynthetasesR01GM054899 · NIGMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI FRANCKLYN, CHRISTOPHER S · 1997 to 2017
$5.7M
HEMOSTASIS &THROMBOSIS PROGRAM FOR ACADEMIC TRAINEEST32HL007594 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI KELM, ROBERT J · 1985 to 2015
$4.6M
Anesthesiology Research Training ProgramT32GM099607 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI KNIGHT III, PAUL R · 2012 to 2021
$1.8M
NHLBI NIH HHS T32 HL007594NIGMS NIH HHS R01 GM054899NIGMS NIH HHS T32 GM099607
6 · The paper itself

Abstract

Differential scanning fluorimetry (DSF) is a fluorescence-based assay to evaluate protein stability by determining protein melting temperatures. Here, we describe the application of DSF to investigate aminoacyl-tRNA synthetase (AARS) stability and interaction with ligands. Employing three bacterial AARS enzymes as model systems, methods are presented here for the use of DSF to measure the apparent temperatures at which AARSs undergo melting transitions, and the effect of AARS substrates and inhibitors. One important observation is that the extent of temperature stability realized by an AARS in response to a particular bound ligand cannot be predicted a priori. The DSF method thus serves as a rapid and highly quantitative approach to measure AARS stability, and the ability of ligands to influence the temperature at which unfolding transitions occur.

Indexed as

Alanine-tRNA LigaseAmino AcidsBenzopyransEnzyme InhibitorsEnzyme StabilityEscherichia coliEscherichia coli ProteinsFluorescent DyesFluorometryHistidine-tRNA LigaseMuramidasePhase TransitionProtein BindingProtein UnfoldingRNA, Transfer, Amino Acid-SpecificSubstrate SpecificityAlanine-tRNA LigaseAmino AcidsBenzopyransEnzyme InhibitorsEscherichia coli ProteinsFluorescent DyesHistidine-tRNA LigaseMuramidaseRNA, Transfer, Amino Acid-SpecificThreonine-tRNA LigaseAmino acidAminoacyl-tRNA synthetaseDifferential scanning fluorimetryHistidyl-tRNA synthetaseSYPRO OrangetRNA

Identifiers

PMID27794454
PMCPMC5493479
OpenAlexW2540648321

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.