Evidence map›Paper›PMID 31743491›Full record

ArticleProteins2020

Escapement mechanisms: Efficient free energy transduction by reciprocally-coupled gating.

Charles W Carter

Open access · greenAbstract read
In one paragraph

Article in Proteins, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-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

10 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Microcalorimetry reveals multi-state thermal denaturation ofStructural dynamics (Melville, N.Y.) · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. The "Water Problem"(Life (Basel, Switzerland) · 2021
    Review
  8. Review
  9. Article
  10. 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

1 author at 1 institution in 1 country.

Charles W CarterDepartment of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina.ORCID 0000-0002-2653-4452
University of North Carolina at Chapel Hill · US

Funding

Sense/Antisense Genetic Coding and the Origins of TranslationR01GM078227 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CARTER, CHARLES W. · 2006 to 2018
$3.9M
Storage and Recovery of ATP binding energy in Metal-Catalyzed Phosphoryl-TransferR01GM090406 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CARTER, CHARLES W. · 2010 to 2013
$1.4M
NIGMS NIH HHS R01-090406NIGMS NIH HHS R01-78227NIGMS NIH HHS R01 GM078227NIGMS NIH HHS R01 GM090406
6 · The paper itself

Abstract

Conversion of the free energy of NTP hydrolysis efficiently into mechanical work and/or information by transducing enzymes sustains living systems far from equilibrium, and so has been of interest for many decades. Detailed molecular mechanisms, however, remain puzzling and incomplete. We previously reported that catalysis of tryptophan activation by tryptophanyl-tRNA synthetase, TrpRS, requires relative domain motion to re-position the catalytic Mg

Indexed as

Adenosine TriphosphateAllosteric RegulationBacterial ProteinsBinding SitesBiocatalysisBiomechanical PhenomenaCatalytic DomainCations, DivalentGeobacillus stearothermophilusKineticsMagnesiumModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsAdenosine TriphosphateBacterial ProteinsCations, DivalentMagnesiumTryptophanTryptophan-tRNA Ligaseallosteric controlcombinatorial mutagenesisenergetic couplingfar from equilibriumfree energy surfacesNTP hydrolysistransducing enzymes

Identifiers

PMID31743491
PMCPMC9486351
OpenAlexW2989929160

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.