Evidence map›Paper›PMID 30875837›Full record

ReviewInternational journal of molecular sciences2019

The Inescapable Effects of Ribosomes on In-Cell NMR Spectroscopy and the Implications for Regulation of Biological Activity.

David S Burz, Leonard Breindel, Alexander Shekhtman

Open access · goldAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

3 authors at 1 institution in 1 country.

David S BurzDepartment of Chemistry, University at Albany, State University of New York, 1400 Washington Ave., Albany, NY 12222, USA. dsburz@albany.edu.
Leonard BreindelDepartment of Chemistry, University at Albany, State University of New York, 1400 Washington Ave., Albany, NY 12222, USA. lbreindel@albany.edu.
Alexander ShekhtmanDepartment of Chemistry, University at Albany, State University of New York, 1400 Washington Ave., Albany, NY 12222, USA. ashekhtman@albany.edu.
Albany State University · US

Funding

Real Time (RT) In-cell NMR technology to study protein interactions in live cellsR01GM085006 · NIGMS · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI SHEKHTMAN, ALEXANDER · 2010 to 2021
$2.4M
NIGMS NIH HHS R01 GM085006NIH HHS GM085006
6 · The paper itself

Abstract

The effects of RNA on in-cell NMR spectroscopy and ribosomes on the kinetic activity of several metabolic enzymes are reviewed. Quinary interactions between labelled target proteins and RNA broaden in-cell NMR spectra yielding apparent megadalton molecular weights in-cell. The in-cell spectra can be resolved by using cross relaxation-induced polarization transfer (CRINEPT), heteronuclear multiple quantum coherence (HMQC), transverse relaxation-optimized, NMR spectroscopy (TROSY). The effect is reproduced in vitro by using reconstituted total cellular RNA and purified ribosome preparations. Furthermore, ribosomal binding antibiotics alter protein quinary structure through protein-ribosome and protein-mRNA-ribosome interactions. The quinary interactions of Adenylate kinase, Thymidylate synthase and Dihydrofolate reductase alter kinetic properties of the enzymes. The results demonstrate that ribosomes may specifically contribute to the regulation of biological activity.

Indexed as

Adenylate KinaseAnti-Bacterial AgentsCatalytic DomainModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Structure, QuaternaryQuantum TheoryRibosomesRNATetrahydrofolate DehydrogenaseThymidylate SynthaseAdenylate KinaseAnti-Bacterial AgentsRNATetrahydrofolate DehydrogenaseThymidylate SynthaseAdenylate kinasecross-correlated relaxationDihydrofolate reductaseenzyme activityenzyme kineticsmRNANMR spectroscopyprotein interactionsprotein structure-functionRibosomerRNAThioredoxinThymidylate synthase

Identifiers

PMID30875837
PMCPMC6471074
OpenAlexW2921156446

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.