Evidence map›Paper›PMID 26143008›Full record

ReviewBiochimie2015

Cooperativity, allostery and synergism in ligand binding to riboswitches.

Alla Peselis, Ang Gao, Alexander Serganov

Open access · greenAbstract readReview
In one paragraph

Review in Biochimie, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. On the Rational Design of Cooperative Receptors.Annual review of biophysics · 2023
    Review
  4. Article
  5. X-Ray Crystallography to Study Conformational Changes in a TPP Riboswitch.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Cooperativity and Allostery in RNA Systems.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  10. Article
  11. Review
  12. Article
  13. Rational design to control the trade-off between receptor affinity and cooperativity.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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.

Alla PeselisDepartment of Biochemistry and Molecular Pharmacology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA.
Ang GaoDepartment of Biochemistry and Molecular Pharmacology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA.
Alexander SerganovDepartment of Biochemistry and Molecular Pharmacology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA. Electronic address: alexander.serganov@nyumc.org.
New York University · US

Funding

Training program in Molecular BiophysicsT32GM088118 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI STOKES, DAVID L. · 2010 to 2019
$1.8M
NIGMS NIH HHS T32 GM088118NIGMS NIH HHS T32GM088118
6 · The paper itself

Abstract

Recent progress in identification and characterization of novel types of non-coding RNAs has proven that RNAs carry out a variety of cellular functions ranging from scaffolding to gene expression control. In both prokaryotic and eukaryotic cells, several classes of non-coding RNAs control expression of dozens of genes in response to specific cues. One of the most interesting and outstanding questions in the RNA field is whether regulatory RNAs are capable of employing basic biological concepts, such as allostery and cooperativity, previously attributed to the function of proteins. Aside from regulatory RNAs that form complementary base pairing with their nucleic acid targets, several RNA classes modulate gene expression via molecular mechanisms which can be paralleled to protein-mediated regulation. Among these RNAs are riboswitches, metabolite-sensing non-coding regulatory elements that adopt intrinsic three-dimensional structures and specifically bind various small molecule ligands. These characteristics of riboswitches make them well-suited for complex regulatory responses observed in allosteric and cooperative protein systems. Here we present an overview of the biochemical, genetic, and structural studies of riboswitches with a major focus on complex regulatory mechanisms and biological principles utilized by riboswitches for such genetic modulation.

Indexed as

Gene Expression RegulationAllosteric RegulationAnimalsBinding SitesEnzyme ActivationHumansLigandsModels, GeneticRiboswitchRNALigandsRiboswitchRNAGene expressionMetaboliteNon-coding RNARNA structureTranscriptionX-ray crystallography

Identifiers

PMID26143008
PMCPMC4643686
OpenAlexW810266158

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.