Evidence map›Paper›PMID 28696260›Full record

ArticleThe Journal of biological chemistry2017

Biophysical analysis of

Franziska Pinker, Cédric Schelcher, Pablo Fernandez-Millan, Anthony Gobert, Catherine Birck, Aurélien Thureau, Pierre Roblin, Philippe Giegé, Claude Sauter

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. How RNases Shape Mitochondrial Transcriptomes.International journal of molecular sciences · 2022
    Review
  7. Review
  8. The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Molecular recognition of pre-tRNA byRNA (New York, N.Y.) · 2017
    Article
  17. 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

9 authors at 5 institutions in 1 country.

Franziska PinkerFrom the Université de Strasbourg, CNRS, Institut de Biologie Moléculaire et Cellulaire, Architecture et Réactivité de l'ARN, UPR 9002, F-67000 Strasbourg, France,; Université de Strasbourg, CNRS, Institut de Biologie Moléculaire des Plantes, UPR 2357, F-67084 Strasbourg, France.
Cédric SchelcherUniversité de Strasbourg, CNRS, Institut de Biologie Moléculaire des Plantes, UPR 2357, F-67084 Strasbourg, France.
Pablo Fernandez-MillanFrom the Université de Strasbourg, CNRS, Institut de Biologie Moléculaire et Cellulaire, Architecture et Réactivité de l'ARN, UPR 9002, F-67000 Strasbourg, France.
Anthony GobertUniversité de Strasbourg, CNRS, Institut de Biologie Moléculaire des Plantes, UPR 2357, F-67084 Strasbourg, France.
Catherine BirckUniversité de Strasbourg, CNRS, Institut de Génétique et de Biologie Moléculaire et Cellulaire, UMR 7104, F-67404 Illkirch, France.
Aurélien ThureauSynchrotron SOLEIL, l'Orme des Merisiers, F-91410 Saint Aubin, France.
Pierre RoblinSynchrotron SOLEIL, l'Orme des Merisiers, F-91410 Saint Aubin, France; Unité de Recherche Biopolymères, Interactions, Assemblages (URBIA-Nantes), Institut National de la Recherche Agronomique Centre de Nantes, 60 rue de la Géraudière, UR 1268, F-44316 Nantes, France.
Philippe GiegéUniversité de Strasbourg, CNRS, Institut de Biologie Moléculaire des Plantes, UPR 2357, F-67084 Strasbourg, France,. Electronic address: philippe.giege@ibmp-cnrs.unistra.fr.
Claude SauterFrom the Université de Strasbourg, CNRS, Institut de Biologie Moléculaire et Cellulaire, Architecture et Réactivité de l'ARN, UPR 9002, F-67000 Strasbourg, France,. Electronic address: c.sauter@ibmc-cnrs.unistra.fr.
Centre National de la Recherche Scientifique · FRInstitut de Biologie Moléculaire et Cellulaire · FRSynchrotron soleil · FRUniversité de Strasbourg · FRInstitut de Biologie Moléculaire des Plantes · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNase P is a universal enzyme that removes 5' leader sequences from tRNA precursors. The enzyme is therefore essential for maturation of functional tRNAs and mRNA translation. RNase P represents a unique example of an enzyme that can occur either as ribonucleoprotein or as protein alone. The latter form of the enzyme, called protein-only RNase P (PRORP), is widespread in eukaryotes in which it can provide organellar or nuclear RNase P activities. Here, we have focused on

Indexed as

Models, MolecularRNA Processing, Post-TranscriptionalAmino Acid MotifsAmino Acid SubstitutionArabidopsisArabidopsis ProteinsBiophysical PhenomenaCatalytic DomainEnzyme StabilityMutationNucleic Acid ConformationNucleotide MotifsPeptide FragmentsProtein ConformationProtein Interaction Domains and MotifsRecombinant Fusion ProteinsArabidopsis ProteinsPeptide FragmentsPRORP2 protein, ArabidopsisRecombinant Fusion ProteinsRecombinant ProteinsRibonuclease PRNARNA, PlantRNA PrecursorsRNA, recombinantRNA, Transfer, Cyspentatricopeptide repeat (PPR)precursor tRNA (pre-tRNA)PRORPribonuclease P (RNase P)RNA processingsmall-angle X-ray scattering (SAXS)tRNA maturationX-ray crystallography

Identifiers

PMID28696260
PMCPMC5572917
OpenAlexW2734696953

What OpenQuestion holds

Textmetadata
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.