Evidence map›Paper›PMID 33483369›Full record

ArticleRNA (New York, N.Y.)2021

High-resolution structure of eukaryotic Fibrillarin interacting with Nop56 amino-terminal domain.

Simone Höfler, Peer Lukat, Wulf Blankenfeldt, Teresa Carlomagno

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in RNA (New York, N.Y.), 2021. 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
0.4field-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, 6 citations in OpenAlex.

  1. Review
  2. Advances in the structure and function of the nucleolar protein fibrillarin.Frontiers in cell and developmental biology · 2024
    Review
  3. The roles of NOP56 in cancer and SCA36.Pathology oncology research : POR · 2023
    Review
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

4 authors at 2 institutions in 1 country.

Simone HöflerLeibniz University Hannover, Institute for Organic Chemistry and Centre for Biomolecular Drug Research (BMWZ), D-30167 Hannover, Germany.
Peer LukatHelmholtz Centre for Infection Research, Department of Structure and Function of Proteins, D-38124 Braunschweig, Germany.
Wulf BlankenfeldtHelmholtz Centre for Infection Research, Department of Structure and Function of Proteins, D-38124 Braunschweig, Germany.ORCID 0000-0001-9886-9668
Teresa CarlomagnoLeibniz University Hannover, Institute for Organic Chemistry and Centre for Biomolecular Drug Research (BMWZ), D-30167 Hannover, Germany.ORCID 0000-0002-2437-2760
Helmholtz Centre for Infection Research · DELeibniz University Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosomal RNA (rRNA) carries extensive 2'-O-methyl marks at functionally important sites. This simple chemical modification is thought to confer stability, promote RNA folding, and contribute to generate a heterogenous ribosome population with a yet-uncharacterized function. 2'-O-methylation occurs both in archaea and eukaryotes and is accomplished by the Box C/D RNP enzyme in an RNA-guided manner. Extensive and partially conflicting structural information exists for the archaeal enzyme, while no structural data is available for the eukaryotic enzyme. The yeast Box C/D RNP consists of a guide RNA, the RNA-primary binding protein Snu13, the two scaffold proteins Nop56 and Nop58, and the enzymatic module Nop1. Here we present the high-resolution structure of the eukaryotic Box C/D methyltransferase Nop1 from

Indexed as

Amino Acid SequenceArchaeal ProteinsBinding SitesChromosomal Proteins, Non-HistoneCrystallography, X-RayGene ExpressionMethylationModels, MolecularNuclear ProteinsProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsPyrococcus furiosusRecombinant ProteinsRibonucleoproteins, Small NuclearArchaeal ProteinsChromosomal Proteins, Non-HistonefibrillarinNOP1 protein, S cerevisiaeNOP56 protein, S cerevisiaeNOP58 protein, S cerevisiaeNuclear ProteinsRecombinant ProteinsRibonucleoproteins, Small NuclearRibonucleoproteins, Small NucleolarRNA, FungalRNA, Guide, CRISPR-Cas SystemsRNA, RibosomalRNA, Small NucleolarSaccharomyces cerevisiae ProteinsSnu13 protein, S cerevisiae2′-O-methylationeukaryotic Box C/D RNPFibrillarinNop56protein–protein complex structure

Identifiers

PMID33483369
PMCPMC7962484
OpenAlexW3122835392

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.