Evidence map›Paper›PMID 28111020›Full record

ArticleStructure (London, England : 1993)2017

The Functional Cycle of Rnt1p: Five Consecutive Steps of Double-Stranded RNA Processing by a Eukaryotic RNase III.

He Song, Xianyang Fang, Lan Jin, Gary X Shaw, Yun-Xing Wang, Xinhua Ji

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Dicer's Helicase Domain: A Meeting Place for Regulatory Proteins.Cold Spring Harbor symposia on quantitative biology · 2019
    Article
  11. Article
  12. 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

6 authors at 2 institutions in 1 country.

He SongMacromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA.
Xianyang FangStructural Biophysics Laboratory, National Cancer Institute, Frederick, MD 21702, USA.
Lan JinMacromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA.
Gary X ShawMacromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA.
Yun-Xing WangStructural Biophysics Laboratory, National Cancer Institute, Frederick, MD 21702, USA.
Xinhua JiMacromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA. Electronic address: jix@mail.nih.gov.
National Cancer Institute · USFrederick National Laboratory for Cancer Research · US

Funding

Search for the Structural Basis of Biomacromolecular Function and ActivityZIABC010379 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WANG, YUN XING M · 2009 to 2025
$30.4M
Biomolecular Structure and Mechanism, Structure-Based Drug DesignZIABC010326 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI JI, XINHUA · 2009 to 2024
$27.3M
Structural of Biomolecular Systems by X Ray DiffractionZ01BC010326 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI JI, XINHUA · 2000 to 2008
$2.6M
Intramural NIH HHS Z01 BC010326
6 · The paper itself

Abstract

Double-stranded RNA (dsRNA)-specific RNase III proteins are required for RNA maturation and gene regulation. The mechanism of prokaryotic RNase IIIs has been well characterized, but how eukaryotic RNase IIIs (exemplified by Rnt1p, Drosha, and Dicer) work is less clear. Recently, we reported the crystal structure of Rnt1p in complex with RNA, revealing a double-ruler mechanism for substrate selection. Here, we present more structures of Rnt1p, either RNA free or RNA bound, featuring two major conformations of the enzyme. Using these structures with existing data, we describe the functional cycle of Rnt1p in five steps, selecting, loading, locking, cleavage, and releasing. We also describe atomic details of the two-Mg

Indexed as

Amino Acid SequenceBinding SitesCations, DivalentCrystallography, X-RayDEAD-box RNA HelicasesGene ExpressionHumansMagnesiumModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsRecombinant ProteinsRibonuclease IIIRNA, Double-StrandedCations, DivalentDEAD-box RNA HelicasesDICER1 protein, humanDROSHA protein, humanMagnesiumRecombinant ProteinsRibonuclease IIIRNA, Double-StrandedRNT1 protein, S cerevisiaeSaccharomyces cerevisiae Proteinsdouble-stranded RNAdsRNAdsRNA processingribonuclease IIIRNA processingRNase IIIRnt1pSAXSsmall-angle X-ray scatteringX-ray crystallography

Identifiers

PMID28111020
PMCPMC5299047
OpenAlexW2576107872

What OpenQuestion holds

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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.