Evidence map›Paper›PMID 30389976›Full record

ArticleScientific reports2018

Crystal Structure of Human Nocturnin Catalytic Domain.

Michael A Estrella, Jin Du, Alexei Korennykh

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Identification of CCR4C as a chloroplast-localized NADP(H) phosphatase regulating NAD(P)(H) balance inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. How RNases Shape Mitochondrial Transcriptomes.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Spatiotemporal regulation of NADP(H) phosphatase Nocturnin and its role in oxidative stress response.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. The metabolites NADPNature communications · 2019
    Article
  13. 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.

Michael A EstrellaDepartment of Molecular Biology, Princeton, NJ, 08544, USA.ORCID http://orcid.org/0000-0002-1721-9418
Jin DuDepartment of Molecular Biology, Princeton, NJ, 08544, USA.ORCID http://orcid.org/0000-0002-8224-250X
Alexei KorennykhDepartment of Molecular Biology, Princeton, NJ, 08544, USA. akorenny@princeton.edu.
Princeton University · US

Funding

Structure and Function of Kinase Family Receptors Regulating TranslationR01GM110161 · NIGMS · PRINCETON UNIVERSITY · PI KORENNYKH, ALEXEI · 2014 to 2022
$2.5M
NIGMS NIH HHS R01 GM110161
6 · The paper itself

Abstract

Nocturnin (NOCT) helps the circadian clock to adjust metabolism according to day and night activity. NOCT is upregulated in early evening and it has been proposed that NOCT serves as a deadenylase for metabolic enzyme mRNAs. We present a 2.7-Å crystal structure of the catalytic domain of human NOCT. Our structure shows that NOCT has a close overall similarity to CCR4 deadenylase family members, PDE12 and CNOT6L, and to a DNA repair enzyme TDP2. All the key catalytic residues present in PDE12, CNOT6L and TDP2 are conserved in NOCT and have the same conformations. However, we observe substantial differences in the surface properties of NOCT, an unexpectedly narrow active site pocket, and conserved structural elements in the vicinity of the catalytic center, which are unique to NOCT and absent in the deadenylases PDE12/CNOT6L. Moreover, we show that in contrast to human PDE12 and CNOT6L, NOCT is completely inactive against poly-A RNA. Our work thus reveals the structure of an intriguing circadian protein and suggests that NOCT has considerable differences from the related deadenylases, which may point to a unique cellular function of this enzyme.

Indexed as

Catalytic DomainDNA-Binding ProteinsExoribonucleasesNuclear ProteinsPhosphoric Diester HydrolasesPoly ARecombinant ProteinsRibonucleasesRNA, MessengerTranscription FactorsCNOT6L protein, humanDNA-Binding ProteinsExoribonucleasesnocturninNuclear ProteinsPDE12 protein, humanPhosphoric Diester HydrolasesPoly ARecombinant ProteinsRibonucleasesRNA, MessengerTDP2 protein, humanTranscription Factors

Identifiers

PMID30389976
PMCPMC6214945
OpenAlexW2949098363

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.