Evidence map›Paper›PMID 29087332›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Role of the nucleotidyl cyclase helical domain in catalytically active dimer formation.

Irene Vercellino, Lenka Rezabkova, Vincent Olieric, Yevhen Polyhach, Tobias Weinert, Richard A Kammerer, Gunnar Jeschke, Volodymyr M Korkhov

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
2.7field-weighted citation impact, top 10% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Pooled it
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  4. Review
  5. Article
  6. Article
  7. Structure ofeLife · 2022
    Article
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  19. The contribution of modern EPR to structural biology.Emerging topics in life sciences · 2018
    Article
  20. Function of Adenylyl Cyclase in Heart: the AKAP Connection.Journal of cardiovascular development and disease · 2018
    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

8 authors at 2 institutions in 1 country.

Irene VercellinoLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institute, 5232 Villigen, Switzerland.
Lenka RezabkovaLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institute, 5232 Villigen, Switzerland.
Vincent OliericMacromolecular Crystallography Group, Paul Scherrer Institute, 5232 Villigen, Switzerland.
Yevhen PolyhachLaboratory of Physical Chemistry, Swiss Federal Institute of Technology in Zurich (ETH Zurich), 8093 Zurich, Switzerland.ORCID 0000-0002-6009-1077
Tobias WeinertLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institute, 5232 Villigen, Switzerland.
Richard A KammererLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institute, 5232 Villigen, Switzerland.
Gunnar JeschkeLaboratory of Physical Chemistry, Swiss Federal Institute of Technology in Zurich (ETH Zurich), 8093 Zurich, Switzerland.
Volodymyr M KorkhovLaboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institute, 5232 Villigen, Switzerland; volodymyr.korkhov@psi.ch.
Paul Scherrer Institute · CHETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleotidyl cyclases, including membrane-integral and soluble adenylyl and guanylyl cyclases, are central components in a wide range of signaling pathways. These proteins are architecturally diverse, yet many of them share a conserved feature, a helical region that precedes the catalytic cyclase domain. The role of this region in cyclase dimerization has been a subject of debate. Although mutations within this region in various cyclases have been linked to genetic diseases, the molecular details of their effects on the enzymes remain unknown. Here, we report an X-ray structure of the cytosolic portion of the membrane-integral adenylyl cyclase Cya from

Indexed as

Catalytic DomainProtein ConformationAdenylyl CyclasesAmino Acid SubstitutionBacterial ProteinsConserved SequenceCrystallography, X-RayCytosolDimerizationEnzyme ActivationEnzyme StabilityGuanylate CyclaseHumansModels, MolecularMutagenesis, Site-DirectedMutant ProteinsAdenylyl Cyclasesadenylyl cyclase type VBacterial ProteinsGuanylate Cyclaseguanylate cyclase 1Mutant ProteinsReceptors, Cell Surfaceadenylyl cyclaseCyadimerizationhelical domainX-ray structure

Identifiers

PMID29087332
PMCPMC5699072
OpenAlexW2766480163

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.