Evidence map›Paper›PMID 31614616›Full record

ArticleCells2019

Lack of a Retinal Phenotype in a Syne-2/Nesprin-2 Knockout Mouse Model.

Nathalie Falk, Anneka Joachimsthaler, Kristin Kessler, Uwe Thorsten Lux, Angelika Anna Noegel, Jan Kremers, Johann Helmut Brandstätter, Andreas Gießl, Nathalie Falk, Anneka Joachimsthaler and 6 more

Open access · goldAbstract read
In one paragraph

Article in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. Single opsin driven white noise ERGs in mice.Frontiers in neuroscience · 2023
    Article
  2. Article
  3. Structure and dynamics of photoreceptor sensory cilia.Pflugers Archiv : European journal of physiology · 2021
    Review
  4. BiallelicGenes · 2021
    Article
  5. 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

16 authors at 3 institutions in 1 country.

Nathalie FalkAnimal Physiology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany. nathalie.falk@ukr.de.
Anneka JoachimsthalerAnimal Physiology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany. Anneka.Joachimsthaler@uk-erlangen.de.
Kristin KesslerAnimal Physiology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany. kristin.kessler@uni-wuerzburg.de.
Uwe Thorsten LuxAnimal Physiology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany. uwe.lux@fau.de.
Angelika Anna NoegelInstitute of Biochemistry I; Medical Faculty, University Hospital, University of Cologne, 50931 Cologne, Germany. noegel@uni-koeln.de.
Jan KremersDepartment of Ophthalmology, University Hospital Erlangen, 91054 Erlangen, Germany. Jan.Kremers@uk-erlangen.de.
Johann Helmut BrandstätterAnimal Physiology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany. johann.helmut.brandstaetter@fau.de.
Andreas GießlAnimal Physiology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany. Andreas.Giessl@uk-Erlangen.de.
Nathalie FalkAnimal Physiology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany.
Anneka JoachimsthalerAnimal Physiology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany.
Kristin KesslerAnimal Physiology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany.
Uwe Thorsten LuxAnimal Physiology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany.
Angelika Anna NoegelInstitute of Biochemistry I; Medical Faculty, University Hospital, University of Cologne, 50931 Cologne, Germany.
Jan KremersDepartment of Ophthalmology, University Hospital Erlangen, 91054 Erlangen, Germany.
Johann Helmut BrandstätterAnimal Physiology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany.
Andreas GießlAnimal Physiology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany. Andreas.Giessl@uk-Erlangen.de.
Friedrich-Alexander-Universität Erlangen-Nürnberg · DEUniversitätsklinikum Erlangen · DEUniversity of Cologne · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Syne-2 (also known as Nesprin-2) is a member of a family of proteins that are found primarily in the outer nuclear membrane, as well as other subcellular compartments. Syne-2 contains a C-terminal KASH transmembrane domain and is part of a protein network that associates the nuclear envelope to the cytoskeleton via the binding to actin filaments. Syne-2 plays a role in nuclear migration, nuclear positioning during retinal development, and in ciliogenesis. In a previous study, we showed a connection between Syne-2 and the multifunctional scaffold protein Pericentrin (Pcnt). The elimination of the interaction of Syne-2 and Pcnt showed defects in nuclear migration and the formation of outer segments during retinal development, as well as disturbances in centrosomal migration at the beginning of ciliogenesis in general. In this study, the Syne-2 KO mouse model Nesprin-2△ABD (Syne-2

Indexed as

Alternative SplicingAnimalsAntigensBinding SitesCell NucleusDown-RegulationMiceMice, KnockoutNerve Tissue ProteinsNuclear ProteinsPhenotypeProtein TransportRetinaAntigensNerve Tissue ProteinsNuclear ProteinspericentrinSyne2 protein, mouseciliogenesisnuclear migrationPericentrinprimary ciliumretinaSyne-2

Identifiers

PMID31614616
PMCPMC6830317
OpenAlexW2980252986

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.