Evidence map›Paper›PMID 24093049›Full record

ReviewBiomolecular concepts2013

NDE1 and NDEL1: twin neurodevelopmental proteins with similar 'nature' but different 'nurture'.

Nicholas J Bradshaw, William Hennah, Dinesh C Soares

Open access · bronzeAbstract readReview
In one paragraph

Review in Biomolecular concepts, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

34 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. CCSer2 gates dynein activity at the cell periphery.The Journal of cell biology · 2025
    Article
  4. Nde1 Promotes Lis1 Binding to Full-Length Autoinhibited Human Dynein-1.bioRxiv : the preprint server for biology · 2025
    Article
  5. CCSer2 gates dynein activity at the cell periphery.bioRxiv : the preprint server for biology · 2024
    Article
  6. Article
  7. Article
  8. Nde1 Promotes Lis1-Mediated Activation of Dynein.bioRxiv : the preprint server for biology · 2023
    Article
  9. Article
  10. Ndel1 modulates dynein activation in two distinct ways.bioRxiv : the preprint server for biology · 2023
    Article
  11. Nde1 and Ndel1: Outstanding Mysteries in Dynein-Mediated Transport.Frontiers in cell and developmental biology · 2022
    Review
  12. Article
  13. Distinct signaling by insulin and IGF-1 receptors and their extra- and intracellular domains.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Behavioral Deficits in Mice with Postnatal Disruption ofCerebral cortex communications · 2021
    Article
  15. Article
  16. Role ofFrontiers in neuroscience · 2020
    Article
  17. Article
  18. Article
  19. Article
  20. TheOpen biology · 2017
    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 3 institutions in 3 countries.

Nicholas J BradshawDepartment of Neuropathology, Heinrich Heine University Düsseldorf, University Medical School, Moorenstrasse 5, D-40225 Düsseldorf, Germany. Nicholas.Bradshaw@uni-duesseldorf.de
William Hennah
Dinesh C Soares
Heinrich Heine University Düsseldorf · DEInstitute for Molecular Medicine Finland · FIMRC Institute of Genetics and Molecular Medicine · GB

Funding

PEPFAR 088179/A/09/ZWellcome Trust 088179
6 · The paper itself

Abstract

Nuclear distribution element 1 (NDE1, also known as NudE) and NDE-like 1 (NDEL1, also known as Nudel) are paralogous proteins essential for mitosis and neurodevelopment that have been implicated in psychiatric and neurodevelopmental disorders. The two proteins possess high sequence similarity and have been shown to physically interact with one another. Numerous lines of experimental evidence in vivo and in cell culture have demonstrated that these proteins share common functions, although instances of differing functions between the two have recently emerged. We review the key aspects of NDE1 and NDEL1 in terms of recent advances in structure elucidation and cellular function, with an emphasis on their differing mechanisms of post-translational modification. Based on a review of the literature and bioinformatics assessment, we advance the concept that the twin proteins NDE1 and NDEL1, while sharing a similar 'nature' in terms of their structure and basic functions, appear to be different in their 'nurture', the manner in which they are regulated both in terms of expression and of post-translational modification within the cell. These differences are likely to be of significant importance in understanding the specific roles of NDE1 and NDEL1 in neurodevelopment and disease.

Indexed as

AnimalsBrainCarrier ProteinsGenetic Association StudiesHumansMicrotubule-Associated ProteinsMitosisNeuronsProtein Processing, Post-TranslationalProtein Structure, SecondaryCarrier ProteinsMicrotubule-Associated ProteinsNde1 protein, humanNDEL1 protein, human

Identifiers

PMID24093049
PMCPMC3787581
OpenAlexW2005015111

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.