Evidence map›Paper›PMID 27338491›Full record

ReviewBiomolecules2016

NMR Meets Tau: Insights into Its Function and Pathology.

Guy Lippens, Isabelle Landrieu, Caroline Smet, Isabelle Huvent, Neha S Gandhi, Benoît Gigant, Clément Despres, Haoling Qi, Juan Lopez

Abstract readReview
In one paragraph

Review in Biomolecules, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Review
  2. Article
  3. Phosphorylation andFrontiers in molecular neuroscience · 2021
    Article
  4. Article
  5. Article
  6. Review
  7. Peptidyl-ProlylFrontiers in cell and developmental biology · 2020
    Review
  8. In-Cell NMR Study of Tau and MARK2 Phosphorylated Tau.International journal of molecular sciences · 2018
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Tau Structures.Frontiers in aging neuroscience · 2016
    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

9 authors.

Guy LippensUnité de Glycobiologie Structurale et Fontionnelle, University of Lille (UGSF), Villeneuve d'Ascq CNRS UMR Lille 8576, France. Guy.Lippens@insa-toulouse.fr.
Isabelle LandrieuUnité de Glycobiologie Structurale et Fontionnelle, University of Lille (UGSF), Villeneuve d'Ascq CNRS UMR Lille 8576, France. isabelle.landrieu@univ-lille1.fr.
Caroline SmetUnité de Glycobiologie Structurale et Fontionnelle, University of Lille (UGSF), Villeneuve d'Ascq CNRS UMR Lille 8576, France. caroline.smet@univ-lille1.fr.
Isabelle HuventUnité de Glycobiologie Structurale et Fontionnelle, University of Lille (UGSF), Villeneuve d'Ascq CNRS UMR Lille 8576, France. isabelle.huvent@univ-lille1.fr.
Neha S GandhiSchool of Mathematical Sciences, Queensland University of Technology, Brisbane 4001 QLD, Australia. neha.gandhi@qut.edu.au.
Benoît GigantInstitute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette 91190, France. Benoit.Gigant@i2bc.paris-saclay.fr.
Clément DespresUnité de Glycobiologie Structurale et Fontionnelle, University of Lille (UGSF), Villeneuve d'Ascq CNRS UMR Lille 8576, France. clement.despres@ed.univ-lille1.fr.
Haoling QiUnité de Glycobiologie Structurale et Fontionnelle, University of Lille (UGSF), Villeneuve d'Ascq CNRS UMR Lille 8576, France. haoling.qi160687@gmail.com.
Juan LopezUnité de Glycobiologie Structurale et Fontionnelle, University of Lille (UGSF), Villeneuve d'Ascq CNRS UMR Lille 8576, France. juan.lopez@pucp.edu.pe.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this review, we focus on what we have learned from Nuclear Magnetic Resonance (NMR) studies on the neuronal microtubule-associated protein Tau. We consider both the mechanistic details of Tau: the tubulin relationship and its aggregation process. Phosphorylation of Tau is intimately linked to both aspects. NMR spectroscopy has depicted accurate phosphorylation patterns by different kinases, and its non-destructive character has allowed functional assays with the same samples. Finally, we will discuss other post-translational modifications of Tau and its interaction with other cellular factors in relationship to its (dys)function.

Indexed as

Nuclear Magnetic Resonance, BiomolecularIntrinsically Disordered ProteinsProtein Processing, Post-Translationaltau ProteinsTubulinIntrinsically Disordered Proteinstau ProteinsTubulinaggregationintrinsically disordered proteinNMR spectroscopyphosphorylationprotein/protein interactionsTautubulin

Identifiers

PMID27338491
PMCPMC4919923

What OpenQuestion holds

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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.