Evidence map›Paper›PMID 28060278›Full record

ArticleJournal of visualized experiments : JoVE2016

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins.

Clément Danis, Clément Despres, Luiza M Bessa, Idir Malki, Hamida Merzougui, Isabelle Huvent, Haoling Qi, Guy Lippens, François-Xavier Cantrelle, Robert Schneider and 3 more

Open access · bronzeAbstract readVideo-Audio Media
In one paragraph

Article in Journal of visualized experiments : JoVE, 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
1.4field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Water-Mediated Phosphoryl Wires Stabilize Pathological Tau Fibrils.Angewandte Chemie (International ed. in English) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Science advances · 2025
    Article
  6. Article
  7. Article
  8. Inhibition of Tau seeding by targeting Tau nucleation core within neurons with a single domain antibody fragment.Molecular therapy : the journal of the American Society of Gene Therapy · 2022
    Article
  9. Phosphorylation andFrontiers in molecular neuroscience · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Direct Crosstalk BetweenFrontiers in endocrinology · 2018
    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

13 authors at 3 institutions in 1 country.

Clément DanisUMR8576, CNRS, Lille University; UMR-S1172, INSERM CNRS, Lille University.
Clément DespresUMR8576, CNRS, Lille University.
Luiza M BessaUMR8576, CNRS, Lille University.
Idir MalkiUMR8576, CNRS, Lille University.
Hamida MerzouguiUMR8576, CNRS, Lille University.
Isabelle HuventUMR8576, CNRS, Lille University.
Haoling QiUMR8576, CNRS, Lille University.
Guy LippensUMR8576, CNRS, Lille University.
François-Xavier CantrelleUMR8576, CNRS, Lille University.
Robert SchneiderUMR8576, CNRS, Lille University.
Xavier HanoulleUMR8576, CNRS, Lille University.
Caroline Smet-NoccaUMR8576, CNRS, Lille University.
Isabelle LandrieuUMR8576, CNRS, Lille University; isabelle.landrieu@univ-lille1.fr.
Université de Lille · FRUnité de Glycobiologie Structurale et Fonctionnelle · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aggregates of the neuronal Tau protein are found inside neurons of Alzheimer's disease patients. Development of the disease is accompanied by increased, abnormal phosphorylation of Tau. In the course of the molecular investigation of Tau functions and dysfunctions in the disease, nuclear magnetic resonance (NMR) spectroscopy is used to identify the multiple phosphorylations of Tau. We present here detailed protocols of recombinant production of Tau in bacteria, with isotopic enrichment for NMR studies. Purification steps that take advantage of Tau's heat stability and high isoelectric point are described. The protocol for in vitro phosphorylation of Tau by recombinant activated ERK2 allows for generating multiple phosphorylations. The protein sample is ready for data acquisition at the issue of these steps. The parameter setup to start recording on the spectrometer is considered next. Finally, the strategy to identify phosphorylation sites of modified Tau, based on NMR data, is explained. The benefit of this methodology compared to other techniques used to identify phosphorylation sites, such as immuno-detection or mass spectrometry (MS), is discussed.

Indexed as

Magnetic Resonance SpectroscopyPhosphorylationAlzheimer DiseaseHumansIntrinsically Disordered ProteinsRecombinant Proteinstau ProteinsIntrinsically Disordered ProteinsRecombinant Proteinstau Proteins

Identifiers

PMID28060278
PMCPMC5226463
OpenAlexW2561403200

What OpenQuestion holds

Textmetadata
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.