Evidence map›Paper›PMID 33106314›Full record

ArticleThe Journal of biological chemistry2020

A combinatorial native MS and LC-MS/MS approach reveals high intrinsic phosphorylation of human Tau but minimal levels of other key modifications.

Friedel Drepper, Jacek Biernat, Senthilvelrajan Kaniyappan, Helmut E Meyer, Eva Maria Mandelkow, Bettina Warscheid, Eckhard Mandelkow

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 53 citations in OpenAlex.

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  14. Quantification of Methylation and Phosphorylation Stoichiometry.Methods in molecular biology (Clifton, N.J.) · 2024
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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

7 authors at 5 institutions in 1 country.

Friedel DrepperGroup of Biochemistry and Functional Proteomics, Institute of Biology II, University of Freiburg, Freiburg, Germany; Signalling Research Centres BIOSS and CIBSS, University of Freiburg, Freiburg, Germany.
Jacek BiernatDZNE (German Center for Neurodegenerative Diseases), Bonn, Germany.
Senthilvelrajan KaniyappanDZNE (German Center for Neurodegenerative Diseases), Bonn, Germany; Department of Neurodegenerative Diseases and Geriatric Psychiatry, University of Bonn, Bonn, Germany.
Helmut E MeyerMedical Proteome Center, Ruhr-University Bochum, Bochum, Germany; Department of Biomedical Research, Leibniz-Institute for Analytical Sciences (ISAS), Dortmund, Germany.
Eva Maria MandelkowDZNE (German Center for Neurodegenerative Diseases), Bonn, Germany; CAESAR Research Center, Bonn, Germany.
Bettina WarscheidGroup of Biochemistry and Functional Proteomics, Institute of Biology II, University of Freiburg, Freiburg, Germany; Signalling Research Centres BIOSS and CIBSS, University of Freiburg, Freiburg, Germany. Electronic address: bettina.warscheid@biologie.uni-freiburg.de.
Eckhard MandelkowDZNE (German Center for Neurodegenerative Diseases), Bonn, Germany; CAESAR Research Center, Bonn, Germany. Electronic address: mand@mpasmb.desy.de.
Center of Advanced European Studies and Research · DEUniversity of Freiburg · DEGerman Center for Neurodegenerative Diseases · DELeibniz Institute for Analytical Sciences - ISAS · DEUniversity of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Abnormal changes of neuronal Tau protein, such as phosphorylation and aggregation, are considered hallmarks of cognitive deficits in Alzheimer's disease. Abnormal phosphorylation is thought to precede aggregation and therefore to promote aggregation, but the nature and extent of phosphorylation remain ill-defined. Tau contains ∼85 potential phosphorylation sites, which can be phosphorylated by various kinases because the unfolded structure of Tau makes them accessible. However, methodological limitations (

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceChromatography, LiquidHumansPhosphorylationSequence HomologyTandem Mass Spectrometrytau Proteinstau ProteinsAlzheimer's diseaseLC-MSmass spectrometry (MS)native mass spectrometryphosphorylationprotein aggregationTau protein (Tau)

Identifiers

PMID33106314
PMCPMC7939451
OpenAlexW3093965237

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.