Evidence map›Paper›PMID 34143912›Full record

ArticleAngewandte Chemie (International ed. in English)2021

Unambiguous Tracking of Protein Phosphorylation by Fast High-Resolution FOSY NMR*.

Dmitry M Lesovoy, Panagiota S Georgoulia, Tammo Diercks, Irena Matečko-Burmann, Björn M Burmann, Eduard V Bocharov, Wolfgang Bermel, Vladislav Y Orekhov

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Fast Ultra-SelectiveAngewandte Chemie (International ed. in English) · 2026
    Article
  3. Article
  4. Unambiguous Tracking of Protein Phosphorylation by Fast High-Resolution FOSY NMR*.Angewandte Chemie (International ed. in English) · 2021
    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

8 authors at 5 institutions in 5 countries.

Dmitry M LesovoyDepartment of Structural Biology, Shemyakin-Ovchinnikov, Institute of Bioorganic Chemistry RAS, 117997, Moscow, Russia.ORCID 0000-0002-9130-715X
Panagiota S GeorgouliaDepartment of Chemistry and Molecular Biology, University of Gothenburg, Box 465, 40530, Gothenburg, Sweden.ORCID 0000-0003-4573-8052
Tammo DiercksNMR Platform, CiC bioGUNE, Bld. 800, Parque Tecnológico de Bizkaia, 48160, Derio, Spain.ORCID 0000-0002-5200-0905
Irena Matečko-BurmannDepartment of Psychiatry and Neurochemistry, University of Gothenburg, 40530, Gothenburg, Sweden.ORCID 0000-0001-8873-8381
Björn M BurmannDepartment of Chemistry and Molecular Biology, University of Gothenburg, Box 465, 40530, Gothenburg, Sweden.ORCID 0000-0002-3135-7964
Eduard V BocharovDepartment of Structural Biology, Shemyakin-Ovchinnikov, Institute of Bioorganic Chemistry RAS, 117997, Moscow, Russia.ORCID 0000-0002-3635-1609
Wolfgang BermelBruker BioSpin GmbH, Silberstreifen 4, 76287, Rheinstetten, Germany.
Vladislav Y OrekhovDepartment of Chemistry and Molecular Biology, University of Gothenburg, Box 465, 40530, Gothenburg, Sweden.ORCID 0000-0002-7892-6896
Moscow Institute of Physics and Technology · RUUniversity of Gothenburg · SEWallenberg Wood Science Center · SEBruker (United States) · USCIC bioGUNE · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dysregulation of post-translational modifications (PTMs) like phosphorylation is often involved in disease. NMR may elucidate exact loci and time courses of PTMs at atomic resolution and near-physiological conditions but requires signal assignment to individual atoms. Conventional NMR methods for this base on tedious global signal assignment that may often fail, as for large intrinsically disordered proteins (IDPs). We present a sensitive, robust alternative to rapidly obtain only the local assignment near affected signals, based on FOcused SpectroscopY (FOSY) experiments using selective polarisation transfer (SPT). We prove its efficiency by identifying two phosphorylation sites of glycogen synthase kinase 3 beta (GSK3β) in human Tau40, an IDP of 441 residues, where the extreme spectral dispersion in FOSY revealed unprimed phosphorylation also of Ser409. FOSY may broadly benefit NMR studies of PTMs and other hotspots in IDPs, including sites involved in molecular interactions.

Indexed as

Nuclear Magnetic Resonance, BiomolecularHumansIntrinsically Disordered ProteinsPhosphorylationProtein Processing, Post-TranslationalIntrinsically Disordered ProteinsNMR spectroscopyS4PTselective polarisation transfertau protein

Identifiers

PMID34143912
PMCPMC8596425
OpenAlexW3171189986

What OpenQuestion holds

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LicenceCC BY-NC
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.