Evidence map›Paper›PMID 31598803›Full record

ArticleJournal of biomolecular NMR2019

Random coil chemical shifts for serine, threonine and tyrosine phosphorylation over a broad pH range.

Ruth Hendus-Altenburger, Catarina B Fernandes, Katrine Bugge, Micha B A Kunze, Wouter Boomsma, Birthe B Kragelund

Open access · hybridAbstract read
In one paragraph

Article in Journal of biomolecular NMR, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

21 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Review
  3. Proline/sidechain C-H/O interactions stabilizePhysical chemistry chemical physics : PCCP · 2026
    Article
  4. Article
  5. A tethering mechanism underlies Pin1-catalyzed prolineProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Anti-Antibiotics (Basel, Switzerland) · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Unambiguous Tracking of Protein Phosphorylation by Fast High-Resolution FOSY NMR*.Angewandte Chemie (International ed. in English) · 2021
    Article
  17. Article
  18. Article
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

Ruth Hendus-AltenburgerStructural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, Copenhagen N, Denmark.ORCID http://orcid.org/0000-0001-5183-1507
Catarina B FernandesStructural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, Copenhagen N, Denmark.ORCID http://orcid.org/0000-0002-6198-3173
Katrine BuggeStructural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, Copenhagen N, Denmark.ORCID http://orcid.org/0000-0002-6286-6243
Micha B A KunzeStructural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, Copenhagen N, Denmark.ORCID http://orcid.org/0000-0001-8922-5510
Wouter BoomsmaDepartment of Computer Science, University of Copenhagen, Universitetsparken 1, 2100, Copenhagen Ø, Denmark.ORCID http://orcid.org/0000-0002-8257-3827
Birthe B KragelundStructural Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, Copenhagen N, Denmark. bbk@bio.ku.dk.ORCID http://orcid.org/0000-0002-7454-1761
University of Copenhagen · DK

Funding

Danish Research Councils 4181-00344Lundbeckfonden MBAKNovo Nordisk Fonden Challenge REPINNovo Nordisk Foundation SynergyVillumfonden instrument
6 · The paper itself

Abstract

Phosphorylation is one of the main regulators of cellular signaling typically occurring in flexible parts of folded proteins and in intrinsically disordered regions. It can have distinct effects on the chemical environment as well as on the structural properties near the modification site. Secondary chemical shift analysis is the main NMR method for detection of transiently formed secondary structure in intrinsically disordered proteins (IDPs) and the reliability of the analysis depends on an appropriate choice of random coil model. Random coil chemical shifts and sequence correction factors were previously determined for an Ac-QQXQQ-NH

Indexed as

Amino AcidsHydrogen-Ion ConcentrationIntrinsically Disordered ProteinsNuclear Magnetic Resonance, BiomolecularPhosphorylationProtein Structure, SecondarySerineTemperatureThreonineTyrosineAmino AcidsIntrinsically Disordered ProteinsSerineThreonineTyrosineIDPNMRPhosphorylationPost translational modificationPTMRandom coilSecondary chemical shift analysisSecondary structure

Identifiers

PMID31598803
PMCPMC6875518
OpenAlexW2979370349

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.