Evidence map›Paper›PMID 34585830›Full record

ArticleAngewandte Chemie (International ed. in English)2022

Selective

Fanni Sebák, Péter Ecsédi, Wolfgang Bermel, Burkhard Luy, László Nyitray, Andrea Bodor

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Impact of C-Terminal AmideMolecules (Basel, Switzerland) · 2026
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  4. Assessment of Energy Effects DeterminingACS physical chemistry Au · 2026
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  5. Robust bilinear rotations II.Magnetic resonance (Gottingen, Germany) · 2026
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  6. Dual bilinear rotations.Magnetic resonance (Gottingen, Germany) · 2026
    Article
  7. Article
  8. Robust bilinear rotations.Science advances · 2025
    Article
  9. Article
  10. Conformational dynamics in specialized CProtein science : a publication of the Protein Society · 2025
    Article
  11. Article
  12. Review
  13. Review
  14. Probing Peptidylprolyl Bond cis/trans Status Using DistalChemistry (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  15. The residual structure of acid-denatured βProtein science : a publication of the Protein Society · 2023
    Article
  16. Article
  17. The Disordered EZH2 Loop: Atomic Level Characterization byInternational journal of molecular sciences · 2022
    Article
  18. SelectiveAngewandte Chemie (International ed. in English) · 2022
    Article
  19. 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 4 institutions in 2 countries.

Fanni SebákEötvös Loránd University, Institute of Chemistry, Pázmány Péter s. 1/a, 1117, Budapest, Hungary.ORCID 0000-0001-9252-9961
Péter EcsédiEötvös Loránd University, Department of Biochemistry, Pázmány Péter s. 1/c, 1117, Budapest, Hungary.ORCID 0000-0002-4700-125X
Wolfgang BermelBruker BioSpin GmbH, Silberstreifen 4, 76287, Rheinstetten, Germany.
Burkhard LuyKIT-Institut für Organische Chemie, IBG4-Magnetische Resonanz, Fritz-Haber-Weg 6, 76131, Karlsruhe, Germany.ORCID 0000-0001-9580-6397
László NyitrayEötvös Loránd University, Department of Biochemistry, Pázmány Péter s. 1/c, 1117, Budapest, Hungary.ORCID 0000-0003-4717-5994
Andrea BodorEötvös Loránd University, Institute of Chemistry, Pázmány Péter s. 1/a, 1117, Budapest, Hungary.ORCID 0000-0002-7422-298X
Eötvös Loránd University · HUBruker (Germany) · DEKarlsruhe Institute of Technology · DESemmelweis University · HU

Funding

EFOP-3.6.3-VEKOP-16-2017-00009Foundation for the Hungarian Peptide and Protein ResearchHGF programme Information 43.35.02nemzeti kutatási és technológiai hivatal K119359nemzeti kutatási és technológiai hivatal K124900nemzeti kutatási és technológiai hivatal K137940nemzeti kutatási fejlesztési és innovációs hivatal, ELTE Thematic Excellence Programme TKP2020-IKA-05, Project no. 2018-1.2.1-NKP-2018-00005Szint+ ProgrammeVirtmat
6 · The paper itself

Abstract

It is important to identify proline cis/trans isomers that appear in several regulatory mechanisms of proteins, and to characterize minor species that are present due to the conformational heterogeneity in intrinsically disordered proteins (IDPs). To obtain residue level information on these mobile systems we introduce two

Indexed as

Nuclear Magnetic Resonance, BiomolecularIntrinsically Disordered ProteinsMolecular ConformationPhosphorylationProlineProteomeProtonsStereoisomerismIntrinsically Disordered ProteinsProlineProteomeProtonsIDP datasetsNMR 1Hα-detectionp53phosphorylationproline cis/trans isomerization

Identifiers

PMID34585830
PMCPMC9299183
OpenAlexW3212741039

What OpenQuestion holds

Textmetadata
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.