Evidence map›Paper›PMID 27763708›Full record

ArticleAngewandte Chemie (International ed. in English)2016

Increasing the Chemical-Shift Dispersion of Unstructured Proteins with a Covalent Lanthanide Shift Reagent.

Christoph Göbl, Moritz Resch, Madeleine Strickland, Christoph Hartlmüller, Martin Viertler, Nico Tjandra, Tobias Madl

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Synthetic Approaches to Break the Chemical Shift Degeneracy of Glycans.Chembiochem : a European journal of chemical biology · 2022
    Article
  4. Review
  5. Article
  6. Review
  7. Nonclassical nuclear localization signals mediate nuclear import of CIRBP.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

7 authors.

Christoph GöblCenter for Integrated Protein Science Munich, Technische Universität München, Department of Chemistry, Lichtenbergstraße 4, 85748, Garching, Germany.ORCID 0000-0001-8614-1434
Moritz ReschCenter for Integrated Protein Science Munich, Technische Universität München, Department of Chemistry, Lichtenbergstraße 4, 85748, Garching, Germany.ORCID 0000-0003-3477-3565
Madeleine StricklandLaboratory of Structural Biophysics Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Building 50, Bethesda, MD, 20814, USA.ORCID 0000-0001-8160-070X
Christoph HartlmüllerCenter for Integrated Protein Science Munich, Technische Universität München, Department of Chemistry, Lichtenbergstraße 4, 85748, Garching, Germany.
Martin ViertlerInstitute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstr. 1, 85764, Neuherberg, Germany.
Nico TjandraLaboratory of Structural Biophysics Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Building 50, Bethesda, MD, 20814, USA.
Tobias MadlCenter for Integrated Protein Science Munich, Technische Universität München, Department of Chemistry, Lichtenbergstraße 4, 85748, Garching, Germany.ORCID 0000-0002-9725-5231

Funding

Regulation of mitochondria morphologyZIAHL006064 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI TJANDRA, NICO · 2010 to 2025
$20.9M
Nmr Studies Of The Regulation Of Cell SignalingZIAHL001048 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI TJANDRA, NICO · 2009 to 2025
$20.1M
Austrian Science Fund FWF P 28854Austrian Science Fund FWF W 1226Intramural NIH HHS ZIA HL001048Intramural NIH HHS ZIA HL006064
6 · The paper itself

Abstract

The study of intrinsically disordered proteins (IDPs) by NMR often suffers from highly overlapped resonances that prevent unambiguous chemical-shift assignments, and data analysis that relies on well-separated resonances. We present a covalent paramagnetic lanthanide-binding tag (LBT) for increasing the chemical-shift dispersion and facilitating the chemical-shift assignment of challenging, repeat-containing IDPs. Linkage of the DOTA-based LBT to a cysteine residue induces pseudo-contact shifts (PCS) for resonances more than 20 residues from the spin-labeling site. This leads to increased chemical-shift dispersion and decreased signal overlap, thereby greatly facilitating chemical-shift assignment. This approach is applicable to IDPs of varying sizes and complexity, and is particularly helpful for repeat-containing IDPs and low-complexity regions. This results in improved efficiency for IDP analysis and binding studies.

Indexed as

Intrinsically Disordered ProteinsLanthanoid Series ElementsMagnetic Resonance SpectroscopyIntrinsically Disordered ProteinsLanthanoid Series Elementschemical-shift dispersionintrinsically disordered proteinslanthanidesNMRpseudo-contact shifts

Identifiers

PMID27763708
PMCPMC5146990

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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.