Evidence map›Paper›PMID 25797004›Full record

ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2015

Structural studies of proteins by paramagnetic solid-state NMR spectroscopy.

Christopher P Jaroniec

Abstract read
In one paragraph

Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2015. 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
–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

21 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Structure of a Protein-RNA Complex by Solid-State NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2020
    Article
  9. Two decades of progress in structural and dynamic studies of amyloids by solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  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

1 author.

Christopher P JaroniecDepartment of Chemistry and Biochemistry, The Ohio State University, 100 West 18th Avenue, Columbus, OH 43210, USA. Electronic address: jaroniec@chemistry.ohio-state.edu.

Funding

Molecular Mechanisms of Prion and Amyloid PropagationR01GM094357 · NIGMS · OHIO STATE UNIVERSITY · PI JARONIEC, CHRISTOPHER P · 2011 to 2022
$3.2M
NIGMS NIH HHS R01GM09435NIGMS NIH HHS R01 GM094357
6 · The paper itself

Abstract

Paramagnetism-based nuclear pseudocontact shifts and spin relaxation enhancements contain a wealth of information in solid-state NMR spectra about electron-nucleus distances on the ∼20 Å length scale, far beyond that normally probed through measurements of nuclear dipolar couplings. Such data are especially vital in the context of structural studies of proteins and other biological molecules that suffer from a sparse number of experimentally-accessible atomic distances constraining their three-dimensional fold or intermolecular interactions. This perspective provides a brief overview of the recent developments and applications of paramagnetic magic-angle spinning NMR to biological systems, with primary focus on the investigations of metalloproteins and natively diamagnetic proteins modified with covalent paramagnetic tags.

Indexed as

AlgorithmsMagnetic FieldsNuclear Magnetic Resonance, BiomolecularProtein ConformationProteinsProteinsMagic-angle spinningParamagnetic relaxation enhancementProtein structurePseudocontact shiftSolid-state NMR

Identifiers

PMID25797004
PMCPMC4371136

What OpenQuestion holds

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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.