Evidence map›Paper›PMID 23850141›Full record

ReviewCurrent opinion in structural biology2013

NMR methods for structural studies of large monomeric and multimeric proteins.

Dominique P Frueh, Andrew C Goodrich, Subrata H Mishra, Scott R Nichols

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Journal of molecular biology · 2026
    Article
  2. Review
  3. Beyond the mono-nucleosome.Biochemical Society transactions · 2025
    Review
  4. Article
  5. Review
  6. Virus-like Particles: Fundamentals and Biomedical Applications.International journal of molecular sciences · 2022
    Review
  7. Spectroscopic and in vitro Investigations of FeChembiochem : a European journal of chemical biology · 2022
    Review
  8. Review
  9. Article
  10. Current Approaches in Supersecondary Structures Investigation.International journal of molecular sciences · 2021
    Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Could confounding the allosteric communication of biotic machinery be an alternative path to antibiotics?Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

4 authors.

Dominique P FruehDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, MD 21205, USA. Electronic address: dfrueh1@jhmi.edu.
Andrew C Goodrich
Subrata H Mishra
Scott R Nichols

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
NMR studies of heterocyclization and epimerization in yersiniabactin synthesisR01GM104257 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI FRUEH, DOMINIQUE PASCAL · 2013 to 2023
$3.0M
NIGMS NIH HHS R01 GM104257NIGMS NIH HHS R01GM104257NIGMS NIH HHS T32 GM007445
6 · The paper itself

Abstract

NMR structural studies of large monomeric and multimeric proteins face distinct challenges. In large monomeric proteins, the common occurrence of frequency degeneracies between residues impedes unambiguous assignment of NMR signals. To overcome this barrier, nonuniform sampling (NUS) is used to measure spectra with optimal resolution within reasonable time, new correlation maps resolve previous impasses in assignment strategies, and novel selective methyl labeling schemes provide additional structural probes without cluttering NMR spectra. These advances push the limits of NMR studies of large monomeric proteins. Large multimeric and multidomain proteins are studied by NMR when individual components can also be studied by NMR and have known structures. The structural properties of large assemblies are obtained by identifying binding surfaces, by orienting domains, and employing limited distance constraints. Segmental labeling and the combination of NMR with other methods have helped popularize NMR studies of such systems.

Indexed as

Models, MolecularMagnetic Resonance SpectroscopyNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein MultimerizationProteinsProteins

Identifiers

PMID23850141
PMCPMC3805735

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.