Evidence map›Paper›PMID 24534088›Full record

ReviewProgress in nuclear magnetic resonance spectroscopy2014

Practical aspects of NMR signal assignment in larger and challenging proteins.

Dominique P Frueh

Abstract readEvaluation StudyReview
In one paragraph

Review in Progress in nuclear magnetic resonance spectroscopy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Modernizing biomolecular NMR: The POKY suite.The Journal of biological chemistry · 2026
    Review
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  13. Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensionalProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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  15. NMR Lineshape Analysis of Intrinsically Disordered Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
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  20. Distance-independent Cross-correlated Relaxation and Isotropic Chemical Shift Modulation in Protein Dynamics Studies.Chemphyschem : a European journal of chemical physics and physical chemistry · 2019
    Review
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.

Dominique P FruehJohns Hopkins University School of Medicine, Biophysics and Biophysical Chemistry, 725 N. Wolfe Street, 701 Hunterian, Baltimore, MD 21205-2105, United States. Electronic address: dfrueh1@jhmi.edu.

Funding

T CELL SPECIFIC TRANSCRIPTION COMPLEXESP01GM047467 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1992 to 2017
$28.6M
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 P01 GM047467NIGMS NIH HHS R01 GM104257NIGMS NIH HHS R01GM104257
6 · The paper itself

Abstract

NMR has matured into a technique routinely employed for studying proteins in near physiological conditions. However, applications to larger proteins are impeded by the complexity of the various correlation maps necessary to assign NMR signals. This article reviews the data analysis techniques traditionally employed for resonance assignment and describes alternative protocols necessary for overcoming challenges in large protein spectra. In particular, simultaneous analysis of multiple spectra may help overcome ambiguities or may reveal correlations in an indirect manner. Similarly, visualization of orthogonal planes in a multidimensional spectrum can provide alternative assignment procedures. We describe examples of such strategies for assignment of backbone, methyl, and nOe resonances. We describe experimental aspects of data acquisition for the related experiments and provide guidelines for preliminary studies. Focus is placed on large folded monomeric proteins and examples are provided for 37, 48, 53, and 81 kDa proteins.

Indexed as

AnimalsHumansMagnetic Resonance SpectroscopyMultiprotein ComplexesProteinsMultiprotein ComplexesProteinsLarge proteinNuclear Magnetic Resonance (NMR)Resonance assignmentSpectra analysisSpectral overlap

Identifiers

PMID24534088
PMCPMC3951217

What OpenQuestion holds

Textmetadata
LicenceTDM
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.