Evidence map›Paper›PMID 29911185›Full record

ArticleEmerging topics in life sciences2018

New applications of solid-state NMR in structural biology.

Patrick C A van der Wel

Abstract read
In one paragraph

Article in Emerging topics in life sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. α-1,3-Glucan-Driven Remodeling of the Conidial Cell Wall in anJournal of the American Chemical Society · 2026
    Article
  3. Review
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  5. Article
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  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. 3D-printed stators & drive caps for magic-angle spinning NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022
    Article
  15. Article
  16. Implementing Digital-Waveform Technology for ExtendedJournal of the American Society for Mass Spectrometry · 2021
    Article
  17. Review
  18. Review
  19. Review
  20. 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.

Patrick C A van der WelDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, U.S.A.

Funding

Structures and Properties of Polyglutamine Proteins and Their AggregatesR01AG019322 · NIA · UNIVERSITY OF TENNESSEE KNOXVILLE · PI WETZEL, RONALD B · 2001 to 2014
$4.6M
The molecular basis of cardiolipin-protein interactions implicated in intrinsic apoptosisR01GM113908 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KAGAN, VALERIAN E · 2016 to 2019
$1.5M
Structural polymorphism in the misfolding and aggregation of expanded polyglutamine proteinsR01GM112678 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CONWAY, JAMES F. · 2015 to 2019
$1.4M
NIA NIH HHS R01 AG019322NIGMS NIH HHS R01 GM112678NIGMS NIH HHS R01 GM113908
6 · The paper itself

Abstract

Various recent developments in solid-state nuclear magnetic resonance (ssNMR) spectroscopy have enabled an array of new insights regarding the structure, dynamics, and interactions of biomolecules. In the ever more integrated world of structural biology, ssNMR studies provide structural and dynamic information that is complementary to the data accessible by other means. ssNMR enables the study of samples lacking a crystalline lattice, featuring static as well as dynamic disorder, and does so independent of higher-order symmetry. The present study surveys recent applications of biomolecular ssNMR and examines how this technique is increasingly integrated with other structural biology techniques, such as (cryo) electron microscopy, solution-state NMR, and X-ray crystallography. Traditional ssNMR targets include lipid bilayer membranes and membrane proteins in a lipid bilayer environment. Another classic application has been in the area of protein misfolding and aggregation disorders, where ssNMR has provided essential structural data on oligomers and amyloid fibril aggregates. More recently, the application of ssNMR has expanded to a growing array of biological assemblies, ranging from non-amyloid protein aggregates, protein-protein complexes, viral capsids, and many others. Across these areas, multidimensional magic angle spinning (MAS) ssNMR has, in the last decade, revealed three-dimensional structures, including many that had been inaccessible by other structural biology techniques. Equally important insights in structural and molecular biology derive from the ability of MAS ssNMR to probe information beyond comprehensive protein structures, such as dynamics, solvent exposure, protein-protein interfaces, and substrate-enzyme interactions.

Identifiers

PMID29911185
PMCPMC6002152

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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.