Evidence map›Paper›PMID 36542732›Full record

ReviewChemical reviews2023

Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy: Advances in Methodology and Applications.

Yusuke Nishiyama, Guangjin Hou, Vipin Agarwal, Yongchao Su, Ayyalusamy Ramamoorthy

Abstract readReview
In one paragraph

Review in Chemical reviews, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing 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

53 citing papers in PubMed.

  1. Article
  2. Controlling the Guanidinium Cation Rotation by Cation-π Interactions.Angewandte Chemie (International ed. in English) · 2026
    Article
  3. Article
  4. Benchtop High-MAS NMR for Paramagnetic Materials.Molecules (Basel, Switzerland) · 2026
    Article
  5. Review
  6. A random fractionalMagnetic resonance letters · 2026
    Article
  7. Breaking theACS measurement science au · 2026
    Article
  8. Article
  9. Broadband cross polarization for ultra-wideline magic-angle spinning NMR.Physical chemistry chemical physics : PCCP · 2026
    Article
  10. Article
  11. The Evolving Landscape of NMR Structural Elucidation.Molecules (Basel, Switzerland) · 2026
    Review
  12. RSC advances · 2026
    Review
  13. Article
  14. Article
  15. bioRxiv : the preprint server for biology · 2025
    Article
  16. High-qualitySolid state nuclear magnetic resonance · 2025
    Article
  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

5 authors.

Yusuke NishiyamaJEOL Ltd., Akishima, Tokyo196-8558, Japan.ORCID 0000-0001-7136-1127
Guangjin HouState Key Laboratory of Catalysis, Dalian National Laboratory for Clean Energy, 2011-Collaborative Innovation Center of Chemistry for Energy Materials, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Zhongshan Road 457, Dalian116023, China.ORCID 0000-0001-8216-863X
Vipin AgarwalTata Institute of Fundamental Research, Sy. No. 36/P, Gopanpally, Hyderabad500 046, India.ORCID 0000-0003-3531-3181
Yongchao SuAnalytical Research and Development, Merck & Co., Inc., Rahway, New Jersey07065, United States.ORCID 0000-0001-5063-3218
Ayyalusamy RamamoorthyBiophysics, Department of Chemistry, Biomedical Engineering, Macromolecular Science and Engineering, Michigan Neuroscience Institute, University of Michigan, Ann Arbor, Michigan41809-1055, United States.ORCID 0000-0003-1964-1900

Funding

Membrane interaction and disruption by the Alzheimer's amyloid-beta peptideR01AG048934 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2016 to 2020
$2.0M
Development of biophysical approaches to investigate high-resolution structure and dynamics of membrane proteinsR35GM139573 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Ayyalusamy Ramamoorthy · 2021 to 2026
$2.0M
Structural Investigation of Amylin Oligomers Associated to Type-2 DiabetesR01DK132214 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2022 to 2025
$1.4M
NIA NIH HHS R01 AG048934NIDDK NIH HHS R01 DK132214NIGMS NIH HHS R35 GM139573
6 · The paper itself

Abstract

Solid-state NMR spectroscopy is one of the most commonly used techniques to study the atomic-resolution structure and dynamics of various chemical, biological, material, and pharmaceutical systems spanning multiple forms, including crystalline, liquid crystalline, fibrous, and amorphous states. Despite the unique advantages of solid-state NMR spectroscopy, its poor spectral resolution and sensitivity have severely limited the scope of this technique. Fortunately, the recent developments in probe technology that mechanically rotate the sample fast (100 kHz and above) to obtain "solution-like" NMR spectra of solids with higher resolution and sensitivity have opened numerous avenues for the development of novel NMR techniques and their applications to study a plethora of solids including globular and membrane-associated proteins, self-assembled protein aggregates such as amyloid fibers, RNA, viral assemblies, polymorphic pharmaceuticals, metal-organic framework, bone materials, and inorganic materials. While the ultrafast-MAS continues to be developed, the minute sample quantity and radio frequency requirements, shorter recycle delays enabling fast data acquisition, the feasibility of employing proton detection, enhancement in proton spectral resolution and polarization transfer efficiency, and high sensitivity per unit sample are some of the remarkable benefits of the ultrafast-MAS technology as demonstrated by the reported studies in the literature. Although the very low sample volume and very high RF power could be limitations for some of the systems, the advantages have spurred solid-state NMR investigation into increasingly complex biological and material systems. As ultrafast-MAS NMR techniques are increasingly used in multidisciplinary research areas, further development of instrumentation, probes, and advanced methods are pursued in parallel to overcome the limitations and challenges for widespread applications. This review article is focused on providing timely comprehensive coverage of the major developments on instrumentation, theory, techniques, applications, limitations, and future scope of ultrafast-MAS technology.

Indexed as

Magnetic Resonance ImagingProtonsMagnetic Resonance SpectroscopyMembrane ProteinsNuclear Magnetic Resonance, BiomolecularMembrane ProteinsProtons

Identifiers

PMID36542732
PMCPMC10319395

What OpenQuestion holds

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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.