Higher magnetic field NMR renders resolution enhancement on ganglioside GD3 catalyzed heterogeneous Aβ

Jhinuk Saha, Thirupathi Ravula, Ayyalusamy Ramamoorthy

Abstract read

In one paragraph

Article in Solid state nuclear magnetic resonance, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

Update of
Higher Magnetic Field NMR Renders Resolution Enhancement on Ganglioside GD3 Catalyzed Aβ2026

5 · Who and what money

Authors and funding

3 authors.

Jhinuk SahaDepartment of Chemical and Biomedical Engineering, FAMU-FSU College of Engineering, Florida State University, Tallahassee, FL, 32310, USA; National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL, 32310, USA; Institute of Molecular Biophysics, Florida State University, 91 Chieftan Way, Tallahassee, FL, 32304, USA.

Thirupathi RavulaThe National Magnetic Resonance Facility at Madison (NMRFAM), Madison, WI, 53706, USA.

Ayyalusamy RamamoorthyDepartment of Chemical and Biomedical Engineering, FAMU-FSU College of Engineering, Florida State University, Tallahassee, FL, 32310, USA; National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL, 32310, USA; Institute of Molecular Biophysics, Florida State University, 91 Chieftan Way, Tallahassee, FL, 32304, USA; Biophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI, 48109, USA. Electronic address: aramamoorthy@fsu.edu.

Funding

NMR User Program at NMRFAMR24GM141526 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Katherine Anne Henzler-Wildman · 2021 to 2026

$6.4M

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

National Science FoundationNIDDK NIH HHS R01 DK132214NIGMS NIH HHS R24 GM141526

6 · The paper itself

Abstract

Magic-angle spinning (MAS) solid-state NMR (SSNMR) has been widely used to determine amyloid fibril structures at atomic resolution. Such studies typically rely on homogeneous fibril preparations that produce narrow linewidths and high spectral resolution, enabling reliable resonance assignment and structural analysis. However, many biologically relevant amyloid aggregates are structurally heterogeneous, resulting in spectral broadening and reduced sensitivity that hinder atomic-resolution characterization. Lipids are known to modulate amyloid aggregation pathways and promote the formation of toxic species that are often less homogeneous, further complicating NMR-based investigations. Here, we evaluate the feasibility of utilizing the benefits associated with high-field (1.1 GHz) SSNMR for studying ganglioside GD3-catalyzed Aβ

Indexed as

Amyloid beta-PeptidesGangliosidesMagnetic FieldsNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein AggregatesCatalysisAmyloid beta-Peptidesamyloid beta-protein (1-42)ganglioside, GD3GangliosidesPeptide FragmentsProtein Aggregates

Identifiers

PMID42061286

DOI10.1016/j.ssnmr.2026.102093

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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.