Evidence map›Paper›PMID 41397060›Full record

ArticleThe journal of physical chemistry letters2025

Atomic Structure of GNNQQNY Nanocrystals: A Validated Approach for Polymorphic Amyloids.

Aditya Mishra, Ravi S Palani, Robert G Griffin

Abstract read
In one paragraph

Article in The journal of physical chemistry letters, 2025. 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

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

3 authors.

Aditya MishraDepartment of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.
Ravi S PalaniDepartment of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.ORCID 0000-0003-3528-7788
Robert G GriffinDepartment of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.ORCID 0000-0003-1589-832X

Funding

High Field DNP and EPR in Biological SystemsR01GM132997 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2019 to 2025
$4.6M
Solid State NMR Studies of Amyloid ProteinsR01AG058504 · NIA · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ROBERT Guy GRIFFIN · 2022 to 2026
$3.5M
NIA NIH HHS R01 AG058504NIGMS NIH HHS R01 GM132997
6 · The paper itself

Abstract

Magic angle spinning (MAS) nuclear magnetic resonance (NMR) is a powerful tool for determining the structures of complex biological systems like amyloid fibrils, which are often challenging to study due to polymorphism. However, traditional MAS NMR techniques are often limited by low signal-to-noise ratios (SNR) for long-range distances and by spectral overlap in degenerate systems. Here we establish an approach to address these challenges using the amyloid heptapeptide GNNQQNY, an ideal model for studying polymorphism due to its ability to assemble into either crystals or fibrils depending on preparation conditions. By employing specific

Indexed as

AmyloidNanoparticlesNuclear Magnetic Resonance, BiomolecularAmyloid

Identifiers

PMID41397060
PMCPMC13334431

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.