Evidence map›Paper›PMID 24304221›Full record

ArticleJournal of the American Chemical Society2013

Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy.

Galia T Debelouchina, Marvin J Bayro, Anthony W Fitzpatrick, Vladimir Ladizhansky, Michael T Colvin, Marc A Caporini, Christopher P Jaroniec, Vikram S Bajaj, Melanie Rosay, Cait E Macphee and 4 more

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Cross polarization stability in multidimensional NMR spectroscopy of biological solids.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2024
    Article
  6. Article
  7. Article
  8. Observation of a four-spin solid effect.The Journal of chemical physics · 2022
    Article
  9. Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. DNPSOUP: A simulation software package for dynamic nuclear polarization.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022
    Review
  11. Article
  12. Article
  13. Dynamic Nuclear Polarization Using 3D Aromatic Boron Cluster Radicals.The journal of physical chemistry letters · 2021
    Article
  14. Article
  15. Adiabatic Solid Effect.The journal of physical chemistry letters · 2020
    Article
  16. Targetable Tetrazine-Based Dynamic Nuclear Polarization Agents for Biological Systems.Chembiochem : a European journal of chemical biology · 2020
    Article
  17. Two decades of progress in structural and dynamic studies of amyloids by solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019
    Review
  18. Article
  19. High-ResolutionThe journal of physical chemistry. B · 2019
    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

14 authors.

Galia T DebelouchinaFrancis Bitter Magnet Laboratory and Department of Chemistry, Massachusetts Institute of Technology , Cambridge, Massachusetts 02139, United States.
Marvin J Bayro
Anthony W Fitzpatrick
Vladimir Ladizhansky
Michael T Colvin
Marc A Caporini
Christopher P Jaroniec
Vikram S Bajaj
Melanie Rosay
Cait E Macphee
Michele Vendruscolo
Werner E Maas
Christopher M Dobson
Robert G Griffin

Funding

OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
High Field DNP in Biological SystemsR01EB002804 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$9.1M
Solid State NMR Studies of Peptides and ProteinsR01EB003151 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2004 to 2015
$6.5M
Biotechnology and Biological Sciences Research Council BB/C00759X/2Biotechnology and Biological Sciences Research Council BB/H003843/1NIBIB NIH HHS EB-002026NIBIB NIH HHS EB-003151NIBIB NIH HHS P41 EB002026NIBIB NIH HHS R01 EB002804NIBIB NIH HHS R01 EB003151Wellcome Trust 089703
6 · The paper itself

Abstract

Protein magic angle spinning (MAS) NMR spectroscopy has generated structural models of several amyloid fibril systems, thus providing valuable information regarding the forces and interactions that confer the extraordinary stability of the amyloid architecture. Despite these advances, however, obtaining atomic resolution information describing the higher levels of structural organization within the fibrils remains a significant challenge. Here, we detail MAS NMR experiments and sample labeling schemes designed specifically to probe such higher order amyloid structure, and we have applied them to the fibrils formed by an eleven-residue segment of the amyloidogenic protein transthyretin (TTR(105-115)). These experiments have allowed us to define unambiguously not only the arrangement of the peptide β-strands into β-sheets but also the β-sheet interfaces within each protofilament, and in addition to identify the nature of the protofilament-to-protofilament contacts that lead to the formation of the complete fibril. Our efforts have resulted in 111 quantitative distance and torsion angle restraints (10 per residue) that describe the various levels of structure organization. The experiments benefited extensively from the use of dynamic nuclear polarization (DNP), which in some cases allowed us to shorten the data acquisition time from days to hours and to improve significantly the signal-to-noise ratios of the spectra. The β-sheet interface and protofilament interactions identified here revealed local variations in the structure that result in multiple peaks for the exposed N- and C-termini of the peptide and in inhomogeneous line-broadening for the residues buried within the interior of the fibrils.

Indexed as

AmyloidAmyloid beta-PeptidesMagnetic Resonance SpectroscopyNuclear Magnetic Resonance, BiomolecularAmyloidAmyloid beta-Peptides

Identifiers

PMID24304221
PMCPMC3909659

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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.