Evidence map›Paper›PMID 24932380›Full record

ReviewThe journal of physical chemistry letters2014

How to Get Insight into Amyloid Structure and Formation from Infrared Spectroscopy.

Sean D Moran, Martin T Zanni

Abstract readReview
In one paragraph

Review in The journal of physical chemistry letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing 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

104 citing papers in PubMed.

  1. Article
  2. Article
  3. From Disordered to Ordered: Nanoscale Spectroscopy Reveals Structural Evolution of Amyloid Beta 40 Fibrils.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Article
  4. Article
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  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
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  12. Article
  13. Article
  14. Article
  15. Low-frequency Raman spectra of amyloid fibrils.The Journal of chemical physics · 2025
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

44 more citing papers are in PubMed but not listed here.

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

2 authors.

Sean D MoranDepartment of Chemistry, University of Wisconsin-Madison , 1101 University Avenue, Madison, Wisconsin 53706, United States.
Martin T ZanniDepartment of Chemistry, University of Wisconsin-Madison , 1101 University Avenue, Madison, Wisconsin 53706, United States.

Funding

Structural mechanism of diabetic amyloid formationR01DK079895 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI Martin T Zanni · 2008 to 2026
$7.7M
NIDDK NIH HHS R01 DK079895
6 · The paper itself

Abstract

There is an enormous amount of interest in the structures and formation mechanisms of amyloid fibers. In this Perspective, we review the most common structural motifs of amyloid fibers and discuss how infrared spectroscopy and isotope labeling can be used to identify their structures and aggregation kinetics. We present three specific strategies, site-specific labeling to obtain residue-by-residue structural information, isotope dilution of uniformly labeled proteins for identifying structural folds and protein mixtures, and expressed protein ligation for studying the domain structures of large proteins. For each of these methods, vibrational couplings are the source of the identifying features in the infrared spectrum. Examples are provided using the proteins hIAPP, Aβ, polyglutamine, and γD-crystallin. We focus on FTIR spectroscopy but also describe new observables made possible by 2D IR spectroscopy.

Identifiers

PMID24932380
PMCPMC4051309

What OpenQuestion holds

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Registered trials

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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.