Evidence map›Paper›PMID 26629790›Full record

ArticleThe journal of physical chemistry. B2016

Crystal Structures of IAPP Amyloidogenic Segments Reveal a Novel Packing Motif of Out-of-Register Beta Sheets.

Angela B Soriaga, Smriti Sangwan, Ramsay Macdonald, Michael R Sawaya, David Eisenberg

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed, 1 pooled it
5.3field-weighted citation impact, top 4% of its field
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

34 citing papers in PubMed, 1 synthesis or guideline pooled it, 65 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Low-frequency Raman spectra of amyloid fibrils.The Journal of chemical physics · 2025
    Article
  4. Unravelling the Complexity of Amyloid Peptide Core Interfaces.Journal of chemical information and modeling · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022
    Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. The Impact of Halogenated Phenylalanine Derivatives on NFGAIL Amyloid Formation.Chembiochem : a European journal of chemical biology · 2020
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  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 at 1 institution in 1 country.

Angela B SoriagaHoward Hughes Medical Institute, ‡UCLA-DOE Institute of Genomics and Proteomics, §Department of Biological Chemistry, and ∥Department of Chemistry & Biochemistry, UCLA , Los Angeles, California 90095, United States.
Smriti SangwanHoward Hughes Medical Institute, ‡UCLA-DOE Institute of Genomics and Proteomics, §Department of Biological Chemistry, and ∥Department of Chemistry & Biochemistry, UCLA , Los Angeles, California 90095, United States.
Ramsay MacdonaldHoward Hughes Medical Institute, ‡UCLA-DOE Institute of Genomics and Proteomics, §Department of Biological Chemistry, and ∥Department of Chemistry & Biochemistry, UCLA , Los Angeles, California 90095, United States.
Michael R SawayaHoward Hughes Medical Institute, ‡UCLA-DOE Institute of Genomics and Proteomics, §Department of Biological Chemistry, and ∥Department of Chemistry & Biochemistry, UCLA , Los Angeles, California 90095, United States.
David EisenbergHoward Hughes Medical Institute, ‡UCLA-DOE Institute of Genomics and Proteomics, §Department of Biological Chemistry, and ∥Department of Chemistry & Biochemistry, UCLA , Los Angeles, California 90095, United States.
Howard Hughes Medical Institute · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Structural Biology of Amyloid DiseaseR01AG029430 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI EISENBERG, DAVID · 2007 to 2016
$3.9M
Howard Hughes Medical InstituteNIA NIH HHS R01 AG029430NIGMS NIH HHS P41 GM103403
6 · The paper itself

Abstract

Structural studies of amyloidogenic segments by X-ray crystallography have revealed a novel packing motif, consisting of out-of-register β sheets, which may constitute one of the toxic species in aggregation related diseases. Here we sought to determine the presence of such a motif in islet amyloid polypeptide (IAPP), whose amyloidogenic properties are associated with type 2 diabetes. We determined four new crystal structures of segments within IAPP, all forming steric zippers. Most interestingly, one of the segments in the fibril core of IAPP forms an out-of-register steric zipper. Analysis of this structure reveals several commonalities with previously solved out-of-register fibrils. Our results provide additional evidence of out-of-register β sheets as a common structural motif in amyloid aggregates.

Indexed as

Protein AggregatesAmino Acid SequenceCrystallography, X-RayHumansIslet Amyloid PolypeptideModels, MolecularPeptidesProtein Conformation, beta-StrandProtein Interaction Domains and MotifsSolutionsThermodynamicsIslet Amyloid PolypeptidePeptidesProtein AggregatesSolutions

Identifiers

PMID26629790
PMCPMC4936935
OpenAlexW2265775199

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.