Evidence map›Paper›PMID 24364734›Full record

ArticleJournal of the American Chemical Society2014

Transmembrane fragment structures of amyloid precursor protein depend on membrane surface curvature.

Laura Dominguez, Stephen C Meredith, John E Straub, David Thirumalai

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

27 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Structure of APP-C99Biochimica et biophysica acta. Biomembranes · 2018
    Article
  15. Impact of membrane curvature on amyloid aggregation.Biochimica et biophysica acta. Biomembranes · 2018
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Impact of membrane lipid composition on the structure and stability of the transmembrane domain of amyloid precursor protein.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

4 authors at 3 institutions in 1 country.

Laura DominguezDepartment of Chemistry, Boston University , Boston, Massachusetts 02215, United States.
Stephen C Meredith
John E Straub
David Thirumalai
Boston University · USUniversity of Chicago · USUniversity of Maryland, College Park · US

Funding

Probing the Principles Governing Protein AggregationR01GM076688 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI STRAUB, JOHN E. · 2006 to 2009
$1.5M
NIGMS NIH HHS R01 GM076688
6 · The paper itself

Abstract

The amyloid β (Aβ) peptide associated with Alzheimer's disease results from processing of the amyloid precursor protein (APP) by secretases. Cleavage of APP by β-secretase produces a 99 amino acid C-terminal fragment of APP (C99) consisting of a single transmembrane (TM) helix. Simulations of C99 congeners and structural studies of C99 in surfactant micelles and lipid vesicles have shown that a key peptide structural motif is a prominent "GG kink," centered at two glycines dividing the TM helix. The flexibility of the GG kink is important in the processing of C99 by γ-secretase. We performed multiscale simulations of C99(15-55) in a DPC surfactant micelle and POPC lipid bilayer in order to elucidate the role of membrane surface curvature in modulating the peptide structure. C99(15-55) in a DPC surfactant micelle possesses a "GG kink," in the TM domain near the dynamic hinge located at G37/G38. Such a kink is not observed in C99(15-55) in a POPC lipid bilayer. Intramolecular interaction between the extracellular and TM domains of C99(15-55) is enhanced in the micelle environment, influencing helical stability, TM helix extension, exposure to water, and depth of insertion in the lipophilic region. Our results show that the fluctuations of the structural ensemble of APP are strongly influenced by membrane surface curvature.

Indexed as

Models, MolecularAmino Acid SequenceAmyloid beta-Protein PrecursorCell MembraneLipid BilayersMolecular Sequence DataPhosphatidylcholinesSurface Properties1-palmitoyl-2-oleoylphosphatidylcholineAmyloid beta-Protein PrecursorLipid BilayersPhosphatidylcholines

Identifiers

PMID24364734
PMCPMC3928069
OpenAlexW2331844696

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.