Evidence map›Paper›PMID 24564538›Full record

ArticleJournal of the American Chemical Society2014

Impact of bilayer lipid composition on the structure and topology of the transmembrane amyloid precursor C99 protein.

Yuanli Song, Kathleen F Mittendorf, Zhenwei Lu, Charles R Sanders

Open access · bronzeAbstract 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 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.8field-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

31 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Formation of extramembraneProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Structure of APP-C99Biochimica et biophysica acta. Biomembranes · 2018
    Article
  16. Membrane properties that shape the evolution of membrane enzymes.Current opinion in structural biology · 2018
    Review
  17. Bicelle size modulates the rate of bacteriorhodopsin folding.Protein science : a publication of the Protein Society · 2018
    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

4 authors at 1 institution in 1 country.

Yuanli SongDepartment of Biochemistry and Center for Structural Biology, Vanderbilt University School of Medicine , Nashville, Tennessee 37232-8725, United States.
Kathleen F Mittendorf
Zhenwei Lu
Charles R Sanders
Vanderbilt University · US

Funding

Project 4 (Goethe University of Frankfurt)U54GM094608 · NIGMS · HARVARD MEDICAL SCHOOL · PI CHOU, JAMES JEIWEN · 2010 to 2014
$11.5M
MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
Structural Basis for KCNE Modulation of the KCNQ1 ChannelR01DC007416 · NIDCD · VANDERBILT UNIVERSITY · PI SANDERS, CHARLES R, VANOYE, CARLOS G. · 2006 to 2014
$3.0M
Structure Function Analysis of Integrins alpha1beta1 and alpha2beta2R01DK083187 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI SANDERS, CHARLES R, ZENT, ROY · 2010 to 2013
$1.3M
Cholesterol and the Amyloid Precursor ProteinR01GM106672 · NIGMS · VANDERBILT UNIVERSITY · PI SANDERS, CHARLES R · 2013 to 2016
$1.2M
Structure, Folding, and Misfolding of PMP22R01NS058815 · NINDS · VANDERBILT UNIVERSITY · PI CARTER, BRUCE D, SANDERS, CHARLES R · 2010 to 2012
$921k
Console upgrades for biological NMR spectrometersS10RR025677 · NCRR · VANDERBILT UNIVERSITY · PI SANDERS, CHARLES R · 2009 to 2009
$460k
NCRR NIH HHS S10 RR025677NIDCD NIH HHS R01 DC007416NIDDK NIH HHS R01 DK083187NIGMS NIH HHS R01 GM106672NIGMS NIH HHS T32 GM008320NIGMS NIH HHS U54 GM094608NINDS NIH HHS R01 NS058815
6 · The paper itself

Abstract

C99 (also known as β-CTF) is the 99 residue transmembrane C-terminal domain (residues 672-770) of the amyloid precursor protein and is the immediate precursor of the amyloid-β (Aβ) polypeptides. To test the dependence of the C99 structure on the composition of the host model membranes, NMR studies of C99 were conducted both in anionic lyso-myristoylphosphatidylglycerol (LMPG) micelles and in a series of five zwitterionic bicelle compositions involving phosphatidylcholine and sphingomyelin in which the acyl chain lengths of these lipid components varied from 14 to 24 carbons. Some of these mixtures are reported for the first time in this work and should be of broad utility in membrane protein research. The site-specific backbone (15)N and (1)H chemical shifts for C99 in LMPG and in all five bicelle mixtures were seen to be remarkably similar, indicating little dependence of the backbone structure of C99 on the composition of the host model membrane. However, the length of the transmembrane span was seen to vary in a manner that alters the positioning of the γ-secretase cleavage sites with respect to the center of the bilayer. This observation may contribute to the known dependency of the Aβ42-to-Aβ40 production ratio on both membrane thickness and the length of the C99 transmembrane domain.

Indexed as

Amyloid beta-Protein PrecursorHumansLipid BilayersMicellesNuclear Magnetic Resonance, BiomolecularPeptide FragmentsAmyloid beta-Protein Precursoramyloid beta-protein precursor C-terminal fragment beta, humanLipid BilayersMicellesPeptide Fragments

Identifiers

PMID24564538
PMCPMC3985881
OpenAlexW2313973094

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.