Evidence map›Paper›PMID 18351682›Full record

ArticleBiotechnology and bioengineering2008

Simultaneous monitoring of peptide aggregate distributions, structure, and kinetics using amide hydrogen exchange: application to Abeta(1-40) fibrillogenesis.

Wei Qi, Aming Zhang, Dhara Patel, Sungmun Lee, Jamie L Harrington, Liming Zhao, David Schaefer, Theresa A Good, Erik J Fernandez

Open access · greenAbstract read
In one paragraph

Article in Biotechnology and bioengineering, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

13 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  4. Insight into amyloid structure using chemical probes.Chemical biology & drug design · 2011
    Review
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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

9 authors at 3 institutions in 1 country.

Wei QiDepartment of Chemical Engineering, University of Virginia, Charlottesville, Virginia 22904, USA.
Aming Zhang
Dhara Patel
Sungmun Lee
Jamie L Harrington
Liming Zhao
David Schaefer
Theresa A Good
Erik J Fernandez
University of Maryland, Baltimore County · USUniversity of Virginia · USTowson University · US

Funding

Molecular Level Mechanisms of beta amyloid ToxicityR01NS042686 · NINDS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI GOOD, THERESA ANN · 2003 to 2006
$1.4M
NINDS NIH HHS (R01 NS042686NINDS NIH HHS R01 NS042686
6 · The paper itself

Abstract

Increasing evidence indicates that soluble aggregates of amyloid beta protein (Abeta) are neurotoxic. However, difficulty in isolating these unstable, dynamic species impedes studies of Abeta and other aggregating peptides and proteins. In this study, hydrogen-deuterium exchange (HX) detected by mass spectrometry (MS) was used to measure Abeta(1-40) aggregate distributions without purification or modification that might alter the aggregate structure or distribution. Different peaks in the mass spectra were assigned to monomer, low molecular weight oligomer, intermediate, and fibril based on HX labeling behavior and complementary assays. After 1 h labeling, the intermediates incorporated approximately ten more deuterons relative to fibrils, indicating a more solvent exposed structure of such intermediates. HX-MS also showed that the intermediate species dissociated much more slowly to monomer than did the very low molecular weight oligomers that were formed at very early times in Abeta aggregation. Atomic force microscopy (AFM) measurements revealed the intermediates were roughly spherical with relatively homogenous diameters of 30-50 nm. Quantitative analysis of the HX mass spectra showed that the amount of intermediate species was correlated with Abeta toxicity patterns reported in a previous study under the same conditions. This study also demonstrates the potential of the HX-MS approach to characterizing complex, multi-component oligomer distributions of aggregating peptides and proteins.

Indexed as

AmidesAmyloidAmyloid beta-PeptidesDeuterium Exchange MeasurementKineticsMass SpectrometryMicroscopy, Atomic ForceMolecular WeightPeptide FragmentsProtein Structure, SecondaryAmidesAmyloidAmyloid beta-Peptidesamyloid beta-protein (1-40)Peptide Fragments

Identifiers

PMID18351682
PMCPMC2763234
OpenAlexW2158440279

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.