Evidence map›Paper›PMID 30816701›Full record

ArticleAnalytical chemistry2019

Separation of β-Amyloid Tryptic Peptide Species with Isomerized and Racemized l-Aspartic Residues with Ion Mobility in Structures for Lossless Ion Manipulations.

Gabe Nagy, Komal Kedia, Isaac K Attah, Sandilya V B Garimella, Yehia M Ibrahim, Vladislav A Petyuk, Richard D Smith

Abstract read
In one paragraph

Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Enhancing the Depth of Analyses with Next-Generation Ion Mobility Experiments.Annual review of analytical chemistry (Palo Alto, Calif.) · 2023
    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

7 authors.

Gabe NagyBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.
Komal KediaBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.
Isaac K AttahBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.
Sandilya V B GarimellaBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.
Yehia M IbrahimBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.ORCID 0000-0001-6085-193X
Vladislav A PetyukBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.
Richard D SmithBiological Sciences Division , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.ORCID 0000-0002-2381-2349

Funding

Equipment Supplement Request for a Research Resource for Ultra-sensitive High Throughput ProteomicsP41GM103493 · NIGMS · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2012 to 2022
$22.6M
High Resolution High Throughput Proteomics Platform for Cancer ResearchR33CA217699 · NCI · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI IBRAHIM, YEHIA · 2017 to 2019
$1.3M
NCI NIH HHS R33 CA217699NIGMS NIH HHS P41 GM103493
6 · The paper itself

Abstract

Accumulation of β-amyloid (Aβ) is one of the hallmarks of Alzheimer's disease. The deposition of β-amyloid plaques is likely to start years in advance of manifestation of clinical symptoms, although the exact timing is unknown. Over the years, Aβ peptides undergo both post-translational modification and stereoisomerization. Analysis of the resulting stereoisomers is particularly challenging because of their identical elemental composition and similar physicochemical properties. Herein, we have utilized our recently developed structures for lossless ion manipulations ion mobility-mass spectrometry platform (SLIM IM-MS), in conjunction with serpentine ultralong path with extended routing (SUPER), to baseline resolve four distinct sets of Aβ17-28 tryptic peptide epimers on a rapid (∼1 s) time scale. We discovered that sodium adduct ions, [M + H + Na]

Indexed as

Amyloid beta-PeptidesAspartic AcidMass SpectrometryPeptide FragmentsStereoisomerismAmyloid beta-PeptidesAspartic AcidPeptide Fragments

Identifiers

PMID30816701
PMCPMC6596305

What OpenQuestion holds

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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.