Evidence map›Paper›PMID 19247641›Full record

ArticleAnalytical and bioanalytical chemistry2009

Characterizing ion mobility-mass spectrometry conformation space for the analysis of complex biological samples.

Larissa S Fenn, Michal Kliman, Ablatt Mahsut, Sophie R Zhao, John A McLean

Abstract read
In one paragraph

Article in Analytical and bioanalytical chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing 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

94 citing papers in PubMed.

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  17. Proteomics and Schizophrenia: The Evolution of a Great Partnership.Advances in experimental medicine and biology · 2022
    Article
  18. Article
  19. Article
  20. Article

34 more citing papers are in PubMed but not listed here.

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.

Larissa S FennDepartment of Chemistry, Vanderbilt Institute of Chemical Biology, Vanderbilt Institute of Integrative Biosystems Research and Education, Vanderbilt University, 7330 Stevenson Center, Nashville, TN 37235, USA.
Michal Kliman
Ablatt Mahsut
Sophie R Zhao
John A McLean

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI ALVAREZ, RICHARD · 2001 to 2010
$80.3M
Infrared Laser Desorption Ion Mobility Mass SpectrometerR44RR020238 · NCRR · IONWERKS, INC. · PI SCHULTZ, JOHN ALBERT · 2007 to 2009
$586k
NCRR NIH HHS 5R44RR020238-03NCRR NIH HHS R44 RR020238NIDA NIH HHS HHSN271200700012CNIDA NIH HHS HHSN271200800020CNIGMS NIH HHS GM62116NIGMS NIH HHS U54 GM062116
6 · The paper itself

Abstract

The conformation space occupied by different classes of biomolecules measured by ion mobility-mass spectrometry (IM-MS) is described for utility in the characterization of complex biological samples. Although the qualitative separation of different classes of biomolecules on the basis of structure or collision cross section is known, there is relatively little quantitative cross-section information available for species apart from peptides. In this report, collision cross sections are measured for a large suite of biologically salient species, including oligonucleotides (n = 96), carbohydrates (n = 192), and lipids (n = 53), which are compared to reported values for peptides (n = 610). In general, signals for each class are highly correlated, and at a given mass, these correlations result in predicted collision cross sections that increase in the order oligonucleotides < carbohydrates < peptides < lipids. The specific correlations are described by logarithmic regressions, which best approximate the theoretical trend of increasing collision cross section as a function of increasing mass. A statistical treatment of the signals observed within each molecular class suggests that the breadth of conformation space occupied by each class increases in the order lipids < oligonucleotides < peptides < carbohydrates. The utility of conformation space analysis in the direct analysis of complex biological samples is described, both in the context of qualitative molecular class identification and in fine structure examination within a class. The latter is demonstrated in IM-MS separations of isobaric oligonucleotides, which are interpreted by molecular dynamics simulations.

Indexed as

CarbohydratesLipidsMolecular ConformationOligonucleotidesPeptidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationCarbohydratesLipidsOligonucleotidesPeptides

Identifiers

PMID19247641
PMCPMC2762638

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Registered trials

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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.