Evidence map›Paper›PMID 37053489›Full record

ArticleJournal of proteome research2023

Preparative Electrophoresis for HDL Particle Size Separation and Intact-Mass Apolipoprotein Proteoform Analysis.

Cameron Lloyd-Jones, Henrique Dos Santos Seckler, Nicholas DiStefano, Allan Sniderman, Phillip D Compton, Neil L Kelleher, John T Wilkins

Abstract read
In one paragraph

Article in Journal of proteome research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. 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

7 authors.

Cameron Lloyd-JonesDepartment of Chemistry, Department of Molecular Biosciences, Proteomics Center of Excellence, Northwestern University, Evanston, Illinois 60208, United States.ORCID 0000-0002-4549-2585
Henrique Dos Santos SecklerDepartment of Chemistry, Department of Molecular Biosciences, Proteomics Center of Excellence, Northwestern University, Evanston, Illinois 60208, United States.
Nicholas DiStefanoDepartment of Chemistry, Department of Molecular Biosciences, Proteomics Center of Excellence, Northwestern University, Evanston, Illinois 60208, United States.ORCID 0000-0002-9423-8823
Allan SnidermanRoyal Victoria Hospital-McGill University Health Centre, Montreal, Quebec H3A 1W9, Canada.
Phillip D ComptonDepartment of Chemistry, Department of Molecular Biosciences, Proteomics Center of Excellence, Northwestern University, Evanston, Illinois 60208, United States.
Neil L KelleherDepartment of Chemistry, Department of Molecular Biosciences, Proteomics Center of Excellence, Northwestern University, Evanston, Illinois 60208, United States.ORCID 0000-0002-8815-3372
John T WilkinsDepartments of Medicine (Cardiology) and Preventive Medicine, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, United States.ORCID 0000-0002-8781-1329

Funding

TR&D 7: Cell Specific ProteomicsP41GM108569 · NIGMS · NORTHWESTERN UNIVERSITY · PI KELLEHER, NEIL L · 2015 to 2024
$13.6M
Chemistry of Life Processes Predoctoral Training ProgramT32GM105538 · NIGMS · NORTHWESTERN UNIVERSITY · PI KELLEHER, NEIL L · 2013 to 2022
$2.7M
Associations Among Apolipoprotein A1 Structural Variants and High-Density Lipoprotein FunctionK23HL133601 · NHLBI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI WILKINS, JOHN THOMAS · 2016 to 2019
$663k
NHLBI NIH HHS HHSN268201800003INHLBI NIH HHS HHSN268201800004INHLBI NIH HHS HHSN268201800005INHLBI NIH HHS HHSN268201800006INHLBI NIH HHS HHSN268201800007INHLBI NIH HHS K23 HL133601NIGMS NIH HHS P41 GM108569NIGMS NIH HHS T32 GM105538
6 · The paper itself

Abstract

The most abundant proteins on high-density lipoproteins (HDLs), apolipoproteins A-I (APOA1) and A-II (APOA2), are determinants of HDL function with 15 and 9 proteoforms (chemical-structure variants), respectively. The relative abundance of these proteoforms in human serum is associated with HDL cholesterol efflux capacity, and cholesterol content. However, the association between proteoform concentrations and HDL size is unknown. We employed a novel native-gel electrophoresis technique, clear native gel-eluted liquid fraction entrapment electrophoresis (CN-GELFrEE) paired with mass spectrometry of intact proteins to investigate this association. Pooled serum was fractionated using acrylamide gels of lengths 8 and 25 cm. Western blotting determined molecular diameter and intact-mass spectrometry determined proteoform profiles of each fraction. The 8- and 25 cm experiments generated 19 and 36 differently sized HDL fractions, respectively. The proteoform distribution varied across size. Fatty-acylated APOA1 proteoforms were associated with larger HDL sizes (Pearson's

Indexed as

ApolipoproteinsLipoproteins, HDLApolipoprotein A-IBlotting, WesternCholesterolCholesterol, HDLHumansParticle SizeApolipoprotein A-IApolipoproteinsCholesterolCholesterol, HDLLipoproteins, HDLAPOA1apolipoproteinscardiovascular diseasecholesterol/effluxHDLproteomics

Identifiers

PMID37053489
PMCPMC10436667

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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.