Evidence map›Paper›PMID 28002079›Full record

ReviewCurrent opinion in lipidology2017

Unbiased and targeted mass spectrometry for the HDL proteome.

Sasha A Singh, Masanori Aikawa

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in lipidology, 2017. 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
1.4field-weighted citation impact, top 17% 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, 20 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Review
  4. Article
  5. Clot or Not? Reviewing the Reciprocal Regulation Between Lipids and Blood Clotting.Arteriosclerosis, thrombosis, and vascular biology · 2024
    Review
  6. Understanding HDL Metabolism and Biology Through In Vivo Tracer Kinetics.Arteriosclerosis, thrombosis, and vascular biology · 2024
    Review
  7. Article
  8. Lipoprotein proteome profile: novel insight into hyperlipidemia.Clinical and translational medicine · 2021
    Article
  9. Article
  10. Review
  11. Deepening our understanding of HDL proteome.Expert review of proteomics · 2019
    Review
  12. Observational
  13. 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

2 authors at 2 institutions in 2 countries.

Sasha A SinghaCenter for Interdisciplinary Cardiovascular Sciences, Cardiovascular Division bCenter for Excellence in Vascular Biology, Cardiovascular Division, Department of Medicine cChanning Division of Network Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Masanori Aikawa
Harvard University · USNational Center for Mathematics and Interdisciplinary Sciences · CN

Funding

PARP9 and PARP14 in atherosclerosisR01HL126901 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI AIKAWA, MASANORI · 2016 to 2019
$2.4M
Dll4 in macrophage activationR01HL107550 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI AIKAWA, MASANORI · 2012 to 2015
$2.1M
NHLBI NIH HHS R01 HL107550NHLBI NIH HHS R01 HL126901
6 · The paper itself

Abstract

purpose of reviewMass spectrometry is an ever evolving technology that is equipped with a variety of tools for protein research. Some lipoprotein studies, especially those pertaining to HDL biology, have been exploiting the versatility of mass spectrometry to understand HDL function through its proteome. Despite the role of mass spectrometry in advancing research as a whole, however, the technology remains obscure to those without hands on experience, but still wishing to understand it. In this review, we walk the reader through the coevolution of common mass spectrometry workflows and HDL research, starting from the basic unbiased mass spectrometry methods used to profile the HDL proteome to the most recent targeted methods that have enabled an unprecedented view of HDL metabolism. RECENT

findingsUnbiased global proteomics have demonstrated that the HDL proteome is organized into subgroups across the HDL size fractions providing further evidence that HDL functional heterogeneity is in part governed by its varying protein constituents. Parallel reaction monitoring, a novel targeted mass spectrometry method, was used to monitor the metabolism of HDL apolipoproteins in humans and revealed that apolipoproteins contained within the same HDL size fraction exhibit diverse metabolic properties. SUMMARY: Mass spectrometry provides a variety of tools and strategies to facilitate understanding, through its proteins, the complex biology of HDL.

Indexed as

AnimalsHumansLipoproteins, HDLMass SpectrometryProteomicsLipoproteins, HDL

Identifiers

PMID28002079
PMCPMC6211176
OpenAlexW2561996729

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.