Evidence map›Paper›PMID 25749369›Full record

ReviewFEBS letters2015

Structural stability and functional remodeling of high-density lipoproteins.

Olga Gursky

Abstract readReview
In one paragraph

Review in FEBS letters, 2015. 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
4.0field-weighted citation impact, top 6% 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

20 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Thermal Remodeling of Human HDL Particles Reveals Diverse Subspecies.Journal of the American Society for Mass Spectrometry · 2024
    Article
  3. Article
  4. Different Pathways of Cellular Cholesterol Efflux.Cell biochemistry and biophysics · 2022
    Review
  5. Review
  6. Article
  7. Article
  8. Effects of triacylglycerol on the structural remodeling of human plasma very low- and low-density lipoproteins.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Kinetic stability of membrane proteins.Biophysical reviews · 2017
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

1 author at 1 institution in 1 country.

Olga GurskyDepartment of Physiology & Biophysics, Boston University School of Medicine, W329, 700 Albany St., Boston, MA 02118, USA. Electronic address: gursky@bu.edu.
Boston University · US

Funding

STRUCTURE AND INTERACTIONS OF COMPLEX POLAR LIPIDSP01HL026335 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SMALL, DONALD M · 1985 to 2010
$23.1M
Structural Thermodynamics of Human Apolipoprotein C-1R01GM067260 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI GURSKY, OLGA · 2003 to 2024
$7.4M
STRUCTURAL THERMODYNAMICS OF HUMAN APOLIPOPROTEIN C 1R29HL061429 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI GURSKY, OLGA · 1999 to 2002
$341k
NHLBI NIH HHS P01 HL026335NHLBI NIH HHS R29 HL061429NIGMS NIH HHS GM067260NIGMS NIH HHS R01 GM067260
6 · The paper itself

Abstract

Lipoproteins are protein-lipid nanoparticles that transport lipids in circulation and are central in atherosclerosis and other disorders of lipid metabolism. Apolipoproteins form flexible structural scaffolds and important functional ligands on the particle surface and direct lipoprotein metabolism. Lipoproteins undergo multiple rounds of metabolic remodeling that is crucial to lipid transport. Important aspects of this remodeling, including apolipoprotein dissociation and particle fusion, are mimicked in thermal or chemical denaturation and are modulated by free energy barriers. Here we review the biophysical studies that revealed the kinetic mechanism of lipoprotein stabilization and unraveled its structural basis. The main focus is on high-density lipoprotein (HDL). An inverse correlation between stability and functions of various HDLs in cholesterol transport suggests the functional role of structural disorder. A mechanism for the conformational adaptation of the major HDL proteins, apoA-I and apoA-II, to the increasing lipid load is proposed. Together, these studies help understand why HDL forms discrete subclasses separated by kinetic barriers, which have distinct composition, conformation and functional properties. Understanding these properties may help improve HDL quality and develop novel therapies for cardiovascular disease.

Indexed as

Protein ConformationThermodynamicsCell MembraneHumansLipid BilayersLipoproteins, HDLModels, BiologicalModels, MolecularProtein BindingProtein StabilityLipid BilayersLipoproteins, HDLCholesterol transport and metabolismConformational ensembleLipid surface-binding proteinsThermodynamic and kinetic stability

Identifiers

PMID25749369
PMCPMC4561042
OpenAlexW2003377543

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.