Evidence map›Paper›PMID 28645735›Full record

ArticleJournal of structural biology2017

Serum amyloid A self-assembles with phospholipids to form stable protein-rich nanoparticles with a distinct structure: A hypothetical function of SAA as a "molecular mop" in immune response.

Nicholas M Frame, Shobini Jayaraman, Donald L Gantz, Olga Gursky

Open access · greenAbstract read
In one paragraph

Article in Journal of structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 27 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Nicholas M FrameDepartment of Physiology & Biophysics, Boston University School of Medicine, 700 Albany St., Boston, MA 02118, USA. Electronic address: nframe1@bu.edu.
Shobini JayaramanDepartment of Physiology & Biophysics, Boston University School of Medicine, 700 Albany St., Boston, MA 02118, USA. Electronic address: Shobini@bu.edu.
Donald L GantzDepartment of Physiology & Biophysics, Boston University School of Medicine, 700 Albany St., Boston, MA 02118, USA. Electronic address: Gantz@bu.edu.
Olga GurskyDepartment of Physiology & Biophysics, Boston University School of Medicine, 700 Albany St., Boston, MA 02118, USA. Electronic address: gursky@bu.edu.
Boston University · US

Funding

Structural Thermodynamics of Human Apolipoprotein C-1R01GM067260 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI GURSKY, OLGA · 2003 to 2024
$7.4M
Training Program in Cardiovascular Biology: Pre-DoctoralT32HL007969 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI RAVID, KATYA · 2003 to 2019
$3.2M
NHLBI NIH HHS T32 HL007969NIGMS NIH HHS R01 GM067260
6 · The paper itself

Abstract

Serum amyloid A (SAA) is an acute-phase protein whose action in innate immunity and lipid homeostasis is unclear. Most circulating SAA binds plasma high-density lipoproteins (HDL) and reroutes lipid transport. In vivo SAA binds existing lipoproteins or generates them de novo upon lipid uptake from cells. We explored the products of SAA-lipid interactions and lipoprotein remodeling in vitro. SAA complexes with palmitoyl-oleoyl phosphocholine (POPC) were analyzed for structure and stability using circular dichroism and fluorescence spectroscopy, electron microscopy, gel electrophoresis and gel filtration. The results revealed the formation of 8-11nm lipoproteins that were∼50% α-helical and stable at near-physiological conditions but were irreversibly remodeled at T

Indexed as

AnimalsCholesterolChromatography, GelCircular DichroismElectrophoresis, Polyacrylamide GelLipoproteins, HDLMiceMicroscopy, ElectronNanoparticlesParticle SizePhosphatidylcholinesPhospholipidsProtein StabilitySerum Amyloid A ProteinSpectrometry, Fluorescence1-palmitoyl-2-oleoylphosphatidylcholineCholesterolLipoproteins, HDLPhosphatidylcholinesPhospholipidsSerum Amyloid A ProteinClearance of dead cells and cell repairLipid homeostasis in acute-phase responseLipoprotein remodeling, fusion and fissionLipoprotein structure, function and stabilityProtein-lipid surface interactionsThermodynamic and kinetic stability

Identifiers

PMID28645735
PMCPMC6042646
OpenAlexW2680441691

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.