Evidence map›Paper›PMID 32035904›Full record

ArticleJournal of molecular biology2020

Structural Basis for Lipid Binding and Function by an Evolutionarily Conserved Protein, Serum Amyloid A.

Nicholas M Frame, Meera Kumanan, Thomas E Wales, Asanga Bandara, Marcus Fändrich, John E Straub, John R Engen, Olga Gursky

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.4field-weighted citation impact, top 16% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

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  8. Clinical characteristics of 25 death cases with COVID-19: A retrospective review of medical records in a single medical center, Wuhan, China.International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases · 2020
    Article
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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

8 authors at 3 institutions in 2 countries.

Nicholas M FrameDepartment of Physiology & Biophysics, Boston University School of Medicine, 700 Albany Street, Boston, MA, 02118, United States.
Meera KumananDepartment of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, MA, 02215, United States.
Thomas E WalesDepartment of Chemistry and Chemical Biology, Northeastern University, 360 Huntington Avenue, Boston, MA, 02115, United States.
Asanga BandaraDepartment of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, MA, 02215, United States.
Marcus FändrichInstitute of Protein Biochemistry, Ulm University, Ulm, 89081, Germany.
John E StraubDepartment of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, MA, 02215, United States. Electronic address: straub@bu.edu.
John R EngenDepartment of Chemistry and Chemical Biology, Northeastern University, 360 Huntington Avenue, Boston, MA, 02115, United States. Electronic address: J.Engen@northeastern.edu.
Olga GurskyDepartment of Physiology & Biophysics, Boston University School of Medicine, 700 Albany Street, Boston, MA, 02118, United States; Amyloidosis Treatment and Research Center, Boston University School of Medicine, Boston, MA, 02118, United States. Electronic address: gursky@bu.edu.
Boston University · USNortheastern University · USUniversität Ulm · DE

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
Probing the roles of membrane and cholesterol on Aβ biogenesis and prion protein interactionsR01GM107703 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI STRAUB, JOHN E., THIRUMALAI, DEVARAJAN · 2015 to 2022
$2.7M
Structure and Function of Serum Amyloid A in Health and DiseaseR01GM135158 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI Olga Gursky · 2020 to 2026
$2.4M
NHLBI NIH HHS T32 HL007969NIGMS NIH HHS R01 GM067260NIGMS NIH HHS R01 GM107703NIGMS NIH HHS R01 GM135158
6 · The paper itself

Abstract

Serum amyloid A (SAA) is a plasma protein that transports lipids during inflammation. To explore SAA solution conformations and lipid-binding mechanism, we used hydrogen-deuterium exchange mass spectrometry, lipoprotein reconstitution, amino acid sequence analysis, and molecular dynamics simulations. Solution conformations of lipid-bound and lipid-free mSAA1 at pH~7.4 agreed in details with the crystal structures but also showed important differences. The results revealed that amphipathic α-helices h1 and h3 comprise a lipid-binding site that is partially pre-formed in solution, is stabilized upon binding lipids, and shows lipid-induced folding of h3. This site sequesters apolar ligands via a concave hydrophobic surface in SAA oligomers. The largely disordered/dynamic C-terminal region is conjectured to mediate the promiscuous binding of other ligands. The h1-h2 linker region is predicted to form an unexpected β-hairpin that may represent an early amyloidogenic intermediate. The results help establish structural underpinnings for understanding SAA interactions with its key functional ligands, its evolutional conservation, and its transition to amyloid.

Indexed as

Protein ConformationAnimalsBinding SitesHydrophobic and Hydrophilic InteractionsLigandsMiceMolecular Dynamics SimulationPhosphatidylcholinesProtein FoldingSerum Amyloid A Protein1-palmitoyl-2-oleoylphosphatidylcholineLigandsPhosphatidylcholinesSerum Amyloid A Proteinhydrogen-deuterium exchange mass spectrometryinflammation and immunitylipoprotein nanoparticlemolecular dynamics simulationsβ-hairpin misfolding intermediate

Identifiers

PMID32035904
PMCPMC7225066
OpenAlexW3005187167

What OpenQuestion holds

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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.