Evidence map›Paper›PMID 39117048›Full record

ArticleBiochimica et biophysica acta. General subjects2024

Key charged residues influence the amyloidogenic propensity of the helix-1 region of serum amyloid A.

Marvin Bilog, Jayson Vedad, Charisse Capadona, Adam A Profit, Ruel Z B Desamero

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochimica et biophysica acta. General subjects, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

5 authors.

Marvin BilogDepartment of Chemistry and the Institute of Macromolecular Assembly, York College of the City University of New York, Jamaica, New York 11451, United States; PhD Programs in Biochemistry, Graduate Center of the City University of New York, NY, New York, 10016, United States.
Jayson VedadPhD Programs in Chemistry, Graduate Center of the City University of New York, NY, New York, 10016, United States; Chemistry and Biochemistry Department, Brooklyn College, 2900 Bedford Avenue, Brooklyn, New York, 11210, United States.
Charisse CapadonaDepartment of Chemistry and the Institute of Macromolecular Assembly, York College of the City University of New York, Jamaica, New York 11451, United States.
Adam A ProfitDepartment of Chemistry and the Institute of Macromolecular Assembly, York College of the City University of New York, Jamaica, New York 11451, United States; PhD Programs in Chemistry, Graduate Center of the City University of New York, NY, New York, 10016, United States; PhD Programs in Biochemistry, Graduate Center of the City University of New York, NY, New York, 10016, United States.
Ruel Z B DesameroDepartment of Chemistry and the Institute of Macromolecular Assembly, York College of the City University of New York, Jamaica, New York 11451, United States; PhD Programs in Chemistry, Graduate Center of the City University of New York, NY, New York, 10016, United States; PhD Programs in Biochemistry, Graduate Center of the City University of New York, NY, New York, 10016, United States. Electronic address: rdesamero@york.cuny.edu.

Funding

Probing the role of helix-1 in amyloid formation by serum amyloid AR15GM119040 · NIGMS · YORK COLLEGE · PI DESAMERO, RUEL Z B, PROFIT, ADAM A · 2016 to 2016
$493k
Helical Peptoids as Potential Amylin Aggregation InhibitorsR15GM134491 · NIGMS · YORK COLLEGE · PI PROFIT, ADAM A · 2019 to 2019
$491k
NIGMS NIH HHS R15 GM119040NIGMS NIH HHS R15 GM134491
6 · The paper itself

Abstract

Increased plasma levels of serum amyloid A (SAA), an acute-phase protein that is secreted in response to inflammation, may lead to the accumulation of amyloid in various organs thereby obstructing their functions. Severe cases can lead to a systemic disorder called AA amyloidosis. Previous studies suggest that the N-terminal helix is the most amyloidogenic region of SAA. Moreover, computational studies implicated a significant role for Arg-1 and the residue-specific interactions formed during the fibrillization process. With a focus on the N-terminal region of helix-1, SAA

Indexed as

Serum Amyloid A ProteinAmino Acid SequenceAmyloidAmyloidosisHumansMutationProtein AggregatesProtein Structure, SecondaryAmyloidProtein AggregatesSAA1 protein, humanSerum Amyloid A ProteinAA amyloidosisCircular dichroism spectroscopyFourier transform infrared spectroscopyMechanism of aggregationSerum amyloid aThioflavin T fluorescence assay

Identifiers

PMID39117048
PMCPMC11547331

What OpenQuestion holds

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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.