Evidence map›Paper›PMID 28928748›Full record

ArticleFrontiers in immunology2017

A Peptide-Fc Opsonin with Pan-Amyloid Reactivity.

James S Foster, Angela D Williams, Sallie Macy, Tina Richey, Alan Stuckey, Daniel Craig Wooliver, Richa Koul-Tiwari, Emily B Martin, Stephen J Kennel, Jonathan S Wall

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Immunoglobulin light chain amyloid aggregation.Chemical communications (Cambridge, England) · 2018
    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

10 authors at 2 institutions in 1 country.

James S FosterDepartment of Medicine, University of Tennessee Medical Center, Knoxville, TN, United States.
Angela D WilliamsDepartment of Medicine, University of Tennessee Medical Center, Knoxville, TN, United States.
Sallie MacyDepartment of Medicine, University of Tennessee Medical Center, Knoxville, TN, United States.
Tina RicheyDepartment of Medicine, University of Tennessee Medical Center, Knoxville, TN, United States.
Alan StuckeyDepartment of Radiology, University of Tennessee Medical Center, Knoxville, TN, United States.
Daniel Craig WooliverDepartment of Medicine, University of Tennessee Medical Center, Knoxville, TN, United States.
Richa Koul-TiwariDepartment of Medicine, University of Tennessee Medical Center, Knoxville, TN, United States.
Emily B MartinDepartment of Medicine, University of Tennessee Medical Center, Knoxville, TN, United States.
Stephen J KennelDepartment of Medicine, University of Tennessee Medical Center, Knoxville, TN, United States.
Jonathan S WallDepartment of Medicine, University of Tennessee Medical Center, Knoxville, TN, United States.
University of Tennessee at Knoxville · USUniversity of Tennessee Medical Center · US

Funding

Preclinical Diagnostic Imaging of AmyloidR01DK079984 · NIDDK · UNIVERSITY OF TENNESSEE KNOXVILLE · PI WALL, JONATHAN S · 2009 to 2016
$3.4M
NIDDK NIH HHS R01 DK079984
6 · The paper itself

Abstract

There is a continuing need for therapeutic interventions for patients with the protein misfolding disorders that result in systemic amyloidosis. Recently, specific antibodies have been employed to treat AL amyloidosis by opsonizing tissue amyloid deposits thereby inducing cell-mediated dissolution and organ improvement. To develop a pan-amyloid therapeutic agent, we have produced an Fc-fusion product incorporating a peptide, p5, which binds many if not all forms of amyloid. This protein, designated Fcp5, expressed in mammalian cells, forms the desired bivalent dimer structure and retains pan-amyloid reactivity similar to the p5 peptide as measured by immunosorbent assays, immunohistochemistry, surface plasmon resonance, and pulldown assays using radioiodinated Fcp5. Additionally, Fcp5 was capable of opsonizing amyloid fibrils

Indexed as

AA amyloidamyloidosisFc-fusionpeptide p5phagocytosis

Identifiers

PMID28928748
PMCPMC5591422
OpenAlexW2752294240

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.