Evidence map›Paper›PMID 23327342›Full record

ArticleAmyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis2013

A novel method for quantifying peripheral tissue amyloid load by using the radiolabeled amyloidophilic peptide, p5.

Jonathan S Wall, Tina Richey, Sally Macy, Eric Heidel, Craig Wooliver, Stephen J Kennel

Abstract read
In one paragraph

Article in Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Article
  2. Thioflavin T in-gel staining forFrontiers in molecular biosciences · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Re-evaluating the potentials and limitations of (99m)Tc-aprotinin scintigraphy for amyloid imaging.American journal of nuclear medicine and molecular imaging · 2013
    Article
  9. 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

6 authors.

Jonathan S WallDepartment of Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN 37920, USA. jwall@utmck.edu
Tina Richey
Sally Macy
Eric Heidel
Craig Wooliver
Stephen J Kennel

Funding

Preclinical Diagnostic Imaging of AmyloidR01DK079984 · NIDDK · UNIVERSITY OF TENNESSEE KNOXVILLE · PI WALL, JONATHAN S · 2009 to 2016
$3.4M
NIDDK NIH HHS R01 DK079984NIDDK NIH HHS R01DK079984
6 · The paper itself

Abstract

Quantitation of peripheral amyloid deposits by non-invasive molecular imaging can be useful for diagnosis, prognostication and monitoring response to therapy. In order to obtain reliable quantitative data, it is necessary to show a linear positive correlation between the uptake of the molecular probe and the tissue amyloid load. The transgenic H-2/IL-6 mouse model of AA amyloidosis was used to generate animals with varied stages of visceral amyloid disease. The mice were injected with 125I-labeled peptide p5 and tissues analyzed 2 h post-injection using Congo red (CR) staining, radioisotope biodistribution and micro-autoradiography (ARG). Micro-ARG confirmed that 125I-p5 was deposited at all amyloid deposits and sites of Congophilia but not at amyloid-free sites within the tissues evaluated. Furthermore, biodistribution studies revealed that the amount of 125I deposited in liver and spleen correlated with the amount of CR birefringence (expressed as 0-4+ or as tissue area [µm2]) in these tissues with correlation coefficients of r > 0.7 (p < 10(-6)). Deposition of 125I-p5 is a quantitative measure of the amount of AA amyloid in liver and spleen in this mouse model. The p5 peptide has potential as a quantitative amyloid imaging agent in human disease.

Indexed as

Amino Acid SequenceAmyloidAmyloidosisAnimalsIodine RadioisotopesLiverMiceMice, TransgenicMolecular Sequence DataNerve Tissue ProteinsPeptide FragmentsSpleenAmyloidIodine RadioisotopesNerve Tissue Proteinsp5 protein, humanPeptide Fragments

Identifiers

PMID23327342
PMCPMC3710708

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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.