Evidence map›Paper›PMID 17046658›Full record

ReviewMethods in enzymology2006

Micro-imaging of amyloid in mice.

Jonathan S Wall, Michael J Paulus, Shaun Gleason, Jens Gregor, Alan Solomon, Stephen J Kennel

Open access · greenAbstract readReview
In one paragraph

Review in Methods in enzymology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. The pattern recognition reagents RAGE VC1 and peptide p5 share common binding sites and exhibit specific reactivity with AA amyloid in mice.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2016
    Article
  5. Article
  6. Article
  7. Article
  8. A novel method for quantifying peripheral tissue amyloid load by using the radiolabeled amyloidophilic peptide, p5.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2013
    Article
  9. Article
  10. Article
  11. Serum amyloid a protein in clinical cancer diagnosis.Pathology oncology research : POR · 2012
    Article
  12. Review
  13. Article
  14. Article
  15. Development and evaluation of agents for targeting visceral amyloid.Tijdschrift voor nu[c]leaire geneeskunde · 2011
    Article
  16. In vivo molecular imaging of peripheral amyloidosis using heparin-binding peptides.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  17. Article
  18. Article
  19. Article
  20. 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 at 1 institution in 1 country.

Jonathan S WallHuman Immunology and Cancer Program, University of Tennessee Graduate School of Medicine, Knoxville, 37920, USA.
Michael J Paulus
Shaun Gleason
Jens Gregor
Alan Solomon
Stephen J Kennel
Knoxville College · US

Funding

SPECT/CT Imaging of Systemic AA-Amyloidosis in MiceR01EB000789 · NIBIB · UNIVERSITY OF TENNESSEE KNOXVILLE · PI WALL, JONATHAN S · 2002 to 2005
$3.8M
NIBIB NIH HHS R01 EB000789
6 · The paper itself

Abstract

Scintigraphic imaging of radioiodinated serum amyloid P-component is a proven method for the clinical detection of peripheral amyloid deposits (Hawkins et al., 1990). However, the inability to perform comparably high-resolution studies in experimental animal models of amyloid disease has impacted not only basic studies into the pathogenesis of amyloidosis but also in the preclinical in vivo evaluation of potential anti-amyloid therapeutic agents. We have developed microimaging technologies, implemented novel computational methods, and established protocols to generate high-resolution images of amyloid deposits in mice. (125)I-labeled serum amyloid P component (SAP) and an amyloid-fibril reactive murine monoclonal antibody (designated 11-1F4) have been used successfully to acquire high-resolution single photon emission computed tomographic (SPECT) images that, when fused with x-ray computed tomographic (CT) data, have provided precise anatomical localization of secondary (AA) and primary (AL) amyloid deposits in mouse models of these diseases. This chapter will provide detailed protocols for the radioiodination and purification of amyloidophilic proteins and the generation of mouse models of AA and AL amyloidosis. A brief description of the available hardware and the parameters used to acquire high-resolution microSPECT and CT images is presented, and the tools used to perform image reconstruction and visualization that permit the analysis and presentation of image data are discussed. Finally, we provide established methods for measuring organ- and tissue-specific activities with which to corroborate the microSPECT and CT images.

Indexed as

AmyloidAmyloidosisAnimalsHumansIodine RadioisotopesMiceMice, TransgenicSerum Amyloid P-ComponentTomography, Emission-Computed, Single-PhotonAmyloidIodine RadioisotopesSerum Amyloid P-Component

Identifiers

PMID17046658
PMCPMC1805492
OpenAlexW1586856256

What OpenQuestion holds

Textmetadata
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.