Evidence map›Paper›PMID 23438476›Full record

ArticleThe American journal of pathology2013

Convergent replication of mouse synthetic prion strains.

Sina Ghaemmaghami, David W Colby, Hoang-Oanh B Nguyen, Shigenari Hayashi, Abby Oehler, Stephen J DeArmond, Stanley B Prusiner

Open access · bronzeAbstract read
In one paragraph

Article in The American journal of pathology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Prion Strains and Transmission Barrier Phenomena.Pathogens (Basel, Switzerland) · 2018
    Review
  6. Review
  7. Review
  8. Article
  9. Biology and Genetics of PrP Prion Strains.Cold Spring Harbor perspectives in medicine · 2017
    Review
  10. Structural Biology of PrP Prions.Cold Spring Harbor perspectives in medicine · 2017
    Review
  11. Prion Strain Diversity.Cold Spring Harbor perspectives in medicine · 2016
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Drug resistance confounding prion therapeutics.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Article
  20. Changes in prion replication environment cause prion strain mutation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Sina GhaemmaghamiInstitute for Neurodegenerative Diseases, University of California San Francisco, San Francisco, California 94143-0518, USA.
David W Colby
Hoang-Oanh B Nguyen
Shigenari Hayashi
Abby Oehler
Stephen J DeArmond
Stanley B Prusiner
Institute for Neurodegenerative Disorders · USUniversity of California, San Francisco · US

Funding

VIRAL DEGENERATIVE DEMENTING DISEASE IN AGING (SUPP)P01AG002132 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 1985 to 2024
$51.7M
UNDERSTANDING AND IMPROVING SMALL MOLECULE INHIBITORS OF PRION REPLICATIONP01AG021601 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI PRUSINER, STANLEY B · 2003 to 2013
$31.9M
SYNTHETIC AND RECOMBINANT PRP PEPTIDES AND PROTEINSP01AG010770 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI PRUSINER, STANLEY B · 1993 to 2015
$30.3M
Towards Therapeutics for Neurodegenerative DiseasesR37AG031220 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI PRUSINER, STANLEY B · 2008 to 2017
$6.2M
NIA NIH HHS AG002132NIA NIH HHS AG021601NIA NIH HHS AG031220NIA NIH HHS AG10770NIA NIH HHS P01 AG002132NIA NIH HHS P01 AG010770NIA NIH HHS P01 AG021601NIA NIH HHS R37 AG031220
6 · The paper itself

Abstract

Prion diseases are neurodegenerative disorders characterized by the aberrant folding of endogenous proteins into self-propagating pathogenic conformers. Prion disease can be initiated in animal models by inoculation with amyloid fibrils formed from bacterially derived recombinant prion protein. The synthetic prions that accumulated in infected organisms are structurally distinct from the amyloid preparations used to initiate their formation and change conformationally on repeated passage. To investigate the nature of synthetic prion transformation, we infected mice with a conformationally diverse set of amyloids and serially passaged the resulting prion strains. At each passage, we monitored changes in the biochemical and biological properties of the adapting strain. The physicochemical properties of each synthetic prion strain gradually changed on serial propagation until attaining a common adapted state with shared physicochemical characteristics. These results indicate that synthetic prions can assume multiple intermediate conformations before converging into one conformation optimized for in vivo propagation.

Indexed as

AmyloidAnimalsBlotting, WesternCells, CulturedKaplan-Meier EstimateMiceMice, TransgenicPrionsProtein ConformationAmyloidPrions

Identifiers

PMID23438476
PMCPMC3586687
OpenAlexW2055046914

What OpenQuestion holds

Textmetadata
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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.