Evidence map›Paper›PMID 25312451›Full record

ReviewVirus research2015

The diversity and relationship of prion protein self-replicating states.

Nina Klimova, Natallia Makarava, Ilia V Baskakov

Abstract readReview
In one paragraph

Review in Virus research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Modeling PrPFrontiers in bioengineering and biotechnology · 2020
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

3 authors.

Nina KlimovaCenter for Biomedical Engineering and Technology, University of Maryland School of Medicine, 725 W. Lombard St., Baltimore, MD 21201, USA; Department of Anatomy and Neurobiology, University of Maryland School of Medicine, 725 W. Lombard St., Baltimore, MD 21201, USA.
Natallia MakaravaCenter for Biomedical Engineering and Technology, University of Maryland School of Medicine, 725 W. Lombard St., Baltimore, MD 21201, USA; Department of Anatomy and Neurobiology, University of Maryland School of Medicine, 725 W. Lombard St., Baltimore, MD 21201, USA.
Ilia V BaskakovCenter for Biomedical Engineering and Technology, University of Maryland School of Medicine, 725 W. Lombard St., Baltimore, MD 21201, USA; Department of Anatomy and Neurobiology, University of Maryland School of Medicine, 725 W. Lombard St., Baltimore, MD 21201, USA. Electronic address: Baskakov@umaryland.edu.

Funding

Self-Propagating Mechanism of Prion DiseasesR01NS045585 · NINDS · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI Ilia V Baskakov · 2003 to 2026
$9.6M
Elucidating molecular structure of mammalian prionsR01NS074998 · NINDS · UNIVERSITY OF MARYLAND BALTIMORE · PI BASKAKOV, ILIA V · 2012 to 2015
$1.4M
Elucidating molecular structure of mammalian prionsR56NS074998 · NINDS · UNIVERSITY OF MARYLAND BALTIMORE · PI BASKAKOV, ILIA V · 2011 to 2011
$405k
NINDS NIH HHS NS045585NINDS NIH HHS NS074998NINDS NIH HHS R01 NS045585NINDS NIH HHS R01 NS074998NINDS NIH HHS R56 NS074998
6 · The paper itself

Abstract

It has become evident that the prion protein (PrP) can form a diverse range of self-replicating structures in addition to bona fide PrP(Sc) or strain-specific PrP(Sc) variants. Some self-replicating states can be only produced in vitro, whereas others can be formed in vivo and in vitro. While transmissible, not all states that replicate in vivo are truly pathogenic. Some of them can replicate silently without causing symptoms or clinical diseases. In the current article we discuss the data on PK-digestion patterns of different self-replicating PrP states in connection with other structural data available to date and assess possible relationships between different self-replicating states. Even though different self-replicating PrP states appear to have significantly different global folding patterns, it seems that the C-terminal region exhibits a cross-β-sheet structure in all self-replicating states, as this region acquires the proteolytically most stable conformation. We also discuss the possibility of the transformation of self-replicating states and triggering of PrP(Sc) formation within the frame of the deformed templating model. The spread of silent self-replicating states is of a particular concern because they can lead to transmissible prion disease. Moreover, examples on how different replication requirements favor different states are discussed. This knowledge can help in designing conditions for selective amplification of a particular PrP state in vitro.

Indexed as

AnimalsHumansPrionsProtein FoldingProteostasis DeficienciesPrionsAmyloid fibrilsDeformed templatingPrion diseasesPrion proteinProtein misfolding cyclic amplificationSynthetic prions

Identifiers

PMID25312451
PMCPMC4395513

What OpenQuestion holds

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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.