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JournalISSN: 1933-6896

Prion 

Landes Bioscience
About: Prion is an academic journal published by Landes Bioscience. The journal publishes majorly in the area(s): Protein aggregation & PRNP. It has an ISSN identifier of 1933-6896. It is also open access. Over the lifetime, 715 publications have been published receiving 16305 citations. The journal is also known as: prions & proteinaceous infectious particle.


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Journal ArticleDOI
01 May 2013-Prion
TL;DR: The estimate of outcrossing suggests that Saccharomyces cerevisiae is far more sexual than previously thought and would therefore be more responsive to the adaptive effects of natural selection compared with a strictly asexual yeast.
Abstract: Yeast prions are infectious proteins that spread exclusively by mating. The frequency of prions in the wild therefore largely reflects the rate of spread by mating counterbalanced by prion growth slowing effects in the host. We recently showed that the frequency of outcross mating is about 1% of mitotic doublings with 23–46% of total matings being outcrosses. These findings imply that even the mildest forms of the [PSI+], [URE3] and [PIN+] prions impart > 1% growth/survival detriment on their hosts. Our estimate of outcrossing suggests that Saccharomyces cerevisiae is far more sexual than previously thought and would therefore be more responsive to the adaptive effects of natural selection compared with a strictly asexual yeast. Further, given its large effective population size, a growth/survival detriment of > 1% for yeast prions should strongly select against prion-infected strains in wild populations of Saccharomyces cerevisiae.

804 citations

Journal Article
01 Jan 2008-Prion
TL;DR: In this article, it was shown that it is possible to transmit bovine spongiform encephalopathy (BSE) to a sheep by transfusion with whole blood taken from another sheep during the symptom-free phase of an experimental BSE infection.
Abstract: We have shown that it is possible to transmit bovine spongiform encephalopathy (BSE) to a sheep by transfusion with whole blood taken from another sheep during the symptom-free phase of an experimental BSE infection. BSE and variant Creutzfeldt-Jakob disease (vCJD) In human beings are caused by the same infectious agent, and the sheep-BSE experimental model has a similar pathogenesis to that of human vCJD. Although UK blood transfusions are leucodepleted--a possible protective measure against any risk from blood transmission--this report suggests that blood donated by symptom-free vCJD-infected human beings may represent a risk of spread of vCJD infection among the human population of the UK.

497 citations

Journal ArticleDOI
01 Jul 2008-Prion
TL;DR: This work will highlight the key scientific findings and discuss how the stability of amyloid fibrils impacts on bionanotechnology.
Abstract: Amyloid refers to the abnormal fibrous, extracellular, proteinaceous deposits found in organs and tissues. Amyloid is insoluble and is structurally dominated by beta-sheet structure. Unlike other fibrous proteins it does not commonly have a structural, supportive or motility role but is associated with the pathology seen in a range of diseases known as the amyloidoses. These diseases include Alzheimer's, the spongiform encephalopathies and type II diabetes, all of which are progressive disorders with associated high morbidity and mortality. Not surprisingly, research into the physicochemical properties of amyloid and its formation is currently intensely pursued. In this chapter we will highlight the key scientific findings and discuss how the stability of amyloid fibrils impacts on bionanotechnology.

385 citations

Journal Article
01 Jan 2013-Prion
TL;DR: There has been renewed interest in the possibility that the proteins causing neurodegeneration are all prions, which would profoundly influence the development of diagnostics and effective therapies.
Abstract: A profound change in thinking about the etiologies of many neurodegenerative diseases has far-reaching implications for developing therapeutics.

369 citations

Journal ArticleDOI
25 Nov 2008-Prion
TL;DR: This article focuses on the structure‑function relationship of the characterized highly repetitive spider silk spidroins and their conformational conversion from solution into fibers and is of crucial importance to understanding the intrinsic properties of spider silk.
Abstract: Biomaterials, having evolved over millions of years, often exceed man-made materials in their properties. Spider silk is one outstanding fibrous biomaterial which consists almost entirely of large proteins. Silk fibers have tensile strengths comparable to steel and some silks are nearly as elastic as rubber on a weight to weight basis. In combining these two properties, silks reveal a toughness that is two to three times that of synthetic fibers like Nylon or Kevlar. Spider silk is also antimicrobial, hypoallergenic and completely biodegradable. This article focuses on the structure-function relationship of the characterized highly repetitive spider silk spidroins and their conformational conversion from solution into fibers. Such knowedge is of crucial importance to understanding the intrinsic properties of spider silk and to get insight into the sophisticated assembly processes of silk proteins. This review further outlines recent progress in recombinant production of spider silk proteins and their assembly into distinct polymer materials as a basis for novel products.

276 citations

Performance
Metrics
No. of papers from the Journal in previous years
YearPapers
202314
202214
202121
202034
201924
201839