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期刊名:Prion

缩写:PRION

ISSN:1933-6896

e-ISSN:1933-690X

IF/分区:1.7/Q4

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共收录本刊相关文章索引737
Clinical Trial Case Reports Meta-Analysis RCT Review Systematic Review
Classical Article Case Reports Clinical Study Clinical Trial Clinical Trial Protocol Comment Comparative Study Editorial Guideline Letter Meta-Analysis Multicenter Study Observational Study Randomized Controlled Trial Review Systematic Review
Carsten Korth Carsten Korth
Chronic mental diseases (CMD) like the schizophrenias are progressive diseases of heterogenous but poorly understood biological origin. An imbalance in proteostasis is a hallmark of dysfunctional neurons, leading to impaired clearance and a...
Silvia Sisó,Francesca Chianini,Sam L Eaton et al. Silvia Sisó et al.
Prion diseases exhibit different disease phenotypes in their natural hosts and when transmitted to rodents, and this variability is regarded as indicative of prion strain diversity. Phenotypic characterization of scrapie strains in sheep ca...
Christina D Orrù,Jason M Wilham,Sarah Vascellari et al. Christina D Orrù et al.
The ability of abnormal TSE-associated forms of PrP to seed the formation of amyloid fibrils from recombinant PrP(Sen) has served as the basis for several relatively rapid and highly sensitive tests for prion diseases. These tests include r...
Justin K Hines,Takashi Higurashi,Mathangi Srinivasan et al. Justin K Hines et al.
Prions of budding yeast serve as a tractable model of amyloid behavior. Here we address the issue of the effect of yeast strain variation on prion stability, focusing also on the effect of amyloid conformation and the involvement of the co-...
Zhiqiang Du Zhiqiang Du
Prions are infectious proteins with altered conformations converted from otherwise normal host proteins. While there is only one known mammalian prion protein, PrP, a handful of prion proteins have been identified in the yeast Saccharomyces...
Hiroshi Kurahashi,Keita Oishi,Yoshikazu Nakamura Hiroshi Kurahashi
Prions are infectious, self-propagating protein conformations. [PSI+], [RNQ+] and [URE3] are well characterized prions in Saccharomyces cerevisiae and represent the aggregated states of the translation termination factor Sup35, a functional...
Elina Radchenko,Tatyana Rogoza,Maria Khokhrina et al. Elina Radchenko et al.
[ISP+] is a prion form of the global transcriptional regulator Sfp1 in Saccharomyces cerevisiae that manifests phenotypically as an antisuppressor of specific sup35 nonsense suppressor mutations. Although SUP35 is a Sfp1 target, the mechani...
Margery L Evans,Jens C Schmidt,Marianne Ilbert et al. Margery L Evans et al.
Amyloid formation is an ordered aggregation process, where β-sheet rich polymers are assembled from unstructured or partially folded monomers. We examined how two Escherichia coli cytosolic chaperones, DnaK and Hsp33, and a more recently c...
Dmitry Kryndushkin,Frank Shewmaker Dmitry Kryndushkin
In recent years there have been several reports of human neurodegenerative diseases that involve protein misfolding being modeled in the yeast Saccharomyces cerevisiae. This review summarizes recent advances in understanding the specific me...
Reed B Wickner,Herman K Edskes,David Bateman et al. Reed B Wickner et al.
The yeast prions [URE3] and [PSI] are not found in wild strains, suggesting they are not an advantage. Prion-forming ability is not conserved, even within Saccharomyces, suggesting it is a disease. Prion domains have non-prion functions, ex...