Prion-like behavior has been in the spotlight since it was first associated with the onset of mammalian neurodegenerative diseases. However, a growing body of evidence suggests that this mechanism could be behind the regulation of processes such as transcription and translation in multiple species. Here, we perform a stringent computational survey to identify prion-like proteins in the human proteome. We detected 242 candidate polypeptides and computationally assessed their function, protein–protein interaction networks, tissular expression, and their link to disease. Human prion-like proteins constitute a subset of modular polypeptides broadly expressed across different cell types and tissues, significantly associated with disease, embedde...
Background The function of the prion protein, involved in the so-called prion disea...
Prions are a particular type of amyloids with the ability to self-perpetuate and propagate in vivo. ...
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2011.This electronic versi...
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammal...
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammal...
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammal...
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammal...
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammal...
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammal...
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammal...
Altres ajuts: ICREA-Academia 2020Prions are self-perpetuating proteins able to switch between a solu...
Prion proteins were initially associated with diseases such as Creutzfeldt Jakob and transmissible s...
Although disease-causing prions are an extreme pathogenic aberration in protein behavior, emerging e...
Altres ajuts: ICREA-Academia 2015 to S.V.Prion-like behaviour is attracting much attention due to th...
Prion diseases, or transmissible spongiform encephalopathies (TSE), are a group of rare fatal neurod...
Background The function of the prion protein, involved in the so-called prion disea...
Prions are a particular type of amyloids with the ability to self-perpetuate and propagate in vivo. ...
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2011.This electronic versi...
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammal...
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammal...
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammal...
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammal...
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammal...
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammal...
Prion-like behavior has been in the spotlight since it was first associated with the onset of mammal...
Altres ajuts: ICREA-Academia 2020Prions are self-perpetuating proteins able to switch between a solu...
Prion proteins were initially associated with diseases such as Creutzfeldt Jakob and transmissible s...
Although disease-causing prions are an extreme pathogenic aberration in protein behavior, emerging e...
Altres ajuts: ICREA-Academia 2015 to S.V.Prion-like behaviour is attracting much attention due to th...
Prion diseases, or transmissible spongiform encephalopathies (TSE), are a group of rare fatal neurod...
Background The function of the prion protein, involved in the so-called prion disea...
Prions are a particular type of amyloids with the ability to self-perpetuate and propagate in vivo. ...
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2011.This electronic versi...