# name
Discovering Putative Prion-Like Proteins in Plasmodium falciparum: A Computational and Experimental Analysis

# metadata.dc.description.abstract[].value
Prions are a singular
                subset of proteins able to switch between a soluble conformation
                and a self-perpetuating amyloid state. Traditionally associated
                with neurodegenerative diseases, increasing evidence indicates
                that organisms exploit prion-like mechanisms for beneficial
                purposes. The ability to transit between conformations is
                encoded in the so-called prion domains, long disordered regions
                usually enriched in glutamine/asparagine residues.
                Interestingly, " - ", the parasite that causes the most virulent
                form of malaria, is exceptionally rich in proteins bearing long
                Q/N-rich sequence stretches, accounting for roughly 30% of the
                proteome. This biased composition suggests that these protein
                regions might correspond to prion-like domains (PrLDs) and
                potentially form amyloid assemblies. To investigate this
                possibility, we performed a stringent computational survey for
                Q/N-rich PrLDs on " - ". Our data indicate that \xE2\x88\xBC10%
                of " - " protein sequences have prionic signatures, and that
                this subproteome is enriched in regulatory proteins, such as
                transcription factors and RNA-binding proteins. Furthermore, we
                experimentally demonstrate for several of the identified PrLDs
                that, despite their disordered nature, they contain inner short
                sequences able to spontaneously self-assemble into amyloid-like
                structures. Although the ability of these sequences to nucleate
                the conformational conversion of the respective full-length
                proteins should still be demonstrated, our analysis suggests
                that, as previously described for other organisms, prion-like
                proteins might also play a functional role in P. falciparum.

# metadata.dc.source[].value
Articles publicats en revistes (ISGlobal)

# metadata.dc.title[].value
Discovering Putative Prion-Like Proteins in Plasmodium falciparum: A Computational and Experimental Analysis