Many neurodegenerative diseases are characterized by aggregates of misfolded endogenous proteins in specific regions of the nervous system. Among these are Creutzfeldt–Jakob disease caused by the accumulation and aggregation of the prion protein PrPsc (prion) which can self-propagate by inducing the conformational conversion of the physiological isoform PrPc into PrPsc. Other diseases such as Parkinson's disease, Multiple System Atrophy, other synucleinopathies, Alzheimer's disease, Frontotemporal Dementia, Amyotrophic lateral sclerosis and other tauopathies are characterized by the accumulation and propagation of misfolded proteins aggregates; these aggregates can propagate from neuron-to-neuron in the CNS following a mechanism defined as prion-like protein, prionoid or quasi-prions depending on the properties shared with the prion such as infectivity or inter-individual transmissibility.
The purpose of this Research Topic is to collect studies that can contribute to understand the mechanisms by which prions and prion-like proteins are involved in the onset of neurodegenerative diseases. New data on different aspects of prion-like proteins such as protein structure, misfolding process, aggregation and precipitation mechanisms, cytotoxic effect and pathological effect at the nervous system level are required for a broader understanding of the pathophysiological mechanisms causing the onset of neurodegenerative disorders with a strong social impact. New information can contribute to the identification of new cellular mechanisms and to define new cellular and organismic models useful for the study of prion and prion-like proteins.
This Research Topic calls for original articles, reviews, and perspectives in relevant research fields on prion and prion-like proteins, including molecular evolution and structure variation in vertebrates, protein misfolding, precipitation and aggregation mechanism, cytotoxicity of prion-like protein aggregates and pathological effect on the nervous system.
Dr. Simona Eleuteri holds a patent (pharmacological chaperone to stabilize retromer complex in the CNS, EP19166534.8) with San Raffaele Hospital and has collaborations with Neuropore Therapies Company and Nestlè Company.
Many neurodegenerative diseases are characterized by aggregates of misfolded endogenous proteins in specific regions of the nervous system. Among these are Creutzfeldt–Jakob disease caused by the accumulation and aggregation of the prion protein PrPsc (prion) which can self-propagate by inducing the conformational conversion of the physiological isoform PrPc into PrPsc. Other diseases such as Parkinson's disease, Multiple System Atrophy, other synucleinopathies, Alzheimer's disease, Frontotemporal Dementia, Amyotrophic lateral sclerosis and other tauopathies are characterized by the accumulation and propagation of misfolded proteins aggregates; these aggregates can propagate from neuron-to-neuron in the CNS following a mechanism defined as prion-like protein, prionoid or quasi-prions depending on the properties shared with the prion such as infectivity or inter-individual transmissibility.
The purpose of this Research Topic is to collect studies that can contribute to understand the mechanisms by which prions and prion-like proteins are involved in the onset of neurodegenerative diseases. New data on different aspects of prion-like proteins such as protein structure, misfolding process, aggregation and precipitation mechanisms, cytotoxic effect and pathological effect at the nervous system level are required for a broader understanding of the pathophysiological mechanisms causing the onset of neurodegenerative disorders with a strong social impact. New information can contribute to the identification of new cellular mechanisms and to define new cellular and organismic models useful for the study of prion and prion-like proteins.
This Research Topic calls for original articles, reviews, and perspectives in relevant research fields on prion and prion-like proteins, including molecular evolution and structure variation in vertebrates, protein misfolding, precipitation and aggregation mechanism, cytotoxicity of prion-like protein aggregates and pathological effect on the nervous system.
Dr. Simona Eleuteri holds a patent (pharmacological chaperone to stabilize retromer complex in the CNS, EP19166534.8) with San Raffaele Hospital and has collaborations with Neuropore Therapies Company and Nestlè Company.
