Transcriptomic analysis of zebrafish prion protein mutants supports conserved cross-species function of the cellular prion protein

Despite the considerable body of research dedicated to the field of neurodegeneration, the gap in knowledge on the prion protein and its intricate involvement in brain diseases remains substantial. However, in the past decades, many steps forward have been taken toward a better understanding of the molecular mechanisms underlying both the physiological role of the prion protein and the misfolding event converting it into its pathological counterpart, the prion. This review aims to provide an overview of the main findings regarding this protein, highlighting the advantages of many different animal models that share a conserved amino acid sequence and/or structure with the human prion protein. A particular focus will be given to the species Danio rerio, a compelling research organism for the investigation of prion biology, thanks to its conserved orthologs, ease of genetic manipulation, and cost-effectiveness of high-throughput experimentation. We will explore its potential in filling some of the gaps on physiological and pathological aspects of the prion protein, with the aim of directing the future development of therapeutic interventions.

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Transcriptomic analysis of zebrafish prion protein mutants supports conserved cross-species function of the cellular prion protein

Abstract: Transcriptomic analysis of zebrafish prion protein mutants supports conserved cross-species function of the cellular prion protein,

Cited by 2 publications

References 67 publications

Zebrafish as a Model Organism for Studying Pathologic Mechanisms of Neurodegenerative Diseases and other Neural Disorders

Zebrafish as a Model Organism for Studying Pathologic Mechanisms of Neurodegenerative Diseases and other Neural Disorders

Comparing Prion Proteins Across Species: Is Zebrafish a Useful Model?

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