Synthesis of double-fluorescent labeled prion protein for FRET analysis

Hosokawa-Muto, Junji; Yamaguchi, Keiichi; Kamatari, Yuji O.; Kuwata, Kazuo

doi:10.1080/09168451.2015.1050991

“…The App NL-G-F/NL-G-F mouse model developed by Sakakibara and colleagues poses the potential to serve as a good base for developing therapeutic treatments for AD-related Aβ plaque formations [56]. Beyond just developing new animal models with better human accuracy, there needs to be a way to trace the presence of the proteins within humans, such as developing ways to flag the proteins, such as what Hosokawa-Muto, J. et al did in order to perform FRET analysis on the protein, albeit this method was used in an attempt to elucidate structural information [57].…”

Section: Pharmaceutical-based and Therapeutic-based Treatment Methodsmentioning

confidence: 99%

Structural Variations of Prions and Prion-Like Proteins Associated with Neurodegeneration

Christensen,

Li,

Yu

et al. 2023

Preprint

0

View full text Add to dashboard Cite

Neurodegeneration is becoming one of the leading causes of death worldwide as the population expands and grows older. There is a growing desire to understand the mechanisms behind prion proteins as well as the prion-like proteins that make up neurodegenerative diseases (NDs) including Alzheimer’s Disease (AD). Both amyloid β (Aβ) and hyperphosphorylated tau (p-tau) proteins behave in ways similar to that of the infectious form of the prion protein, PrPSc, such as aggregating, seeding, and replicating under not yet fully understood mechanisms, thus the designation of prion-like. This review aims to highlight the shared mechanisms between prion-like proteins and prion proteins in the structural variations associated with aggregation and disease development. These mechanisms are largely focusing on the dysregulation of protein homeostasis, self-replication, and protein aggregation, and how this knowledge could contribute to diagnoses and treatments for the given NDs.

show abstract

“…The App NL-G-F/NL-G-F mouse model developed by Sakakibara and colleagues poses the potential to serve as a good base for developing therapeutic treatments for AD-related Aβ plaque formations [74]. Beyond just developing new animal models with better human accuracy, there needs to be a way to trace the presence of the proteins within humans, such as developing ways to flag the proteins, such as what Hosokawa-Muto, J. et al did in order to perform FRET analysis on the protein, albeit this method was used in an attempt to elucidate structural information [75].…”

Section: Pharmaceutical-based and Therapeutic-based Treatment Methodsmentioning

confidence: 99%

Structural Variations of Prions and Prion-Like Proteins Associated with Neurodegeneration

Christensen,

Li,

Yu

et al. 2023

Preprint

0

View full text Add to dashboard Cite

Neurodegeneration is becoming one of the leading causes of death worldwide as the population expands and grows older. There is a growing desire to understand the mechanisms behind prion proteins as well as the prion-like proteins that make up neurodegenerative diseases (NDs) including Alzheimer’s Disease (AD). Both amyloid β (Aβ) and hyperphosphorylated tau (p-tau) proteins behave in ways similar to that of the infectious form of the prion protein, PrPSc, such as aggregating, seeding, and replicating under not yet fully understood mechanisms, thus the designation of prion-like. This review aims to highlight the shared mechanisms between prion-like proteins and prion proteins in the structural variations associated with aggregation and disease development. These mechanisms are largely focusing on the dysregulation of protein homeostasis, self-replication, and protein aggregation, and how this knowledge could contribute to diagnoses and treatments for the given NDs.

show abstract

Expression and purification of single cysteine-containing mutant variants of the mouse prion protein by oxidative refolding

Sengupta

¹

,

Udgaonkar

²

2017

Protein Expression and Purification

View full text Add to dashboard Cite

Synthesis of double-fluorescent labeled prion protein for FRET analysis

Cited by 5 publications

References 37 publications

Structural Variations of Prions and Prion-Like Proteins Associated with Neurodegeneration

Structural Variations of Prions and Prion-Like Proteins Associated with Neurodegeneration

Structural Variations of Prions and Prion-Like Proteins Associated with Neurodegeneration

Expression and purification of single cysteine-containing mutant variants of the mouse prion protein by oxidative refolding

Contact Info

Product

Resources

About