Next Article in Journal
Hereditary Gastrointestinal Tumor Syndromes: When Risk Comes with Your Genes
Next Article in Special Issue
Editorial of Special Issue “Latest Multifactorial Developments on Neuropsychiatric Disorders and Manifestations”
Previous Article in Journal
Implications of a De Novo Variant in the SOX12 Gene in a Patient with Generalized Epilepsy, Intellectual Disability, and Childhood Emotional Behavioral Disorders
Previous Article in Special Issue
A Novel Mutation in Sacsin, p.Val1335IIe, May Cause Late-Onset Sacsinopathy Due to Haploinsufficiency
 
 
Font Type:
Arial Georgia Verdana
Font Size:
Aa Aa Aa
Line Spacing:
Column Width:
Background:
Review

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

by
Carter Sky Christensen
,
Sean Wang
,
Wenshu Li
,
Danyang Yu
and
Henry James Li
*
School of Arts and Sciences, New York University Shanghai, 567 West Yang Si Road, Shanghai 200122, China
*
Author to whom correspondence should be addressed.
Curr. Issues Mol. Biol. 2024, 46(7), 6423-6439; https://doi.org/10.3390/cimb46070384
Submission received: 23 May 2024 / Revised: 18 June 2024 / Accepted: 21 June 2024 / Published: 26 June 2024

Abstract

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) and Parkinson’s disease (PD). Both amyloid-β (Aβ) and hyperphosphorylated tau (p-tau) proteins behave in ways similar to those 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 largely focus on the dysregulation of protein homeostasis, self-replication, and protein aggregation, and this knowledge could contribute to diagnoses and treatments for the given NDs.
Keywords: prions; neurodegeneration; Alzheimer’s disease; protein homeostasis; aggregation; prion-like proteins; amyloid beta; hyperphosphorylated tau; alpha-synuclein prions; neurodegeneration; Alzheimer’s disease; protein homeostasis; aggregation; prion-like proteins; amyloid beta; hyperphosphorylated tau; alpha-synuclein

Share and Cite

MDPI and ACS Style

Christensen, C.S.; Wang, S.; Li, W.; Yu, D.; Li, H.J. Structural Variations of Prions and Prion-like Proteins Associated with Neurodegeneration. Curr. Issues Mol. Biol. 2024, 46, 6423-6439. https://doi.org/10.3390/cimb46070384

AMA Style

Christensen CS, Wang S, Li W, Yu D, Li HJ. Structural Variations of Prions and Prion-like Proteins Associated with Neurodegeneration. Current Issues in Molecular Biology. 2024; 46(7):6423-6439. https://doi.org/10.3390/cimb46070384

Chicago/Turabian Style

Christensen, Carter Sky, Sean Wang, Wenshu Li, Danyang Yu, and Henry James Li. 2024. "Structural Variations of Prions and Prion-like Proteins Associated with Neurodegeneration" Current Issues in Molecular Biology 46, no. 7: 6423-6439. https://doi.org/10.3390/cimb46070384

APA Style

Christensen, C. S., Wang, S., Li, W., Yu, D., & Li, H. J. (2024). Structural Variations of Prions and Prion-like Proteins Associated with Neurodegeneration. Current Issues in Molecular Biology, 46(7), 6423-6439. https://doi.org/10.3390/cimb46070384

Article Metrics

Back to TopTop