Protein Misfolding and Functional Impairment in Neurodegenerative Diseases

Dear Colleagues,

Proteins play an integral role in almost every aspect of cellular processes. The problem of protein folding is a major concern in modern biology. Neurodegenerative diseases often involve the misfolding and aggregation of specific proteins, which leads to the formation of abnormal and harmful structures. While misfolded disease proteins primarily exert their effects through toxic gain-of-function and/or dominant-negative effects, instances of loss-of-function effects have also been recorded. Significant experimental efforts have been undertaken to comprehend the fundamental principles of folding and to unravel the mechanisms underlying misfolding and related diseases. Furthermore, computational techniques such as homology modeling and ab initio methods are widely applied in this direction. Recent progress in AI models such as AlphaFold and RoseTTAFold has significantly transformed the study of protein folding. Understanding the fundamentals of protein quality control and the relationships between structure and function can be instrumental in comprehending the mechanisms and pathological roles of disordered proteins.

This Special Issue intent to present recent studies that contribute to our understanding of protein misfolding, as well as on the role of functional impermeant in neurodegenerative diseases. Original research articles and reviews on molecular mechanisms, experimental and computational approaches for studying folding issues are expected and welcome.

Dr. Marios Krokidis
Dr. Themis Exarchos
Prof. Dr. Panayiotis Vlamos
Guest Editors

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• protein misfolding
• chaperones
• energy landscape
• neurodegenerative diseases
• amyloidogenesis
• intrinsically disordered proteins
• structure prediction algorithms
• bioinformatics
• molecular dynamic simulations