The aggregation of the protein alpha-synuclein (α-SYN) is believed to be a critical event in Parkinson's disease (PD). α-SYN is characterized by a remarkable conformational plasticity, adopting different conformations depending on the environment. In vitro, α-SYN lacks a well-defined structure. Therefore, it was classified as an 'intrinsically disordered protein'. A debate has recently begun over how α-SYN behaves in the cell: is it an intrinsically disordered protein or a stable tetramer with a low propensity for aggregation? In this review, we discuss the aggregation of α-SYN and describe factors that influence this process and their potential relevance in PD pathogenesis. We address the ways in which aggregated α-SYN mediates toxicity and might lead to PD, and propose possible therapeutic strategies.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.molmed.2013.04.002 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Lessons from Deep Learning Structural Prediction of Multistate Multidomain Proteins-The Case Study of Coiled-Coil NOD-like Receptors.
Int J Mol Sci
January 2025
Department of Bioinformatics and Structural Biochemistry, Institute of Biochemistry of the Romanian Academy, Splaiul Independentei 296, 060031 Bucharest, Romania.
We test here the prediction capabilities of the new generation of deep learning predictors in the more challenging situation of multistate multidomain proteins by using as a case study a coiled-coil family of Nucleotide-binding Oligomerization Domain-like (NOD-like) receptors from and a few extra examples for reference. Results reveal a truly remarkable ability of these platforms to correctly predict the 3D structure of modules that fold in well-established topologies. A lower performance is noticed in modeling morphing regions of these proteins, such as the coiled coils.
View Article and Find Full Text PDFA Novel Nitrite Reductase from for Efficient Degradation of Nitrite.
Biomolecules
January 2025
Xingzhi College, Zhejiang Normal University, Jinhua 321100, China.
Nitrite reductases play a crucial role in the nitrogen cycle, demonstrating significant potential for applications in the food industry and environmental remediation, particularly for nitrite degradation and detection. In this study, we identified a novel nitrite reductase (NiR) from a newly isolated denitrifying bacterium, YD01. We constructed a heterologous expression system using BL21/pET28a-Nir, which exhibited remarkable nitrite reductase enzyme activity of 29 U/mL in the culture broth, substantially higher than that reported for other strains.
View Article and Find Full Text PDFPaleAle 6.0: Prediction of Protein Relative Solvent Accessibility by Leveraging Pre-Trained Language Models (PLMs).
Biomolecules
January 2025
School of Computer Science, University College Dublin (UCD), D04 V1W8 Dublin, Ireland.
Predicting the relative solvent accessibility (RSA) of a protein is critical to understanding its 3D structure and biological function. RSA prediction, especially when homology transfer cannot provide information about a protein's structure, is a significant step toward addressing the protein structure prediction challenge. Today, deep learning is arguably the most powerful method for predicting RSA and other structural features of proteins.
View Article and Find Full Text PDFContribution of Phosphorylation Modification to Stability and Antibacterial Activity of Egg White Protein Nanogels Loaded with Cinnamon Bark Essential Oil.
Gels
December 2024
College of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China.
This study evaluated the potential usage of phosphorylated egg white protein (P-EWP) nanogels fabricated via microwave-induced phosphorylation modification and gel process and further ultrasonic nanometrization as novel delivery systems for cinnamon bark essential oil (CBEO). Compared to EWP-CBEO nanogels without chemical phosphorylation, the obtained P-EWP-CBEO nanogels have shown smaller average hydrodynamic diameter (133.6 nm), relatively uniform size distribution (polydispersity index around 0.
View Article and Find Full Text PDFEvolution of intrinsic disorder in the structural domains of viral and cellular proteomes.
Sci Rep
January 2025
Evolutionary Bioinformatics Laboratory, Department of Crop Sciences, University of Illinois, Urbana, IL, 61801, USA.
Intrinsically disordered regions are flexible regions that complement the typical structured regions of proteins. Little is known however about their evolution. Here we leverage a comparative and evolutionary genomics approach to analyze intrinsic disorder in the structural domains of thousands of proteomes.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!