Protein aggregation is a pathological feature in various neurodegenerative diseases and is thought to play a crucial role in the onset and progression of neurological disorders. This pathological phenomenon has attracted increasing attention from researchers, but the underlying mechanism has not been fully elucidated yet. Researchers are increasingly interested in identifying chemicals or methods that can effectively detect protein aggregation or maintain protein stability to prevent aggregation formation. To date, several methods are available for detecting protein aggregates, including fluorescence correlation spectroscopy, electron microscopy, and molecular detection methods. Unfortunately, there is still a lack of methods to observe protein aggregation in situ under a microscope. This article reviews the two main aspects of protein aggregation: the mechanisms and detection methods of protein aggregation. The aim is to provide clues for the development of new methods to study this pathological phenomenon.
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http://dx.doi.org/10.1016/j.jchemneu.2024.102420 | DOI Listing |
Curr Res Food Sci
December 2024
Medical Food Laboratory, Shanghai Key Laboratory of Pediatric Gastroenterology and Nutrition, Shanghai Institute for Pediatric Research, Xinhua Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200092, China.
In this work, three types of benzenedialdehydes (1,2-, 1,3-, and 1,4-BDAs) were used to prepare BDA-crosslinked gelatin nanoparticles and the 1,2-BDA-crosslinked gelatin nanoparticle was explored to stabilize fish oil-loaded Pickering emulsions. The nanoparticle preparation was dependent on both pH and crosslinker types. 1,2-BDA and preparation pH of 12.
View Article and Find Full Text PDFACS Pharmacol Transl Sci
January 2025
Department of Genetics and Microbiology, Charles University and Research Center BIOCEV, Pru°myslová 595, Vestec 252 50, Czech Republic.
The 26S proteasome degrades the majority of cellular proteins and affects all aspects of cellular life. Therefore, the 26S proteasome abundance, proper assembly, and activity in different life contexts need to be precisely controlled. Impaired proteasome activity is considered a causative factor in several serious disorders.
View Article and Find Full Text PDFMicrob Cell Fact
January 2025
Lab of Environmental and Life Sciences, University of Nova Gorica, Vipavska cesta 13, Nova Gorica, 5000, Slovenia.
Background: E. coli still remains the most commonly used organism to produce recombinant proteins in research labs. This condition is mirrored by the attention that researchers dedicate to understanding the biology behind protein expression, which is then exploited to improve the effectiveness of the technology.
View Article and Find Full Text PDFChromosome Res
January 2025
Saint-Petersburg State University, Saint-Petersburg, Russia.
Danio rerio, commonly known as zebrafish, is an established model organism for the developmental and cell biology studies. Although significant progress has been made in the analysis of the D. rerio genome, cytogenetic studies face challenges due to the unclear identification of chromosomes.
View Article and Find Full Text PDFNature
January 2025
Immuno-Oncology Service, Human Oncology and Pathogenesis Program, Memorial Sloan Kettering Cancer Center, New York, NY, USA.
Tertiary lymphoid structures (TLSs) are de novo ectopic lymphoid aggregates that regulate immunity in chronically inflamed tissues, including tumours. Although TLSs form due to inflammation-triggered activation of the lymphotoxin (LT)-LTβ receptor (LTβR) pathway, the inflammatory signals and cells that induce TLSs remain incompletely identified. Here we show that interleukin-33 (IL-33), the alarmin released by inflamed tissues, induces TLSs.
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