Results 141 to 150 of about 514,761 (295)

Fusion Proteins are Able to Form Amyloid Structure [PDF]

open access: bronze, 2012
Vitaly A. Balobanov   +5 more
openalex   +1 more source

A Prion‐Like Domain in EBV EBNA1 Promotes Phase Separation and Enables SRRM1 Splicing

open access: yesAdvanced Science, EarlyView.
This study discoveries that EBV EBNA1 behaves as a prion‐like protein, verified using cell‐based assays and the Saccharomyces cerevisiae Sup35p prion identification system. The prion‐like domain of EBNA1 drives liquid–liquid phase separation. EBNA1 interacts with the splicing factor SRSF1 to regulate the expression of the SRRM1 splicing isoforms ...
Xiaoyue Zhang   +17 more
wiley   +1 more source

Polyhalogenated Carbazole Impairs Dopaminergic Neurons through Dysregulation of Liquid–Liquid Phase Separation in Caenorhabditis elegans

open access: yesAdvanced Science, EarlyView.
Polyhalogenated carbazoles (PHCZ), persistent environmental contaminants, preferentially accumulate in neuronal tissues. Studies using Caenorhabditis elegans and human neuronal cell lines reveal that PHCZ induce dopaminergic neurodegeneration by promoting liquid–liquid phase separation of α‐synuclein, reducing condensate fluidity, impairing ...
Yuhang Luo   +13 more
wiley   +1 more source

Modulation of Biological Membranes Using Small-Molecule Compounds to Counter Toxicity Caused by Amyloidogenic Proteins

open access: yesMembranes
The transition of peptides or proteins along a misfolding continuum from soluble functional states to pathological aggregates, to ultimately deposit as amyloid fibrils, is a process that underlies an expanding group of human diseases—collectively known ...
Raina Marie Seychell   +2 more
doaj   +1 more source

Potentiating Cerebral Perfusion Normalizes Glymphatic Dynamics in Systemic Inflammation

open access: yesAdvanced Science, EarlyView.
LPS‐induced systemic inflammation increases glymphatic influx but delays cervical lymphatic drainage, accompanied by AQP4 depolarization and impaired glymphatic clearance. Enhancing cerebral blood flow via the inotropic agent levosimendan effectively restored AQP4 polarization, improving glymphatic flux and amyloid‐β clearance.
Ruoyu Zhao   +9 more
wiley   +1 more source

Are Women with Polycystic Ovary Syndrome at Increased Risk of Alzheimer Disease? Lessons from Insulin Resistance, Tryptophan and Gonadotropin Disturbances and Their Link with Amyloid-Beta Aggregation

open access: yesBiomolecules
Alzheimer disease, the leading cause of dementia, and polycystic ovary syndrome, one of the most prevalent female endocrine disorders, appear to be unrelated conditions.
Joachim Sobczuk   +4 more
doaj   +1 more source

Targeting Multilayered Metabolic Networks in Brain Diseases: Emerging Perspectives on Nanodelivery Strategies

open access: yesAdvanced Science, EarlyView.
Brain diseases involve multilayered metabolic disruptions that reshape cellular interactions and microenvironments. This review outlines core metabolic features across disease states and presents emerging nanodelivery strategies as precision tools to reprogram pathological metabolism.
Jingyi Zhou, Chen Jiang
wiley   +1 more source

Capillary Flow-Based One-Minute Quantification of Amyloid Proteolysis

open access: yesBiosensors
Quantifying the formation and decomposition of amyloid is a crucial issue in the development of new drugs and therapies for treating amyloidosis. The current technologies for grasping amyloid formation and decomposition include fluorescence analysis ...
Taeha Lee   +5 more
doaj   +1 more source

Structural and Functional Versatility of the Amyloidogenic Non‐Amidated Variant of the Antimicrobial Peptide Citropin 1.3

open access: yesAdvanced Science, EarlyView.
Citropin 1.3 is an antimicrobial peptide derived from amphibians that forms amyloid structures. Here, the structural and functional properties of citropin 1.3 are characterized. Using high‐resolution imaging approaches, a variety of canonical and undescribed fibril morphologies are identified.
Fabio Strati   +8 more
wiley   +1 more source

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