Results 111 to 120 of about 75,180 (286)

Nucleation Kinetics Reveals a Distinct Biological Function Space of Biomolecular Condensates

open access: yesAdvanced Science, EarlyView.
This study utilizes microfluidics to quantify the nucleation rates of dense liquid phases within dilute solutions and of the reverse process, in which dilute voids nucleate inside condensates. The interfacial tension is identified as the key determinant of both processes.
Leif‐Thore Deck   +5 more
wiley   +1 more source

Polyphenol Interactions with Amyloid Fibrils: A Molecular Docking Study

open access: yesEast European Journal of Physics
Polyphenols, a versatile group of naturally occurring compounds with many favorable biological properties currently attract increasing research interest in the context of their ability to inhibit the formation and to destabilize special protein ...
Uliana Malovytsia   +5 more
doaj   +1 more source

Domain swapping and amyloid fibril conformation [PDF]

open access: yes, 2012
For several different proteins an apparent correlation has been observed between the propensity for dimerization by domain-swapping and the ability to aggregate into amyloid-like fibrils.
Van Der Wel, PCA
core   +1 more source

Brain and Liver Dual‐Targeting Oridonin Nanoparticles to Enhance Aβ Clearance for Alzheimer's Disease Therapy

open access: yesAdvanced Science, EarlyView.
We developed a nanoparticle named OAF, which simultaneously targeted to both the brain and liver via the transferrin receptor 1 (TfR1) receptor, promoting lipoprotein receptor‐related protein 1 (LRP1) expression to enhance amyloid‐beta (Aβ) clearance. In AD mice model, OAF significantly reduced Aβ deposition and cognitive impairment, while a mitigating
Wenshuai Gong   +8 more
wiley   +1 more source

Orthogonal Ionic Liquid‐Based Extraction Strategy Enables Amyloid‐Specific Profiling of Aggregate Proteome

open access: yesAdvanced Science, EarlyView.
An orthogonal ionic‐liquid extraction (Orth‐iEA) enables selective isolation of amyloid fibrils. TMGBF4 disrupts hydrogen‐bonded β‐sheet networks to solubilize amyloid aggregates, whereas C12ImCl interacts with hydrophobic regions of non‐amyloid proteins.
Shiying Zheng   +10 more
wiley   +1 more source

Dimensionality of Carbon Nanomaterials Determines the Binding and Dynamics of Amyloidogenic Peptides: Multiscale Theoretical Simulations [PDF]

open access: yes, 2013
Experimental studies have demonstrated that nanoparticles can affect the rate of protein self-assembly, possibly interfering with the development of protein misfolding diseases such as Alzheimer's, Parkinson's and prion disease caused by aggregation and ...
A Albanese   +88 more
core   +4 more sources

Smart Nanotechnologies for Multimodal Neuromodulation and Brain Interfacing

open access: yesAdvanced Science, EarlyView.
Recent advances in smart nanotechnologies are expanding the toolbox for brain interfacing, from wireless neuromodulation and high‐resolution sensing to targeted delivery within the central nervous system. By combining responsive nanomaterials with bioinspired design, these platforms enable multimodal interactions with neurons and glia, while also ...
Tommaso Curiale   +6 more
wiley   +1 more source

Nanoplastics and Neurodegeneration: A Roadmap From Mechanism to Causation

open access: yesAdvanced Science, EarlyView.
Nanoplastics are pervasive environmental contaminants with potentially profound implications for human health. Emerging evidence suggests a possible link between nanoplastic exposure and neurodegeneration, a key driver of ageing and dementia, yet causality remains unresolved.
Yuhuan Li   +5 more
wiley   +1 more source

Sensing and Filtering Environmental Fluctuations: The Case of Biomolecular Condensates in Plants

open access: yesAdvanced Science, EarlyView.
The diversity of plant condensates reflects constraints of sessile organisms to coordinate postembryonic development with environmental adaptation. This review examines how plants employ condensates to integrate temperature, light, redox, and nutrient signals.
Panagiotis N. Moschou, Dorothee Staiger
wiley   +1 more source

Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue

open access: yesNature Communications, 2019
Alzheimer’s disease is characterised by the deposition of Aβ amyloid fibrils and tau protein neurofibrillary tangles. Here the authors use cryo-EM to structurally characterise brain derived Aβ amyloid fibrils and find that they are polymorphic and right ...
Marius Kollmer   +9 more
doaj   +1 more source

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