Results 151 to 160 of about 516,976 (376)
Protein can undergo liquid–liquid phase separation and liquid‐to‐solid transition to form liquid condensates and solid aggregates. These phase transitions can be influenced by post‐translational modifications, mutations, and various environmental factors.
Tianchen Li+3 more
wiley +1 more source
A Cubic Equation of State for Amyloid Plaque Formation [PDF]
Protein function depends on both protein structure and amino acid (aa) sequence. Here we show that modular features of both structure and function can be quantified from the aa sequence alone for the amyloid 770 aa precursor protein A4. Both the new second order hydropathicity scale, based on evolutionary optimization (self-organized criticality), and ...
arxiv
A NEW AND MORE PERMANENT METHOD OF MOUNTING AMYLOID SECTIONS, STAINED WITH IODINE. [PDF]
AlanB. Green
openalex +1 more source
Manipulating the Assembly and Architecture of Fibrillar Silk
In this study, advanced in situ AFM, PiFM, and Cryo‐EM are leveraged to realize in situ observations of nucleation, growth, and degradation of silk nanofibrils. A clear picture of the assembly and structural evolution of regenerated silk nanofibrils is defined and demonstrates a novel strategy for manipulating their structure and properties, which ...
Chenyang Shi+3 more
wiley +1 more source
Fractal Scaling of Cortical Matter, Amyloid Fragmentation and Plaque Formation across Rodents and Primates [PDF]
Thermodynamic tools are well suited to connecting evolution of protein functionalities to mutations of amino acid sequences, especially for neuronal network structures. These tools enable one to quantify changes in modular structure and correlate them with corresponding changes in observable properties.
arxiv
A hydrophilic, stretchable, nonwoven electrospun fiber mat targeted to be applied in long‐term bioelectronic devices. By incorporating amphiphilic polyethylene glycol block copolymers in a polydimethylsiloxane matrix, the material develops stable hydrophilicity, enhanced breathability, as well as enhanced adhesion to cells.
Joab S. Dorsainvil+7 more
wiley +1 more source
Quantitative diagnosis of amyloid without Congo red staining using polarized light microscopy [PDF]
Amyloidosis is a protein misfolding disease caused by the deposition of large, insoluble aggregates (amyloid fibrils) of protein in a tissue, which has been associated with various conditions, such as lymphoid disorders, Alzheimer's disease, diabetes mellitus type 2, chronic inflammatory processes, and cancers. Amyloid fibrils are commonly diagnosed by
arxiv
An evaluation of current methods for the diagnostic histochemistry of amyloid [PDF]
H. John Cooper
openalex +1 more source
Thermodynamics of beta-amyloid fibril formation
Amyloid fibers are aggregates of proteins. They are built out of a peptide called $\beta$--amyloid (A$\beta$) containing between 41 and 43 residues, produced by the action of an enzyme which cleaves a much larger protein known as the Amyloid Precursor ...
F. Simona+4 more
core +1 more source