Results 311 to 320 of about 288,605 (343)
Some of the next articles are maybe not open access.
Preparative Biochemistry, 1982
An amyloid fibril isolation procedure is proposed which uses citrate as well as saline washes to dissociate the calcium dependent linkage of amyloid P-component (AP) from the amyloid fibril. In two amyloid rich tissues, the amount of AP was quantitated in each saline and citrate wash and totalled 13.8% and 20.8% of the amyloid fibrils isolated.
M, Skinner +3 more
openaire +2 more sources
An amyloid fibril isolation procedure is proposed which uses citrate as well as saline washes to dissociate the calcium dependent linkage of amyloid P-component (AP) from the amyloid fibril. In two amyloid rich tissues, the amount of AP was quantitated in each saline and citrate wash and totalled 13.8% and 20.8% of the amyloid fibrils isolated.
M, Skinner +3 more
openaire +2 more sources
Structural mechanism for specific binding of chemical compounds to amyloid fibrils
Nature Chemical Biology, 2023Youqi Tao +11 more
semanticscholar +1 more source
Mesoscopic Properties of Semiflexible Amyloid Fibrils
Langmuir, 2004We have determined the contour length, persistence length, bending rigidity, and critical percolation concentration for semiflexible amyloid fibrils formed from the globular proteins beta-lactoglobulin, bovine serum albumin, and ovalbumin. The persistence length was estimated using an adjusted random contact model for highly charged semiflexible chains.
Sagis, L.M.C. +2 more
openaire +3 more sources
Inhibitors of amyloid fibril formation
Many diseases are caused by misfolded and denatured proteins, leading to neurodegenerative diseases. In recent decades researchers have developed a variety of compounds, including polymeric inhibitors and natural compounds, antibodies, and chaperones, to inhibit protein aggregation, decrease the toxic effects of amyloid fibrils, and facilitate ...Elaheh, Tavili +2 more
openaire +2 more sources
Biotechnological applications of amyloid fibrils
Protein aggregates and amyloid fibrils have special qualities and are used in a variety of biotechnological applications. They are extensively employed in bioremediation, biomaterials, and biocatalysis. Because of their capacity to encapsulate and release pharmaceuticals and their sensitivity to certain molecules, respectively, they are also used in ...Mohsen, Nabi Afjadi +3 more
openaire +2 more sources
Amyloid Neuropathy: Relationship between Amyloid Fibrils and Macrophages
Ultrastructural Pathology, 1984A case of amyloid neuropathy associated with a multiple myeloma IgG light chain is reported. Under light microscopy the peripheral nerve exhibited several amyloid deposits. Electron microscopy revealed numerous amyloid deposits; at their periphery, macrophagic histiocytes were observed, containing a few tufts of parallel fibrils in their cytoplasm.
A, Vital, C, Vital
openaire +2 more sources
Self-Assembly of Ovalbumin into Amyloid and Non-Amyloid Fibrils
Biomacromolecules, 2012We study the fibrillation pathway of ovalbumin protein and report the simultaneous formation of several types of fibrils, with clear structural and physical differences. We compare the fibrillation mechanisms at low pH with and without salt, and follow the kinetics of fibrils growth by atomic force microscopy (AFM), static and dynamic light scattering (
Lara C +4 more
openaire +3 more sources
Amyloid Fibrils in Bionanotechnology
Australian Journal of Chemistry, 2004An amyloid fibril is a highly ordered, insoluble form of protein that results when a normally soluble protein aggregates via a self-association process to form a structured nanotube. Such fibrils can now be routinely generated from purified proteins in the laboratory, and have attracted burgeoning interest due to their role in a variety of disease ...
Sarah H. Waterhouse, Juliet A. Gerrard
openaire +1 more source

