Results 41 to 50 of about 3,689,678 (299)
Bottom-up synthesis of protein-based nanomaterials from engineered β-solenoid proteins.
Biomolecular self-assembly is an emerging bottom-up approach for the synthesis of novel nanomaterials. DNA and viruses have both been used to create scaffolds but the former lacks chemical diversity and the latter lack spatial control.
Zeyu Peng +3 more
doaj +1 more source
Protein Fibrillation under Crowded Conditions
Protein amyloid fibrils have widespread implications for human health. Over the last twenty years, fibrillation has been studied using a variety of crowding agents to mimic the packed interior of cells or to probe the mechanisms and pathways of the process.
Annelise H. Gorensek-Benitez +2 more
openaire +3 more sources
β-microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH [PDF]
Although the molecular mechanisms underlying the pathology of amyloidoses are not well understood, the interaction between amyloid proteins and cell membranes is thought to play a role in several amyloid diseases. Amyloid fibrils of β-microglobulin (βm),
Eric W. Hewitt +49 more
core +1 more source
Bacteria develop a variety of extracellular fibrous structures crucial for their survival, such as flagella and pili. In this study, we use cryo-EM to identify protein fibrils surrounding lab-cultured Bacillus amyloiquefaciens and discover an unreported ...
Yijia Cheng +4 more
doaj +1 more source
Bacterial inclusion bodies contain amyloid-like structure. [PDF]
Protein aggregation is a process in which identical proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as amorphous, lacking any long-range order, or highly ordered fibrils. Protein fibrils can
Lei Wang +4 more
doaj +1 more source
Protein Biomarkers and Risk of Atrial Fibrillation [PDF]
Background: Identification of protein biomarkers associated with incident atrial fibrillation (AF) may improve the understanding of the pathophysiology, risk prediction, and development of new therapeutics for AF.
Laila, Staerk +7 more
openaire +2 more sources
Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates
Although the function of biopolymer hydrogels in nature depends on structural anisotropy at mesoscopic length scales, the self-assembly of such anisotropic structures in vitro is challenging.
Slav A. Semerdzhiev +3 more
doaj +1 more source
Amyloidogenic cross-seeding of Tau protein: Transient emergence of structural variants of fibrils. [PDF]
Amyloid aggregates of Tau protein have been implicated in etiology of many neurodegenerative disorders including Alzheimer's disease (AD). When amyloid growth is induced by seeding with preformed fibrils assembled from the same protein, structural ...
Bartosz Nizynski +5 more
doaj +1 more source
Prediction of Amyloid Fibril-forming Proteins [PDF]
In Alzheimer's disease and spongiform encephalopathies proteins transform from their native states into fibrils. We find that several amyloid-forming proteins harbor an alpha-helix in a polypeptide segment that should form a beta-strand according to secondary structure predictions.
Y, Kallberg +4 more
openaire +2 more sources
Top-down Approach to Produce Protein Functionalized and Highly Thermally Stable Cellulose Fibrils [PDF]
Protein-functionalized cellulose fibrils, having various amounts of covalently bonded proteins at their surface, were successfully extracted from the tunic of Pyura chilensis tunicates using successive alkaline extractions.
Yadong Zhao +13 more
core +2 more sources

