Results 91 to 100 of about 3,255,404 (222)

What makes functional amyloids work? [PDF]

open access: yesCrit Rev Biochem Mol Biol, 2022
Siemer AB.
europepmc   +1 more source

A Coumarin-Based Array for the Discrimination of Amyloids

open access: yes
Self-assembly of misfolded proteins can lead to the formation of amyloids, which are implicated in the onset of many pathologies including Alzheimer’s disease and Parkinson’s disease.
Fiona M. McCutcheon (17903851)   +10 more
core   +1 more source

Beyond Primary Nucleation: Molecular Basis of Peptide Crystal Secondary Nucleation at Soft Interface

open access: yesAdvanced Functional Materials, EarlyView.
High spatiotemporal‐resolution atomic force microscopy directly resolved peptide secondary nucleation (SN) and growth characteristics and mechanisms on HOPG. The landscape of peptide nucleation sites, growth dynamics, molecular‐scale structures, phase transitions, and cross‐seeding processes were realized.
Linhao Sun   +2 more
wiley   +1 more source

Immunoprecipitation of amyloid fibrils by the use of an antibody that recognizes a generic epitope common to amyloid fibrils.

open access: yesPLoS ONE, 2014
Amyloid fibrils are associated with many maladies, including Alzheimer's disease (AD). The isolation of amyloids from natural materials is very challenging because the extreme structural stability of amyloid fibrils makes it difficult to apply ...
Erin R Greiner   +2 more
doaj   +1 more source

All‐Amyloid Functional Coacervates

open access: yesAdvanced Materials, EarlyView.
This study introduces an all‐amyloid interfacial complex coacervate technique that employs charge‐mediated or functionalization‐assisted complexation of oppositely charged food protein‐derived amyloid nanofibrils to engineer functional soft constructs across multiple length scales.
Seyyed Alireza Hashemi   +4 more
wiley   +1 more source

Identification of key amino acid residues modulating intracellular and in vitro microcin E492 amyloid formation

open access: yesFrontiers in Microbiology, 2016
Microcin E492 (MccE492) is a pore-forming bacteriocin produced and exported by Klebsiella pneumoniae RYC492. Besides its antibacterial activity, excreted MccE492 can form amyloid fibrils in vivo as well as in vitro.
Paulina eAguilera   +6 more
doaj   +1 more source

Amyloids: From molecular structure to mechanical properties [PDF]

open access: yes, 2013
Many proteins of diverse sequence, structure and function self-assemble into morphologically similar fibrillar aggregates known as amyloids. Amyloids are remarkable polymers in several respects.
Velikov, K.   +20 more
core   +1 more source

Culinary Chemistry as a Platform for Interfacial Materials Design

open access: yesAdvanced Materials Interfaces, EarlyView.
Culinary processes control interfaces through heating, shear, gelation, and molecular transport. This Review connects selected gastronomic examples with food‐derived nanomaterials, plasmonic sensing, anthocyanin photovoltaics, and intelligent packaging. Original agar‐based plasmonic films illustrate the proposed translation.
Josep Moreno   +12 more
wiley   +1 more source

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