Results 51 to 60 of about 202,201 (346)
Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils
Nature Structural & Molecular Biology, 2020 Human islet amyloid polypeptide (hIAPP) functions as a glucose-regulating hormone but deposits as amyloid fibrils in more than 90% of patients with type II diabetes (T2D). Here we report the cryo-EM structure of recombinant full-length hIAPP fibrils. The
Q. Cao +4 more
semanticscholar +1 more source
The Cellular Prion Protein Increases the Uptake and Toxicity of TDP-43 Fibrils
Viruses, 2021 Cytoplasmic aggregation of the primarily nuclear TAR DNA-binding protein 43 (TDP-43) affects neurons in most amyotrophic lateral sclerosis (ALS) and approximately half of frontotemporal lobar degeneration (FTLD) cases.
Carlo Scialò +8 more
doaj +1 more source
Cryo-EM structure of alpha-synuclein fibrils
bioRxiv, 2018 Intracellular inclusions of alpha-synuclein are the neuropathological hallmark of progressive disorders called synucleinopathies. Alpha-synuclein fibrils are associated with transmissive cell-to-cell propagation of pathology.
R. Guerrero-Ferreira +7 more
semanticscholar +1 more source
mBio, 2019 Big defensins, ancestors of β-defensins, are composed of a β-defensin-like C-terminal domain and a globular hydrophobic ancestral N-terminal domain.
Karine Loth +16 more
doaj +1 more source
Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods
Molecules, 2020 The self-assembly of proteins is an essential process for a variety of cellular functions including cell respiration, mobility and division. On the other hand, protein or peptide misfolding and aggregation is related to the development of Parkinson’s ...
María Florencia Pignataro +2 more
doaj +1 more source
eLife, 2019 Intracellular inclusions rich in alpha-synuclein are a hallmark of several neuropathological diseases including Parkinson’s disease (PD). Previously, we reported the structure of alpha-synuclein fibrils (residues 1–121), composed of two protofibrils that
R. Guerrero-Ferreira +15 more
semanticscholar +1 more source
Mimiviruses Interfere With IκBα Degradation
Frontiers in Virology, 2022 Many aspects of giant viruses biology still eludes scientists, with viruses such as Acanthamoeba polyphaga mimivirus (APMV) and Tupanvirus (TPV) possessing large virions covered by fibrils and are cultivated in laboratories using Acanthamoeba cells as ...
Juliana dos Santos Oliveira +10 more
doaj +1 more source
Formation and properties of whey protein fibrils [PDF]
, 2011 Protein fibrils are threadlike aggregates that are about one molecule thick and more than thousand molecules long. Due to their threadlike structure they could potentially be used to form meat-like structures.
Kroes-Nijboer, A.
core
, 2016 We reported a facile method for preparing self-assembled noble metal nanoparticle chains by using lysozyme amyloid fibrils as a biotemplate in an aqueous environ‐ ment. The nanoparticle chains of gold (AuNPCs), palladi‐ um (PdNPCs), platinum (PtNPCs) and
Hou Li, Ziming Xu, Faming Gao, Lili Li
core +1 more source