Results 61 to 70 of about 202,201 (346)

Trypsin Induced Degradation of Amyloid Fibrils

open access: yes, 2021
Proteolytic enzymes are known to be involved in the formation and degradation of various monomeric proteins, but the effect of proteases on the ordered protein aggregates, amyloid fibrils, which are considered to be extremely stable, remains poorly ...
Irina Kuznetsova   +6 more
core   +1 more source

Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation

open access: yesFEBS Letters, EarlyView.
Peptides and antibodies occupy complementary therapeutic niches. Peptides recognize difficult targets in a compact format, while antibodies add specificity, long half‐life, and effector functions. This review examines strategies that merge both modalities—peptide grafting into loops, terminal and Fc fusions, and bioconjugation—highlighting how ...
Jinling Wang   +2 more
wiley   +1 more source

The role of autophagy in synucleinopathy: clearance versus spread of α-synuclein

open access: yesAutophagy Reports
Emerging evidence suggests that the propagation of α-synuclein pathology underlies the progression of Parkinson’s disease and supports the hypothesis that transmission of α-synuclein aggregates contributes to dopaminergic degeneration.
Emily Birnbaum, Zhenyu Yue
doaj   +1 more source

Impact of Aβ40 and Aβ42 Fibrils on the Transcriptome of Primary Astrocytes and Microglia

open access: yesBiomedicines, 2022
Fibrillar amyloid β-protein (Aβ) deposits in the brain, which are primarily composed of Aβ40 or Aβ42 peptides, are key pathological features of Alzheimer’s disease (AD) and related disorders. Although the underlying mechanisms are still not clear, the Aβ
Xiaoyue Zhu   +4 more
doaj   +1 more source

α‐synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicities

open access: yesJournal of Neurochemistry, 2019
This review article provides an overview of the different species that α‐synuclein aggregates can populate. It also attempts to reconcile conflicting views regarding the cytotoxic roles of oligomers versus fibrils.
P. Alam, L. Bousset, R. Melki, D. Otzen
semanticscholar   +1 more source

Supporting Data for Internal Structure of Methylcellulose Fibrils

open access: yes, 2018
Data files used to generate all figures in the manuscript "Internal Structure of Methylcellulose Fibrils" and its supplementary information.The collection of this data was supported primarily by the National Science Foundation through University of ...
Coughlin, McKenzie L   +8 more
core   +1 more source

The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation

open access: yesFEBS Letters, EarlyView.
Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge   +6 more
wiley   +1 more source

Transgenic Tobacco as a Bioreactor for the Production of Bioactive and Triple-Helical Recombinant Type III Collagen

open access: yesPlants
Collagen is the primary protein in the extracellular matrix of human cells and the body and is essential for cell structure and function. Here, for the first time, we report a method for producing recombinant triple-helical collagen type III (rhCOL3) in ...
Tairu Wu   +6 more
doaj   +1 more source

Ca2+-Induced Cold-Set Gelation of Whey Protein Isolate Fibrils

open access: yesApplied Rheology, 2006
In this paper we describe the rheological behaviour of Ca2+-induced cold-set gels of whey protein mixtures. Cold- set gels are important applications for products with a low thermal stability.
Bolder Suzanne G.   +3 more
doaj   +1 more source

Extracellular Alpha-Synuclein: Mechanisms for Glial Cell Internalization and Activation

open access: yesBiomolecules, 2022
Alpha-synuclein (α-syn) is a small protein composed of 140 amino acids and belongs to the group of intrinsically disordered proteins. It is a soluble protein that is highly expressed in neurons and expressed at low levels in glial cells.
Cecilia Chavarría   +2 more
doaj   +1 more source

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