Results 51 to 60 of about 3,689,678 (299)
The contrasting effect of macromolecular crowding on amyloid fibril formation. [PDF]
PLoS ONE, 2012 Amyloid fibrils associated with neurodegenerative diseases can be considered biologically relevant failures of cellular quality control mechanisms.
Qian Ma +7 more
doaj +1 more source
Evolution of protein interfaces in multimers and fibrils [PDF]
The Journal of Chemical Physics, 2019 A majority of cellular proteins function as part of multimeric complexes of two or more subunits. Multimer formation requires interactions between protein surfaces that lead to closed structures, such as dimers and tetramers. If proteins interact in an open-ended way, uncontrolled growth of fibrils can occur, which is likely to be detrimental in most ...
W. Jeffrey Zabel +6 more
openaire +3 more sources
Beat shock proteins and atrial fibrillation [PDF]
Cell Stress & Chaperones, 2005 In this mini-review, the role of heat shock proteins in susceptability to induction of atrial fibrillation (AF) or in the process of AF is discussed. AF is the most common arrhythmia in humans, is self-perpetuating in nature and hence tends to become more persistent in time.
Harm H, Kampinga +3 more
openaire +2 more sources
Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation
FEBS 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
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
Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly [PDF]
, 2008 Self-assembly of misfolded proteins into ordered fibrillar aggregates known as amyloid results in numerous human diseases. Despite an increasing number of proteins and peptide fragments being recognised as amyloidogenic, how these amyloid aggregates ...
Xue, Wei-Feng +2 more
core +1 more source
PLoS ONE, 2021 Amyloid fibrils are widely studied both as target in conformational disorders and as basis for the development of protein-based functional materials.
Svitlana Chernii +9 more
doaj +1 more source
Electrospinning Induced Orientation of Protein Fibrils
Biomacromolecules, 2020 Amyloid-like fibrils are prepared from protein in the lab by controlled heat treatments, yet these must be further assembled to match the desirable mechanical and structural properties of biological fibers. Here, β-lactoglobulin fibrils were incorporated into poly(ethylene oxide) fibers of 40-180 nm diameter by electrospinning.
Da Chen +9 more
openaire +3 more sources
The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation
FEBS 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
Nanoscale imaging of major and minor ampullate silk from the orb-web spider Nephila Madagascariensis
Scientific Reports, 2023 Spider silk fibres have unique mechanical properties due to their hierarchical structure and the nanoscale organization of their proteins. Novel imaging techniques reveal new insights into the macro- and nanoscopic structure of Major (MAS) and Minor (MiS)
Irina Iachina +4 more
doaj +1 more source