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.
Kampinga, Harm H. +3 more
openaire +3 more sources
Epigallocatechin Gallate Remodelling of Hfq Amyloid-Like Region Affects Escherichia coli Survival
Pathogens, 2018 Hfq is a pleiotropic regulator that has key roles in the control of genetic expression. The protein noticeably regulates translation efficiency and RNA decay in Gram-negative bacteria, due to the Hfq-mediated interaction between small regulatory ...
David Partouche +7 more
doaj +1 more source
A common beta-sheet architecture underlies in vitro and in vivo beta(2)-microglobulin amyloid fibrils [PDF]
, 2008 Misfolding and aggregation of normally soluble proteins into amyloid fibrils and their deposition and accumulation underlies a variety of clinically significant diseases.
Jahn, T.R., Radford, S.E., Tennent, G.A.
core +2 more sources
In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study
Pathogens, 2019 Hfq is a bacterial protein that regulates gene expression at the post-transcriptional level in Gram-negative bacteria. We have previously shown that Escherichia coli Hfq protein, and more precisely its C-terminal region (CTR), self-assembles into an ...
David Partouche +5 more
doaj +1 more source
The LBFGS Quasi-Newtonian Method for Molecular Modeling Prion AGAAAAGA Amyloid Fibrils [PDF]
, 2012 Experimental X-ray crystallography, NMR (Nuclear Magnetic Resonance) spectroscopy, dual polarization interferometry, etc are indeed very powerful tools to determine the 3-Dimensional structure of a protein (including the membrane protein); theoretical ...
Hou, Yating +4 more
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Bottom-up synthesis of protein-based nanomaterials from engineered β-solenoid proteins.
PLoS ONE, 2020 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
Polymorphic Aβ42 fibrils adopt similar secondary structure but differ in cross-strand side chain stacking interactions within the same β-sheet. [PDF]
, 2020 Formation of polymorphic amyloid fibrils is a common feature in neurodegenerative diseases involving protein aggregation. In Alzheimer's disease, different fibril structures may be associated with different clinical sub-types.
Duo, Lan +5 more
core +1 more source
Prediction of Amyloid Fibril-forming Proteins [PDF]
Journal of Biological Chemistry, 2001 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
Mechanical forces regulate the interactions of fibronectin and collagen I in extracellular matrix [PDF]
, 2015 Despite the crucial role of extracellular matrix (ECM) in directing cell fate in healthy and diseased tissues--particularly in development, wound healing, tissue regeneration and cancer--the mechanisms that direct the assembly and regulate hierarchical ...
Gourdon, Delphine +7 more
core +2 more sources
Prediction of peptide and protein propensity for amyloid formation [PDF]
, 2014 Understanding which peptides and proteins have the potential to undergo amyloid formation and what driving forces are responsible for amyloid-like fiber formation and stabilization remains limited.
A Quintas +80 more
core +5 more sources