A designed protein interface that blocks fibril formation [PDF]
, 2004 Protein fibril formation is implicated in many diseases, and therefore much effort has been focused toward the development of inhibitors of this process.
Huang, Po-Ssu +4 more
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Nucleation of protein fibrillation by nanoparticles [PDF]
Proceedings of the National Academy of Sciences, 2007 Nanoparticles present enormous surface areas and are found to enhance the rate of protein fibrillation by decreasing the lag time for nucleation. Protein fibrillation is involved in many human diseases, including Alzheimer's, Creutzfeld-Jacob disease, and dialysis-related amyloidosis. Fibril formation occurs by nucleation-dependent
Linse, Sara +7 more
openaire +2 more sources
Concentration-dependent polymorphism of insulin amyloid fibrils [PDF]
PeerJ, 2019 Protein aggregation into highly structured fibrils has long been associated with several neurodegenerative disorders, such as Alzheimer’s or Parkinson’s disease.
Andrius Sakalauskas +2 more
doaj +2 more sources
Limited proteolysis in the investigation of beta2-microglobulin amyloidogenic and fibrillar states. [PDF]
, 2005 Amyloid fibrils of patients treated with regular haemodialysis essentially consists of β2-microglobulin (β2-m) and its truncated species ΔN6β2-m lacking six residues at the amino terminus.
AMORESANO, ANGELA +4 more
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Toxic species in amyloid disorders: Oligomers or mature fibrils
Annals of Indian Academy of Neurology, 2015 Protein aggregation is the hallmark of several neurodegenerative disorders. These protein aggregation (fibrillization) disorders are also known as amyloid disorders. The mechanism of protein aggregation involves conformation switch of the native protein,
Meenakshi Verma +2 more
doaj +1 more source
Molecular Strategies to Target Protein Aggregation in Huntington’s Disease
Frontiers in Molecular Biosciences, 2021 Huntington’s disease (HD) is a neurodegenerative disorder caused by the aggregation of the mutant huntingtin (mHTT) protein in nerve cells. mHTT self-aggregates to form soluble oligomers and insoluble fibrils, which interfere in a number of key cellular ...
Olga D. Jarosińska +3 more
doaj +1 more source
Co-populated Conformational Ensembles of β(2)-Microglobulin Uncovered Quantitatively by Electrospray Ionization Mass Spectrometry [PDF]
, 2004 Ordered assembly of monomeric human β(2)-microglobulin (β(2)m) into amyloid fibrils is associated with the disorder hemodialysis-related amyloidosis. Previously, we have shown that under acidic conditions (pH
Bjorkman +46 more
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Uncovering the Mechanism of Aggregation of Human Transthyretin. [PDF]
, 2015 The tetrameric thyroxine transport protein transthyretin (TTR) forms amyloid fibrils upon dissociation and monomer unfolding. The aggregation of transthyretin has been reported as the cause of the life-threatening transthyretin amyloidosis.
Cascio, Duilio +9 more
core +2 more sources
Structure-mechanics relationships of collagen fibrils in the Osteogenesis Imperfecta Mouse model [PDF]
, 2015 The collagen molecule, which is the building block of collagen fibrils, is a triple helix of two α1(I) chains and one α2(I) chain. However, in the severe mouse model of osteogenesis imperfecta (OIM), deletion of the COL1A2 gene results in the ...
Andriotis, OG +7 more
core +4 more sources
Crystallin proteins and amyloid fibrils
Cellular and Molecular Life Sciences, 2008 Improper protein folding (misfolding) can lead to the formation of disordered (amorphous) or ordered (amyloid fibril) aggregates. The major lens protein, alpha-crystallin, is a member of the small heat-shock protein (sHsp) family of intracellular molecular chaperone proteins that prevent protein aggregation.
Ecroyd, Heath, Carver, John
openaire +4 more sources