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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Macromolecular crowding induces holo α-lactalbumin aggregation by converting to its apo form.
PLoS ONE, 2014 Macromolecular crowding has been shown to have an exacerbating effect on the aggregation propensity of amyloidogenic proteins; while having an inhibitory effect on the non-amyloidogenic proteins.
Shruti Mittal +1 more
doaj +1 more source
Molecular Mechanisms of Aggregation of Canine SOD1 E40K Amyloidogenic Mutant Protein
Molecules, 2022 Canine degenerative myelopathy (DM) is a human amyotrophic lateral sclerosis (ALS)-like neurodegenerative disease. It is a unique, naturally occurring animal model of human ALS.
Kento Wakayama +7 more
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The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. [PDF]
, 2004 Formation of misfolded aggregates is an essential part of what proteins can do. The process of protein aggregation is central to many human diseases and any aggregating event needs to be prevented within a cell and in protein design.
AMORESANO, ANGELA +6 more
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β-cell dysfunctional ERAD/ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCH-L1 deficiency. [PDF]
, 2010 ObjectiveThe islet in type 2 diabetes is characterized by β-cell apoptosis, β-cell endoplasmic reticulum stress, and islet amyloid deposits derived from islet amyloid polypeptide (IAPP).
Butler, Alexandra E +7 more
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Mysterious oligomerization of the amyloidogenic proteins [PDF]
The FEBS Journal, 2010 Misfolding and subsequent self‐assembly of protein molecules into various aggregates is a common molecular mechanism for a number of important human diseases. Curing protein misfolding pathologies and designing successful drugs for the inhibition or reversal of protein aggregation depends on understanding the peculiarities of the misfolding process ...
openaire +3 more sources
Capturing the Interaction Potential of Amyloidogenic Proteins
Physical Review Letters, 2007 Experimentally derived static structure factors obtained for the aggregation-prone protein insulin were analyzed with a statistical mechanical model based on the Derjaguin-Landau-Verwey-Overbeek potential. The data reveal that the protein self-assembles into equilibrium clusters already at low concentrations. Furthermore, striking differences regarding
Javid, Nadeem +4 more
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Cryptic amyloidogenic regions in intrinsically disordered proteins: Function and disease association
Computational and Structural Biotechnology Journal, 2021 The amyloid conformation is considered a fundamental state of proteins and the propensity to populate it a generic property of polypeptides. Multiple proteome-wide analyses addressed the presence of amyloidogenic regions in proteins, nurturing our ...
Jaime Santos +3 more
doaj +1 more source
The relationship between amyloid structure and cytotoxicity [PDF]
, 2014 Self-assembly of proteins and peptides into amyloid structures has been the subject of intense and focused research due to their association with neurodegenerative, age-related human diseases and transmissible prion diseases in humans and mammals. Of the
Marchante, Ricardo +3 more
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Mechanism of Amyloid Gel Formation by Several Short Amyloidogenic Peptides
Nanomaterials, 2021 Under certain conditions, many proteins/peptides are capable of self-assembly into various supramolecular formations: fibrils, films, amyloid gels. Such formations can be associated with pathological phenomena, for example, with various neurodegenerative
Oxana V. Galzitskaya +5 more
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