Results 31 to 40 of about 36,527 (232)
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
Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain. [PDF]
, 2015 Overproduction of immunoglobulin light chains leads to systemic amyloidosis, a lethal disease characterized by the formation of amyloid fibrils in patients' tissues. Excess light chains are in equilibrium between dimers and less stable monomers which can
Brumshtein, Boris +7 more
core +1 more source
Journal of Integrative Neuroscience, 2021 The abnormal deposition of the extracellular amyloid-β peptide is the typical pathological hallmark of Alzheimer’s disease. Strategies to reduce the amyloid-β deposition effectively alleviate the neuronal degeneration and cognitive deficits of Alzheimer’s disease.
Cong Yang +9 more
openaire +3 more sources
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
core +1 more source
European Heart Journal, 2022 Cardiac light chain amyloidosis (AL-CA) is a life-threatening disease and the major determinant of prognosis in AL amyloidosis. The management of heart failure (HF) in AL is challenging and gold standard therapies for HF are poorly tolerated or ...
P. Nikolaou +13 more
semanticscholar +1 more source
PLoS ONE, 2022 Aggregation of unfolded or misfolded proteins into amyloid fibrils can cause various diseases in humans. However, the fibrils synthesized in vitro can be developed toward useful biomaterials under some physicochemical conditions. In this study, atomistic
Husnul Fuad Zein +3 more
doaj +1 more source
Medicina, 2021 Amyloidoses are characterized by aggregation of proteins into highly ordered amyloid fibrils, which deposit in the extracellular space of tissues, leading to organ dysfunction.
Paola Rognoni +4 more
semanticscholar +1 more source
C-src Enriched Serum Microvesicles Are Generated in Malignant Plasma Cell Dyscrasia [PDF]
, 2013 Plasma cell dyscrasias are immunosecretory disorders that can lead to hematological malignancies such as Multiple Myeloma (MM). MM accounts for 15% of all hematologic cancers, and those diagnosed with MM typically become severely ill and have a low life
Andrea, Zendrini +5 more
core +10 more sources
Insight into the protein solubility driving forces with neural attention.
PLoS Computational Biology, 2020 Protein solubility is a key aspect for many biotechnological, biomedical and industrial processes, such as the production of active proteins and antibodies.
Daniele Raimondi +3 more
doaj +1 more source
Quantitative Assessment of Serine-8 Phosphorylated β-Amyloid Using MALDI-TOF Mass Spectrometry
Molecules, 2022 The study of the molecular mechanisms of the pathogenesis of Alzheimer’s disease (AD) is extremely important for identifying potential therapeutic targets as well as early markers. In this regard, the study of the role of post-translational modifications
Andrey A. Kuzin +6 more
doaj +1 more source