نتایج جستجو برای: amyloid

تعداد نتایج: 37689  

Protein aggregation is phenomenon wherein protein loses its native structure and aggregates due to the adaption of non-native conformation. Amyloid aggregation formed by the accumulation of various proteins causes many diseases in humans and other organisms. Antioxidants can prevent proteins aggregation. Pulicaria undulata  extract along with phenolic compounds can increase protein stability an...

2014
Hui Wang Daniel P. Raleigh Yaakov Koby Levy

Islet amyloid polypeptide (IAPP or amylin) forms amyloid deposits in the islets of Langerhans; a process that is believed to contribute to the progression of type 2 diabetes and to the failure of islet transplants. An emerging theme in amyloid research is the hypothesis that the toxic species produced during amyloid formation by different polypeptides share common features and exert their effec...

2012
Takeshi Kuroda Naohito Tanabe Daisuke Kobayashi Yoko Wada Shuichi Murakami Masaaki Nakano Ichiei Narita

BACKGROUND The kidney is a major target organ for systemic amyloidosis that often affects the kidney including proteinura, and elevated serum creatinine (Cr). The correlation between amount of amyloid deposits and clinical parameters is not known. The aim of this study was to clarify correlation the amyloid area in all renal biopsy specimen and clinical parameters. METHODS Fifty-eight patient...

2016
Sebastian Palmqvist Niklas Mattsson Oskar Hansson

Cerebral accumulation of amyloid-β is thought to be the starting mechanism in Alzheimer's disease. Amyloid-β can be detected by analysis of cerebrospinal fluid amyloid-β42 or amyloid positron emission tomography, but it is unknown if any of the methods can identify an abnormal amyloid accumulation prior to the other. Our aim was to determine whether cerebrospinal fluid amyloid-β42 change before...

2015
Melissa E. Murray Val J. Lowe Neill R. Graff-Radford Amanda M. Liesinger Ashley Cannon Scott A. Przybelski Bhupendra Rawal Joseph E. Parisi Ronald C. Petersen Kejal Kantarci Owen A. Ross Ranjan Duara David S. Knopman Clifford R. Jack Dennis W. Dickson

Thal amyloid phase, which describes the pattern of progressive amyloid-b plaque deposition in Alzheimer’s disease, was incorporated into the latest National Institute of Ageing – Alzheimer’s Association neuropathologic assessment guidelines. Amyloid biomarkers (positron emission tomography and cerebrospinal fluid) were included in clinical diagnostic guidelines for Alzheimer’s disease dementia ...

Journal: :Journal of cell science 1996
E H Koo S L Squazzo D J Selkoe C H Koo

Amyloid beta-protein, the principal constituent of amyloid fibrils found in senile plaques and blood vessels in Alzheimer's disease, is constitutively produced and released into medium of cultured cells. Amyloid beta-protein is derived by proteolysis of the beta-amyloid precursor protein by unclear mechanisms. Beta-amyloid precursor protein is a transmembrane protein which can be processed to r...

Journal: :Biochemistry 2003
Robert Tycko

Amyloid fibrils are filamentous aggregates, with typical diameters of 10 nm and lengths on the order of microns, formed by a large class of peptides and proteins with disparate sequences and with molecular masses ranging from less than 1 kDa to tens of kilodaltons. Figure 1 shows typical amyloid fibrils as they appear in electron microscopy (EM)1 measurements. Current interest in amyloid fibril...

Journal: :The Journal of Experimental Medicine 1995
W A Gonnerman R Elliott-Bryant I Carreras J D Sipe E S Cathcart

Inbred strains of mice provide a model for studies of the pathogenesis of amyloid A (AA) amyloidosis. All susceptible strains of mice described to date codominantly express two serum amyloid A (apoSAA) isoforms, apoSAA1 and apoSAA2, of which only apoSAA2 serves as a precursor for amyloid fibrils. In previous studies, we have shown that the CE/J strain, which produces a single, novel apoSAA isof...

2015
Boris Brumshtein Shannon R Esswein Lukasz Salwinski Martin L Phillips Alan T Ly Duilio Cascio Michael R Sawaya David S Eisenberg

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 undergo irreversible aggregation to the amyloid state. The dimers therefore must disassociate into monomers prior to forming amyloid fibrils. ...

Journal: :Brain : a journal of neurology 2014
David L Brody Michael L Gross

Despite many years of intensive study, the specific amyloid-b species in the human brain responsible for the pathophysiological processes underlying Alzheimer’s disease have yet to be identified. In part, this may be because we have been ‘searching under the streetlight’: examination of other sources of amyloid-b such as synthetic preparations, material derived from the brains of transgenic ani...

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