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
Proteomic Analysis for the Diagnosis of Fibrinogen Aα-chain Amyloidosis
Kidney International Reports, 2019 Introduction: Hereditary fibrinogen Aα-chain (AFib) amyloidosis is a relatively uncommon renal disease associated with a small number of pathogenic fibrinogen Aα (FibA) variants; wild-type FibA normally does not result in amyloid deposition.
Graham W. Taylor +11 more
doaj +1 more source
International Journal of Cardiology: Heart & Vasculature, 2020 Objectives: Left atrial (LA) function is an important marker of hemodynamic status in cardiac amyloidosis (CA), and its characterization may provide relevant prognostic information.
Giovanni Donato Aquaro +10 more
doaj +1 more source
Pathophysiology and Therapeutic Approaches to Cardiac Amyloidosis.
Circulation Research, 2021 Often considered a rare disease, cardiac amyloidosis is increasingly recognized by practicing clinicians. The increased rate of diagnosis is in part due the aging of the population and increasing incidence and prevalence of cardiac amyloidosis with ...
J. Griffin, H. Rosenblum, M. Maurer
semanticscholar +1 more source
Renal Amyloidosis Associated With 5 Novel Variants in the Fibrinogen A Alpha Chain Protein
Kidney International Reports, 2017 Fibrinogen A alpha chain amyloidosis is an autosomal dominant disease associated with mutations in the fibrinogen A alpha chain (FGA) gene, and it is the most common cause of hereditary renal amyloidosis in the UK.
Dorota Rowczenio +18 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
High-precision plasma β-amyloid 42/40 predicts current and future brain amyloidosis
Neurology, 2019 Objective We examined whether plasma β-amyloid (Aβ)42/Aβ40, as measured by a high-precision assay, accurately diagnosed brain amyloidosis using amyloid PET or CSF p-tau181/Aβ42 as reference standards.
S. Schindler +11 more
semanticscholar +1 more source
Amyloidosis from the patient perspective: the French daily impact of amyloidosis study
Amyloid: Journal of Protein Folding Disorders, 2022 Background Amyloidosis is a complex group of rare conditions. For patients, amyloidosis is severely debilitating: physically and psychologically. Currently, data are lacking to evaluate the medical, economic, and social burden of systemic amyloidosis ...
T. Damy +11 more
semanticscholar +1 more source
Clinical and functional characterisation of a novel TNFRSF1A c.605T > A/V173D cleavage site mutation associated with tumour necrosis factor receptor-associated periodic fever syndrome (TRAPS), cardiovascular complications and excellent response to etanercept treatment. [PDF]
, 2008 Objectives: To study the clinical outcome, treatment response, T-cell subsets and functional consequences of a novel tumour necrosis factor (TNF) receptor type 1 (TNFRSF1A) mutation affecting the receptor cleavage site.
B H Belohradsky +7 more
core +1 more source
Gastrointestinal Amyloidosis: Diagnostic Approach and Treatment [PDF]
, 2015 Amyloidosis is a disease marked by deposition of misfolded proteins, known as amyloids, in the extracellular space, including gastrointestinal tract.
Budyono, C. (Catarina) +2 more
core +2 more sources