Nanobody interaction unveils structure, dynamics and proteotoxicity of the Finnish-type amyloidogenic gelsolin variant [PDF]
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease.
Volume 1865, Issue 3, 1 March 2019, Pages 648-660, 2019 AGel amyloidosis, formerly known as familial amyloidosis of the Finnish-type, is caused by pathological aggregation of proteolytic fragments of plasma gelsolin. So far, four mutations in the gelsolin gene have been reported as responsible for the disease.
arxiv +1 more source
Circulation: Heart Failure, 2019 Cardiomyopathy is a manifestation of transthyretin amyloidosis (ATTR), which is an underrecognized systemic disease whereby the transthyretin protein misfolds to form fibrils that deposit in various tissues and organs.
M. Maurer +14 more
semanticscholar +1 more source
Abnormal Myocardial Blood Flow Reserve Observed in Cardiac Amyloidosis [PDF]
, 2016 We performed real-time myocardial contrast echocardiography on a patient with cardiac amyloidosis and previous normal coronary angiography presenting with atypical chest pain to assess myocardial blood flow reserve (MBFR).
Greaves, K, Nam, MC, Nel, K, Senior, R
core +1 more source
Expert consensus recommendations to improve diagnosis of ATTR amyloidosis with polyneuropathy
Journal of Neurology, 2020 Amyloid transthyretin (ATTR) amyloidosis with polyneuropathy (PN) is a progressive, debilitating, systemic disease wherein transthyretin protein misfolds to form amyloid, which is deposited in the endoneurium. ATTR amyloidosis with PN is the most serious
D. Adams +9 more
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
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
doaj +1 more source
Human central nervous system (CNS) ApoE isoforms are increased by age, differentially altered by amyloidosis, and relative amounts reversed in the CNS compared with plasma [PDF]
, 2016 The risk of Alzheimer's disease (AD) is highly dependent on apolipoprotein-E (apoE) genotype. The reasons for apoE isoform-selective risk are uncertain; however, both the amounts and structure of human apoE isoforms have been hypothesized to lead to ...
Baker-Nigh, Alaina T +11 more
core +3 more sources
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
High-resolution crystal structure of gelsolin domain 2 in complex with the physiological calcium ion [PDF]
Biochem Biophys Res Commun. 2019 Oct 8;518(1):94-99, 2019 The second domain of gelsolin (G2) hosts mutations responsible for a hereditary form of amyloidosis. The active form of gelsolin is Ca2+-bound; it is also a dynamic protein, hence structural biologists often rely on the study of the isolated G2.
arxiv +1 more source
A new staging system for cardiac transthyretin amyloidosis
European Heart Journal, 2018 Aims Cardiac transthyretin (ATTR) amyloidosis is an increasingly recognized, progressive, and fatal cardiomyopathy, the natural history of which remains unclear.
J. Gillmore +14 more
semanticscholar +1 more source