Results 41 to 50 of about 181,705 (382)
Amyloid: Journal of Protein Folding Disorders, 2020 The ISA Nomenclature Committee met electronically before and directly after the XVII ISA International Symposium on Amyloidosis, which, unfortunately, had to be virtual in September 2020 due to the ongoing COVID-19 pandemic instead of a planned meeting ...
M. Benson +7 more
semanticscholar +1 more source
Transthyretin cardiac amyloidosis
Cardiovascular Research, 2022 Transthyretin cardiac amyloidosis (ATTR-CA) is an increasingly recognized cause of heart failure (HF) and mortality worldwide. Advances in non-invasive diagnosis, coupled with the development of effective treatments, have shifted ATTR-CA from a rare and ...
A. Porcari, M. Fontana, J. Gillmore
semanticscholar +1 more source
Patisiran, an RNAi Therapeutic, for Hereditary Transthyretin Amyloidosis
New England Journal of Medicine, 2018 BACKGROUND Patisiran, an investigational RNA interference therapeutic agent, specifically inhibits hepatic synthesis of transthyretin. METHODS In this phase 3 trial, we randomly assigned patients with hereditary transthyretin amyloidosis with ...
D. Adams +35 more
semanticscholar +1 more source
The prevalence and distribution of the amyloidogenic transthyretin (TTR) V122I allele in Africa [PDF]
, 2016 Transthyretin (TTR) pV142I (rs76992529-A) is one of the 113 variants in the human TTR gene associated with systemic amyloidosis. It results from a G to A transition at a CG dinucleotide in the codon for amino acid 122 of the mature protein (TTR V122I ...
Alexander, Alice A +10 more
core +1 more source
Orphanet Journal of Rare Diseases, 2022 Background Transthyretin amyloidosis (ATTR amyloidosis) is a rare, life-threatening disease caused by the accumulation of variant or wild-type (ATTRwt amyloidosis) transthyretin amyloid fibrils in the heart, peripheral nerves, and other tissues and ...
A. Dispenzieri +86 more
semanticscholar +1 more source
Natural history and outcome in systemic AA amyloidosis [PDF]
, 2007 BACKGROUND:Deposition of amyloid fibrils derived from circulating acute-phase reactant serum amyloid A protein (SAA) causes systemic AA amyloidosis, a serious complication of many chronic inflammatory disorders.
Gallimore, JR +6 more
core +1 more source
Clinical Amyloid Typing by Proteomics: Performance Evaluation and Data Sharing between Two Centres
Molecules, 2021 Amyloidosis is a relatively rare human disease caused by the deposition of abnormal protein fibres in the extracellular space of various tissues, impairing their normal function. Proteomic analysis of patients’ biopsies, developed by Dogan and colleagues
Diana Canetti +12 more
doaj +1 more source
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
Blood Reviews, 1988 Amyloidosis is a disorder of protein folding in which normally soluble proteins are deposited in the interstitial space as insoluble and remarkably stable fibrils that progressively disrupt tissue structure and function of organs throughout the body.
openaire +5 more sources
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