Results 21 to 30 of about 125,062 (284)
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
Marked progress in AL amyloidosis survival: a 40-year longitudinal natural history study
Blood Cancer Journal, 2021 The recent decades have ushered in considerable advancements in the diagnosis and treatment of systemic light chain (AL) amyloidosis. As disease outcomes improve, AL amyloidosis-unrelated factors may impact mortality. In this study, we evaluated survival
Andrew Staron +6 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
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
Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 2023 Background Transthyretin cardiac amyloidosis (ATTR‐CM), found in 6% to 15% of cohorts with heart failure with preserved ejection fraction, has long been considered a rare disease with poor prognosis.
Morris M. Kim +7 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
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
Scandinavian Journal of Rheumatology, 1988 Recent studies have provided new insight into the pathogenesis of amyloidosis and have broadened our knowledge of the mechanisms of deposition and resolution of amyloid. In particular, the structure, synthesis and plasma clearance of the inflammation-associated amyloid precursor, SAA, have been extensively studied and the precursor-product relationship
openaire +5 more sources