Results 31 to 40 of about 162,440 (399)

Renal AA-amyloidosis in intravenous drug users - a role for HIV-infection? [PDF]

open access: yes, 2012
Background: Chronic renal disease is a serious complication of long-term intravenous drug use (IVDU). Recent reports have postulated a changing pattern of underlying nephropathy over the last decades.
Amann, Kerstin Ute   +7 more
core   +2 more sources

High-Throughput Precision Phenotyping of Left Ventricular Hypertrophy with Cardiovascular Deep Learning [PDF]

open access: yes, 2021
Left ventricular hypertrophy (LVH) results from chronic remodeling caused by a broad range of systemic and cardiovascular disease including hypertension, aortic stenosis, hypertrophic cardiomyopathy, and cardiac amyloidosis. Early detection and characterization of LVH can significantly impact patient care but is limited by under-recognition of ...
arxiv   +1 more source

Tensorial tomographic Fourier Ptychography with applications to muscle tissue imaging [PDF]

open access: yesTensorial tomographic Fourier Ptychography with applications to muscle tissue imaging, Adv. Photon. 6(2), 026004 (2024), 2023
We report Tensorial tomographic Fourier Ptychography (ToFu), a new non-scanning label-free tomographic microscopy method for simultaneous imaging of quantitative phase and anisotropic specimen information in 3D. Built upon Fourier Ptychography, a quantitative phase imaging technique, ToFu additionally highlights the vectorial nature of light.
arxiv   +1 more source

Patisiran, an RNAi Therapeutic, for Hereditary Transthyretin Amyloidosis

open access: yesNew 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

Clinical Amyloid Typing by Proteomics: Performance Evaluation and Data Sharing between Two Centres

open access: yesMolecules, 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

Health-related quality of life in hereditary transthyretin amyloidosis polyneuropathy: a prospective, observational study [PDF]

open access: yes, 2020
Background Hereditary Transthyretin Amyloidosis Polyneuropathy is a rare life-threatening neurologic disease that imposes considerable mortality and it is associated with progressive related disabilities.
Coelho, Teresa   +5 more
core   +2 more sources

Amyloid nomenclature 2020: update and recommendations by the International Society of Amyloidosis (ISA) nomenclature committee

open access: yesAmyloid: 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

Clinical and genetic profile of patients enrolled in the Transthyretin Amyloidosis Outcomes Survey (THAOS): 14-year update

open access: yesOrphanet 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]

open access: yes, 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

Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain. [PDF]

open access: yes, 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

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