Results 61 to 70 of about 162,440 (399)

Systemic amyloidosis from A (AA) to T (ATTR): a review

open access: yesJournal of Internal Medicine, 2020
Systemic amyloidosis is a rare protein misfolding and deposition disorder leading to progressive organ failure. There are over 15 types of systemic amyloidosis, each caused by a different precursor protein which promotes amyloid formation and tissue ...
Eli Muchtar   +11 more
semanticscholar   +1 more source

Cardiac transplantation in transthyretin amyloid cardiomyopathy: Outcomes from three decades of tertiary center experience

open access: yesFrontiers in Cardiovascular Medicine, 2023
AimsTransthyretin cardiac amyloidosis (ATTR-CM) is a progressive and fatal cardiomyopathy. Treatment options in patients with advanced ATTR-CM are limited to cardiac transplantation (CT).
Yousuf Razvi   +30 more
doaj   +1 more source

Amyloid nomenclature 2018: recommendations by the International Society of Amyloidosis (ISA) nomenclature committee

open access: yesAmyloid: Journal of Protein Folding Disorders, 2018
The nomenclature committee of the International Society of Amyloidosis (ISA) meets every second year to discuss and formulate recommendations. The conclusions from the discussion at the XVI International Symposium on Amyloidosis in Kumamoto, Japan, 25–29
M. Benson   +7 more
semanticscholar   +1 more source

Dataset on the use of 3D speckle tracking echocardiography in light-chain amyloidosis [PDF]

open access: yes, 2018
The dataset presented in this article is related to the research article entitled “Biventricular assessment of light-chain amyloidosis using 3D speckle tracking echocardiography: Differentiation from other forms of myocardial hypertrophy” (Vitarelli et ...
Antonio Vitarelli   +10 more
core   +2 more sources

A novel hotspot of gelsolin instability and aggregation propensity triggers a new mechanism of amyloidosis [PDF]

open access: yesarXiv, 2021
The multidomain protein gelsolin (GSN) is composed of six homologous modules, sequentially named G1 to G6. Single point substitutions in this protein are responsible for AGel amyloidosis, a hereditary disease characterized by progressive corneal lattice dystrophy, cutis laxa, and polyneuropathy. Several different amyloidogenic variants of GSN have been
arxiv  

Inotersen Treatment for Patients with Hereditary Transthyretin Amyloidosis

open access: yesNew England Journal of Medicine, 2018
BACKGROUND Hereditary transthyretin amyloidosis is caused by pathogenic single‐nucleotide variants in the gene encoding transthyretin (TTR) that induce transthyretin misfolding and systemic deposition of amyloid. Progressive amyloid accumulation leads to
M. Benson   +34 more
semanticscholar   +1 more source

Citrate stabilized gold nanoparticles interfere with amyloid fibril formation: D76N and ΔN6 \b{eta}2-microglobulin variants [PDF]

open access: yesNanoscale, 2018, 10, 4793, 2018
Protein aggregation including the formation of dimers and multimers in solution, underlies an array of human diseases such as systemic amyloidosis which is a fatal disease caused by misfolding of native globular proteins damaging the structure and function of affected organs.
arxiv   +1 more source

Pathophysiology and Therapeutic Approaches to Cardiac Amyloidosis.

open access: yesCirculation 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

Evaluation of a new ELISA assay for monoclonal free‐light chain detection in patients with cardiac amyloidosis

open access: yeseJHaem, 2022
The causal protein of amyloid light‐chain (AL) amyloidosis is a monoclonal immunoglobulin free light chain (mFLC), which must be quantified in the serum for patient diagnosis and monitoring.
Hajer Abroud   +18 more
doaj   +1 more source

The structure of N184K amyloidogenic variant of gelsolin highlights the role of the H-bond network for protein stability and aggregation properties [PDF]

open access: yesEur Biophys J. 2019 Nov 13, 2019
Mutations in the gelsolin protein are responsible for a rare conformational disease known as AGel amyloidosis. Four of these mutations are hosted by the second domain of the protein (G2): D187N/Y, G167R and N184K. The impact of the latter has been so far evaluated only by studies on the isolated G2.
arxiv   +1 more source

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