Results 61 to 70 of about 162,440 (399)
Systemic amyloidosis from A (AA) to T (ATTR): a review
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
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
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]
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]
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
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]
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.
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
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]
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