Results 71 to 80 of about 162,440 (399)
Neurological Therapeutics, 2020 Hereditary variant transthyretin amyloidosis (ATTRv) is a rare genetic defect that affects about 5000–10,000 people worldwide, causing amyloidosis secondary to misfolding of mutant transthyretin (TTR) protein fibrils.
Ivan Urits +9 more
semanticscholar +1 more source
Dual‐Phase C‐11 PiB PET Images for Detecting Tau Pathology in Cerebral Amyloid Angiopathy
Annals of Clinical and Translational Neurology, EarlyView.ABSTRACT Background Cerebral amyloid angiopathy (CAA) is a major cause of lobar intracerebral hemorrhage and cognitive dysfunction in the elderly, and frequently coexists with Alzheimer's disease and tau pathology. Dual‐phase 11C‐PiB PET detects amyloid deposition and cerebral perfusion changes and may have diagnostic value for identifying tau in CAA ...
Meng‐Ting Chiang +4 more
wiley +1 more source
Transthyretin Cardiac Amyloidosis: A Cardio-Orthopedic Disease
Biomedicines, 2022 Orthopaedic manifestations of wild-type transthyretin amyloidosis are frequent and characteristic, including idiopathic bilateral carpal tunnel syndrome, idiopathic lumbar canal stenosis, atraumatic rupture of the brachial biceps tendon, and, more rarely,
Federico Perfetto +9 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
Clinical Research in Cardiology, 2021 Systemic forms of amyloidosis affecting the heart are mostly light-chain (AL) and transthyretin (ATTR) amyloidoses. The latter is caused by deposition of misfolded transthyretin, either in wild-type (ATTRwt) or mutant (ATTRv) conformation.
Yilmaz +12 more
semanticscholar +1 more source
Avian Pathology, 1998 Although amyloid deposits have been described for more than a century and a half, its proteinaceous and fibrillar nature was not revealed until after 1950. Biochemical characterization of amyloids has brought to light that several non-related proteins can re-organize into amyloid fibrils. In some domestic and caged wild birds, and especially waterfowl,
Landman, W.J.M. +2 more
openaire +3 more sources
Recent Applications of Mesoporous Silica Nanoparticles in Gene Therapy
Advanced Healthcare Materials, EarlyView.The review summarizes the synthesis of mesoporous silica nanoparticles (MSNs) with modifiable surface properties, functionalization strategies, mechanism of therapeutic payload release, and current applications in gene therapy, focusing on their capabilities in the targeted delivery of therapeutic nucleic acids, CRISPR‐Cas systems, and other genetic ...
Tamanna Binte Huq +4 more
wiley +1 more source
Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 2022 Background Idiopathic recurrent pericarditis (IRP) is an orphan disease that carries significant morbidity, partly driven by corticosteroid dependence.
Claire J. Peet +7 more
doaj +1 more source
Misdiagnosis of hereditary amyloidosis as AL (Primary) amyloidosis [PDF]
, 2002 Background: Hereditary, autosomal dominant amyloidosis, caused by mutations in the genes encoding transthyretin, fibrinogen A -chain, lysozyme, or apolipoprotein A-I, is thought to be extremely rare and is not routinely included in the differential ...
Booth, D.R. +7 more
core
Identification of Causal Relationship between Amyloid-beta Accumulation and Alzheimer's Disease Progression via Counterfactual Inference [PDF]
arXiv, 2023 Alzheimer's disease (AD) is a neurodegenerative disorder that is beginning with amyloidosis, followed by neuronal loss and deterioration in structure, function, and cognition. The accumulation of amyloid-beta in the brain, measured through 18F-florbetapir (AV45) positron emission tomography (PET) imaging, has been widely used for early diagnosis of AD.
arxiv