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
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
Electronic Structure of ThPd$_2$Al$_3$: an impact of the U $5f$ states in the electronic structure of UPd$_2$Al$_3$ [PDF]
The electronic structure of ThPd$_2$Al$_3$, which is isostructural to the heavy fermion superconductor UPd$_2$Al$_3$, was investigated by photoelectron spectroscopy. The band structure and Fermi surfaces of ThPd$_2$Al$_3$ were obtained by angle-resolved photoelectron spectroscopy (ARPES), and the results were well-explained by the band-structure ...
arxiv +1 more source
About 10-15% of patients with multiple myeloma develop light chain (AL) amyloidosis. AL amyloidosis is a systemic disease that may involve multiple organs, often including the heart. It may present clinically with bradyarrhythmia and syncope.
Navin Jaipaul+2 more
doaj +1 more source
Light chain (AL) amyloidosis is a form of systemic amyloidosis, causing organ dysfunction, mainly affecting the heart and kidney. Patient-tailored and risk-adapted decision making is critical in AL amyloidosis management.
Maria Lourdes Posadas-Martinez+7 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
Upfront CyBorD in AL amyloidosis [PDF]
In this issue of Blood , [Palladini et al][1] report on the outcome of a large series of 230 patients with systemic immunoglobulin (Ig) amyloid light chain (AL) amyloidosis treated frontline with cyclophosphamide, bortezomib, and dexamethasone (CyBorD) at 2 referral centers.[1][2] ![Figure][3]
M. Teresa Cibeira, Joan Bladé
openaire +3 more sources
Kidney-limited AL amyloidosis: a case report and review of the literature
Amyloidosis involves the deposition of abnormal proteins in various tissues and results in progressive organ dysfunction, commonly affecting multiple organs.
Sara Velayati+5 more
doaj +1 more source
Beyond Survival in AL amyloidosis: Identifying and Satisfying Patients’ Needs
The survivorship needs of patients with light-chain (AL) amyloidosis are complex, as is the diagnosis and treatment itself. Early diagnosis is critical in improving patient outcomes; however, given the nonspecific nature of the symptoms, most patients ...
Hamza Hassan, Vaishali Sanchorawala
doaj +1 more source
An unusual case of chronic lymphocytic leukemia, multiple myeloma and cardiac amyloidosis
Light chain amyloidosis has very rarely been reported in association with chronic lymphocytic leukemia (CLL). We reported on a 76-years-old female who presented with simultaneous kappa-restricted chronic lymphocytic leukemia (CLL) and a lambda-restricted
Dongyan Liu+2 more
doaj +1 more source