Results 81 to 90 of about 17,175,483 (375)

Self‐Assembly, Rearrangement, and Disassembly of {Cr6} Horseshoe Oligomers

open access: yesAngewandte Chemie, EarlyView.
Using a combination of ion mobility mass spectrometry (IM‐MS), tandem mass spectrometry (MS2), and low‐temperature scanning tunneling microscopy (STM), we elucidate the self‐assembly, rearrangement, and disassembly processes of polymetallic {Cr6}x (x = 1 – 5) horseshoe oligomers.
Niklas Geue   +8 more
wiley   +2 more sources

Upfront CyBorD in AL amyloidosis [PDF]

open access: yesBlood, 2015
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

Clinical and functional characterisation of a novel TNFRSF1A c.605T > A/V173D cleavage site mutation associated with tumour necrosis factor receptor-associated periodic fever syndrome (TRAPS), cardiovascular complications and excellent response to etanercept treatment. [PDF]

open access: yes, 2008
Objectives: To study the clinical outcome, treatment response, T-cell subsets and functional consequences of a novel tumour necrosis factor (TNF) receptor type 1 (TNFRSF1A) mutation affecting the receptor cleavage site.
B H Belohradsky   +7 more
core   +1 more source

Dissection of the amyloid formation pathway in AL amyloidosis

open access: yesNature Communications, 2021
In antibody light chain (AL) amyloidosis, overproduced light chain (LC) fragments accumulate as fibrils in organs and tissues of patients. In vitro, AL fibril formation is a slow process, characterized by a pronounced lag phase.
P. Kazman   +3 more
semanticscholar   +1 more source

Cholesterol in mRNA‐Lipid Nanoparticles can be Replaced with the Synthetic Mycobacterial Monomycoloyl Glycerol Analogue MMG‐1

open access: yesAdvanced Functional Materials, EarlyView.
This study demonstrates that cholesterol in messenger RNA‐lipid nanoparticles (mRNA‐LNPs) can be completely replaced with an immunopotentiating lipid, i.e., a synthetic analogue of the C‐type lectin receptor agonist monomycoloyl glycerol (MMG‐1), without compromising physicochemical properties, in vivo transfection efficiency, and immunogenicity of the
Abhijeet G. Lokras   +19 more
wiley   +1 more source

Treatment patterns and outcomes in light chain amyloidosis: An institutional registry of amyloidosis report in Argentina.

open access: yesPLoS ONE, 2022
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

Localized AL amyloidosis

open access: yesTerapevticheskii arkhiv
Localized light chain (AL) amyloidosis (amyloidoma) is a rare disease with unclear pathogenesis and undeveloped approaches to therapy. This article presents 3 clinical observations of localized AL amyloidosis with lesions of the respiratory tract, eyes, and soft tissues of the face.
Nelly A. Kashchavtseva   +4 more
openaire   +3 more sources

Biomaterial Strategies for Targeted Intracellular Delivery to Phagocytes

open access: yesAdvanced Functional Materials, EarlyView.
Phagocytes are essential to a functional immune system, and their behavior defines disease outcomes. Engineered particles offer a strategic opportunity to target phagocytes, harnessing inflammatory modulation in disease. By tuning features like size, shape, and surface, these systems can modulate immune responses and improve targeted treatment for a ...
Kaitlyn E. Woodworth   +2 more
wiley   +1 more source

First third-generation CAR T cell application targeting CD19 for the treatment of systemic IgM AL amyloidosis with underlying marginal zone lymphoma

open access: yesBiomarker Research, 2023
Light chain amyloidosis (AL) is a rare disease caused by the generalized deposition of misfolded free light chains. Patients with immunoglobulin M gammopathy (IgM) and indolent B-cell lymphoma such as marginal zone lymphoma (MZL) may in some instances ...
Felix Korell   +8 more
doaj   +1 more source

Nuclear Imaging for the Diagnosis of Cardiac Amyloidosis in 2021

open access: yesDiagnostics, 2021
Cardiac amyloidosis is caused by the deposition of misfolded protein fibrils into the extracellular space of the heart. The diagnosis of cardiac amyloidosis remains challenging because of the heterogeneous manifestations of the disease.
Weijia Li   +6 more
doaj   +1 more source

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