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Pinch Purpura: A Clinical Clue to Primary Systemic Amyloidosis.
Indian Dermatol Online J
September 2024
Department of Dermatology, IMS and SUM Hospital, Bhubaneswar, Odisha, India.
The critical role of the variable domain in driving proteotoxicity and aggregation in full-length light chains.
J Mol Biol
January 2025
Department of Biosciences, University of Milan, Italy; Institute of Molecular and Translational Cardiology, IRCCS, Policlinico San Donato, Milan, Italy. Electronic address:
Light chain (AL) amyloidosis is the most common systemic amyloid disease characterized by abnormal accumulation of amyloid fibrils derived from immunoglobulin light chains (LCs). Both full-length (FL) LCs and their isolated variable (VL) and constant (CL) domains contribute to amyloid deposits in multiple organs, with the VL domain predominantly forming the fibril core. However, the role and interplay of these domains in amyloid aggregation and toxicity are poorly understood.
View Article and Find Full Text PDFConduction disease in cardiac amyloidosis patients: A case series suggesting a role for left bundle branch area pacing.
Indian Pacing Electrophysiol J
January 2025
Royal Jubilee Hospital, Vancouver Island Health Authority, British Columbia, Canada.
Transthyretin Cardiac amyloidosis (ATTR-CA) is an increasingly recognised cause of heart failure in our elderly patients with preserved ejection fraction. Patients with ATTR-CA who require permanent pacemaker implantation often have preserved ejection fraction and do not meet the clinical indication for cardiac resynchronization therapy (CRT). In these patients, left bundle branch area pacing (LBBAP) can be a reasonable option to maximise physiological activation of the left ventricle.
View Article and Find Full Text PDFFrom Self-Assembly to Drug Delivery: Understanding and Exploring Protein Fibrils.
Langmuir
January 2025
Department of Chemistry, Indian Institute of Technology Bombay, Powai, Mumbai 400076, India.
It is crucial to comprehend protein misfolding and aggregation in the domains of biomedicine, pharmaceuticals, and proteins. Amyloid fibrils are formed when proteins misfold and assemble, resulting in the debilitating illness known as "amyloidosis". This work investigates lysozyme fibrillation with pluronics (F68 and F127).
View Article and Find Full Text PDFAmyloid Secreting Jejunal Plasmacytoma.
Indian J Hematol Blood Transfus
October 2024
Department of Hematopathology, Sir Ganga Ram Hospital, Old Rajinder Nagar, New Delhi-110060, India.
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