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Int Med Case Rep J
January 2025
Department of Neurology, The Lishui Hospital of Wenzhou Medical University, The First Affiliated Hospital of Lishui University, Lishui People's Hospital, Lishui, Zhejiang, 323000, People's Republic of China.
Primary amyloidosis (AL type) is a systemic disease that can lead to structural and functional damage to organs and tissues such as the kidney, heart and liver with non-specific symptoms. Most of the affected patients develop thyroid infiltration and thus diffuse enlargement of the thyroid gland, while cases leading to hypothyroidism are exceedingly rare. Some researchers have analyzed thyroid function in newly diagnosed patients with AL amyloidosis, and found that the incidence of overt hypothyroidism is only 7%.
View Article and Find Full Text PDFCirc Heart Fail
January 2025
Pathology Unit, Istituto di Ricovero e Cura a Carattere Scientifico (IRCCS) Azienda Ospedaliero-Universitaria di Bologna, Italy (M.R.).
Circ Heart Fail
January 2025
Department of Cardiology, Angiology and Intensive Care Medicine, Deutsches Herzzentrum der Charité, Berlin, Germany (M.L.M., U.L., B.H., D.M., A.B., I.M., S.S.).
Background: Despite previous histopathologic evidence for its presence, the role of myocardial inflammation in the development and progression of cardiac transthyretin amyloidosis (ATTR-CA) remains insufficiently understood. Thus, this study sought to characterize the prevalence and potential prognostic implications of myocardial inflammation in ATTR-CA.
Methods: A retrospective observational study including patients with ATTR-CA diagnosed by endomyocardial biopsy was conducted.
Protein Sci
February 2025
Amherst College, Amherst, Massachusetts, USA.
Hydrogen exchange mass spectrometry (HXMS) is a powerful tool to understand protein folding pathways and energetics. However, HXMS experiments to date have used exchange conditions termed EX1 or EX2 which limit the information that can be gained compared to the more general EXX exchange regime. If EXX behavior could be understood and analyzed, a single HXMS timecourse on an intact protein could fully map its folding landscape without requiring denaturation.
View Article and Find Full Text PDFBiochemistry (Mosc)
December 2024
Faculty of Biology, St. Petersburg State University, St. Petersburg, 199034, Russia. ARRAY(0x5ae2b7af6df8).
Amyloids are protein fibrils with a characteristic cross-β structure that is responsible for the unusual resistance of amyloids to various physical and chemical factors, as well as numerous pathogenic and functional consequences of amyloidogenesis. The greatest diversity of functional amyloids was identified in bacteria. The majority of bacterial amyloids are involved in virulence and pathogenesis either via facilitating formation of biofilms and adaptation of bacteria to colonization of a host organism or through direct regulation of toxicity.
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