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Annals of Clinical Biochemistry: International Journal of Laboratory Medicine, 2012 The term amyloid describes the deposition in the extracellular space of certain proteins in a highly characteristic, insoluble fibrillar form. Amyloidosis describes the various clinical syndromes that occur as a result of damage by amyloid deposits in tissues and organs throughout the body.
Jennifer H, Pinney, Philip N, Hawkins
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Health-related quality of life in hereditary transthyretin amyloidosis polyneuropathy: a prospective, observational study [PDF]
, 2020 Background Hereditary Transthyretin Amyloidosis Polyneuropathy is a rare life-threatening neurologic disease that imposes considerable mortality and it is associated with progressive related disabilities.
Coelho, Teresa +5 more
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Postgraduate Medical Journal, 2001 Abstract Amyloidosis is not a single disease but a series of diseases in which there is extracellular deposition of a protein which, although it may be derived from different and unrelated sources, folds into a β pleated sheet. There have recently been significant advances in elucidating the pathogenesis and in the ...
M F, Khan, R H, Falk
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Renal AA-amyloidosis in intravenous drug users - a role for HIV-infection? [PDF]
, 2012 Background: Chronic renal disease is a serious complication of long-term intravenous drug use (IVDU). Recent reports have postulated a changing pattern of underlying nephropathy over the last decades.
Amann, Kerstin Ute +7 more
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Orphanet Journal of Rare Diseases, 2012 Abstract Definition of the disease AL amyloidosis results from extra-cellular deposition of fibril-forming monoclonal immunoglobulin (Ig) light chains (LC) (most commonly of lambda isotype) usually secreted by a small plasma cell clone.
Desport, Estelle +13 more
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Abnormal Myocardial Blood Flow Reserve Observed in Cardiac Amyloidosis [PDF]
, 2016 We performed real-time myocardial contrast echocardiography on a patient with cardiac amyloidosis and previous normal coronary angiography presenting with atypical chest pain to assess myocardial blood flow reserve (MBFR).
Greaves, K, Nam, MC, Nel, K, Senior, R
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Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain. [PDF]
, 2015 Overproduction of immunoglobulin light chains leads to systemic amyloidosis, a lethal disease characterized by the formation of amyloid fibrils in patients' tissues. Excess light chains are in equilibrium between dimers and less stable monomers which can
Brumshtein, Boris +7 more
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The prevalence and distribution of the amyloidogenic transthyretin (TTR) V122I allele in Africa [PDF]
, 2016 Transthyretin (TTR) pV142I (rs76992529-A) is one of the 113 variants in the human TTR gene associated with systemic amyloidosis. It results from a G to A transition at a CG dinucleotide in the codon for amino acid 122 of the mature protein (TTR V122I ...
Alexander, Alice A +10 more
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Blood Reviews, 1988 Amyloidosis is a disorder of protein folding in which normally soluble proteins are deposited in the interstitial space as insoluble and remarkably stable fibrils that progressively disrupt tissue structure and function of organs throughout the body.
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Uncovering the Mechanism of Aggregation of Human Transthyretin. [PDF]
, 2015 The tetrameric thyroxine transport protein transthyretin (TTR) forms amyloid fibrils upon dissociation and monomer unfolding. The aggregation of transthyretin has been reported as the cause of the life-threatening transthyretin amyloidosis.
Cascio, Duilio +9 more
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