Results 271 to 280 of about 504,545 (312)
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Seminars in Respiratory and Critical Care Medicine, 2020
AbstractAmyloidosis is the term given to abnormal deposition of misfolded precursor proteins at single or multiple sites, leading to organ dysfunction or clinical signs and symptoms. Pulmonary manifestations are nonspecific and may be associated with several amyloid protein subtypes, commonly AL (light chain) and AA (autoimmune) amyloids.
Misbah, Baqir, Anja C, Roden, Teng, Moua
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AbstractAmyloidosis is the term given to abnormal deposition of misfolded precursor proteins at single or multiple sites, leading to organ dysfunction or clinical signs and symptoms. Pulmonary manifestations are nonspecific and may be associated with several amyloid protein subtypes, commonly AL (light chain) and AA (autoimmune) amyloids.
Misbah, Baqir, Anja C, Roden, Teng, Moua
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Current Opinion in Neurology, 2012
As amyloid neuropathies have benefited from recent major progress, this review is timely and relevant.The main recent articles on amyloid neuropathy cover its description, methods for diagnosis and therapies. Varied clinical presentations are described in transthyretin (TTR)-familial amyloidosis with polyneuropathy (FAP) and light chain amyloid ...
David, Adams +2 more
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As amyloid neuropathies have benefited from recent major progress, this review is timely and relevant.The main recent articles on amyloid neuropathy cover its description, methods for diagnosis and therapies. Varied clinical presentations are described in transthyretin (TTR)-familial amyloidosis with polyneuropathy (FAP) and light chain amyloid ...
David, Adams +2 more
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Essays in Biochemistry, 2014
Amyloid fibrils are formed by numerous proteins and peptides that share little sequence homology. The structures formed are highly ordered and extremely stable, being composed of β-sheet structure and stabilized along their length by hydrogen bonding. The fibrils are formed by several protofilaments that wind around one another in rope-like structures,
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Amyloid fibrils are formed by numerous proteins and peptides that share little sequence homology. The structures formed are highly ordered and extremely stable, being composed of β-sheet structure and stabilized along their length by hydrogen bonding. The fibrils are formed by several protofilaments that wind around one another in rope-like structures,
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Annual Review of Medicine, 1974
The nature of the unique proteinaceous deposits in tissues in both systemic and localized amyloidosis has eluded investigative efforts for well over a century. Recent chemical and immunochemical evidence has demonstrated that in many cases of amyloidosis, the amyloid fibrils, which constitute one of the distinguishing features of the deposits, have as ...
G G, Glenner, W D, Terry
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The nature of the unique proteinaceous deposits in tissues in both systemic and localized amyloidosis has eluded investigative efforts for well over a century. Recent chemical and immunochemical evidence has demonstrated that in many cases of amyloidosis, the amyloid fibrils, which constitute one of the distinguishing features of the deposits, have as ...
G G, Glenner, W D, Terry
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2016
When proteins do not fold correctly, it can lead to very serious diseases. One such group of diseases is the amyloid diseases, of which Alzheimer’s disease (AD), Parkinson’s disease, and type 2 diabetes mellitus (T2DM) are members. The amyloid diseases are characterized by the aggregation of a specific protein into amyloid fibrils. During this process,
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When proteins do not fold correctly, it can lead to very serious diseases. One such group of diseases is the amyloid diseases, of which Alzheimer’s disease (AD), Parkinson’s disease, and type 2 diabetes mellitus (T2DM) are members. The amyloid diseases are characterized by the aggregation of a specific protein into amyloid fibrils. During this process,
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Nature Neuroscience, 2011
The sustained metabolic activation of the brain's default-mode network is thought to render the system vulnerable to Alzheimer's disease. Recent results with transgenic mice support this view by linking neuronal activity to interstitial fluid amyloid-β levels and the development of amyloid-β plaques.
Walker, Lary C, Jucker, Mathias
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The sustained metabolic activation of the brain's default-mode network is thought to render the system vulnerable to Alzheimer's disease. Recent results with transgenic mice support this view by linking neuronal activity to interstitial fluid amyloid-β levels and the development of amyloid-β plaques.
Walker, Lary C, Jucker, Mathias
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Diseases of the Colon & Rectum, 1982
Amyloidosis not infrequently involves the gastrointestinal tract and may result in a variety of symptoms, including those related to impaired motility, malabsorption, and ulceration due to ischemia. This report describes the case of a 74-year-old man with systemic amyloidosis secondary to multiple myeloma, with striking gross morphologic findings ...
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Amyloidosis not infrequently involves the gastrointestinal tract and may result in a variety of symptoms, including those related to impaired motility, malabsorption, and ulceration due to ischemia. This report describes the case of a 74-year-old man with systemic amyloidosis secondary to multiple myeloma, with striking gross morphologic findings ...
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Journal of the American Academy of Dermatology, 1988
Cutaneous lesions are present in up to 40% of patients with primary and myeloma-associated systemic amyloidosis and occur as a result of tissue deposition of immunoglobulin light chain material derived from a circulating paraprotein. The occurrence of waxy, purpuric mucocutaneous lesions provides a crucial early pointer to underlying occult plasma cell
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Cutaneous lesions are present in up to 40% of patients with primary and myeloma-associated systemic amyloidosis and occur as a result of tissue deposition of immunoglobulin light chain material derived from a circulating paraprotein. The occurrence of waxy, purpuric mucocutaneous lesions provides a crucial early pointer to underlying occult plasma cell
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Structural evolution of fibril polymorphs during amyloid assembly
Cell, 2023Martin Wilkinson +2 more
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