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  2. Amyloid - Wikipedia

    en.wikipedia.org/wiki/Amyloid

    To date, 37 human proteins have been found to form amyloid in pathology and be associated with well-defined diseases. [2] The International Society of Amyloidosis classifies amyloid fibrils and their associated diseases based upon associated proteins (for example ATTR is the group of diseases and associated fibrils formed by TTR). [3]

  3. Amyloidosis - Wikipedia

    en.wikipedia.org/wiki/Amyloidosis

    Amyloid deposits in tissue can cause enlargement of structures. Twenty percent of people with AL amyloidosis have an enlarged tongue, that can lead to obstructive sleep apnea, difficulty swallowing, and altered taste. [11] Tongue enlargement does not occur in ATTR or AA amyloidosis. [10] Deposition of amyloid in the throat can cause hoarseness ...

  4. Amyloid plaques - Wikipedia

    en.wikipedia.org/wiki/Amyloid_plaques

    Amyloid beta (Aβ) is a small protein, most often 40 or 42 amino acids in length, that is released from a longer parent protein called the Aβ-precursor protein (APP). [24] APP is produced by many types of cell in the body, but it is especially abundant in neurons .

  5. Amyloid beta - Wikipedia

    en.wikipedia.org/wiki/Amyloid_beta

    Amyloid beta is commonly thought to be intrinsically unstructured, meaning that in solution it does not acquire a unique tertiary fold but rather populates a set of structures. As such, it cannot be crystallized and most structural knowledge on amyloid beta comes from NMR and molecular dynamics .

  6. Protein aggregation - Wikipedia

    en.wikipedia.org/wiki/Protein_aggregation

    Misfolded proteins can form protein aggregates or amyloid fibrils, get degraded, or refold back to its native structure. In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly.

  7. AL amyloidosis - Wikipedia

    en.wikipedia.org/wiki/AL_amyloidosis

    Amyloid light-chain (AL) amyloidosis, also known as primary amyloidosis, is the most common form of systemic amyloidosis. [1] The disease is caused when a person's antibody -producing cells do not function properly and produce abnormal protein fibers made of components of antibodies called light chains .

  8. Serum amyloid A - Wikipedia

    en.wikipedia.org/wiki/Serum_amyloid_A

    Acute-phase serum amyloid A proteins (A-SAAs) are secreted during the acute phase of inflammation.These proteins have several roles, including the transport of cholesterol to the liver for secretion into the bile, the recruitment of immune cells to inflammatory sites, and the induction of enzymes that degrade extracellular matrix.

  9. Haemodialysis-associated amyloidosis - Wikipedia

    en.wikipedia.org/wiki/Haemodialysis-associated...

    Haemodialysis-associated amyloidosis is a form of systemic amyloidosis associated with chronic kidney failure. [1] Amyloidosis is the accumulation of misfolded protein fibers in the body that can be associated with many chronic illnesses.