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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. Amyloid (mycology) - Wikipedia

    en.wikipedia.org/wiki/Amyloid_(mycology)

    The term "amyloid" is derived from the Latin amyloideus ("starch-like"). [1] It refers to the fact that starch gives a similar reaction, also called an amyloid reaction. The test can be on microscopic features, such as spore walls or hyphal walls, or the apical apparatus or entire ascus wall of an ascus , or be a macroscopic reaction on tissue ...

  4. Amyloid plaques - Wikipedia

    en.wikipedia.org/wiki/Amyloid_plaques

    Amyloid plaques naturally occur in the aging brains of nonhuman species ranging from birds to great apes. [4] In nonhuman primates, which are the closest biological relatives of humans, plaques have been found in all species examined thus far. [ 47 ]

  5. Amyloidosis - Wikipedia

    en.wikipedia.org/wiki/Amyloidosis

    Amyloid light chains deposition in shoulder joint causes enlarged shoulders, also known as "shoulder pad sign". [18] Amyloid light chain depositions can also cause bilateral symmetric polyarthritis. [18] The deposition of amyloid proteins in the bone marrow without causing plasma cell dyscrasias is called amyloidoma. It is commonly found in ...

  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. 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 .

  8. Amyloid-beta precursor protein - Wikipedia

    en.wikipedia.org/wiki/Amyloid-beta_precursor_protein

    Amyloid-beta precursor protein (APP) is an integral membrane protein expressed in many tissues and concentrated in the synapses of neurons. It functions as a cell surface receptor [ 5 ] and has been implicated as a regulator of synapse formation , [ 6 ] neural plasticity , [ 7 ] antimicrobial activity, [ 8 ] and iron export . [ 9 ]

  9. Amyloplast - Wikipedia

    en.wikipedia.org/wiki/Amyloplast

    [6] [7] A plant lacking in phosphoglucomutase (pgm), for example, is a starchless mutant plant, thus preventing the settling of the statoliths. [8] This mutant shows a significantly weaker gravitropic response as compared to a non-mutant plant. [8] [9] A normal gravitropic response can be rescued with hypergravity. [9]