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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. [1] [2] Protein aggregates have been implicated in a wide variety of diseases known as amyloidoses, including ALS, Alzheimer's, Parkinson's and prion ...
Inclusion bodies have a non-unit (single) lipid membrane [citation needed].Protein inclusion bodies are classically thought to contain misfolded protein.However, this has been contested, as green fluorescent protein will sometimes fluoresce in inclusion bodies, which indicates some resemblance of the native structure and researchers have recovered folded protein from inclusion bodies.
In functional programming, fold (also termed reduce, accumulate, aggregate, compress, or inject) refers to a family of higher-order functions that analyze a recursive data structure and through use of a given combining operation, recombine the results of recursively processing its constituent parts, building up a return value.
The accumulation of platelets to the site of a wound to form a platelet plug or a thrombus; Flocculation, a process where a solute comes out of solution in the form of floccules or flakes; Overdispersion or statistical aggregation, where the variance of a distribution is higher than which we expect. Aggregation pheromone
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]
In medicine, proteinopathy ([pref. protein]; -pathy [suff. disease]; proteinopathies pl.; proteinopathic adj), or proteopathy, protein conformational disorder, or protein misfolding disease, is a class of diseases in which certain proteins become structurally abnormal, and thereby disrupt the function of cells, tissues and organs of the body.
Georgia earned a spot in the national rankings for the first time in 14 years after notching back-to-back upset wins. Checking in at No. 23 in both major polls, the Bulldogs attempt to validate ...
Neurofibrillary tangles are formed by hyperphosphorylation of a microtubule-associated protein known as tau, causing it to aggregate, or group, in an insoluble form. (These aggregations of hyperphosphorylated tau protein are also referred to as PHF, or "paired helical filaments"). The precise mechanism of tangle formation is not completely ...