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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. 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 .

  4. 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 ...

  5. Cardiac amyloidosis - Wikipedia

    en.wikipedia.org/wiki/Cardiac_amyloidosis

    Amyloid, the aggregation, or clumping, of proteins, is resistant to degradation by the body. Amyloids are mostly fibrils, while also containing a P component, apolipoprotein, collagen, fibronectin, and laminin. [2] The P component, a pentameric protein, stabilizes the fibrils of the amyloid, which reduces their clearance from the body. [1]

  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. Familial amyloid polyneuropathy - Wikipedia

    en.wikipedia.org/wiki/Familial_amyloid_poly...

    The transthyretin protein is a tetramer. The tetramer has to dissociate into misfolded monomers to aggregate into a variety of structures including amyloid fibrils. Because most patients are heterozygotes, they deposit both mutant and wild type TTR subnits. [citation needed] FAP is inherited in an autosomal dominant manner. [2]

  8. I Tried 10 Brands of American Cheese Singles, and These Were ...

    www.aol.com/finance/tried-10-brands-american...

    5. Borden American Cheese Singles. The truth is, so many of these cheeses taste identical. Borden and Harris Teeter are really similar, both lacking any distinct flavors that make them unique or ...

  9. Familial amyloid cardiomyopathy - Wikipedia

    en.wikipedia.org/wiki/Familial_amyloid_cardiomyo...

    Due to this resistance to degradation, when amyloid fibrils accumulate in the heart's walls, specifically the left ventricle, rigidity prevents the heart from properly relaxing and refilling with blood: this is called diastolic dysfunction which can ultimately lead to heart failure.