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  2. Inclusion bodies - Wikipedia

    en.wikipedia.org/wiki/Inclusion_bodies

    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.

  3. 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]

  4. Hereditary inclusion body myopathy - Wikipedia

    en.wikipedia.org/wiki/Hereditary_inclusion_body...

    Inclusion body myopathy with early-onset Paget disease and frontotemporal dementia (IBMPFD), now more commonly referred to as multisystem proteinopathy (MSP), is an autosomal dominant condition caused by mutations in VCP, HNRPA2B1 or HNRNPA1; it is a multisystem degenerative disorder that can affect muscle, bone, and/or the central nervous system.

  5. 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.

  6. Proteinopathy - Wikipedia

    en.wikipedia.org/wiki/Proteinopathy

    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.

  7. Inclusion body myositis - Wikipedia

    en.wikipedia.org/wiki/Inclusion_body_myositis

    Inclusion body myositis (IBM) (/ m aɪ oʊ ˈ s aɪ t ɪ s /) (sometimes called sporadic inclusion body myositis, sIBM) is the most common inflammatory muscle disease in older adults. [2] The disease is characterized by slowly progressive weakness and wasting of both proximal muscles (located on or close to the torso ) and distal muscles (close ...

  8. Serum amyloid P component - Wikipedia

    en.wikipedia.org/wiki/Serum_amyloid_P_component

    20219 Ensembl ENSG00000132703 ENSMUSG00000026542 UniProt P02743 P12246 RefSeq (mRNA) NM_001639 NM_011318 RefSeq (protein) NP_001630 NP_035448 Location (UCSC) Chr 1: 159.59 – 159.59 Mb Chr 1: 172.72 – 172.72 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse The serum amyloid P component (SAP) is the identical serum form of the amyloid P component (AP), a 25 kDa pentameric protein ...

  9. 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 ...