Journal•ISSN: 1350-6129
Amyloid
Informa
About: Amyloid is an academic journal published by Informa. The journal publishes majorly in the area(s): Amyloidosis & Transthyretin. It has an ISSN identifier of 1350-6129. Over the lifetime, 1530 publications have been published receiving 31946 citations.
Topics: Amyloidosis, Transthyretin, Amyloid, AL amyloidosis, AA amyloidosis
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TL;DR: The list presented here documents all TTR gene mutations reported to date and includes information on a total of 100 separate forms of the protein, including 1 1 nonamyloidogenic TTR proteins.
Abstract: (2003). Tabulation of human transthyretin (TTR) variants, 2003. Amyloid: Vol. 10, No. 3, pp. 160-184.
472 citations
TL;DR: Two proteins which were previously characterized as intracellular inclusions, tau and α-synuclein, are now recognized to form extracellular deposits upon cell death and thus have been included in Table 1 as ATau and AαSyn.
Abstract: The Nomenclature Committee of the International Society of Amyloidosis (ISA) met during the XVth Symposium of the Society, 3 July–7 July 2016, Uppsala, Sweden, to assess and formulate recommendatio...
461 citations
TL;DR: The Nomenclature Committee of the International Society of Amyloidosis met during the XIVth Symposium of the Society, April 27–May 1, 2014, Indianapolis, IN, to assess and formulate recommend new names for amyloid beta-cell types.
Abstract: The Nomenclature Committee of the International Society of Amyloidosis (ISA) met during the XIVth Symposium of the Society, April 27–May 1, 2014, Indianapolis, IN, to assess and formulate recommend...
433 citations
TL;DR: The nomenclature committee of the International Society of Amyloidosis (ISA) meets every second year to discuss and formulate recommendations as discussed by the authors, and the conclusions from the discussion at the XVI International Symposium on Amyloids in Kumamoto, Japan, 25-29 March 2018 and afterwards are summarized in this Nomenclatures Article.
Abstract: The nomenclature committee of the International Society of Amyloidosis (ISA) meets every second year to discuss and formulate recommendations. The conclusions from the discussion at the XVI International Symposium on Amyloidosis in Kumamoto, Japan, 25-29 March 2018 and afterwards are summarized in this Nomenclature Article. From having recommended the use of the designation "amyloid fibril" for in vivo material only, ISA's nomenclature committee now accepts its use more broadly following the international scientific literature. However, it is important always to stress the origin of the β-fibrils in order to avoid misunderstanding. Given the more broad use of the word "amyloid" several classes of amyloid fibrils may be distinguished. For the medical in vivo situation, and to be included in the amyloid nomenclature list, "amyloid" still means mainly extracellular tissue deposits of protein fibrils, recognized by specific properties, such as green-yellow birefringence after staining with Congo red. It should also be underlined that in vivo amyloid fibrils, in addition to the main protein contain associated compounds, particularly serum amyloid P-component (SAP) and proteoglycans, mainly heparan sulfate proteoglycan. With this definition there are presently 36 human amyloid proteins of which 14 appear only associated with systemic amyloidosis and 19 as localized forms. Three proteins can occur both as localized and systemic amyloidosis. Strictly intracellular aggregates are not included in this list.
363 citations
TL;DR: Current nomenclature lists of 27 human and nine animal fibril proteins are provided together with a list of eight inclusion bodies that exhibit some of the properties of amyloid fibrils.
Abstract: A system of amyloid fibril nomenclature based on the chemical identity of the amyloid fibril forming protein is recommended. This system has been in use for approximately 40 years, but current literature remains confused with clinical and histochemical designations used when the amyloid disease processes were poorly understood. To be designated an amyloid fibril protein, the protein must occur in tissue deposits and exhibit affinity for Congo red and green birefringence when viewed by polarisation microscopy. Furthermore, the protein must have been unambiguously characterised by protein sequence analysis (DNA sequencing in the case of familial diseases). Current nomenclature lists of 27 human and nine animal fibril proteins are provided together with a list of eight inclusion bodies that exhibit some of the properties of amyloid fibrils.
344 citations