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Details on Person Amyloid precursor proteins form ordered fibrils
Class:Id Polymerisation:977136 _displayName Amyloid precursor proteins form ordered fibrils _doRelease TRUE _timestamp 2015-11-18 11:47:13 authored [InstanceEdit:977142] Jupe, S, 2010-10-15 compartment [Compartment:984] extracellular region created [InstanceEdit:977142] Jupe, S, 2010-10-15 disease [Disease:3322973] Amyloidosis edited [InstanceEdit:1247884] Jupe, S, 2011-04-08 input [DefinedSet:977175] Amyloid fibril monomers [extracellular region] [Homo sapiens] isChimeric FALSE literatureReference [LiteratureReference:1247791] Pathogenic potential of human monoclonal immunoglobulin light chains: relationship of in vitro aggregation to in vivo organ deposition [LiteratureReference:1247809] Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of alpha-synuclein protein implicated in Parkinson's disease [LiteratureReference:1247702] Immunoglobulin heavy-chain-associated amyloidosis [LiteratureReference:1247697] Serum levels of beta 2-microglobulin as a new form of amyloid protein in patients undergoing long-term hemodialysis [LiteratureReference:1247691] Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy [LiteratureReference:1247711] Isolation and partial characterization of SAA-an amyloid-related protein from human serum [LiteratureReference:976941] Variant apolipoprotein AI as a major constituent of a human hereditary amyloid [LiteratureReference:976942] A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene [LiteratureReference:976949] Codeposition of apolipoprotein A-IV and transthyretin in senile systemic (ATTR) amyloidosis [LiteratureReference:976852] Gelsolin-related amyloidosis. Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin [LiteratureReference:976877] Human lysozyme gene mutations cause hereditary systemic amyloidosis [LiteratureReference:976921] Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain [LiteratureReference:976879] Mutation in cystatin C gene causes hereditary brain haemorrhage [LiteratureReference:976939] A stop-codon mutation in the BRI gene associated with familial British dementia [LiteratureReference:1247724] Leukocyte chemotactic factor 2: A novel renal amyloid protein [LiteratureReference:1247757] The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease [LiteratureReference:1247784] Assignment of the human and mouse prion protein genes to homologous chromosomes [LiteratureReference:976970] Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells [LiteratureReference:1247766] Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation [LiteratureReference:1247781] Atrial amyloid deposits in the failing human heart display both atrial and brain natriuretic peptide-like immunoreactivity [LiteratureReference:976959] Prolactin-derived amyloid in the aging pituitary gland [LiteratureReference:1247801] An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing [LiteratureReference:977154] Medin: an integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid [LiteratureReference:977166] Kerato-epithelin mutations in four 5q31-linked corneal dystrophies [LiteratureReference:1247709] Localized amyloidosis of the seminal vesicle: identification of lactoferrin immunoreactivity in the amyloid material [LiteratureReference:1247717] Odontogenic ameloblast-associated protein nature of the amyloid found in calcifying epithelial odontogenic tumors and unerupted tooth follicles [LiteratureReference:977189] Senile seminal vesicle amyloid is derived from semenogelin I modified [InstanceEdit:1247813] Jupe, S, 2011-04-05 [InstanceEdit:1247881] Jupe, S, 2011-04-08 [InstanceEdit:1247885] Jupe, S, 2011-04-08 [InstanceEdit:1247886] Jupe, S, 2011-04-08 [InstanceEdit:3322972] Jupe, S, 2013-05-08 [InstanceEdit:6783329] Jassal, Bijay, 2015-06-12 [InstanceEdit:6810581] Jupe, Steve, 2015-11-18 [InstanceEdit:9830342] Matthews, Lisa, 2023-03-08 name Amyloid precursor proteins form ordered fibrils output [DefinedSet:977144] Amyloid fibril main peptide chains [extracellular region] [Homo sapiens] precedingEvent
releaseDate 2011-06-14 reviewed [InstanceEdit:1247882] Perry, G, 2011-04-08 [InstanceEdit:6809157] Perry, George, 2015-11-09 reviewStatus [ReviewStatus:9821382] five stars species [Species:48887] Homo sapiens stableIdentifier [StableIdentifier:1357608] R-HSA-977136.4 summation [Summation:977111] Amyloid fibril formation is associated with a wide range of ... (hasEvent) [Pathway:977225] Amyloid fiber formation [Homo sapiens] (precedingEvent) [Reaction:976734] Amyloid fibrils have additional components [Homo sapiens] (updatedInstance) [_UpdateTracker:9783867] Update Tracker - [Polymerisation:977136] Amyloid precursor proteins form ordered fibrils - v55:[modifyText] [_UpdateTracker:9785072] Update Tracker - [Polymerisation:977136] Amyloid precursor proteins form ordered fibrils - v52:[modifyText]
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