Mutation in gelsolin gene in Finnish hereditary amyloidosis.
about
The 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenicThe IC3D classification of the corneal dystrophiesMultiple β-sheet molecular dynamics of amyloid formation from two ABl-SH3 domain peptides.Idiopathic AA amyloidosis manifested by autonomic neuropathy, vestibulocochleopathy, and lattice corneal dystrophy.Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca(2+) stabilizationHereditary renal amyloidosis with a novel variant fibrinogen.Familial conformational diseases and dementias.Prediction of regulatory networks in mouse abdominal wallMetalloendoprotease cleavage triggers gelsolin amyloidogenesisFamilial hypercholesterolaemia in Finland: common, rare and mild mutations of the LDL receptor and their clinical consequences. Finnish FH-group.Cutis laxa in hereditary gelsolin amyloidosis.Database for the mutations of the Finnish disease heritage.Severe ataxia with neuropathy in hereditary gelsolin amyloidosis: a case report.Genetics of population isolates.Exclusion of the gelsolin gene on 9q32-34 as the cause of familial lattice corneal dystrophy type I.Finnish type of familial amyloidosis: cosegregation of Asp187----Asn mutation of gelsolin with the disease in three large families.Danish type gelsolin related amyloidosis: 654G-T mutation is associated with a disease pathogenetically and clinically similar to that caused by the 654G-A mutation (familial amyloidosis of the Finnish type).Apolipoprotein AI and transthyretin as components of amyloid fibrils in a kindred with apoAI Leu178His amyloidosis.Hereditary amyloid cardiomyopathy caused by a variant apolipoprotein A1.Lewy bodies are immunoreactive with antibodies raised to gelsolin related amyloid-Finnish type.Current perspectives on cardiac amyloidosis.Cerebral amyloidosis: amyloid subunits, mutants and phenotypes.Induction of complement proteins in a mouse model for cerebral microvascular A beta depositionThe polymerase chain reaction and its applications in neuropathology.The genetics of the amyloidoses: interactions with immunity and inflammation.Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro.Development of a smart nano-vehicle to target cerebrovascular amyloid deposits and brain parenchymal plaques observed in Alzheimer's disease and cerebral amyloid angiopathy.Immunohistochemical analysis of lattice corneal dystrophies types I and II.Hereditary hepatic and systemic amyloidosis caused by a new deletion/insertion mutation in the apolipoprotein AI geneGenetic animal models of cerebral vasculopathies.A new prion disease: relationship with central and peripheral amyloidoses.Hereditary renal amyloidosis caused by a heterozygous G654A gelsolin mutation: a report of two casesFamilial amyloid polyneuropathy.Modifications of transthyretin in amyloid fibrils: analysis of amyloid from homozygous and heterozygous individuals with the Met30 mutation.Peripheral nerve amyloidosis.The First Argentinian Family with Familial Amyloidosis of the Finnish Type.Messages from an isolate: lessons from the Finnish gene pool.Ophthaproblem. Lattice corneal dystrophy.Gelsolin amyloid angiopathy causes severe disruption of the arterial wall.Gene mutations in inherited amyloidopathies of the nervous system.
P2860
Q24316253-C47E5F6E-4095-4326-8DC3-6B1DEEF9A50BQ24625598-26D00716-542A-41CB-B79A-5018E7A69441Q30009967-CB2868B1-783E-46DF-81B6-C917CA81FB26Q30495771-7880C09F-AEE8-4B76-A232-32FF0203752DQ34078036-6E98A72C-6A89-48A6-8683-54342EDA8559Q34126123-D960DC3A-B5B7-4995-B11D-7483993CB2C8Q34138249-02F9F9B3-9357-467F-98AC-2D9FD4C34A9EQ34209394-DDED0437-DA3B-4F5A-85EE-C0AC25D8219DQ34324885-3BDFEB7E-17FC-495E-8055-E8F5D5B378E7Q34390416-4A75E113-2EB9-467C-98D7-F91F07DA2B35Q34396968-A27B539C-2A30-487D-9526-69C1CBC182C2Q34520022-FA5939EC-32AE-4AFE-8BAD-1AD8AC5648E5Q34622028-AC29166A-4225-4A5C-B3CB-932AC433E467Q34657331-2B9A0008-4C1C-4191-ADCA-DB3C1471E36EQ35196209-71317CA4-3FBA-41F6-8857-06CCAC0CE450Q35196805-52BC365D-FB5D-42ED-AB36-2F9CAFEC1BEEQ35571936-4CA1F404-6236-4F9F-B80B-7A6AAA5AD776Q35745590-44FF019F-78DC-420E-AA44-15003FFA601DQ35754591-EB5CB789-721D-4574-925D-5DDB89B147F9Q35830303-C5C526D7-5A44-4291-8E22-C9533B203D20Q35964900-D2DD5198-E00D-4E76-BC71-4310EE8D7F6FQ36136387-B4C1B501-225D-4415-8CB8-57E8B1FDC245Q36177112-F3DEA77D-4F38-4708-82CE-CB16C69512BEQ36276019-8BD2FE9F-4680-461E-A3AC-C61A1C6FA94CQ36534748-03AE6D5C-7235-43EB-BC0E-11E330641DD1Q36606154-126638E7-9E86-4513-9ADF-D4A6977F3004Q37154213-55CD0DDB-9989-4075-9A0C-C1A389779F08Q37304076-6D04F1A3-F8C9-4346-8943-93706A37CC77Q37356259-5028B8A2-8AA5-4B12-8B5E-B426C05A88A1Q37542635-B4102F97-9B0C-44B3-B7A1-1EAC6DCAF2EFQ38333529-0B123A03-85D5-45CD-8519-87941FEEF3F5Q40685688-AF792B9C-4127-43B5-996F-5A2B0FFDBCBBQ40807251-37E912EA-0AD1-416D-B7D6-876BA2E2715AQ40872054-625038C9-3316-43B2-A8B8-11E0147EB68DQ41061839-91562586-C67B-40E6-AE33-D76BEC4737A2Q41112203-A0B74F7A-FFDA-4B8F-BA4D-A98AC500782BQ41386249-85EAF107-B2E9-4AE9-BF39-9FA7F51A0E47Q41646092-368CE192-D9CF-481F-94C0-BB3D8399089AQ42493395-7D5BA9C6-BA95-4AFE-8F10-894EFD52EAE5Q43146002-56B46959-E665-4FB3-B4A7-FCF240C771EA
P2860
Mutation in gelsolin gene in Finnish hereditary amyloidosis.
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年学术文章
@wuu
1990年学术文章
@zh-cn
1990年学术文章
@zh-hans
1990年学术文章
@zh-my
1990年学术文章
@zh-sg
1990年學術文章
@yue
1990年學術文章
@zh
1990年學術文章
@zh-hant
name
Mutation in gelsolin gene in Finnish hereditary amyloidosis.
@ast
Mutation in gelsolin gene in Finnish hereditary amyloidosis.
@en
type
label
Mutation in gelsolin gene in Finnish hereditary amyloidosis.
@ast
Mutation in gelsolin gene in Finnish hereditary amyloidosis.
@en
prefLabel
Mutation in gelsolin gene in Finnish hereditary amyloidosis.
@ast
Mutation in gelsolin gene in Finnish hereditary amyloidosis.
@en
P2093
P2860
P356
P1476
Mutation in gelsolin gene in Finnish hereditary amyloidosis.
@en
P2093
B Frangione
I Fernandez-Madrid
O Koivunen
P2860
P304
P356
10.1084/JEM.172.6.1865
P407
P577
1990-12-01T00:00:00Z