Physical, chemical, and ultrastructural studies of water-soluble human amyloid fibrils. Comparative analyses of nine amyloid preparations
about
The Prevalence and Management of Systemic Amyloidosis in Western CountriesC-terminal sequence of amyloid-resistant type F apolipoprotein A-II inhibits amyloid fibril formation of apolipoprotein A-II in mice.Mouse senile amyloid deposition is suppressed by adenovirus-mediated overexpression of amyloid-resistant apolipoprotein A-IIAmyloid in familial amyloidosis, Finnish type, is antigenically and structurally related to gelsolin.A serum component related to nonimmunoglobulin amyloid protein AS, a possible precursor of the fibrils.Role of altered vascular permeability amyloid formation.The relationship of a serum protein, C1t, to a common nonfibrillar constituent of amyloid (P component) as revealed by immunohistochemical studiesImmunologic studies of water-soluble human amyloid fibrils. Comparative studies of eight amyloid preparationsCaloric restriction reduces the systemic progression of mouse AApoAII amyloidosis.Characterization of an amyloid fibril protein from senile cardiac amyloid.Specific localization and imaging of amyloid deposits in vivo using 123I-labeled serum amyloid P component.Coexistence of protein AA and immunoglobulin light-chain fragments in amyloid fibrils.Ammonium hydroxide treatment of Aβ produces an aggregate free solution suitable for biophysical and cell culture characterization.Demonstration of protein AA in subcutaneous fat tissue obtained by fine needle biopsy.Senile cardiac amyloidosis: evidence of two different amyloid substances in the ageing heart.Comparison of some murine and human amyloid preparations.R202Q/M694V as novel MEFV gene mutations in chronic periodontitis and familial Mediterranean fever.Peptide fibrils as monomer storage of the covalent HIV-1 integrase inhibitor.Characterization of amyloid of ageing obese-hyperglycaemic mice and their lean littermates.The amyloid P-component (protein AP): an integral part of the amyloid substance?Accumulation of pro-apolipoprotein A-II in mouse senile amyloid fibrilsMechanisms of transthyretin amyloidogenesis. Antigenic mapping of transthyretin purified from plasma and amyloid fibrils and within in situ tissue localizationsExtension of A beta2M amyloid fibrils with recombinant human beta2-microglobulin.Antigenic and chemical characterization of non-immunoglobulin amyloid proteins.The amyloid in familial amyloid cardiomyopathy of Danish origin is related to pre-albumin.Extracellular deposition of mouse senile AApoAII amyloid fibrils induced different unfolded protein responses in the liver, kidney, and heart.In vitro production of an amyloid-like substance from gamma 3 heavy chain disease protein.Mouse model to study human A β2M amyloidosis: generation of a transgenic mouse with excessive expression of human β2-microglobulinSelective localization of murine ApoSAA1/SAA2in endosomes-lysosomes in activated macrophages and their degradation products
P2860
Q26740436-A0A0D9CC-FDF0-4BFB-B100-E2CA90840788Q35134538-5A50940F-F76D-408C-999D-66C1C0A1BD1BQ35788311-11B8148D-B8C6-4437-A190-091F2AE1907CQ35811731-EB00C099-947D-41A2-AFF4-47342D83DC0BQ35901198-3FDCC44C-D71C-4E46-B8EB-3E3F6217ABD5Q36076994-5F11E3D2-3F7D-43D3-B3AE-2E2211783029Q36077734-0E6A91D2-1715-4B67-9C60-C36E51CC2109Q36269988-95D00927-66B3-4A85-A81F-09E4AAB73C1FQ36287560-3266C9EE-D2B0-4FB6-979A-8198C813BBE1Q36335737-F9589A9F-E689-48D5-820F-7FF7AB0A2489Q36354563-89FFE7B4-FC4B-49C0-9151-803EF64D0FEBQ39378734-CB702D5A-CCA0-4162-832A-C97BD44F6BFAQ39418248-EA1B4A71-AA4B-4106-97F5-2C7E3BE7C93DQ39658652-6B35B103-D576-4BC7-AFC9-3182077A1ED7Q39710038-F895294C-D093-4943-9B26-65E1DE31CF90Q39951300-A0BA8D99-F558-42DD-AE0F-5A73EBE359C5Q40053555-9E380292-1B33-4A1B-A762-3C1FBB241CC8Q40387790-4FAF04FD-FDC5-432A-86B1-D79E6B1F753FQ41466086-3D3EC282-813B-4C05-9195-6F9EA523B650Q41760085-772CD41E-5018-4F09-8BE1-24156CBA79B4Q41831639-2D9CB00A-1963-412C-9D0E-9064A90FD89EQ41837998-8791AA9F-66F2-46BB-87BA-28BDDEB3B494Q43568860-0BA5B7D2-2C13-4B9F-8BD6-AE6529EAC52BQ44321345-98ED3730-5DAF-40BB-BA01-5BBCBD64EC66Q50549575-9193BD2C-4E30-40BD-96CC-C72CB93A780AQ53657401-1F8B517E-7232-4E06-9756-33D852AC4F3CQ53779160-FE5D2902-6398-4095-B7EE-B6AE99D25216Q58125044-57B43801-AFC2-4D40-B4CD-BFC249407349Q58158262-60E2B3CE-E984-422C-8FE4-1438FB8C5349
P2860
Physical, chemical, and ultrastructural studies of water-soluble human amyloid fibrils. Comparative analyses of nine amyloid preparations
description
1969 nî lūn-bûn
@nan
1969年の論文
@ja
1969年学术文章
@wuu
1969年学术文章
@zh-cn
1969年学术文章
@zh-hans
1969年学术文章
@zh-my
1969年学术文章
@zh-sg
1969年學術文章
@yue
1969年學術文章
@zh
1969年學術文章
@zh-hant
name
Physical, chemical, and ultras ...... s of nine amyloid preparations
@ast
Physical, chemical, and ultras ...... s of nine amyloid preparations
@en
type
label
Physical, chemical, and ultras ...... s of nine amyloid preparations
@ast
Physical, chemical, and ultras ...... s of nine amyloid preparations
@en
prefLabel
Physical, chemical, and ultras ...... s of nine amyloid preparations
@ast
Physical, chemical, and ultras ...... s of nine amyloid preparations
@en
P2093
P2860
P356
P1476
Physical, chemical, and ultras ...... s of nine amyloid preparations
@en
P2093
D Zucker-Franklin
E C Franklin
P2860
P304
P356
10.1084/JEM.130.4.777
P407
P577
1969-10-01T00:00:00Z