Heparin promotes fibril formation by the N-terminal fragment of amyloidogenic apolipoprotein A-I.

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Immunochemical Approach for Monitoring of Structural Transition of ApoA-I upon HDL Formation Using Novel Monoclonal Antibodies Effect of Phosphatidylserine and Cholesterol on Membrane-mediated Fibril Formation by the N-terminal Amyloidogenic Fragment of Apolipoprotein A-I.

P2860

Q33774419-915CFB43-7B86-4668-8640-964AFBC8FA9C Q55243030-5F847C64-8772-4123-9750-302FD20E9F0B

P2860

Heparin promotes fibril formation by the N-terminal fragment of amyloidogenic apolipoprotein A-I.

Item

http://www.wikidata.org/entity/Q51478393

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年学术文章

@wuu

2016年学术文章

@zh

2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

@zh-sg

2016年學術文章

@yue

2016年學術文章

@zh-hant

name

Heparin promotes fibril format ...... loidogenic apolipoprotein A-I.

@en

Heparin promotes fibril format ...... loidogenic apolipoprotein A-I.

@nl

type

Item

label

Heparin promotes fibril format ...... loidogenic apolipoprotein A-I.

@en

Heparin promotes fibril format ...... loidogenic apolipoprotein A-I.

@nl

prefLabel

Heparin promotes fibril format ...... loidogenic apolipoprotein A-I.

@en

Heparin promotes fibril format ...... loidogenic apolipoprotein A-I.

@nl

P1476

Heparin promotes fibril format ...... yloidogenic apolipoprotein A-I

@en

P2093

Akira Otaka

http://www.w3.org/2001/XMLSchema#string

Akira Shigenaga

http://www.w3.org/2001/XMLSchema#string

Chiharu Mizuguchi

http://www.w3.org/2001/XMLSchema#string

Hiroyuki Saito

http://www.w3.org/2001/XMLSchema#string

Kazuchika Nishitsuji

http://www.w3.org/2001/XMLSchema#string

Kenichi Akaji

http://www.w3.org/2001/XMLSchema#string

Naomi Sakashita

http://www.w3.org/2001/XMLSchema#string

Shiho Mikawa

http://www.w3.org/2001/XMLSchema#string

Toshinori Shimanouchi

http://www.w3.org/2001/XMLSchema#string

P2860

The extreme N-terminal region of human apolipoprotein A-I has a strong propensity to form amyloid fibrils

Identification of an amyloid fibril forming peptide comprising residues 46-59 of apolipoprotein A-I

New insights into the determination of HDL structure by apolipoproteins: Thematic review series: high density lipoprotein structure, function, and metabolism

Amyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosis

Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis

Amyloidogenic propensity of a natural variant of human apolipoprotein A-I: stability and interaction with ligands

The crystal structure of the C-terminal truncated apolipoprotein A-I sheds new light on amyloid formation by the N-terminal fragment.

In vivo fragmentation of heparan sulfate by heparanase overexpression renders mice resistant to amyloid protein A amyloidosis

Heparin induces harmless fibril formation in amyloidogenic W7FW14F apomyoglobin and amyloid aggregation in wild-type protein in vitro.

Divergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid A

P304

3492-3500

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P31

scholarly article

P356

10.1002/1873-3468.12426

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P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

590

http://www.w3.org/2001/XMLSchema#string

P50

Teruhiko Baba

P577

2016-10-04T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

27654470

http://www.w3.org/2001/XMLSchema#string

Heparin promotes fibril formation by the N-terminal fragment of amyloidogenic apolipoprotein A-I.

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P2860

P2860

Heparin promotes fibril formation by the N-terminal fragment of amyloidogenic apolipoprotein A-I.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698