Effect of Phosphatidylserine and Cholesterol on Membrane-mediated Fibril Formation by the N-terminal Amyloidogenic Fragment of Apolipoprotein A-I.

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Effect of Phosphatidylserine and Cholesterol on Membrane-mediated Fibril Formation by the N-terminal Amyloidogenic Fragment of Apolipoprotein A-I.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

@zh-cn

2018年学术文章

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2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

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2018年學術文章

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name

Effect of Phosphatidylserine a ...... ragment of Apolipoprotein A-I.

@en

Effect of Phosphatidylserine a ...... ragment of Apolipoprotein A-I.

@nl

type

Item

label

Effect of Phosphatidylserine a ...... ragment of Apolipoprotein A-I.

@en

Effect of Phosphatidylserine a ...... ragment of Apolipoprotein A-I.

@nl

prefLabel

Effect of Phosphatidylserine a ...... ragment of Apolipoprotein A-I.

@en

Effect of Phosphatidylserine a ...... ragment of Apolipoprotein A-I.

@nl

P1476

Effect of Phosphatidylserine a ...... ragment of Apolipoprotein A-I.

@en

P2093

Akira Otaka

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Chiharu Mizuguchi

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Hiroyuki Saito

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Kazuchika Nishitsuji

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Keiichiro Okuhira

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Mitsuki Nakamura

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Naoko Kurimitsu

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Takashi Ohgita

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Toshinori Shimanouchi

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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

Membrane lipids: where they are and how they behave

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

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

Variant apolipoprotein AI as a major constituent of a human hereditary amyloid

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

Cholesterol is an important factor affecting the membrane insertion of beta-amyloid peptide (A beta 1-40), which may potentially inhibit the fibril formation.

Amyloidogenicity and clinical phenotype associated with five novel mutations in apolipoprotein A-I.

Lipid packing determines protein-membrane interactions: challenges for apolipoprotein A-I and high density lipoproteins.

P304

5497

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P31

scholarly article

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10.1038/S41598-018-23920-3

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P407

English

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P478

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P50

Akira Shigenaga

Teruhiko Baba

P577

2018-04-03T00:00:00Z

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P698

29615818

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P932

5882889

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