Induction of AApoAII amyloidosis by various heterogeneous amyloid fibrils (Q28254598)

1

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Tatsumi Korenaga

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Li Fu

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Yanming Xing

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Zhanjun Guo

5

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Takatoshi Matsushita

6

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Masanori Hosokawa

7

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Hironobu Naiki

8

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Satoshi Baba

9

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Yasushi Kawata

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Shu-Ichi Ikeda

11

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Tokuhiro Ishihara

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Masayuki Mori

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Keiichi Higuchi

Amyloid fibril protein nomenclature -- 2002.

14

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language of work or name

English

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publication date

9 April 2004

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published in

FEBS Letters

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volume

563

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issue

1-3

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page(s)

179-84

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cites work

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Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?

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A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene

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Development of congenic strains of mice carrying amyloidogenic apolipoprotein A-II (Apoa2c). Apoa2c reduces the plasma level and the size of high density lipoprotein

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Transmissibility of systemic amyloidosis by a prion-like mechanism

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Amyloid fibrils from muscle myoglobin

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Enhancement of AA-amyloid formation in mice by transthyretin amyloid fragments and polyethylene glycol.

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Acceleration of amyloid protein A amyloidosis by amyloid-like synthetic fibrils

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New clothes for amyloid enhancing factor (AEF): silk as AEF.

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Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein

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Prions affect the appearance of other prions: the story of [PIN(+)].

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Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques.

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Conformational diversity in a yeast prion dictates its seeding specificity

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Conformational Abs recognizing a generic amyloid fibril epitope

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Antibody-mediated resolution of light chain-associated amyloid deposits.

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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

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Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II.

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Role of Escherichia coli curli operons in directing amyloid fiber formation

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Molecular genetics of transmissible spongiform encephalopathies

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In vitro propagation of the prion-like state of yeast Sup35 protein

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High homology is present in the primary structures between murine senile amyloid protein (ASSAM) and human apolipoprotein A-II

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Transmission of mouse senile amyloidosis

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Induction of protein conformational change in mouse senile amyloidosis

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10.1016/S0014-5793(04)00295-9

21 January 2018

Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

849768

849768

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference