Unfolding and aggregation of transthyretin by the truncation of 50 N-terminal amino acids. (Q46794944)

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1 January 2020

title

Unfolding and aggregation of transthyretin by the truncation of 50 N-terminal amino acids (English)

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7

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Makoto Demura

8

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author name string

Mineyuki Mizuguchi

1

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Ayumi Hayashi

2

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Makoto Takeuchi

3

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Mizuki Dobashi

4

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Yoshihiro Mori

5

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Hiroyuki Shinoda

6

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Keiichi Kawano

9

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language of work or name

English

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publication date

1 July 2008

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volume

72

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issue

1

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page(s)

261-269

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The characterization of soluble amyloid prepared in water

1 January 2020

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Familial meningocerebrovascular amyloidosis, Hungarian type, with mutant transthyretin (TTR Asp18Gly)

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Variant-sequence transthyretin (isoleucine 122) in late-onset cardiac amyloidosis in black Americans

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Only amyloidogenic intermediates of transthyretin induce apoptosis

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Dimeric transthyretin variant assembles into spherical neurotoxins.

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Transthyretin oligomers induce calcium influx via voltage-gated calcium channels.

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Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro

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Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity

21 January 2018

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Comparison of Lethal and Nonlethal Transthyretin Variants and Their Relationship to Amyloid Disease

21 January 2018

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The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions

21 January 2018

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The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis

21 January 2018

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Transthyretin fibrillogenesis entails the assembly of monomers: a molecular model for in vitro assembled transthyretin amyloid-like fibrils

21 January 2018

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Biophysical analyses of the transthyretin variants, Tyr114His and Tyr116Ser, associated with familial amyloidotic polyneuropathy

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Destabilization of transthyretin by pathogenic mutations in the DE loop.

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The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid

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Amyloid deposits in transthyretin-derived amyloidosis: cleaved transthyretin is associated with distinct amyloid morphology

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Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1.

21 January 2018

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Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation

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Expression of a synthetic gene encoding human transthyretin in Escherichia coli

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Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation

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A glimpse of a possible amyloidogenic intermediate of transthyretin

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Transthyretin Pro55, a variant associated with early-onset, aggressive, diffuse amyloidosis with cardiac and neurologic involvement

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Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin).

21 January 2018

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Primary structure of an amyloid prealbumin variant in familial polyneuropathy of Jewish origin

21 January 2018

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Detailed Structural Analysis of Amyloidogenic Wild-Type Transthyretin Using a Novel Purification Strategy and Mass Spectrometry

21 January 2018

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Electron Microscopic Observations on a Fibrous Component in Amyloid of Diverse Origins

21 January 2018

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21 January 2018

Identifiers

DOI

10.1002/PROT.21919

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1 January 2020

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