Co-precipitation molecules hemopexin and transferrin may be key molecules for fibrillogenesis in TTR V30M amyloidogenesis.

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Co-precipitation molecules hemopexin and transferrin may be key molecules for fibrillogenesis in TTR V30M amyloidogenesis.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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Co-precipitation molecules hem ...... s in TTR V30M amyloidogenesis.

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Co-precipitation molecules hem ...... s in TTR V30M amyloidogenesis.

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Item

label

Co-precipitation molecules hem ...... s in TTR V30M amyloidogenesis.

@en

Co-precipitation molecules hem ...... s in TTR V30M amyloidogenesis.

@nl

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Co-precipitation molecules hem ...... s in TTR V30M amyloidogenesis.

@en

Co-precipitation molecules hem ...... s in TTR V30M amyloidogenesis.

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P1476

Co-precipitation molecules hem ...... s in TTR V30M amyloidogenesis.

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P2093

Aki Sugano

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Hajime Tei

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

Hirofumi Shimada

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Hirotaka Sato

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Hitoshi Niwa

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Ken-Ichi Yamamura

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Mika Ohta

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Naoya Hatano

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

Toshiyuki Sakaeda

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

Yoshiyuki Sakaki

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P2860

ModBase, a database of annotated comparative protein structure models, and associated resources

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

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

The biological and chemical basis for tissue-selective amyloid disease.

Human transthyretin (prealbumin) gene and molecular genetics of familial amyloidotic polyneuropathy.

Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversion

Cysteine 10 is a key residue in amyloidogenesis of human transthyretin Val30Met.

Why is Leu55-->Pro55 transthyretin variant the most amyloidogenic: insights from molecular dynamics simulations of transthyretin monomers

Analysis of a single-codon E746 deletion in exon 19 of the epidermal growth factor receptor.

Amyloid deposits and amyloidosis. The beta-fibrilloses (first of two parts).

P2888

s11248-017-0054-x

P304

15-23

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scholarly article

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10.1007/S11248-017-0054-X

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P433

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

P478

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P50

Yutaka Takaoka

P577

2017-12-29T00:00:00Z

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29288430

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5847157

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