Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin (Q57665572)

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3 November 2019

title

Comparative calorimetric study of non-amyloidogenic and amyloidogenic variants of the homotetrameric protein transthyretin (English)

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3 November 2019

author

Jose Manuel Sanchez Ruiz

4

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3 November 2019

Alexandre Quintas

5

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3 November 2019

Maria João Saraiva

6

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3 November 2019

Rui M. Brito

7

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3 November 2019

author name string

V L Shnyrov

1

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3 November 2019

E Villar

2

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3 November 2019

G G Zhadan

3

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3 November 2019

publication date

1 December 2000

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3 November 2019

published in

Biophysical Chemistry

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3 November 2019

volume

88

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3 November 2019

issue

1-3

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3 November 2019

page(s)

61-67

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An X-ray study of the subunit structure of prealbumin

3 November 2019

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Biochemical and clinical characterization of prealbuminCHICAGO: an apparently benign variant of serum prealbumin (transthyretin) discovered with high-resolution two-dimensional electrophoresis

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The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils

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Production of recombinant human transthyretin with biological activities toward the understanding of the molecular basis of familial amyloidotic polyneuropathy (FAP).

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The amyloidogenic potential of transthyretin variants correlates with their tendency to aggregate in solution

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Identifiers

DOI

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3 November 2019

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