Equilibria and kinetics of folding of gelsolin domain 2 and mutants involved in familial amyloidosis-Finnish type (Q35645325)

9 August 2017

title

Equilibria and kinetics of folding of gelsolin domain 2 and mutants involved in familial amyloidosis-Finnish type (English)

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9 August 2017

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3

Fersht AR

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9 August 2017

Isaacson RL

1

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9 August 2017

Weeds AG

series ordinal

2

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9 August 2017

language of work or name

English

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publication date

1 September 1999

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Proceedings of the National Academy of Sciences of the United States of America

9 August 2017

published in

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9 August 2017

volume

96

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9 August 2017

issue

20

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9 August 2017

page(s)

11247-11252

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9 August 2017

cites work

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12 July 2018

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12 July 2018

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Alternative conformations of amyloidogenic proteins govern their behavior

12 July 2018

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12 July 2018

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12 July 2018

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Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin

12 July 2018

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12 July 2018

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Familial systemic paramyloidosis with lattice dystrophy of the cornea, progressive cranial neuropathy, skin changes and various internal symptoms. A previously unrecognized heritable syndrome

12 July 2018

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Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain

12 July 2018

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Calculation of protein extinction coefficients from amino acid sequence data

12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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12 July 2018

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Cells of the neuronal lineage play a major role in the generation of amyloid precursor fragments in gelsolin-related amyloidosis

12 July 2018

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Gelsolin–derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187

25 September 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073/PNAS.96.20.11247

Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073/PNAS.96.20.11247

Movement of the position of the transition state in protein folding

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073/PNAS.96.20.11247

Variant plasma gelsolin responsible for familial amyloidosis (Finnish type) has defective actin severing activity

21 January 2018

1 reference

12 December 2020

Reduction in viscosity of cystic fibrosis sputum in vitro by gelsolin

1 reference

12 December 2020

Amyloid protein in familial amyloidosis (Finnish type) is homologous to gelsolin, an actin-binding protein

1 reference

12 December 2020

In vitro expression analysis shows that the secretory form of gelsolin is the sole source of amyloid in gelsolin-related amyloidosis

1 reference

12 December 2020

Gelsolin Activates DNase Iin Vitroand in Cystic Fibrosis Sputum

1 reference

12 December 2020

Identification of the circulating amyloid precursor and other gelsolin metabolites in patients with G654A mutation in the gelsolin gene (Finnish familial amyloidosis): pathogenetic and diagnostic implications

1 reference

12 December 2020

The amyloidogenicity of gelsolin is controlled by proteolysis and pH

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.96.20.11247

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9 August 2017

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9 August 2017

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