(Q47954592)

7 February 2018

title

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

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7 February 2018

author name string

Paunio T

1

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7 February 2018

Kangas H

2

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7 February 2018

Heinonen O

3

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7 February 2018

Buc-Caron MH

4

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7 February 2018

Robert JJ

5

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7 February 2018

Kaasinen S

6

1 reference

7 February 2018

Julkunen I

7

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7 February 2018

Mallet J

8

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7 February 2018

Peltonen L

9

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7 February 2018

language of work or name

English

0 references

publication date

1 June 1998

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7 February 2018

Journal of Biological Chemistry

published in

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7 February 2018

volume

273

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7 February 2018

issue

26

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7 February 2018

page(s)

16319-16324

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7 February 2018

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

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Gelsolin variant (Asn-187) in familial amyloidosis, Finnish type

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The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure

21 January 2018

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Solid-phase minisequencing test reveals Asp187 → Asn (G654 → A) mutation of gelsolin in all affected individuals with finnish type of familial amyloidosis

21 January 2018

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Neuroepithelial progenitor cells explanted from human fetal brain proliferate and differentiate in vitro

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Widespread long-term gene transfer to mouse skeletal muscles and heart

21 January 2018

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The actin filament-severing domain of plasma gelsolin

21 January 2018

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Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface

21 January 2018

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The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation

21 January 2018

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

21 January 2018

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

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Postmortem pathological findings in a Japanese patient with familial amyloidosis, Finnish type (FAF)

21 January 2018

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Quantification of serum and cerebrospinal fluid gelsolin in familial amyloidosis, Finnish type (AGel)

21 January 2018

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Familial amyloidosis of the Finnish type (FAF). A clinical study of 30 patients

21 January 2018

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Comparative histopathological and clinical findings in eyes with lattice corneal dystrophy of two different types

21 January 2018

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Isolation and characterization of cardiac amyloid in familial amyloid polyneuropathy type IV (Finnish): relation of the amyloid protein to variant gelsolin

21 January 2018

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Toward understanding the pathogenic mechanisms in gelsolin-related amyloidosis: in vitro expression reveals an abnormal gelsolin fragment

21 January 2018

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

21 January 2018

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Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline

21 January 2018

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

21 January 2018

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Tissue distribution and levels of gelsolin mRNA in normal individuals and patients with gelsolin-related amyloidosis

21 January 2018

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Amyloid precursor protein metabolism in primary cell cultures of neurons, astrocytes, and microglia

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.26.16319

1 reference

7 February 2018

PubMed ID

9632693

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7 February 2018