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GSN gene

Known as: amyloidosis, Finnish type, GSN, GELSOLIN 
National Institutes of Health

Related topics

Related topics

4 relations
Familial Amyloid Polyneuropathy, Type VGelsolinMeretoja syndrome

Broader (1)

Genes

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2005
2005
Immunodepletion of albumin for two‐dimensional gel detection of new mouse acute‐phase protein and other plasma proteins
Immunodepletion of albumin to improve the 2‐D gel resolution of human plasma proteins has recently been described. With the… 
Highly Cited
1999
Highly Cited
1999
The 135 kDa actin-bundling protein fromLilium longiflorum pollen is the plant homologue of villin
SummaryActin microfilaments, which are essential for cell growth and cytoplasmic streaming in pollen tubes, are closely dependent… 
Highly Cited
1998
Highly Cited
1998
Spermine causes caspase activation in leukaemia cells
1997
1997
Analogous F-actin Binding by Cofilin and Gelsolin Segment 2 Substantiates Their Structural Relationship*
Cofilin is representative for a family of low molecular weight actin filament binding and depolymerizing proteins. Recently the… 
1996
1996
In vitro expression analysis shows that the secretory form of gelsolin is the sole source of amyloid in gelsolin-related amyloidosis.
Amyloidoses are a group of diseases where abnormal fibrillar protein deposits accumulate in patients' tissues. In familial… 
Highly Cited
1995
Highly Cited
1995
Structure of severin domain 2 in solution.
The three-dimensional structure of domain 2 of severin in aqueous solution was determined by nuclear magnetic resonance… 
Highly Cited
1988
Highly Cited
1988
Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats.
Highly Cited
1988
Highly Cited
1988
Localization of gelsolin proximal to ABL on chromosome 9.
Gelsolin is a plasma and cytoskeletal protein that severs actin filaments and is regulated by both Ca+2 and polyphosphoinositides… 
Highly Cited
1984
Highly Cited
1984
Gelsolin inhibition of fast axonal transport indicates a requirement for actin microfilaments
The actions of actin-based microfilaments in cell motility suggest a possible role in the mechanism of fast axonal transport1–3… 
1983
1983
Isolation of a Ca2+‐Dependent Actin‐Fragmenting Protein from Brain, Spinal Cord, and Cultured Neurones
Extracts of ox spinal cord and chicken brain were fractionated by ion‐exchange chromatography and assayed for their ability to… 
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