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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.
Highly Cited
2007
Highly Cited
2007
Effect of oxidative stress on protein thiols in the blue mussel Mytilus edulis: Proteomic identification of target proteins
Protein thiols are targets of oxidative stress. Their modification was analysed in gill extracts of the mussel Mytilus edulis… 
Highly Cited
2004
Highly Cited
2004
A dynamic podosome-like structure of epithelial cells.
Highly Cited
2001
Highly Cited
2001
Mechanisms of Cold-induced Platelet Actin Assembly*
Various agonists but also chilling cause blood platelets to increase cytosolic calcium, polymerize actin, and change shape. We… 
Highly Cited
1998
Highly Cited
1998
Spermine causes caspase activation in leukaemia cells
Highly Cited
1996
Highly Cited
1996
Dependence of Fibroblast Migration on Actin Severing Activity of Gelsolin*
Gelsolin nucleates actin filament assembly, blocks the fast-exchanging ends of actin filaments, and severs filaments, processes… 
Highly Cited
1989
Highly Cited
1989
Association of gelsolin with actin filaments and cell membranes of macrophages and platelets
Recent evidence that polyphosphoinositides regulate the function of the actin-modulating protein gelsolin in vitro raises the… 
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
1985
Highly Cited
1985
Isolation and properties of two actin-binding domains in gelsolin.
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… 
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