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Gelsolin

Known as: Gelsolin Protein, Gelsolin [Chemical/Ingredient], Serum Actin Inhibitory Protein 
A 90-kDa protein produced by macrophages that severs ACTIN filaments and forms a cap on the newly exposed filament end. Gelsolin is activated by… 
National Institutes of Health

Related topics

Related topics

13 relations

Broader (1)

Actin-Binding Protein
GSN geneIn BloodProcess of secretionagonists

Narrower (3)

brevingelsolin (160-169)scinderin

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
1999
1999
Actin-rich structures formed during the invasion of cultured cells by infective forms of Trypanosoma cruzi.
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
1994
Highly Cited
1994
Characterisation of the F‐actin binding domains of villin: classification of F‐actin binding proteins into two groups according to their binding sites on actin
Highly Cited
1990
Highly Cited
1990
Amyloid in familial amyloidosis, Finnish type, is antigenically and structurally related to gelsolin.
Immunohistochemical studies of six patients with familial amyloidosis, Finnish type, showed that their amyloid deposits did not… 
1990
1990
Inhibition of actin regulatory activity of the 74-kDa protein from bovine adrenal medulla (adseverin) by some phospholipids.
Highly Cited
1986
Highly Cited
1986
Secretory cell actin-binding proteins: identification of a gelsolin- like protein in chromaffin cells
Chromaffin cells, secretory cells of the adrenal medulla, have been shown to contain actin and other contractile proteins, which… 
Highly Cited
1985
Highly Cited
1985
Kinetic analysis of F-actin depolymerization in the presence of platelet gelsolin and gelsolin-actin complexes
Platelet gelsolin (G), a 90,000-mol-wt protein, binds tightly to actin (A) and calcium at low ionic strength to form a 1:2:2… 
1985
1985
Effects of semi-dilute actin solutions on the mobility of fibrin protofibrils during clot formation.
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… 
Highly Cited
1982
Highly Cited
1982
Human platelets contain gelsolin. A regulator of actin filament length.
Morphologic and biochemical studies suggest that actin in human platelets polymerizes in response to various stimuli and that… 
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