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brevin

National Institutes of Health

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Broader (2)

GelsolinMicrofilament Proteins

Papers overview

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Review
2002
Review
2002
Preparation and Purification of Polyclonal Antibodies to Gelsolin and Brevin
Gelsolin is a 90,000-mol-wt Ca2+-binding, actin-associated protein that can nucleate actin filament growth, sever filaments, and… 
1990
1990
The action of brevin, an F-actin severing protein, on the mechanical properties and ATPase activity of skinned smooth muscle
SummaryBrevin is a protein which regulates the actin gel-sol transformation: it severs F-actin filaments into shorter ones. This… 
Highly Cited
1986
Highly Cited
1986
Definition of an N-terminal actin-binding domain and a C-terminal Ca2+ regulatory domain in human brevin
Brevin is a Ca2+-modulated actin-associated protein that will sever F- actin and cap barbed filament ends. Limited proteolysis… 
1986
1986
A re-evaluation of cytoplasmic gelsolin localization
Gelsolin is a 90,000-mol-wt Ca2+-binding, actin-associated protein that can nucleate actin filament growth, sever filaments, and… 
1985
1985
Fluorescence study of brevin, the Mr 92 000 actin-capping and -fragmenting protein isolated from serum. Effect of Ca2+ on protein conformation.
The fluorescence characteristics of brevin and the effects of Ca2+ on the protein conformation were fully investigated. Brevin… 
Highly Cited
1984
Highly Cited
1984
Brevin and vitamin D binding protein: comparison of the effects of two serum proteins on actin assembly and disassembly.
Actin depolymerizing activity in serum can be attributed to the two proteins brevin and vitamin D binding protein (DBP). To… 
Highly Cited
1984
Highly Cited
1984
Actin polymerization. The effect of brevin on filament size and rate of polymerization.
Fluorescent probes covalently bound to actin or to the actin binding protein, brevin, have been utilized to provide information… 
1983
1983
Brevin, a serum protein that acts on the barbed end of actin filaments.
Highly Cited
1981
Highly Cited
1981
Characterization of brevin, a serum protein that shortens actin filaments.
We have purified a protein from rabbit serum with a molecular weight of 90,000 that inhibits the polymerization of actin measured… 
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