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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…
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National Institutes of Health
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Related topics
Related topics
13 relations
Broader (1)
Actin-Binding Protein
GSN gene
In Blood
Process of secretion
agonists
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Narrower (3)
brevin
gelsolin (160-169)
scinderin
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2007
Highly Cited
2007
Actin limits enhancement of nanoparticle diffusion through cystic fibrosis sputum by mucolytics.
Victoria J Broughton-Head
,
James R. Smith
,
J. Shur
,
J. Shute
Pulmonary Pharmacology & Therapeutics
2007
Corpus ID: 45801325
2002
2002
Rapid turnover of actin in dendritic spines and its regulation by activity
Erin N. Star
,
D. Kwiatkowski
,
V. Murthy
Nature Neuroscience
2002
Corpus ID: 52837284
Nat. Neurosci. 5, 239–246 (2002) Due to a printing error, the green in Fig. 2a was difficult to see. The corrected figure is…
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Highly Cited
1997
Highly Cited
1997
Probing the effects of calcium on gelsolin.
B. Pope
,
J. Gooch
,
A. Weeds
Biochemistry
1997
Corpus ID: 21527658
Gelsolin is a calcium-regulated actin severing and capping protein that binds two calcium ions and has three sites for actin; two…
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Highly Cited
1996
Highly Cited
1996
Dependence of Fibroblast Migration on Actin Severing Activity of Gelsolin*
P. Arora
,
C. McCulloch
Journal of Biological Chemistry
1996
Corpus ID: 27681155
Gelsolin nucleates actin filament assembly, blocks the fast-exchanging ends of actin filaments, and severs filaments, processes…
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Highly Cited
1994
Highly Cited
1994
Determination of the alpha-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis
A. McGough
,
Michael Way
,
D. DeRosier
Journal of Cell Biology
1994
Corpus ID: 1167246
The three-dimensional structure of actin filaments decorated with the actin-binding domain of chick smooth muscle alpha-actinin…
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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
B. Pope
,
M. Way
,
P. Matsudaira
,
A. Weeds
FEBS Letters
1994
Corpus ID: 24739213
Highly Cited
1990
Highly Cited
1990
Gelsolin variant (Asn-187) in familial amyloidosis, Finnish type.
J. Ghiso
,
M. Haltia
,
F. Prelli
,
J. Novello
,
B. Frangione
Biochemical Journal
1990
Corpus ID: 28973411
Familial amyloidosis, Finnish type (FAF), is an inherited form of systemic amyloidosis clinically characterized by cranial…
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Highly Cited
1989
Highly Cited
1989
Association of gelsolin with actin filaments and cell membranes of macrophages and platelets
J. H. Hartwig
,
Kristen A Chambers
,
Thomas P. Stossel
Journal of Cell Biology
1989
Corpus ID: 17478849
Recent evidence that polyphosphoinositides regulate the function of the actin-modulating protein gelsolin in vitro raises the…
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Highly Cited
1985
Highly Cited
1985
Kinetic analysis of F-actin depolymerization in the presence of platelet gelsolin and gelsolin-actin complexes
J. Bryan
,
L. M. Coluccio
Journal of Cell Biology
1985
Corpus ID: 8342059
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…
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Highly Cited
1984
Highly Cited
1984
Gelsolin inhibition of fast axonal transport indicates a requirement for actin microfilaments
S. Brady
,
R. Lasek
,
R. Allen
,
H. Yin
,
T. Stossel
Nature
1984
Corpus ID: 4343876
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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