Found: 13
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ATP competes with PIP<sub>2</sub> for binding to gelsolin.
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- PLoS ONE, 2018, v. 13, n. 8, p. 1, doi. 10.1371/journal.pone.0201826
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- Article
An ER-directed gelsolin nanobody targets the first step in amyloid formation in a gelsolin amyloidosis mouse model.
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- Human Molecular Genetics, 2015, v. 24, n. 9, p. 2492, doi. 10.1093/hmg/ddv010
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- Article
Single-molecule force spectroscopy reveals force-enhanced binding of calcium ions by gelsolin.
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- Nature Communications, 2014, v. 5, n. 8, p. 4623, doi. 10.1038/ncomms5623
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- Article
The structures of the neurotrophin 4 homodimer and the brain-derived neurotrophic factor/neurotrophin 4 heterodimer reveal a common Trk-binding site.
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- Protein Science: A Publication of the Protein Society, 1999, v. 8, n. 12, p. 2589, doi. 10.1110/ps.8.12.2589
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- Article
The expanding superfamily of gelsolin homology domain proteins.
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- Cytoskeleton, 2013, v. 70, n. 11, p. 775, doi. 10.1002/cm.21149
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- Article
Gelsolin: The tail of a molecular gymnast.
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- Cytoskeleton, 2013, v. 70, n. 7, p. 360, doi. 10.1002/cm.21117
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- Article
Structural basis of actin sequestration by thymosin-ß4: implications for WH2 proteins.
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- EMBO Journal, 2004, v. 23, n. 18, p. 3599, doi. 10.1038/sj.emboj.7600372
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- Article
Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF.
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- EMBO Journal, 2004, v. 23, n. 14, p. 2713, doi. 10.1038/sj.emboj.7600280
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- Article
The structure of native G-actin.
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- Cytoskeleton, 2010, v. 67, n. 7, p. 456, doi. 10.1002/cm.20458
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- Article
The state of the filament.
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- EMBO Reports, 2005, v. 6, n. 3, p. 220, doi. 10.1038/sj.embor.7400363
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- Article
The cellulose-binding domain of endoglucanase A (CenA) from Cellulomonas fimi: evidence for the involvement of tryptophan residues in binding.
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- Molecular Microbiology, 1994, v. 11, n. 4, p. 747, doi. 10.1111/j.1365-2958.1994.tb00352.x
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- Article
From the first to the second domain of gelsolin: a common path on the surface of actin?<sup>1</sup><FN ID="FN1"><NO>1</NO>Data deposition: The atomic coordinates and merged structure factors have been deposited in the Protein Data Bank, www.rcsb.org (PDB ID code 1P8Z).</FN>
- Published in:
- FEBS Letters, 2003, v. 552, n. 2/3, p. 86, doi. 10.1016/S0014-5793(03)00934-7
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- Article
Activation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin<sup>1</sup><FN ID="FN1"><NO>1</NO>Data deposition: The atomic coordinates and merged structure factors have been deposited in the Protein Data Bank, www.rcsb.org (PDB ID code 1P8X).</FN>
- Published in:
- FEBS Letters, 2003, v. 552, n. 2/3, p. 82, doi. 10.1016/S0014-5793(03)00933-5
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- Article