DOI: 10.1016/j.jmb.2007.10.076. Actin Hydrophobic Loop 262–274 and Filament Nucleation and Elongation

Actin Hydrophobic Loop 262–274 and Filament Nucleation and Elongation

10.1016/j.jmb.2007.10.076

Crossref journal-article

Elsevier BV

Journal of Molecular Biology (78)

Bibliography

Shvetsov, A., Galkin, V. E., Orlova, A., Phillips, M., Bergeron, S. E., Rubenstein, P. A., Egelman, E. H., & Reisler, E. (2008). Actin Hydrophobic Loop 262â274 and Filament Nucleation and Elongation. Journal of Molecular Biology, 375(3), 793â801.

Authors 8

Alexander Shvetsov (first)
Vitold E. Galkin (additional)
Albina Orlova (additional)
Martin Phillips (additional)
Sarah E. Bergeron (additional)
Peter A. Rubenstein (additional)
Edward H. Egelman (additional)
Emil Reisler (additional)

References 33 Referenced 15

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{'year': '2004', 'series-title': 'Cell Biology', 'author': 'Polard', 'key': '10.1016/j.jmb.2007.10.076_bib3'} / Cell Biology by Polard (2004)
10.1152/physrev.00026.2002 / Physiol. Rev. / Actin binding proteins: regulation of cytoskeletal microfilaments by Dos Remedios (2003)
10.1083/jcb.153.1.75 / J. Cell Biol. / Actin depolymerizing factor stabilizes an existing state of F-actin and changes the tilt of F-actin subunits by Galkin (2001)
10.1073/pnas.0407525102 / Proc. Natl Acad. Sci. USA / Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization by Orlova (2004)
10.1038/347044a0 / Nature / Atomic model of the actin filament by Holmes (1990)
10.1006/jmbi.1993.1628 / J. Mol. Biol. / Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm by Lorenz (1993)
10.1038/35092500 / Nature / Prokaryotic origin of the actin cytoskeleton by van den Ent (2001)
10.1093/emboj/cdf672 / EMBO J. / F-actin-like filaments formed by plasmid segregation protein ParM by van den Ent (2002)
10.1021/bi020205f / Biochemistry / Locking the hydrophobic loop 262–274 to G-actin surface by a disulfide bridge prevents filament formation by Shvetsov (2002)
10.1021/bi052558v / Biochemistry / Conformational dynamics of loop 262–274 in G- and F-actin by Shvetsov (2006)
10.1021/bi061229f / Biochemistry / Hydrophobic loop dynamics and actin filament stability by Scoville (2006)
10.1083/jcb.138.4.771 / J. Cell Biol. / Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function by McGough (1997)
10.1093/emboj/16.18.5520 / EMBO J. / Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis by Lappalainen (1997)
10.1006/jmbi.2001.5280 / J. Mol. Biol. / Determining the differences in actin binding by human ADF and cofilin by Yeoh (2002)
10.1021/bi049797n / Biochemistry / In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups by Chen (2004)
10.1016/j.molcel.2006.08.006 / Mol. Cell / Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin by Andrianantoandro (2006)
10.1529/biophysj.104.042242 / Biophys. J. / Formation and destabilization of actin filaments with tetramethylrhodamine-modified actin by Kudryashov (2004)
10.1073/pnas.84.15.5262 / Proc. Natl Acad. Sci. USA / Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells by Nishida (1987)
10.1006/jmbi.1997.1062 / J. Mol. Biol. / Control of actin dynamics in cell motility by Carlier (1997)
10.1146/annurev.cellbio.15.1.185 / Annu. Rev. Cell Dev. Biol. / Proteins of the ADF/cofilin family: essential regulators of actin dynamics by Bamburg (1999)
10.1016/j.jmb.2004.01.014 / J. Mol. Biol. / Cofilin (ADF) affects lateral contacts in F-actin by Bobkov (2004)
10.1074/jbc.272.7.4412 / J. Biol. Chem. / The effects of severely decreased hydrophobicity in a subdomain 3/4 loop on the dynamics and stability of yeast G-actin by Kuang (1997)
10.1016/S0304-3991(00)00062-0 / Ultramicroscopy / A robust algorithm for the reconstruction of helical filaments using single-particle methods by Egelman (2000)
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10.1021/bi0117697 / Biochemistry / Identification of yeast cofilin residues specific for actin monomer and PIP2 binding by Ojala (2001)
10.1016/j.jmb.2006.10.102 / J. Mol. Biol. / Actin filament severing by cofilin by Pavlov (2007)
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Dates

Type	When
Created	17 years, 8 months ago (Nov. 28, 2007, 7:16 a.m.)
Deposited	1 year, 6 months ago (Feb. 23, 2024, 12:18 p.m.)
Indexed	6 months ago (Feb. 20, 2025, 9:36 p.m.)
Issued	17 years, 7 months ago (Jan. 1, 2008)
Published	17 years, 7 months ago (Jan. 1, 2008)
Published Print	17 years, 7 months ago (Jan. 1, 2008)

Funders 2

U.S. Public Health Service 10.13039/100007197
Region: Americas
gov (National government)
Labels6
1. United States Public Health Service
2. Commissioned Corps of the U.S. Public Health Service
3. USPHS Commissioned Corps
4. U.S. Public Health Service Commissioned Corps
5. USPHS
6. PHS
Awards1
1. GM 077190
National Science Foundation 10.13039/100000001
Region: Americas
gov (National government)
Labels4
1. U.S. National Science Foundation
2. NSF
3. US NSF
4. USA NSF
Awards3
1. GM33689
2. MCB 0316269
3. AR042023

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