DOI: 10.1016/j.jmb.2010.02.010. Polymeric Structures and Dynamic Properties of the Bacterial Actin AlfA

Polymeric Structures and Dynamic Properties of the Bacterial Actin AlfA

10.1016/j.jmb.2010.02.010

Crossref journal-article

Elsevier BV

Journal of Molecular Biology (78)

Bibliography

Popp, D., Narita, A., Ghoshdastider, U., Maeda, K., MaÃ©da, Y., Oda, T., Fujisawa, T., Onishi, H., Ito, K., & Robinson, R. C. (2010). Polymeric Structures and Dynamic Properties of the Bacterial Actin AlfA. Journal of Molecular Biology, 397(4), 1031â1041.

Authors 10

David Popp (first)
Akihiro Narita (additional)
Umesh Ghoshdastider (additional)
Kayo Maeda (additional)
Yuichiro Maéda (additional)
Toshiro Oda (additional)
Tetsuro Fujisawa (additional)
Hirufumi Onishi (additional)
Kazuki Ito (additional)
Robert C. Robinson (additional)

References 29 Referenced 32

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10.1016/0022-2836(91)90212-O / J. Mol. Biol. / Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein–DNA interactions in vivo by Cayley (1991)
10.1073/pnas.77.5.2470 / Proc. Natl Acad. Sci. USA / Measurement of the internal pH of yeast spores by 31P nuclear magnetic resonance by Barton (1980)
10.1128/jb.176.8.2252-2258.1994 / J. Bacteriol. / The internal pH of the forespore compartment of Bacillus magaterium decreases by about 1 pH unit during sporulation by MacGill (1994)
10.1038/sj.emboj.7601443 / EMBO J. / DNA segregation by the bacterial actin AlfA during Bacillus subtilis growth and development by Becker (2006)
10.1242/jcs.01670 / J. Cell Sci. / Actin-binding proteins by Winder (2005)
10.1016/S0092-8674(01)00287-2 / Cell / Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis by Jones (2001)
10.1093/emboj/cdf320 / EMBO J. / Prokaryotic DNA segregation by an actin-like filament by Møller-Jensen (2002)
10.1021/bi701538e / Biochemistry / Polymerization properties of the Thermatoga maritima actin MreB: roles of temperature, nucleotides and ions by Bean (2008)
10.1529/biophysj.104.044149 / Biophys. J. / A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus by Chen (2005)
10.1038/sj.emboj.7601978 / EMBO J. / Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instability by Popp (2008)
10.1016/S0021-9258(18)52391-7 / J. Biol. Chem. / Actin: protein structure and filament dynamics by Carlier (1991)
10.1073/pnas.89.11.4884 / Proc. Natl Acad. Sci. / A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems by Webb (1992)
10.1074/jbc.M800570200 / J. Biol. Chem. / Dual roles of Gln137 of actin revealed by recombinant human cardiac muscle α-actin mutants by Iwasa (2008)
10.1038/ncb841 / Nat. Cell Biol. / Microscopic analysis of polymerization dynamics with individual actin filaments by Fujiwara (2002)
10.1038/352126a0 / Nature / Actin microfilament dynamics in locomotive cells by Theriot (1991)
10.1046/j.0014-2956.2001.02664.x / Eur. J. Biochem. / Fluorescence study of high pressure-induced denaturation of skeletal muscle actin by Ikeuchi (2002)
{'key': '10.1016/j.jmb.2010.02.010_bib18', 'series-title': 'The Use of X-ray Diffraction in the Study of Protein and Nucleic Acid Structure', 'first-page': '209', 'author': 'Holmes', 'year': '1965'} / The Use of X-ray Diffraction in the Study of Protein and Nucleic Acid Structure by Holmes (1965)
10.1021/bi00278a021 / Biochemistry / Kinetic evidence for a monomer activation step in actin polymerization by Cooper (1983)
10.1128/JB.00676-09 / J. Bacteriol. / The structure and assembly dynamics of plasmid actin AlfA imply a novel mechanism of DNA segregation by Polka (2009)
10.1038/347044a0 / Nature / Atomic model of the actin filament by Holmes (1990)
10.1038/35092500 / Nature / Prokaryotic origin of the actin cytoskeleton by Van den Ent (2001)
10.1096/fasebj.22.1_supplement.537.3 / FASEB J. / Polymorphic perversity in protein polymers by Egelman (2008)
10.1002/bip.20999 / Biopolymers / Effect of short-range forces on the length distribution of cytoskeletal proteins by Popp (2008)
10.1042/bj1410331 / Biochem. J. / The characterization of myosin–product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphate reaction by Bagshaw (1973)
10.1006/abio.1996.0238 / Ann. Biochem. / Program DYNAFIT for the analysis of enzyme kinetic data: applications to the HIV proteinase by Kuzmic (1996)
10.1006/jsbi.1996.0025 / J. Struct. Biol. / Extensible and object-oriented system Eos supplies a new environment for image analysis of electron micrographs of macromolecules by Yasunaga (1996)
10.1016/S0168-9002(01)00738-0 / Nucl. Instrum. Methods Phys. Res. Sect. A / Improvement of a high pressure cell with diamond windows for solution X-ray scattering of proteins by Nishikawa (2001)
10.5940/jcrsj.42.97 / J. Crystallogr. Soc. Jpn. / Structural studies on protein solutions by using solution X-ray scattering technique at RIKEN structural biology beamline I (BL45XU) by Fujisawa (2000)

Dates

Type	When
Created	15 years, 6 months ago (Feb. 13, 2010, 4:24 a.m.)
Deposited	1 year, 6 months ago (Feb. 23, 2024, 12:38 p.m.)
Indexed	1 year ago (Aug. 3, 2024, 10:36 p.m.)
Issued	15 years, 4 months ago (April 1, 2010)
Published	15 years, 4 months ago (April 1, 2010)
Published Print	15 years, 4 months ago (April 1, 2010)

Funders 0

None

BibTeX

@article{Popp_2010, title={Polymeric Structures and Dynamic Properties of the Bacterial Actin AlfA}, volume={397}, ISSN={0022-2836}, url={http://dx.doi.org/10.1016/j.jmb.2010.02.010}, DOI={10.1016/j.jmb.2010.02.010}, number={4}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Popp, David and Narita, Akihiro and Ghoshdastider, Umesh and Maeda, Kayo and Maéda, Yuichiro and Oda, Toshiro and Fujisawa, Tetsuro and Onishi, Hirufumi and Ito, Kazuki and Robinson, Robert C.}, year={2010}, month=apr, pages={1031–1041} }

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