DOI: 10.1006/jmbi.2001.5281. Polymerisation of chemically cross-linked actin:thymosin β 4 complex to filamentous actin: alteration in helical parameters and visualisation of thymosin β 4 binding on F-actin 1 1Edited by W. Baumeister

Polymerisation of chemically cross-linked actin:thymosin β 4 complex to filamentous actin: alteration in helical parameters and visualisation of thymosin β 4 binding on F-actin 1 1Edited by W. Baumeister

10.1006/jmbi.2001.5281

Crossref journal-article

Elsevier BV

Journal of Molecular Biology (78)

Bibliography

Ballweber, E., Hannappel, E., Huff, T., Stephan, H., Haener, M., Taschner, N., Stoffler, D., Aebi, U., & Mannherz, H. G. (2002). Polymerisation of chemically cross-linked actin:thymosin Î² 4 complex to filamentous actin: alteration in helical parameters and visualisation of thymosin Î² 4 binding on F-actin 1 1Edited by W. Baumeister. Journal of Molecular Biology, 315(4), 613â625.

Authors 9

Edda Ballweber (first)
Ewald Hannappel (additional)
Thomas Huff (additional)
Harald Stephan (additional)
Markus Haener (additional)
Nicole Taschner (additional)
Daniel Stoffler (additional)
Ueli Aebi (additional)
Hans Georg Mannherz (additional)

References 42 Referenced 48

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{'key': '10.1006/jmbi.2001.5281_BIB7', 'series-title': 'Untersuchungen zur Polymerisation des Aktins aus dem Komplex mit β-Thymosinen', 'author': 'Ballweber', 'year': '1995'} / Untersuchungen zur Polymerisation des Aktins aus dem Komplex mit β-Thymosinen by Ballweber (1995)
10.1042/bj3270787 / Biochem. J. / Mapping the binding site of thymosin β4 on actin by competition with G-actin binding proteins indicates negative cooperativity between binding sites located on subdomains 1 and 2 of actin by Ballweber (1997)
10.1016/S0014-5793(98)00240-3 / FEBS-Letters / Plant profilin induces actin polymerisation from actin:thymosin complexes and competes directly with β-thymosins and with negative co-operativity with DNase I for binding to actin by Ballweber (1998)
10.1111/j.1432-1033.1994.tb19009.x / Eur. J. Biochem. / Induction of the repolymerisation of actin from the actin:thymosin β4 complex by calcium, phalloidin, free ends of filamentous actin, skeletal muscle subfragment 1 and chicken intestinal myosin I by Ballweber (1994)
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10.1016/S0014-5793(99)01670-1 / FEBS Letters / Thymosin β4 serves as a glutaminyl substrate of transglutaminase. Labelling with fluorescent dansylcadaverine does not abolish interaction with G-actin by Huff (1999)
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Dates

Type	When
Created	22 years, 10 months ago (Oct. 6, 2002, 2:37 p.m.)
Deposited	4 years, 3 months ago (May 3, 2021, 1:40 a.m.)
Indexed	1 year, 3 months ago (May 22, 2024, 10:32 a.m.)
Issued	23 years, 8 months ago (Jan. 1, 2002)
Published	23 years, 8 months ago (Jan. 1, 2002)
Published Print	23 years, 8 months ago (Jan. 1, 2002)

Funders 0

None

BibTeX

@article{Ballweber_2002, title={Polymerisation of chemically cross-linked actin:thymosin β 4 complex to filamentous actin: alteration in helical parameters and visualisation of thymosin β 4 binding on F-actin 1 1Edited by W. Baumeister}, volume={315}, ISSN={0022-2836}, url={http://dx.doi.org/10.1006/jmbi.2001.5281}, DOI={10.1006/jmbi.2001.5281}, number={4}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Ballweber, Edda and Hannappel, Ewald and Huff, Thomas and Stephan, Harald and Haener, Markus and Taschner, Nicole and Stoffler, Daniel and Aebi, Ueli and Mannherz, Hans Georg}, year={2002}, month=jan, pages={613–625} }

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