Calponin homology domains at a glance-Reference-Cited by-同舟云学术

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Calponin homology domains at a glance

Published:2002-09-15 Issue:18 Volume:115 Page:3543-3545
ISSN:1477-9137
Container-title:Journal of Cell Science
language:en
Short-container-title:

Author:

Korenbaum Elena¹,Rivero Francisco²

Affiliation:

1. Institut für Biochemie I, Medizinische Fakultät,Universität zu Köln, Joseph-Stelzmann-Strasse 52, D-50931 Köln,Germany

2. Present address: Abteilung Biophysikalische Chemie, OE 4350, Medizinische Hochschule Hannover, Carl-Neuberg-Str. 1, D-30625, Hannover, Germany

Publisher

The Company of Biologists

Subject

Cell Biology

Link

http://journals.biologists.com/jcs/article-pdf/115/18/3543/1360535/3543.pdf

Reference9 articles.

1. Banuelos, S., Saraste, M. and Carugo, K. D.(1998). Structural comparisons of calponin homology domains:implications for actin binding. Structure6, 1419-1431.

2. Bramham, J., Hodgkinson, J. L., Smith, B. O., Uhrin, D., Barlow,P. N. and Winder, S. J. (2002). Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin:calponin. Structure10, 249-258.

3. Dubreuil, R. R. (1991). Structure and evolution of the actin crosslinking proteins. Bioessays13, 219-226.

4. Fu, Y., Liu, H. W., Forsythe, S. M., Kogut, P., McConville, J. F., Halayko, A. J., Camoretti-Mercado, B. and Solway, J.(2000). Mutagenesis analysis of human SM22: characterization of actin binding. J. Appl. Physiol.89, 1985-1990.

5. Gimona, M. and Mital, R. (1998). The single CH domain of calponin is neither sufficient nor necessary for F-actin binding.J. Cell Sci.111, 1813-1821.

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