Unique Structural Changes in Calcium-Bound Calmodulin Upon Interaction with Protein 4.1R FERM Domain: Novel Insights into the Calcium-dependent Regulation of 4.1R FERM Domain Binding to Membrane Proteins by Calmodulin-Reference-Cited by-同舟云学术

Unique Structural Changes in Calcium-Bound Calmodulin Upon Interaction with Protein 4.1R FERM Domain: Novel Insights into the Calcium-dependent Regulation of 4.1R FERM Domain Binding to Membrane Proteins by Calmodulin

Published:2013-10-01 Issue:1 Volume:69 Page:7-19
ISSN:1085-9195
Container-title:Cell Biochemistry and Biophysics
language:en
Short-container-title:Cell Biochem Biophys

Author:

Nunomura Wataru,Isozumi Noriyoshi,Nakamura Shigeyoshi,Jinbo Yuji,Ohki Shinya,Kidokoro Shun-ichi,Wakui Hideki,Takakuwa Yuichi

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Biochemistry,General Medicine,Biophysics

Link

http://link.springer.com/content/pdf/10.1007/s12013-013-9758-6.pdf

Reference48 articles.

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2. Nunomura, W., & Takakuwa, Y. (2006). Regulation of protein 4.1R interactions with membrane proteins by Ca2+ and calmodulin. Frontier Bioscience, 11, 1522–1539.

3. Pasternack, G. R., Anderson, R. A., Leto, T. L., & Marchesi, V. T. (1985). Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton. Journal of Biological Chemistry, 260, 3676–3683.

4. Anderson, R. A., & Lovrien, R. E. (1984). Glycophorin is linked by band 4.1 protein to the human erythrocyte membrane skeleton. Nature, 307(5952), 655–658.

5. Nunomura, W., Takakuwa, Y., Tokimitsu, R., Krauss, S. W., Kawashima, M., & Mohandas, N. (1997). Regulation of CD44-protein 4.1 interaction by Ca2+ and calmodulin. Implications for modulation of CD44-ankyrin interaction. Journal of Biological Chemistry, 272, 30322–30328.

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