Structural and motional changes in glyceraldehyde-3-phosphate dehydrogenase upon binding to the band-3 protein of the erythrocyte membrane examined with [15N,2H]maleimide spin label and electron paramagnetic resonance.-Reference-Cited by-同舟云学术

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Structural and motional changes in glyceraldehyde-3-phosphate dehydrogenase upon binding to the band-3 protein of the erythrocyte membrane examined with [15N,2H]maleimide spin label and electron paramagnetic resonance.

Published:1981-08-01 Issue:8 Volume:78 Page:4955-4959
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Beth A. H.,Balasubramanian K.,Wilder R. T.,Venkataramu S. D.,Robinson B. H.,Dalton L. R.,Pearson D. E.,Park J. H.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Cited by 40 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Solution Structure of the Cytoplasmic Domain of Erythrocyte Membrane Band 3 Determined by Site-Directed Spin Labeling;Biochemistry;2005-10-29

2. High Field/High Frequency Saturation Transfer Electron Paramagnetic Resonance Spectroscopy: Increased Sensitivity to Very Slow Rotational Motions;Biophysical Journal;2004-06

3. The complex of band 3 protein of the human erythrocyte membrane and glyceraldehyde-3-phosphate dehydrogenase: stoichiometry and competition by aldolase;Biochimica et Biophysica Acta (BBA) - Biomembranes;2002-02

4. Rotational Dynamics of the Epidermal Growth Factor Receptor;Biochemistry;2002-01-18

5. Flexibility of the Cytoplasmic Domain of the Anion Exchange Protein, Band 3, in Human Erythrocytes;Biophysical Journal;2001-12

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