A gel-encapsulated bioreactor system for NMR studies of protein-protein interactions in living mammalian cells

Angewandte Chemie - International Edition

Volumn 52, Issue 4, 2013, Pages 1208-1211

  Kubo, Satoshi ^a   Nishida, Noritaka ^a   Udagawa, Yuko ^a   Takarada, Osamu ^a   Ogino, Shinji ^a   Shimada, Ichio ^a,b  

^a UNIVERSITY OF TOKYO   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

analytical methods; biophysics; NMR spectroscopy; protein protein interactions; structural biology

Indexed keywords

ANALYTICAL METHOD; BIOREACTOR SYSTEM; MAMMALIAN CELLS; NMR MEASUREMENTS; NMR STUDIES; NMR TUBES; PROTEIN-PROTEIN INTERACTIONS; STRUCTURAL BIOLOGY;

BINDING SITES; BIOPHYSICS; BIOREACTORS; CELL DEATH; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SPECTROSCOPIC ANALYSIS;

PROTEINS;

ARTICLE; BIOREACTOR; CHEMISTRY; GEL; HELA CELL; HUMAN; METABOLISM; MICROTUBULE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN PROTEIN INTERACTION; PROTEIN TERTIARY STRUCTURE;

BIOREACTORS; GELS; HELA CELLS; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MICROTUBULES; PROTEIN INTERACTION MAPS; PROTEIN STRUCTURE, TERTIARY;

EID: 84872413122     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201207243     Document Type: Article

References (18)

1. Z. Serber, V. Dotsch, Biochemistry 2001, 40, 14317.
2. Z. Serber, A. T. Keatinge-Clay, R. Ledwidge, A. E. Kelly, S. M. Miller, V. Dotsch, J. Am. Chem. Soc. 2001, 123, 2446.
3. P. Selenko, Z. Serber, B. Gadea, J. Ruderman, G. Wagner, Proc. Natl. Acad. Sci. USA 2006, 103, 11904.
4. T. Sakai, H. Tochio, T. Tenno, Y. Ito, T. Kokubo, H. Hiroaki, M. Shirakawa, J. Biomol. NMR 2006, 36, 179.
5. K. Inomata, et al., Nature 2009, 458, 106.
6. S. Ogino, S. Kubo, R. Umemoto, S. Huang, N. Nishida, I. Shimada, J. Am. Chem. Soc. 2009, 131, 10834.
7. P. Selenko, D. P. Frueh, S. J. Elsaesser, W. Haas, S. P. Gygi, G. Wagner, Nat. Struct. Mol. Biol. 2008, 15, 321.
8. Y. Eguchi, S. Shimizu, Y. Tsujimoto, Cancer Res. 1997, 57, 1835.
9. W. Lieberthal, S. A. Menza, J. S. Levine, Am. J. Physiol. 1998, 274, F 315.
10. C. O. Barnes, G. J. Pielak, Proteins Struct. Funct. Genet. 2011, 79, 347.
11. D. Sakakibara, et al., Nature 2009, 458, 102.
12. D. L. Foxall, J. S. Cohen, J. Magn. Reson. 1983, 52, 346.
13. D. L. Foxall, J. S. Cohen, J. B. Mitchell, Exp. Cell Res. 1984, 154, 521.
14. V. Tugarinov, P. M. Hwang, J. E. Ollerenshaw, L. E. Kay, J. Am. Chem. Soc. 2003, 125, 10420.
15. P. Schanda, B. Brutscher, J. Am. Chem. Soc. 2005, 127, 8014.
16. I. Shimada, T. Ueda, M. Matsumoto, M. Sakakura, M. Osawa, K. Takeuchi, N. Nishida, H. Takahashi, Prog. Nucl. Magn. Reson. Spectrosc. 2009, 54, 123.
17. M. Mishima, R. Maesaki, M. Kasa, T. Watanabe, M. Fukata, K. Kaibuchi, T. Hakoshima, Proc. Natl. Acad. Sci. USA 2007, 104, 10346.
18. N. G. Sharaf, C. O. Barnes, L. M. Charlton, G. B. Young, G. J. Pielak, J. Magn. Reson. 2010, 202, 140.