NMR relaxation parameters of methyl groups as a tool to map the interfaces of helix–helix interactions in membrane proteins-Reference-Cited by-同舟云学术

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NMR relaxation parameters of methyl groups as a tool to map the interfaces of helix–helix interactions in membrane proteins

Published:2017-10-23 Issue:3 Volume:69 Page:165-179
ISSN:0925-2738
Container-title:Journal of Biomolecular NMR
language:en
Short-container-title:J Biomol NMR

Author:

Lesovoy D. M.,Mineev K. S.,Bragin P. E.,Bocharova O. V.,Bocharov E. V.,Arseniev A. S.

Funder

Russian Science Foundation

Publisher

Springer Science and Business Media LLC

Subject

Spectroscopy,Biochemistry

Link

http://link.springer.com/article/10.1007/s10858-017-0146-1/fulltext.html

Reference54 articles.

1. Aguirre C, ten Brink T, Cala O et al (2014) Protein–ligand structure guided by backbone and side-chain proton chemical shift perturbations. J Biomol NMR 60:147–156. doi: 10.1007/s10858-014-9864-9

2. Bargmann CI, Hung MC, Weinberg RA (1986) Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185. Cell 45:649–657

3. Barrett PJ, Song Y, Van Horn WD et al (2012) The amyloid precursor protein has a flexible transmembrane domain and binds cholesterol. Science 336:1168–1171. doi: 10.1126/science.1219988

4. Bennasroune A, Fickova M, Gardin A et al (2004) Transmembrane peptides as inhibitors of ErbB receptor signaling. Mol Biol Cell 15:3464–3474. doi: 10.1091/mbc.E03-10-0753

5. Bennasroune A, Gardin A, Auzan C et al (2005) Inhibition by transmembrane peptides of chimeric insulin receptors. Cell Mol Life Sci 62:2124–2131. doi: 10.1007/s00018-005-5226-9

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