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Fleming, K. G., Engelman, D. M. (2001) Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants. Proceedings of the National Academy of Sciences, 98 (25) 14340-14344 doi:10.1073/pnas.251367498

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Reference TypeJournal (article/letter/editorial)
TitleSpecificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants
JournalProceedings of the National Academy of Sciences
AuthorsFleming, K. G.Author
Engelman, D. M.Author
Year2001 (December 4)Volume98
Issue25
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.251367498Search in ResearchGate
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Mindat Ref. ID1664892Long-form Identifiermindat:1:5:1664892:0
GUID0
Full ReferenceFleming, K. G., Engelman, D. M. (2001) Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants. Proceedings of the National Academy of Sciences, 98 (25) 14340-14344 doi:10.1073/pnas.251367498
Plain TextFleming, K. G., Engelman, D. M. (2001) Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants. Proceedings of the National Academy of Sciences, 98 (25) 14340-14344 doi:10.1073/pnas.251367498
In(2001, December) Proceedings of the National Academy of Sciences Vol. 98 (25) Proceedings of the National Academy of Sciences

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Senes, A., Ubarretxena-Belandia, I., Engelman, D. M. (2001) The C --H***O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions. Proceedings of the National Academy of Sciences, 98 (16) 9056-9061 doi:10.1073/pnas.161280798
MacKenzie, K. R., Engelman, D. M. (1998) Structure-based prediction of the stability of transmembrane helix-helix interactions: The sequence dependence of glycophorin A dimerization. Proceedings of the National Academy of Sciences, 95 (7) 3583-3590 doi:10.1073/pnas.95.7.3583
Russ, W. P., Engelman, D. M. (1999) TOXCAT: A measure of transmembrane helix association in a biological membrane. Proceedings of the National Academy of Sciences, 96 (3) 863-868 doi:10.1073/pnas.96.3.863
Barrera, F. N., Fendos, J., Engelman, D. M. (2012) Membrane physical properties influence transmembrane helix formation. Proceedings of the National Academy of Sciences, 109 (36) 14422-14427 doi:10.1073/pnas.1212665109
Reshetnyak, Y. K., Andreev, O. A., Lehnert, U., Engelman, D. M. (2006) Translocation of molecules into cells by pH-dependent insertion of a transmembrane helix. Proceedings of the National Academy of Sciences, 103 (17) 6460-6465 doi:10.1073/pnas.0601463103
Chou, K. C., Maggiora, G. M., Scheraga, H. A. (1992) Role of loop-helix interactions in stabilizing four-helix bundle proteins. Proceedings of the National Academy of Sciences, 89 (16) 7315-7319 doi:10.1073/pnas.89.16.7315
Howard, K. P., Lear, J. D., DeGrado, W. F. (2002) Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein. Proceedings of the National Academy of Sciences, 99 (13) 8568-8572 doi:10.1073/pnas.132266099
Urry, D. W. (1971) The Gramicidin A Transmembrane Channel: A Proposed  (L,D) Helix. Proceedings of the National Academy of Sciences, 68 (3) 672-676 doi:10.1073/pnas.68.3.672
Abdulaev, N. G., Ridge, K. D. (1998) Light-induced exposure of the cytoplasmic end of transmembrane helix seven in rhodopsin. Proceedings of the National Academy of Sciences, 95 (22) 12854-12859 doi:10.1073/pnas.95.22.12854
Zhou, F. X., Merianos, H. J., Brunger, A. T., Engelman, D. M. (2001) Polar residues drive association of polyleucine transmembrane helices. Proceedings of the National Academy of Sciences, 98 (5) 2250-2255 doi:10.1073/pnas.041593698
Dorairaj, S., Allen, T. W. (2007) On the thermodynamic stability of a charged arginine side chain in a transmembrane helix. Proceedings of the National Academy of Sciences, 104 (12) 4943-4948 doi:10.1073/pnas.0610470104
 
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