Low-barrier hydrogen bonds in enzyme cooperativity-Reference-Cited by-同舟云学术

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Low-barrier hydrogen bonds in enzyme cooperativity

Published:2019-09-18 Issue:7775 Volume:573 Page:609-613
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Dai Shaobo,Funk Lisa-Marie,von Pappenheim Fabian Rabe,Sautner Viktor,Paulikat Mirko,Schröder Benjamin,Uranga Jon,Mata Ricardo A.,Tittmann Kai

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/s41586-019-1581-9.pdf

Reference64 articles.

1. Perutz, M. F. Stereochemistry of cooperative effects in haemoglobin: haem–haem interaction and the problem of allostery. Nature 228, 726–734 (1970).

2. Kantrowitz, E. R. & Lipscomb, W. N. Escherichia coli aspartate transcarbamylase: the relation between structure and function. Science 241, 669–674 (1988).

3. Koshland, D. E., Jr, Némethy, G. & Filmer, D. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5, 365–385 (1966).

4. Monod, J., Wyman, J. & Changeux, J. P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12, 88–118 (1965).

5. Perutz, M. F. Mechanisms of cooperativity and allosteric regulation in proteins. Q. Rev. Biophys. 22, 139–237 (1989).

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