@article{34b3034423d9496fb162ffcbbef285fd,
title = "Allosteric post-translational modification codes",
abstract = "Post-translational modifications (PTMs) have been recognized to impact protein function in two ways: (i) orthosterically, via direct recognition by protein domains or through interference with binding; and (ii) allosterically, via conformational changes induced at the functional sites. Because different chemical types of PTMs elicit different structural alterations, the effects of combinatorial codes of PTMs are vastly larger than previously believed. Combined with orthosteric PTMs, the impact of PTMs on cellular regulation is immense. From an evolutionary standpoint, harnessing this immense, yet highly specific, PTM code is an extremely efficient vehicle that can save a cell several-fold in gene number and speed up its response to environmental change.",
keywords = "Allostery, Conformational ensembles, Conformational selection, Induced fit, Population shift, Propagation, Protein structure, Signaling pathways, Signaling proteins",
author = "Ruth Nussinov and Tsai, {Chung Jung} and Fuxiao Xin and Predrag Radivojac",
note = "Funding Information: This project was funded, in whole or in part, with Federal funds from the National Cancer Institute, National Institutes of Health (NIH), under contract number HHSN261200800001E. This research was supported (in part) by the Intramural Research Program of the NIH, National Cancer Institute, Center for Cancer Research, and National Science Foundation (NSF) award DBI-0644017.",
year = "2012",
month = oct,
doi = "10.1016/j.tibs.2012.07.001",
language = "אנגלית",
volume = "37",
pages = "447--455",
journal = "Trends in Biochemical Sciences",
issn = "0968-0004",
publisher = "Elsevier Ltd.",
number = "10",
}