Networks for the allosteric control of protein kinases Export

@article{citeulike:971396, abstract = {The allosteric regulation of protein kinases serves as an efficient strategy for molecular communication, event coupling and interconversion between catalytic states. Recent co-crystal structures have revealed novel ways in which kinases control activity and substrate specificity following phosphorylation, dimerization, or binding to regulatory proteins, substrates and scaffolds. In addition, hydrogen exchange coupled with mass spectrometry is emerging as a complementary strategy to probe the solution behavior of kinases; recent results have shown that allosteric regulation may involve transitions in protein motions as well as structural rearrangements.}, author = {Shi, Zhengshuang and Resing, Katheryn A. and Ahn, Natalie G.}, booktitle = {Catalysis and regulation / Proteins}, citeulike-article-id = {971396}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.sbi.2006.10.011}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0959440X06001849}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/17085044}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=17085044}, citeulike-linkout-4 = {http://www.sciencedirect.com/science/article/B6VS6-4M936FF-4/2/81f26291f6854cdb45083d3324df78d5}, doi = {10.1016/j.sbi.2006.10.011}, journal = {Current Opinion in Structural Biology}, keywords = {allostery, kinases}, month = {December}, number = {6}, pages = {686--692}, posted-at = {2008-09-02 09:07:48}, priority = {2}, title = {Networks for the allosteric control of protein kinases}, url = {http://dx.doi.org/10.1016/j.sbi.2006.10.011}, volume = {16}, year = {2006} }

TY - JOUR ID - citeulike:971396 L3 - citeulike-article-id:971396 N2 - The allosteric regulation of protein kinases serves as an efficient strategy for molecular communication, event coupling and interconversion between catalytic states. Recent co-crystal structures have revealed novel ways in which kinases control activity and substrate specificity following phosphorylation, dimerization, or binding to regulatory proteins, substrates and scaffolds. In addition, hydrogen exchange coupled with mass spectrometry is emerging as a complementary strategy to probe the solution behavior of kinases; recent results have shown that allosteric regulation may involve transitions in protein motions as well as structural rearrangements. IS - 6 JF - Current Opinion in Structural Biology EP - 692 TI - Networks for the allosteric control of protein kinases VL - 16 T2 - Catalysis and regulation / Proteins SP - 686 KW - allostery KW - kinases AU - Shi, Zhengshuang AU - Resing, Katheryn AU - Ahn, Natalie PY - 2006/12// UR - http://dx.doi.org/10.1016/j.sbi.2006.10.011 ER -