Nearly every cellular activity, such as cell growth, proliferation, protein synthesis, and nuclear division, is regulated by protein phosphorylation/dephosphorylation on tyrosine residues as initiation events.Synchronization occurs through interaction of protein tyrosine kinases and phosphatases. This book unveils signal pathways that connect extracellular signals with changes of phosphorylation state of target proteins allowing coordinated and integrated modulation of mitogenic signalling. Specifically, cascades involving ...
Read More
Nearly every cellular activity, such as cell growth, proliferation, protein synthesis, and nuclear division, is regulated by protein phosphorylation/dephosphorylation on tyrosine residues as initiation events.Synchronization occurs through interaction of protein tyrosine kinases and phosphatases. This book unveils signal pathways that connect extracellular signals with changes of phosphorylation state of target proteins allowing coordinated and integrated modulation of mitogenic signalling. Specifically, cascades involving protein serine/threonine kinases and connections to phosphoinositides derived second messengers are discussed.
Read Less
Add this copy of Tyrosine Phosphorylation/Dephosphorylation and to cart. $79.11, good condition, Sold by Bonita rated 4.0 out of 5 stars, ships from Santa Clarita, CA, UNITED STATES, published 2011 by Springer.
Add this copy of Tyrosine Phosphorylation/Dephosphorylation and to cart. $103.32, new condition, Sold by Ingram Customer Returns Center rated 5.0 out of 5 stars, ships from NV, USA, published 2011 by Springer.
Add this copy of Tyrosine Phosphorylation/Dephosphorylation and to cart. $132.45, new condition, Sold by Ria Christie Books rated 4.0 out of 5 stars, ships from Uxbridge, MIDDLESEX, UNITED KINGDOM, published 2011 by Springer.
Add this copy of Tyrosine Phosphorylation/Dephosphorylation and to cart. $45.63, very good condition, Sold by ThriftBooks-Reno rated 5.0 out of 5 stars, ships from Reno, NV, UNITED STATES, published 1993 by Springer.