Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domains. Export

@article{citeulike:180194, abstract = {The effects of tyrosine phosphorylation are manifested and regulated through protein domains that bind to specific phosphotyrosine motifs. STYX is a unique modular domain found within proteins implicated in mediating the effects of tyrosine phosphorylation in vivo. Individual STYX domains are not catalytically active; however, they resemble protein tyrosine phosphatase (PTP) domains and, like PTPs, contain core sequences that recognize phosphorylated substrates. Thus, the STYX domain adds to the repertoire of modular domains that can mediate intracellular signaling in response to protein phosphorylation.}, address = {Dept of Physiology, University of Michigan, Ann Arbor 48109-0606, USA.}, author = {Wishart, M. J. and Dixon, J. E.}, citeulike-article-id = {180194}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/9757831}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=9757831}, issn = {0968-0004}, journal = {Trends Biochem Sci}, keywords = {dead\_ptp, styx}, month = {August}, number = {8}, pages = {301--306}, posted-at = {2005-05-04 18:56:08}, priority = {2}, title = {Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domains.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/9757831}, volume = {23}, year = {1998} }

TY - JOUR ID - citeulike:180194 L3 - citeulike-article-id:180194 N2 - The effects of tyrosine phosphorylation are manifested and regulated through protein domains that bind to specific phosphotyrosine motifs. STYX is a unique modular domain found within proteins implicated in mediating the effects of tyrosine phosphorylation in vivo. Individual STYX domains are not catalytically active; however, they resemble protein tyrosine phosphatase (PTP) domains and, like PTPs, contain core sequences that recognize phosphorylated substrates. Thus, the STYX domain adds to the repertoire of modular domains that can mediate intracellular signaling in response to protein phosphorylation. IS - 8 JF - Trends Biochem Sci SN - 0968-0004 AD - Dept of Physiology, University of Michigan, Ann Arbor 48109-0606, USA. EP - 306 TI - Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domains. VL - 23 SP - 301 KW - dead_ptp KW - styx AU - Wishart, MJ AU - Dixon, JE PY - 1998/08// UR - http://view.ncbi.nlm.nih.gov/pubmed/9757831 ER -