Global Changes in and Characterization of Specific Sites of Phosphorylation in Mouse and Human Histone H1 Isoforms upon CDK Inhibitor Treatment Using Mass Spectrometry

@article{citeulike:2680121, abstract = {Abstract: Global changes in the phosphorylation state of human H1 isoforms isolated from UL3 cells have been investigated using mass spectrometry. Relative changes in H1 phosphorylation between untreated cells and cells treated with dexamethasone or various CDK inhibitors were determined. The specific cyclin-dependent kinase consensus sites of phosphorylation on the histone H1 isoforms that show changes in phosphorylation were also investigated. Three sites of phosphorylation on histone H1.4 isoforms have been identified.}, address = {Laboratory of Structural Biology and Laboratory of Molecular Carcinogenesis, National Institute of Environmental Health Sciences, National Institutes of Health, DHHS, P.O. Box 12233, RTP, North Carolina 27709}, author = {Deterding, Leesa J. and Bunger, Maureen K. and Banks, Geoffrey C. and Tomer, Kenneth B. and Archer, Trevor K. }, citeulike-article-id = {2680121}, doi = {http://dx.doi.org/10.1021/pr700790a}, journal = {J. Proteome Res.}, keywords = {cdk, histone, human, inhibitor, mass-spec, mouse, phosphorylation}, month = {April}, posted-at = {2008-04-17 06:32:57}, priority = {2}, title = {Global Changes in and Characterization of Specific Sites of Phosphorylation in Mouse and Human Histone H1 Isoforms upon CDK Inhibitor Treatment Using Mass Spectrometry}, url = {http://dx.doi.org/10.1021/pr700790a}, year = {2008} }

TY - JOUR ID - citeulike:2680121 L3 - citeulike-article-id:2680121 TI - Global Changes in and Characterization of Specific Sites of Phosphorylation in Mouse and Human Histone H1 Isoforms upon CDK Inhibitor Treatment Using Mass Spectrometry JF - J. Proteome Res. AD - Laboratory of Structural Biology and Laboratory of Molecular Carcinogenesis, National Institute of Environmental Health Sciences, National Institutes of Health, DHHS, P.O. Box 12233, RTP, North Carolina 27709 N2 - Abstract: Global changes in the phosphorylation state of human H1 isoforms isolated from UL3 cells have been investigated using mass spectrometry. Relative changes in H1 phosphorylation between untreated cells and cells treated with dexamethasone or various CDK inhibitors were determined. The specific cyclin-dependent kinase consensus sites of phosphorylation on the histone H1 isoforms that show changes in phosphorylation were also investigated. Three sites of phosphorylation on histone H1.4 isoforms have been identified. KW - cdk KW - histone KW - human KW - inhibitor KW - mass-spec KW - mouse KW - phosphorylation AU - Deterding, Leesa AU - Bunger, Maureen AU - Banks, Geoffrey AU - Tomer, Kenneth AU - Archer, Trevor PY - 2008/04/17/ UR - http://dx.doi.org/10.1021/pr700790a ER -