Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Raghu K. Chitta"'
Publikováno v:
Molecular and Cellular Biochemistry. 456:123-134
Downstream of insulin-like growth factor receptor, the TSC1/2/ TCB1D7 (tuberous sclerosis complex) and mTOR (mechanistic target of rapamycin) pathways are implicated in many human diseases, including cancer and diabetes. Targeting this pathway is cur
Publikováno v:
Molecular and cellular biochemistry. 456(1-2)
Downstream of insulin-like growth factor receptor, the TSC1/2/ TCB1D7 (tuberous sclerosis complex) and mTOR (mechanistic target of rapamycin) pathways are implicated in many human diseases, including cancer and diabetes. Targeting this pathway is cur
Autor:
David Shechter, Jeffrey Shabanowitz, Brian T. Chait, Eileen Woo, Carola Wilczek, Raghu K. Chitta, Donald F. Hunt
Publikováno v:
Journal of Biological Chemistry. 286:42221-42231
Histone proteins carry information contained in post-translational modifications. Eukaryotic cells utilize this histone code to regulate the usage of the underlying DNA. In the maturing oocytes and eggs of the frog Xenopus laevis, histones are synthe
Autor:
Donald F. Hunt, Andrew Xiao, C. David Allis, Jeffrey Shabanowitz, David Shechter, Raghu K. Chitta
Publikováno v:
Proceedings of the National Academy of Sciences. 106:749-754
Histone H2A.X is an H2A variant present in multicellular organisms that is specifically phosphorylated on the serine in the C-terminal consensus sequence, canonically “SQEY,” in response to DNA damage. We have recently shown the significance of p
Autor:
Donald F. Hunt, Benjamin A. Garcia, David Shechter, Jeffrey Shabanowitz, Joshua J. Nicklay, C. David Allis, Raghu K. Chitta
Publikováno v:
Journal of Biological Chemistry. 284:1075-1085
Epigenetic information is hypothesized to be encoded in histone variants and post-translational modifications. Varied cell- and locus-specific combinations of these epigenetic marks are likely contributors to regulation of chromatin-templated transac
Autor:
Raghu K. Chitta, Joshua J. Nicklay, Jeffrey Shabanowitz, C. David Allis, David Shechter, Donald F. Hunt
Publikováno v:
Journal of Biological Chemistry. 284:1064-1074
Histone proteins contain epigenetic information that is encoded both in the relative abundance of core histones and variants and particularly in the post-translational modification of these proteins. We determined the presence of such variants and co
Publikováno v:
Journal of the American Society for Mass Spectrometry. 17:1526-1534
The propensity of various insulins and their analogs to oligomerize was investigated by mass spectrometric methods including measurement of the relative abundances of oligomers in the gas phase and the kinetics of H/D amide exchange. The kinetics of
Autor:
Thomas W. Sturgill, Sirlester A. Parker, Jeffrey Shabanowitz, Katherine A. Larson, Konstantin Galaktionov, Philipp Kaldis, Zheng Fu, Raghu K. Chitta, Benjamin E. Turk, Steven M. Cohn, Matthew W. Lawrence, Donald F. Hunt
Publikováno v:
Molecular and Cellular Biology. 26:8639-8654
MAK (male germ cell-associated protein kinase) and MRK/ICK (MAK-related kinase/intestinal cell kinase) are human homologs of Ime2p in Saccharomyces cerevisiae and of Mde3 and Pit1 in Schizosaccharomyces pombe and are similar to human cyclin-dependent
Autor:
Donald F. Hunt, C. David Allis, Swati Joshi, Rachel R. Ogorzalek Loo, Phillip C. Andrews, Neil L. Kelleher, Scott A. Busby, C. Eric Thomas, Raghu K. Chitta, Craig A. Mizzen, Benjamin A. Garcia, Jeffrey Shabanowitz, Robert L. Diaz
Publikováno v:
Molecular & Cellular Proteomics. 5:1593-1609
Linker histone H1 is highly phosphorylated in normal growing Tetrahymena thermophila but becomes noticeably dephosphorylated in response to certain conditions such as prolonged starvation. Because phosphorylation of H1 has been associated with the re
Publikováno v:
International Journal of Mass Spectrometry. 240:213-220
Protein–ligand interactions by mass spectrometry, titration, and H/D exchange (PLIMSTEX) is a new mass spectrometric method for determining association constants and binding stoichiometry for interactions of proteins with various ligands, as well a