Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Frank I. Comer"'
Autor:
Lu Wen, Frank I. Comer, Michael Oberst, Mary Jane Hinrichs, Tao Zhang, Alfred E. Chang, Yangyi Bao, Yuanyuan Liu, Hannah E. Dobson, Steven R. Coats, Qiao Li, Max S. Wicha, Fu Dai, You Qin, Leiming Xia
Publikováno v:
Cell Chem Biol
We previously tested HER2-targeted antibody drug conjugates (ADC) in immunocompromised (SCID) mice, precluding evaluation of host immunity, impact on cancer stem cells (CSCs), and potential benefit when combined with PD-L1 blockade. In this study, we
Autor:
Zihao Wang, Linda C. Hsieh-Wilson, Gerald W. Hart, Christopher D. Saudek, Frank I. Comer, Kyoungsook Park
Publikováno v:
Diabetes. 58:309-317
OBJECTIVE— O-linked N-acetylglucosamine (O-GlcNAc) is upregulated in diabetic tissues and plays a role in insulin resistance and glucose toxicity. Here, we investigated the extent of GlcNAcylation on human erythrocyte proteins and compared site-spe
Autor:
Frank I. Comer, Carole A. Parent
Publikováno v:
Molecular Biology of the Cell. 17:357-366
The binding of chemoattractants to cognate G protein-coupled receptors activates a variety of signaling cascades that provide spatial and temporal cues required for chemotaxis. When subjected to uniform stimulation, these responses are transient, sho
Autor:
Hiroshi Hirano, Akihiko Kudo, Gerald W. Hart, Robert N. Cole, Yoshihiro Akimoto, Hayato Kawakami, Frank I. Comer
Publikováno v:
Brain Research. 966:194-205
O-linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous nucleocytoplasmic protein modification that has a complex interplay with phosphorylation on cytoskeletal proteins, signaling proteins and transcription factors. O-GlcNAc is essential for life at
Publikováno v:
Journal of Biological Chemistry. 277:19229-19235
Previously, we reported that c-Myc is glycosylated by O-linked N-acetylglucosamine at Thr-58, a known phosphorylation site and a mutational hot spot in lymphomas. In this paper, we describe the production and characterization of two Thr-58 site-speci
Autor:
Frank I. Comer, Carole A. Parent
Publikováno v:
Cell. 109:541-544
Phosphatidylinositol lipids, such as PI(4,5)P2 and PI(3,4,5)P3, are key mediators in diverse intracellular signaling pathways. Two recent reports examine how the metabolism of these lipids by phosphatidylinositol 3-kinases and the PTEN 3-phosphoinosi
Autor:
Frank I. Comer, Gerald W. Hart
Publikováno v:
Biochemistry. 40:7845-7852
The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery. Specific phosphorylation events are associated
Publikováno v:
Journal of Biological Chemistry. 276:9838-9845
Dynamic modification of cytoplasmic and nuclear proteins by O-linked N-acetylglucosamine (O-GlcNAc) on Ser/Thr residues is ubiquitous in higher eukaryotes and is analogous to protein phosphorylation. The enzyme for the addition of this modification,
Autor:
Gerald W. Hart, Frank I. Comer
Publikováno v:
Journal of Biological Chemistry. 275:29179-29182
Autor:
Bradley K. Hayes, Zhengyi Ye, Yoshihiro Akimoto, Lisa K. Kreppel, B. J. Earles, Frank I. Comer, Robert N. Cole, Xiaogang Cheng, Diane M. Snow, D. S. Caine, D. Dellamanna, Gerald W. Hart, C. S. Arnold
Publikováno v:
Glycobiology. 6:711-716
O-Linked N-acetylglucosamine, O-GlcNAc, was discovered (Torres and Hart, 1984) as part of our studies using highlypurified glycosyltransferases to investigate saccharide structures on lymphocytes and tumor cells (Powell et al, 1987; Whiteheart and Ha