Relevant bibliographies by topics / "CK2,Substrate,Identification"

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Academic literature on the topic '"CK2,Substrate,Identification"'

Author: Grafiati
Published: 11 March 2023
Last updated: 31 July 2025

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Journal articles on the topic ""CK2,Substrate,Identification""

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Calvert, Meredith E. K., Kristin M. Keck, Celeste Ptak, Jeffrey Shabanowitz, Donald F. Hunt, and Lucy F. Pemberton. "Phosphorylation by Casein Kinase 2 Regulates Nap1 Localization and Function." Molecular and Cellular Biology 28, no. 4 (2007): 1313–25. http://dx.doi.org/10.1128/mcb.01035-07.

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ABSTRACT In Saccharomyces cerevisiae, the evolutionarily conserved nucleocytoplasmic shuttling protein Nap1 is a cofactor for the import of histones H2A and H2B, a chromatin assembly factor and a mitotic factor involved in regulation of bud formation. To understand the mechanism by which Nap1 function is regulated, Nap1-interacting factors were isolated and identified by mass spectrometry. We identified several kinases among these proteins, including casein kinase 2 (CK2), and a new bud neck-associated protein, Nba1. Consistent with our identification of the Nap1-interacting kinases, we showed
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Bai, Xiyuan, Derek Silvius, Edward D. Chan, Denise Escalier, and Shaun Xin Xu. "Identification and characterization of a novel testis-specific gene CKT2 , which encodes a substrate for protein kinase CK2." Nucleic Acids Research 37, no. 8 (2009): 2699–711. http://dx.doi.org/10.1093/nar/gkp094.

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Holland, Zoë, Renaud Prudent, Jean-Baptiste Reiser, Claude Cochet, and Christian Doerig. "Functional Analysis of Protein Kinase CK2 of the Human Malaria Parasite Plasmodium falciparum." Eukaryotic Cell 8, no. 3 (2008): 388–97. http://dx.doi.org/10.1128/ec.00334-08.

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ABSTRACT Protein kinase CK2 (casein kinase 2) is a eukaryotic serine/threonine protein kinase with multiple substrates and roles in diverse cellular processes, including differentiation, proliferation, and translation. The mammalian holoenzyme consists of two catalytic alpha or alpha′ subunits and two regulatory beta subunits. We report the identification and characterization of a Plasmodium falciparum CK2α orthologue, PfCK2α, and two PfCK2β orthologues, PfCK2β1 and PfCK2β2. Recombinant PfCK2α possesses protein kinase activity, exhibits similar substrate and cosubstrate preferences to those of
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Liu, Shan-shan, Hong-xia Zheng, Hua-dong Jiang, et al. "Identification and characterization of a novel gene, c1orf109, encoding a CK2 substrate that is involved in cancer cell proliferation." Journal of Biomedical Science 19, no. 1 (2012): 49. http://dx.doi.org/10.1186/1423-0127-19-49.

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Gyenis, Laszlo, James S. Duncan, Jacob P. Turowec, Maria Bretner, and David W. Litchfield. "Unbiased Functional Proteomics Strategy for Protein Kinase Inhibitor Validation and Identification ofbona fideProtein Kinase Substrates: Application to Identification of EEF1D as a Substrate for CK2." Journal of Proteome Research 10, no. 11 (2011): 4887–901. http://dx.doi.org/10.1021/pr2008994.

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Gyenis, Laszlo, Jacob P. Turowec, Maria Bretner, and David W. Litchfield. "Chemical proteomics and functional proteomics strategies for protein kinase inhibitor validation and protein kinase substrate identification: Applications to protein kinase CK2." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1834, no. 7 (2013): 1352–58. http://dx.doi.org/10.1016/j.bbapap.2013.02.006.

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Trujillo, Ramon, Francesc Miró, Maria Plana, et al. "Substrates for Protein Kinase CK2 in Insulin Receptor Preparations from Rat Liver Membranes: Identification of a 210-kDa Protein Substrate as the Dimeric Form of Endoplasmin." Archives of Biochemistry and Biophysics 344, no. 1 (1997): 18–28. http://dx.doi.org/10.1006/abbi.1997.0155.

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Vetter, Daniel, Roland Kissmehl, Tilman Treptau, Karin Hauser, Josef Kellermann, and Helmut Plattner. "Molecular Identification of a Calcium-Inhibited Catalytic Subunit of Casein Kinase Type 2 from Paramecium tetraurelia." Eukaryotic Cell 2, no. 6 (2003): 1220–33. http://dx.doi.org/10.1128/ec.2.6.1220-1233.2003.

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ABSTRACT We have previously described the occurrence in Paramecium of a casein kinase (CK) activity (EC 2.7.1.37) with some unusual properties, including inhibition by Ca2+ (R. Kissmehl, T. Treptau, K. Hauser, and H. Plattner, FEBS Lett. 402:227-235, 1995). We now have cloned four genes, PtCK2α1 to PtCK2α4, all of which encode the catalytic α subunit of type 2 CK (CK2) with calculated molecular masses ranging from 38.9 to 39.4 kDa and pI values ranging from 8.8 to 9.0. They can be classified into two groups, which differ from each other by 28% on the nucleotide level and by 18% on the derived
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Barkova, Anastasia, Indranil Adhya, Christine Conesa, et al. "A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition." Mobile DNA 13, no. 1 (2022). http://dx.doi.org/10.1186/s13100-022-00284-0.

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Abstract Background Transposable elements are ubiquitous and play a fundamental role in shaping genomes during evolution. Since excessive transposition can be mutagenic, mechanisms exist in the cells to keep these mobile elements under control. Although many cellular factors regulating the mobility of the retrovirus-like transposon Ty1 in Saccharomyces cerevisiae have been identified in genetic screens, only very few of them interact physically with Ty1 integrase (IN). Results Here, we perform a proteomic screen to establish Ty1 IN interactome. Among the 265 potential interacting partners, we
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Niinae, Tomoya, Naoyuki Sugiyama, and Yasushi Ishihama. "Validity of the cell‐extracted proteome as a substrate pool for exploring phosphorylation motifs of kinases." Genes to Cells, September 2, 2023. http://dx.doi.org/10.1111/gtc.13063.

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AbstractThree representative protein kinases with different substrate preferences, ERK1 (Pro‐directed), CK2 (acidophilic), and PKA (basophilic), were used to investigate phosphorylation sequence motifs in substrate pools consisting of the proteomes from three different cell lines, MCF7 (human mammary carcinoma), HeLa (human cervical carcinoma), and Jurkat (human acute T‐cell leukemia). Specifically, recombinant kinases were added to the cell‐extracted proteomes to phosphorylate the substrates in vitro. After trypsin digestion, the phosphopeptides were enriched and subjected to nanoLC/MS/MS ana
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Dissertations / Theses on the topic ""CK2,Substrate,Identification""

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khan, shahbaz. "Chemical genetic approach to identify substrates of CK2 kinase using Mass spectrometry." Doctoral thesis, 2018. http://hdl.handle.net/11562/978731.

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Protein kinase CK2 plays major roles in multiple biological processes, as has been reported in literature. Phosphoproteomic and bioinformatics data suggests that CK2 is involved in many cellular pathways however there is no report published on the unbiased global validation of its bona fine cellular substrates and how the CK2 dependent phosphorylation is modulating these pathways. Therefore, there is a need for methods that can do this validation process. Since the kinases have similar nature to phosphorylate their substrates, it is a great challenge to find or validate new substrates of a tar
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