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15 results on '"Krogager, Toke P."'

5. Labeling and identifying cell-specific proteomes in the mouse brain

Author

Krogager, Toke P, primary, Ernst, Russell J, additional, Elliott, Thomas S, additional, Calo, Laura, additional, Beránek, Václav, additional, Ciabatti, Ernesto, additional, Spillantini, Maria Grazia, additional, Tripodi, Marco, additional, Hastings, Michael H, additional, and Chin, Jason W, additional

Published
2017
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6. Genetic code expansion in the mouse brain

Author

Ernst, Russell J, primary, Krogager, Toke P, additional, Maywood, Elizabeth S, additional, Zanchi, Roberto, additional, Beránek, Václav, additional, Elliott, Thomas S, additional, Barry, Nicholas P, additional, Hastings, Michael H, additional, and Chin, Jason W, additional

Published
2016
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7. Visualizing and Quantifying Intracellular Behavior and Abundance of the Core Circadian Clock Protein PERIOD2

Author

Smyllie, Nicola J., primary, Pilorz, Violetta, additional, Boyd, James, additional, Meng, Qing-Jun, additional, Saer, Ben, additional, Chesham, Johanna E., additional, Maywood, Elizabeth S., additional, Krogager, Toke P., additional, Spiller, David G., additional, Boot-Handford, Raymond, additional, White, Michael R.H., additional, Hastings, Michael H., additional, and Loudon, Andrew S.I., additional

Published
2016
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9. Labeling and identifying cell-specific proteomes in the mouse brain.

Author

Krogager, Toke P, Ernst, Russell J, Elliott, Thomas S, Calo, Laura, Beránek, Václav, Ciabatti, Ernesto, Spillantini, Maria Grazia, Tripodi, Marco, Hastings, Michael H, and Chin, Jason W

Abstract

We develop an approach to tag proteomes synthesized by specific cell types in dissociated cortex, brain slices, and the brains of live mice. By viral-mediated expression of an orthogonal pyrrolysyl-tRNA synthetase-tRNAXXX pair in a cell type of interest and providing a non-canonical amino acid with a chemical handle, we selectively label neuronal or glial proteomes. The method enables the identification of proteins from spatially and genetically defined regions of the brain. [ABSTRACT FROM AUTHOR]

Published
2018
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13. Proteomics of Fuchs’ Endothelial Corneal Dystrophy Support That the Extracellular Matrix of Descemet’s Membrane Is Disordered

Author

Poulsen, Ebbe Toftgaard, Dyrlund, Thomas F., Runager, Kasper, Scavenius, Carsten, Krogager, Toke Peter, Højrup, Peter, Thøgersen, Ida B., Sanggaard, Kristian W., Vorum, Henrik, Hjortdal, Jesper, and Enghild, Jan J.

Abstract

Fuchs’ endothelial corneal dystrophy (FECD) is a major corneal disorder affecting the innermost part of the cornea, leading to visual impairment. As the morphological changes in FECD are mainly observed in the extracellular matrix of the Descemet’s membrane/endothelial layer, we determined the protein profiles of diseased and control tissues using two relative quantitation MS methods. The first quantitation method, based on the areas of the extracted ion chromatograms, quantified the 51 and 48 most abundant proteins of the Descemet’s membrane/endothelial layer in patient and control tissues, respectively, of which 10 were significantly regulated. The results indicated that the level of type VIII collagen was unaltered even though the protein previously has been shown to be implicated in familial early-onset forms of the disease. Using the second relative quantitation method, iTRAQ, we identified 22 differentially regulated proteins, many of which are extracellular proteins known to be involved in proper assembly of the basement membrane in other tissues. In total, 26 differentially regulated proteins were identified, of which 6 proteins were regulated in both methods. These results support that the morphological changes observed in FECD are caused in part by an aberrant assembly of the extracellular matrix within the Descemet’s membrane/endothelial layer.

Published
2014
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14. Labeling and identifying cell-specific proteomes in the mouse brain

Author

Krogager, Toke P, Ernst, Russell J, Elliott, Thomas S, Calo, Laura, Beránek, Václav, Ciabatti, Ernesto, Spillantini, Maria Grazia, Tripodi, Marco, Hastings, Michael H, and Chin, Jason W

Subjects
Amino Acyl-tRNA Synthetases, Neurons, Mice, Proteome, RNA, Transfer, Animals, Brain, Amino Acids, Neuroglia, Gene Expression Regulation, Enzymologic, 3. Good health
Abstract

We develop an approach to tag proteomes synthesized by specific cell types in dissociated cortex, brain slices, and the brains of live mice. By viral-mediated expression of an orthogonal pyrrolysyl-tRNA synthetase-tRNAXXX pair in a cell type of interest and providing a non-canonical amino acid with a chemical handle, we selectively label neuronal or glial proteomes. The method enables the identification of proteins from spatially and genetically defined regions of the brain., Michael J Fox Foundation (MJFF) (unknown), Parkinson's UK (None), Cure Parkinson's Trust (unknown)

15. TSG-6 Transfers Proteins between Glycosaminoglycans via a Ser28-mediated Covalent Catalytic Mechanism.

Author

Sanggaard, Kristian W., Sonne-Schmidt, Carsten S., Krogager, Toke P., Kristensen, Torsten, Wisniewski, Hans-Georg, Thøgersen, Ida B., and Enghild, Jan J.

Subjects
*PROTEINS, *GLYCOSAMINOGLYCANS, *TUMOR necrosis factors, *CATALYSIS, *GROWTH factors
Abstract

Studies of the interaction between Bikunin proteins, tumor necrosis factor-stimulated gene-6 protein (TSG-6), and glycosaminoglycans have revealed a unique catalytic activity where TSG-6/heavy chain 2 transfer heavy chain subunits between glycosaminoglycan chains. The activity is mediated by TSG-6/heavy chain 2 and involves a transient SDS stable interaction between TSG-6 and the heavy chain to be transferred. The focus of this study was to characterize the molecular structure of this cross-link to gain further insight into the catalytic mechanism. The result showed that the C-terminal Asp residue of the heavy chains forms an ester bond to Ser28 β-carbon of TSG-6 suggesting that this residue plays a role during catalysis. [ABSTRACT FROM AUTHOR]

Published
2008
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