Literatura académica sobre el tema "Nucleoside diphosphate kinase isoenzymes"

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Artículos de revistas sobre el tema "Nucleoside diphosphate kinase isoenzymes"

1

GUIGNARD, Florence, and Michèle MARKERT. "The nucleoside diphosphate kinase of human neutrophils." Biochemical Journal 316, no. 1 (1996): 233–38. http://dx.doi.org/10.1042/bj3160233.

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Nucleoside diphosphate kinase (NDP kinase) catalyses the phosphate transfer between nucleoside triphosphates and nucleoside diphosphates. As formation of guanosine triphosphate could be dependent on ATP in neutrophils, the presence of NDP kinase was tested in these phagocytic cells. Both membrane and cytosolic fractions of human neutrophils were found to contain NDP kinase activity. The specific activity measured in the cytosol appeared 10-fold higher than in the membrane and was not modified when the cells were activated with phorbol 12-myristate 13-acetate. Interestingly, stimulation with N-
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2

Karlsson, Anna, Sébastien Mesnildrey, Yingwu Xu, Solange Moréra, Joël Janin, and Michel Véron. "Nucleoside Diphosphate Kinase." Journal of Biological Chemistry 271, no. 33 (1996): 19928–34. http://dx.doi.org/10.1074/jbc.271.33.19928.

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3

Martínez-Alonso, Emma, Natalia Guerra-Pérez, Alejandro Escobar-Peso, Ignacio Regidor, Jaime Masjuan, and Alberto Alcázar. "Differential Association of 4E-BP2-Interacting Proteins Is Related to Selective Delayed Neuronal Death after Ischemia." International Journal of Molecular Sciences 22, no. 19 (2021): 10327. http://dx.doi.org/10.3390/ijms221910327.

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Cerebral ischemia induces an inhibition of protein synthesis and causes cell death and neuronal deficits. These deleterious effects do not occur in resilient areas of the brain, where protein synthesis is restored. In cellular stress conditions, as brain ischemia, translational repressors named eukaryotic initiation factor (eIF) 4E-binding proteins (4E-BPs) specifically bind to eIF4E and are critical in the translational control. We previously described that 4E-BP2 protein, highly expressed in brain, can be a molecular target for the control of cell death or survival in the reperfusion after i
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4

Mizuki, T., M. Kamekura, M. Ishibashi, et al. "Nucleoside diphosphate kinase of halobacteria." Journal of Japanese Society for Extremophiles 3, no. 1 (2004): 1_18–1_27. http://dx.doi.org/10.3118/jjse.3.1_18.

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5

Choi, Chul Hee. "Nucleoside Diphosphate Kinase from Microorganisms." Journal of Bacteriology and Virology 43, no. 2 (2013): 92. http://dx.doi.org/10.4167/jbv.2013.43.2.92.

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6

Randazzo, P., R. Kahn, and J. Northup. "Nucleoside diphosphate kinase: conclusions withdrawn." Science 257, no. 5072 (1992): 862. http://dx.doi.org/10.1126/science.1323875.

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7

Attwood, Paul V., and Thomas Wieland. "Nucleoside diphosphate kinase as protein histidine kinase." Naunyn-Schmiedeberg's Archives of Pharmacology 388, no. 2 (2014): 153–60. http://dx.doi.org/10.1007/s00210-014-1003-3.

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8

Lopez-Zavala, Alonso A., Rogerio R. Sotelo-Mundo, Jose M. Hernandez-Flores, Maria E. Lugo-Sanchez, Rocio Sugich-Miranda, and Karina D. Garcia-Orozco. "Arginine kinase shows nucleoside diphosphate kinase-like activity toward deoxythymidine diphosphate." Journal of Bioenergetics and Biomembranes 48, no. 3 (2016): 301–8. http://dx.doi.org/10.1007/s10863-016-9660-1.

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9

Almaula, N., Q. Lu, J. Delgado, S. Belkin, and M. Inouye. "Nucleoside diphosphate kinase from Escherichia coli." Journal of bacteriology 177, no. 9 (1995): 2524–29. http://dx.doi.org/10.1128/jb.177.9.2524-2529.1995.

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10

Brodbeck, Michel, Annette Rohling, Wolfgang Wohlleben, Charles J. Thompson, and Urs Susstrunk. "Nucleoside-Diphosphate Kinase from Streptomyces coelicolor." European Journal of Biochemistry 239, no. 1 (1996): 208–13. http://dx.doi.org/10.1111/j.1432-1033.1996.0208u.x.

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