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

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Publicado: 4 de junio de 2021
Última modificación: 1 de febrero de 2022

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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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11

Hunger-Glaser, Isabel, Andrew Hemphill, Tarek Shalaby, Michel Hänni, and Thomas Seebeck. "Nucleoside diphosphate kinase of Trypanosoma brucei." Gene 257, no. 2 (2000): 251–57. http://dx.doi.org/10.1016/s0378-1119(00)00401-7.

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12

Dumas, C., I. Lascu, S. Moréra, et al. "X-ray structure of nucleoside diphosphate kinase." EMBO Journal 11, no. 9 (1992): 3203–8. http://dx.doi.org/10.1002/j.1460-2075.1992.tb05397.x.

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13

Urano, Yoshio, and Seiji Arase. "Nucleoside diphosphate kinase expression in human skin." Journal of Dermatological Science 6, no. 1 (1993): 85. http://dx.doi.org/10.1016/0923-1811(93)91204-8.

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14

Ouatas, T., B. Abdallah, and A. Mazabraud. "The nucleoside diphosphate kinase of Xenopus laevis." Biology of the Cell 84, no. 1-2 (1995): 122. http://dx.doi.org/10.1016/0248-4900(96)81475-4.

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15

Schneider, Benoit, Yingwu Xu, Olivier Sellam, et al. "Phosphorylation of Anti-HIV Nucleoside Analogs by Nucleoside Diphosphate Kinase." Nucleosides and Nucleotides 18, no. 4-5 (1999): 829–30. http://dx.doi.org/10.1080/15257779908041571.

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16

Islam, K., and R. G. Burns. "Microtubules and nucleoside diphosphate kinase. Nucleoside diphosphate kinase binds to co-purifying contaminants rather than to microtubule proteins." Biochemical Journal 232, no. 3 (1985): 651–56. http://dx.doi.org/10.1042/bj2320651.

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Nucleoside diphosphate (NDP) kinase has been postulated to generate GTP from the GDP bound to tubulin. The purified chick brain enzyme was studied with respect to its kinetic parameters, and the protein-protein interactions between the NDP kinase and tubulin were examined. No specific interaction is observed between the enzyme and assembled microtubules, tubulin dimers, or tubulin-microtubule-associated protein (MAP) oligomers under a variety of nucleotide conditions. The apparent association is demonstrated to result from NDP kinase binding to a co-purifying contaminant. The absence of detect
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17

Lu, Q., and M. Inouye. "Adenylate kinase complements nucleoside diphosphate kinase deficiency in nucleotide metabolism." Proceedings of the National Academy of Sciences 93, no. 12 (1996): 5720–25. http://dx.doi.org/10.1073/pnas.93.12.5720.

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18

Stenberg, Leisa M., Johan Stenflo, Paul Holmgren, and Mark A. Brown. "Post-translational processing of Drosophila nucleoside diphosphate kinase." Biochemical and Biophysical Research Communications 295, no. 3 (2002): 689–94. http://dx.doi.org/10.1016/s0006-291x(02)00737-4.

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19

Muñoz-Dorado, J., N. Almaula, S. Inouye, and M. Inouye. "Autophosphorylation of nucleoside diphosphate kinase from Myxococcus xanthus." Journal of Bacteriology 175, no. 4 (1993): 1176–81. http://dx.doi.org/10.1128/jb.175.4.1176-1181.1993.

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20

Bardak, Yavuz, Osman Çekiç, Ayşe Ayhan, İlhan Günalp, and Orhan Bulay. "Nucleoside Diphosphate Kinase (nm23 Protein) Expression in Retinoblastoma." Ophthalmic Research 32, no. 2-3 (2000): 73–78. http://dx.doi.org/10.1159/000055593.

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21

Chen, Yuxing, Solange Morera, Julia Mocan, Ioan Lascu, and Jo�l Janin. "X-ray structure ofMycobacterium tuberculosis nucleoside diphosphate kinase." Proteins: Structure, Function, and Genetics 47, no. 4 (2002): 556–57. http://dx.doi.org/10.1002/prot.10113.

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22

Biondi, Ricardo M., Benoit Schneider, Eduardo Passeron, and Susana Passeron. "Role of Mg2+in Nucleoside Diphosphate Kinase Autophosphorylation." Archives of Biochemistry and Biophysics 353, no. 1 (1998): 85–92. http://dx.doi.org/10.1006/abbi.1997.0617.

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23

Inoue, Hiroko, Masami Takahashi, Akira Oomori, Mariko Sekiguchi, and Tohru Yoshioka. "A Novel Function for Nucleoside Diphosphate Kinase inDrosophila." Biochemical and Biophysical Research Communications 218, no. 3 (1996): 887–92. http://dx.doi.org/10.1006/bbrc.1996.0158.

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24

Schneider, Benoit, Manuel Babolat, Ying Wu Xu, Joël Janin, Michel Véron, and Dominique Deville-Bonne. "Mechanism of phosphoryl transfer by nucleoside diphosphate kinase." European Journal of Biochemistry 268, no. 7 (2001): 1964–71. http://dx.doi.org/10.1046/j.1432-1327.2001.02070.x.

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25

Shen, Rongkun, Linda J. Wheeler, and Christopher K. Mathews. "Molecular interactions involving Escherichia coli nucleoside diphosphate kinase." Journal of Bioenergetics and Biomembranes 38, no. 3-4 (2006): 255–59. http://dx.doi.org/10.1007/s10863-006-9041-2.

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26

Muhonen, Wallace W., and David O. Lambeth. "The compartmentation of nucleoside diphosphate kinase in mitochondria." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 110, no. 1 (1995): 211–23. http://dx.doi.org/10.1016/0305-0491(94)00123-c.

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27

Klinker, J., A. Hagelüken, B. Nürnberg, and R. Seifert. "SC12 G-protein activation via nucleoside diphosphate kinase." European Journal of Pharmaceutical Sciences 2, no. 1-2 (1994): 93. http://dx.doi.org/10.1016/0928-0987(94)90094-9.

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28

Murakami, Masanao, Rajeev Kaul, Pankaj Kumar, and Erle S. Robertson. "Nucleoside diphosphate kinase/Nm23 and Epstein–Barr virus." Molecular and Cellular Biochemistry 329, no. 1-2 (2009): 131–39. http://dx.doi.org/10.1007/s11010-009-0123-4.

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29

Morera, Solange, Ioan Lascu, Christian Dumas, et al. "Adenosine 5'-diphosphate binding and the active site of nucleoside diphosphate kinase." Biochemistry 33, no. 2 (1994): 459–67. http://dx.doi.org/10.1021/bi00168a010.

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30

Xu, Y., O. Sellam, S. Morera, et al. "X-ray analysis of azido-thymidine diphosphate binding to nucleoside diphosphate kinase." Proceedings of the National Academy of Sciences 94, no. 14 (1997): 7162–65. http://dx.doi.org/10.1073/pnas.94.14.7162.

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31

Meena, Laxman S., Puneet Chopra, R. S. Bedwal, and Yogendra Singh. "Nucleoside diphosphate kinase-like activity in adenylate kinase of Mycobacterium tuberculosis." Biotechnology and Applied Biochemistry 38, no. 2 (2003): 169. http://dx.doi.org/10.1042/ba20020122.

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32

ANN, KYOUNG-SOOK, and DAVID L. NELSON. "A Nucleoside Diphosphate Kinase from Paramecium tetraurelia with Protein Kinase Activity." Journal of Eukaryotic Microbiology 43, no. 5 (1996): 365–72. http://dx.doi.org/10.1111/j.1550-7408.1996.tb05045.x.

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33

Zhou, Y. "Nucleoside diphosphate kinase: a new player in heart failure?" Cardiovascular Research 49, no. 1 (2001): 7–10. http://dx.doi.org/10.1016/s0008-6363(00)00273-x.

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34

Muñoz-Dorado, J., S. Inouye, and M. Inouye. "Nucleoside diphosphate kinase from Myxococcus xanthus. II. Biochemical characterization." Journal of Biological Chemistry 265, no. 5 (1990): 2707–12. http://dx.doi.org/10.1016/s0021-9258(19)39859-x.

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35

Miranda, Mariana R., Maria de los Milagros Camara, León A. Bouvier, and Claudio A. Pereira. "TcNDPK2, a Trypanosoma cruzi microtubule-associated nucleoside diphosphate kinase." Molecular and Biochemical Parasitology 177, no. 2 (2011): 152–55. http://dx.doi.org/10.1016/j.molbiopara.2011.02.008.

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36

Magnani Dinamarco, Taísa, Neil Andrew Brown, Ricardo Sergio Couto de Almeida, et al. "Aspergillus fumigatus calcineurin interacts with a nucleoside diphosphate kinase." Microbes and Infection 14, no. 11 (2012): 922–29. http://dx.doi.org/10.1016/j.micinf.2012.05.003.

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37

YONEZAWA, Yasushi, Hiroko TOKUNAGA, Matsujiro ISHIBASHI, and Masao TOKUNAGA. "Characterization of Nucleoside Diphosphate Kinase from Moderately Halophilic Eubacteria." Bioscience, Biotechnology, and Biochemistry 65, no. 10 (2001): 2343–46. http://dx.doi.org/10.1271/bbb.65.2343.

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38

FINAN, PETER M., IAN R. WHITE, JOHN B. C. FINDLAY, and PAUL A. MILLNER. "Identification of nucleoside diphosphate kinase from Pea microsomal membranes." Biochemical Society Transactions 20, no. 1 (1992): 10S. http://dx.doi.org/10.1042/bst020010s.

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39

Xu, Y., A. Lecroisey, M. Veron, M. Delepierre, and Joël Janin. "NMR studies on the flexibility of nucleoside diphosphate kinase." Proteins: Structure, Function, and Genetics 28, no. 2 (1997): 150–52. http://dx.doi.org/10.1002/(sici)1097-0134(199706)28:2<150::aid-prot3>3.0.co;2-j.

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40

Bominaar, Anthony A., Annemiek D. Tepper, and Michel Véron. "Autophosphorylation of nucleoside diphosphate kinase on non-histidine residues." FEBS Letters 353, no. 1 (1994): 5–8. http://dx.doi.org/10.1016/0014-5793(94)00997-x.

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41

Keim, D., N. Hailat, R. Melhem, et al. "Proliferation-related expression of p19/nm23 nucleoside diphosphate kinase." Journal of Clinical Investigation 89, no. 3 (1992): 919–24. http://dx.doi.org/10.1172/jci115672.

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42

Gallois-Montbrun, Sarah, Benoit Schneider, Yuxing Chen, et al. "Improving Nucleoside Diphosphate Kinase for Antiviral Nucleotide Analogs Activation." Journal of Biological Chemistry 277, no. 42 (2002): 39953–59. http://dx.doi.org/10.1074/jbc.m206360200.

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43

Choi, Giltsu, Hankuil Yi, Jaeho Lee, et al. "Phytochrome signalling is mediated through nucleoside diphosphate kinase 2." Nature 401, no. 6753 (1999): 610–13. http://dx.doi.org/10.1038/44176.

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44

Pan, Ling, Maki Kawai, Akira Yano, and Hirofumi Uchimiya. "Nucleoside Diphosphate Kinase Required for Coleoptile Elongation in Rice." Plant Physiology 122, no. 2 (2000): 447–52. http://dx.doi.org/10.1104/pp.122.2.447.

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45

Wagner, Paul D., and Ngoc-Diep Vu. "Phosphorylation of ATP-Citrate Lyase by Nucleoside Diphosphate Kinase." Journal of Biological Chemistry 270, no. 37 (1995): 21758–64. http://dx.doi.org/10.1074/jbc.270.37.21758.

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46

Quintero-Reyes, Idania E., Karina D. Garcia-Orozco, Rocio Sugich-Miranda, et al. "Shrimp oncoprotein nm23 is a functional nucleoside diphosphate kinase." Journal of Bioenergetics and Biomembranes 44, no. 3 (2012): 325–31. http://dx.doi.org/10.1007/s10863-012-9436-1.

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47

Lacombe, Marie-Lise, Xavier Sastre-Garau, Ioan Lascu, et al. "Overexpression of nucleoside diphosphate kinase (nm23) in solid tumours." European Journal of Cancer and Clinical Oncology 27, no. 10 (1991): 1302–7. http://dx.doi.org/10.1016/0277-5379(91)90101-i.

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48

Ghosh, Inca, Nithyakalyani Raghavan, Peter C. Fitzgerald, and Alan L. Scott. "Nucleoside diphosphate kinase from the parasitic nematode Brugia malayi." Gene 164, no. 2 (1995): 261–66. http://dx.doi.org/10.1016/0378-1119(95)00500-6.

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49

Besir, Hüseyin, Kornelius Zeth, Andreas Bracher, et al. "Structure of a halophilic nucleoside diphosphate kinase fromHalobacterium salinarum." FEBS Letters 579, no. 29 (2005): 6595–600. http://dx.doi.org/10.1016/j.febslet.2005.10.052.

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50

MARCINIAK, Stefan J., and J. Michael EDWARDSON. "Association of nucleoside diphosphate kinase with pancreatic zymogen granules: effects of local GTP generation on granule membrane characteristics." Biochemical Journal 316, no. 1 (1996): 99–106. http://dx.doi.org/10.1042/bj3160099.

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It is well established that both GTP-binding proteins and phosphoproteins are involved in the control of exocytosis in the exocrine pancreas. Exocytotic membrane fusion is stimulated by guanosine 5′-[γ-thio]triphosphate, and the phosphorylation states of several proteins, including at least one on the zymogen granule membrane, are known to change during exocytosis. We show here that a nucleoside diphosphate kinase is associated with the cytoplasmic face of pancreatic zymogen granules. This enzyme behaves as a phosphoprotein of apparent molecular mass 21 kDa on SDS/polyacrylamide gels, and is a
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