Soluble tankyrase located in cytosol of human embryonic kidney cell line 293

Biochemistry (Moscow)

Volumn 68, Issue 3, 2003, Pages 260-268

  Kuimov, A N ^a   Terekhov, S M ^b  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b RESEARCH CENTRE FOR MEDICAL GENETICS   (Russian Federation)

Author keywords

ADP ribosylation; Poly(ADP ribose); Tankyrase

Indexed keywords

CELL MEMBRANES; CHROMOSOMES; ENZYMES; MONOMERS; SIZE EXCLUSION CHROMATOGRAPHY;

MICROSOMES;

CELL CULTURE;

ANKYRIN; HYBRID PROTEIN; MEMBRANE PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; POLY(ADENOSINE DIPHOSPHATE RIBOSE); TANKYRASE; TNKS PROTEIN, HUMAN;

AMINO ACID SEQUENCE; ARTICLE; CELL LINE; CHEMISTRY; CYTOLOGY; CYTOSOL; ENZYMOLOGY; FLUORESCENCE MICROSCOPY; GEL CHROMATOGRAPHY; GENETICS; HUMAN; ISOLATION AND PURIFICATION; KIDNEY; METABOLISM; MICROSOME; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PRENATAL DEVELOPMENT; PROTEIN TERTIARY STRUCTURE; SOLUBILITY;

AMINO ACID SEQUENCE; ANKYRINS; CELL LINE; CHROMATOGRAPHY, GEL; CONSERVED SEQUENCE; CYTOSOL; HUMANS; KIDNEY; MEMBRANE PROTEINS; MICROSCOPY, FLUORESCENCE; MICROSOMES; MOLECULAR SEQUENCE DATA; POLY ADENOSINE DIPHOSPHATE RIBOSE; POLY(ADP-RIBOSE) POLYMERASES; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SOLUBILITY; TANKYRASES;

EID: 0037359885     PISSN: 00062979     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1023046031434     Document Type: Article

References (16)

1. Smith, S., Giriat, I., Schmitt, A., and de Lange, T. (1998) Science, 282, 1484-1487.
2. Cook, B. D., Dynek, J. N., Chang, W., Shostak, G., and Smith, S. (2002) Mol. Cell Biol., 22, 332-342.
3. Smith, S., and de Lange, T. (1999) J. Cell Sci., 112, 3649-3656.
4. Chi, N.-W., and Lodish, H. F. (2000) J. Biol. Chem., 275, 38437-38444.
5. Seimiya, H., and Smith, S. (2002) J. Biol. Chem., 277, 14116-14126.
6. Sbodio, J. I., and Chi, N.-W. (2002) J. Biol. Chem., 217, 31887-331892.
7. Monz, D., Munnia, A., Comtesse, N., Fischer, U., Steudel, W. I., Feiden, W., Glass, B., and Meese, E. U. (2001) Clin. Cancer Res., 7, 113-119.
8. Kuimov, A. N., Kuprash, D. V., Petrov, V. N., Vdovichenko, K. K., Scanlan, M. J., Jongeneel, C. V., Lagarkova, M. A., and Nedospasov, S. A. (2001) Genes Immunol., 2, 52-55.
9. Lyons, R. J., Deane, R., Lynch, D. K., Ye, Z. S., Sanderson, G. M., Eyre, H. J., Sutherland, G. R., and Daly, R. J. (2001) J. Biol. Chem., 276, 17172-17180.
10. Kaminker, P. G., Kim, S. H., Taylor, R. D., Zebarjadian, Y., Funk, W. D., Morin, G. B., Yaswen, P., and Campisi, J. (2001) J. Biol. Chem., 276, 35891-35899.
11. Sbodio, J. I., Lodish, H. F., and Chi, N.-W. (2002) Biochem. J., 361, 451-459.
12. Ham, R. G., and McKeehan, W. L. (1979) Meth. Enzymol., 58, 44-93.
13. Laemmli, U. K. (1970) Nature, 227, 680-685.
14. Bradford, M. M. (1976) Analyt. Biochem., 72, 248-254.
15. Wilson, C. M. (1983) Meth. Enzymol, 91, 236-247.
16. Smith, S. (2001) Trends Biochem. Sci., 26, 174-179.