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Volumn 54, Issue 1, 2007, Pages 139-146

Mouse Aurora A: Expression in Escherichia coli and purification

Author keywords

Expression in Escherichia coli; Lambda phosphatase; Mouse Aurora A

Indexed keywords

AURORA KINASE; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; PROTEIN SERINE THREONINE KINASE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 34247337692     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.03.002     Document Type: Article
Times cited : (8)

References (35)
  • 1
    • 0028938482 scopus 로고
    • Mutations in aurora prevent centrosome separation leading to the formation of monopolar spindles
    • Glover D.M., Leibowitz M.H., McLean D.A., and Parry H. Mutations in aurora prevent centrosome separation leading to the formation of monopolar spindles. Cell 81 (1995) 95-105
    • (1995) Cell , vol.81 , pp. 95-105
    • Glover, D.M.1    Leibowitz, M.H.2    McLean, D.A.3    Parry, H.4
  • 2
    • 0030876766 scopus 로고    scopus 로고
    • A novel mammalian, mitotic spindle-associated kinase is related to yeast and fly chromosome segregation regulators
    • Gopalan G., Chan C.S., and Donovan P.J. A novel mammalian, mitotic spindle-associated kinase is related to yeast and fly chromosome segregation regulators. J. Cell Biol. 138 (1997) 643-656
    • (1997) J. Cell Biol. , vol.138 , pp. 643-656
    • Gopalan, G.1    Chan, C.S.2    Donovan, P.J.3
  • 3
    • 0030946109 scopus 로고    scopus 로고
    • Cell cycle-dependent expression and spindle pole localization of a novel human protein kinase, Aik, related to Aurora of Drosophila and yeast Ipl1
    • Kimura M., Kotani S., Hattori T., Sumi N., Yoshioka T., Todokoro K., and Okano Y. Cell cycle-dependent expression and spindle pole localization of a novel human protein kinase, Aik, related to Aurora of Drosophila and yeast Ipl1. J. Biol. Chem. 272 (1997) 13766-13771
    • (1997) J. Biol. Chem. , vol.272 , pp. 13766-13771
    • Kimura, M.1    Kotani, S.2    Hattori, T.3    Sumi, N.4    Yoshioka, T.5    Todokoro, K.6    Okano, Y.7
  • 4
    • 0030746889 scopus 로고    scopus 로고
    • ayk1, a novel mammalian gene related to Drosophila aurora centrosome separation kinase, is specifically expressed during meiosis
    • Yanai A., Arama E., Kilfin G., and Motro B. ayk1, a novel mammalian gene related to Drosophila aurora centrosome separation kinase, is specifically expressed during meiosis. Oncogene 14 (1997) 2943-2950
    • (1997) Oncogene , vol.14 , pp. 2943-2950
    • Yanai, A.1    Arama, E.2    Kilfin, G.3    Motro, B.4
  • 5
    • 0032212717 scopus 로고    scopus 로고
    • Cloning of STK13, a third human protein kinase related to Drosophila aurora and budding yeast Ipl1 that maps on chromosome 19q13.3-ter
    • Bernard M., Sanseau P., Henry C., Couturier A., and Prigent C. Cloning of STK13, a third human protein kinase related to Drosophila aurora and budding yeast Ipl1 that maps on chromosome 19q13.3-ter. Genomics 53 (1998) 406-409
    • (1998) Genomics , vol.53 , pp. 406-409
    • Bernard, M.1    Sanseau, P.2    Henry, C.3    Couturier, A.4    Prigent, C.5
  • 6
    • 0032509431 scopus 로고    scopus 로고
    • Human AIM-1: cDNA cloning and reduced expression during endomitosis in megakaryocyte-lineage cells
    • Katayama H., Ota T., Morita K., Terada Y., Suzuki F., Katoh O., and Tatsuka M. Human AIM-1: cDNA cloning and reduced expression during endomitosis in megakaryocyte-lineage cells. Gene 224 (1998) 1-7
    • (1998) Gene , vol.224 , pp. 1-7
    • Katayama, H.1    Ota, T.2    Morita, K.3    Terada, Y.4    Suzuki, F.5    Katoh, O.6    Tatsuka, M.7
  • 10
    • 18744377748 scopus 로고    scopus 로고
    • Drugging cell-cycle kinases in cancer therapy
    • Blagden S., and de Bono J. Drugging cell-cycle kinases in cancer therapy. Curr. Drug Targets 6 (2005) 325-335
    • (2005) Curr. Drug Targets , vol.6 , pp. 325-335
    • Blagden, S.1    de Bono, J.2
  • 11
    • 0035824660 scopus 로고    scopus 로고
    • Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle
    • Katayama H., Zhou H., Li Q., Tatsuka M., and Sen S. Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle. J. Biol. Chem. 276 (2001) 46219-46224
    • (2001) J. Biol. Chem. , vol.276 , pp. 46219-46224
    • Katayama, H.1    Zhou, H.2    Li, Q.3    Tatsuka, M.4    Sen, S.5
  • 12
    • 0242330123 scopus 로고    scopus 로고
    • Structural basis of Aurora-A activation by TPX2 at the mitotic spindle
    • Bayliss R., Sardon T., Vernos I., and Conti E. Structural basis of Aurora-A activation by TPX2 at the mitotic spindle. Mol. Cell 12 (2003) 851-862
    • (2003) Mol. Cell , vol.12 , pp. 851-862
    • Bayliss, R.1    Sardon, T.2    Vernos, I.3    Conti, E.4
  • 18
    • 0037115829 scopus 로고    scopus 로고
    • The centrosomal kinase Aurora-A/STK15 interacts with a putative tumor suppressor NM23-H1
    • Du J., and Hannon G.J. The centrosomal kinase Aurora-A/STK15 interacts with a putative tumor suppressor NM23-H1. Nucleic Acids Res. 30 (2002) 5465-5475
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5465-5475
    • Du, J.1    Hannon, G.J.2
  • 19
    • 0037160088 scopus 로고    scopus 로고
    • Aurora-A kinase interacting protein (AIP), a novel negative regulator of human Aurora-A kinase
    • Kiat L.S., Hui K.M., and Gopalan G. Aurora-A kinase interacting protein (AIP), a novel negative regulator of human Aurora-A kinase. J. Biol. Chem. 277 (2002) 45558-45565
    • (2002) J. Biol. Chem. , vol.277 , pp. 45558-45565
    • Kiat, L.S.1    Hui, K.M.2    Gopalan, G.3
  • 24
    • 2942590333 scopus 로고    scopus 로고
    • Activation of Aurora-A kinase by protein phosphatase inhibitor-2, a bifunctional signaling protein
    • Satinover D.L., Leach C.A., Stukenberg P.T., and Brautigan D.L. Activation of Aurora-A kinase by protein phosphatase inhibitor-2, a bifunctional signaling protein. Proc. Natl. Acad. Sci. USA 101 (2004) 8625-8630
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8625-8630
    • Satinover, D.L.1    Leach, C.A.2    Stukenberg, P.T.3    Brautigan, D.L.4
  • 26
    • 0016610995 scopus 로고
    • Determinant of cistron specificity in bacterial ribosomes
    • Shine J., and Dalgarno L. Determinant of cistron specificity in bacterial ribosomes. Nature 254 (1975) 34-38
    • (1975) Nature , vol.254 , pp. 34-38
    • Shine, J.1    Dalgarno, L.2
  • 27
    • 0016829942 scopus 로고
    • Terminal-sequence analysis of bacterial ribosomal RNA. Correlation between the 3′-terminal-polypyrimidine sequence of 16-S RNA and translational specificity of the ribosome
    • Shine J., and Dalgarno L. Terminal-sequence analysis of bacterial ribosomal RNA. Correlation between the 3′-terminal-polypyrimidine sequence of 16-S RNA and translational specificity of the ribosome. Eur. J. Biochem. 57 (1975) 221-230
    • (1975) Eur. J. Biochem. , vol.57 , pp. 221-230
    • Shine, J.1    Dalgarno, L.2
  • 28
    • 4143096903 scopus 로고    scopus 로고
    • Crystal structures of a ligand-free and malonate-bound human caspase-1: implications for the mechanism of substrate binding
    • Romanowski M.J., Scheer J.M., O'Brien T., and McDowell R.S. Crystal structures of a ligand-free and malonate-bound human caspase-1: implications for the mechanism of substrate binding. Structure (Camb.) 12 (2004) 1361-1371
    • (2004) Structure (Camb.) , vol.12 , pp. 1361-1371
    • Romanowski, M.J.1    Scheer, J.M.2    O'Brien, T.3    McDowell, R.S.4
  • 30
    • 0030158243 scopus 로고    scopus 로고
    • A method for the separation of GST fusion proteins from co-purifying GroEL
    • Thain A., Gaston K., Jenkins O., and Clarke A.R. A method for the separation of GST fusion proteins from co-purifying GroEL. Trends Genet. 12 (1996) 209-210
    • (1996) Trends Genet. , vol.12 , pp. 209-210
    • Thain, A.1    Gaston, K.2    Jenkins, O.3    Clarke, A.R.4
  • 31
    • 19644378636 scopus 로고    scopus 로고
    • Allosteric inhibition of PTP1B activity by selective modification of a non-active site cysteine residue
    • Hansen S.K., Cancilla M.T., Shiau T.P., Kung J., Chen T., and Erlanson D.A. Allosteric inhibition of PTP1B activity by selective modification of a non-active site cysteine residue. Biochemistry 44 (2005) 7704-7712
    • (2005) Biochemistry , vol.44 , pp. 7704-7712
    • Hansen, S.K.1    Cancilla, M.T.2    Shiau, T.P.3    Kung, J.4    Chen, T.5    Erlanson, D.A.6
  • 32
    • 0025272639 scopus 로고
    • Current approaches to macromolecular crystallization
    • McPherson A. Current approaches to macromolecular crystallization. Eur. J. Biochem. 189 (1990) 1-23
    • (1990) Eur. J. Biochem. , vol.189 , pp. 1-23
    • McPherson, A.1
  • 33
    • 0000898340 scopus 로고
    • Biological Macromolecule Crystallization Database, Version 3.0: new features, data and the NASA archive for protein crystal growth data
    • Gilliland G.L., Tung M., Blakeslee D.M., and Ladner J.E. Biological Macromolecule Crystallization Database, Version 3.0: new features, data and the NASA archive for protein crystal growth data. Acta Crystallogr. D 50 (1994) 408-413
    • (1994) Acta Crystallogr. D , vol.50 , pp. 408-413
    • Gilliland, G.L.1    Tung, M.2    Blakeslee, D.M.3    Ladner, J.E.4
  • 34
    • 0035108006 scopus 로고    scopus 로고
    • A comparison of salts for the crystallization of macromolecules
    • McPherson A. A comparison of salts for the crystallization of macromolecules. Protein Sci. 10 (2001) 418-422
    • (2001) Protein Sci. , vol.10 , pp. 418-422
    • McPherson, A.1
  • 35
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath J.W. The finer things in X-ray diffraction data collection. Acta Crystallogr. D 55 (1999) 1718-1725
    • (1999) Acta Crystallogr. D , vol.55 , pp. 1718-1725
    • Pflugrath, J.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.