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Volumn 12, Issue 11, 2005, Pages 1211-1219

Inspecting the structure-activity relationship of protein kinase CK2 inhibitors derived from tetrabromo-benzimidazole

Author keywords

[No Author keywords available]

Indexed keywords

4,5,6,7 TETRABROMOBENZIMIDAZOLE; 4,5,6,7-TETRABROMOBENZIMIDAZOLE; BENZIMIDAZOLE; BENZIMIDAZOLE DERIVATIVE; BROMINE; CASEIN KINASE II; PROTEIN KINASE INHIBITOR;

EID: 27744504303     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2005.08.015     Document Type: Article
Times cited : (119)

References (55)
  • 2
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • P. Blume-Jensen, and T. Hunter Oncogenic kinase signalling Nature 411 2001 355 365
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 3
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases-the major drug targets of the twenty-first century?
    • P. Cohen Protein kinases-the major drug targets of the twenty-first century? Nat. Rev. Drug Discov. 1 2002 309 315
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 309-315
    • Cohen, P.1
  • 4
    • 0036467568 scopus 로고    scopus 로고
    • Rational therapeutic intervention in cancer: Kinases as drug targets
    • C.L. Sawyers Rational therapeutic intervention in cancer: kinases as drug targets Curr. Opin. Genet. Dev. 12 2002 111 115
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 111-115
    • Sawyers, C.L.1
  • 5
    • 0036667385 scopus 로고    scopus 로고
    • Protein tyrosine kinase inhibitors: New treatment modalities?
    • D. Fabbro, D. Parkinson, and A. Matter Protein tyrosine kinase inhibitors: new treatment modalities? Curr. Opin. Pharmacol. 2 2002 374 381
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 374-381
    • Fabbro, D.1    Parkinson, D.2    Matter, A.3
  • 7
    • 1642323740 scopus 로고    scopus 로고
    • Protein kinase inhibitors: Insights into drug design from structure
    • M.E. Noble, J.A. Endicott, and L.N. Johnson Protein kinase inhibitors: insights into drug design from structure Science 303 2004 1800 1805
    • (2004) Science , vol.303 , pp. 1800-1805
    • Noble, M.E.1    Endicott, J.A.2    Johnson, L.N.3
  • 8
    • 0033026444 scopus 로고    scopus 로고
    • Strategies toward the design of novel and selective protein tyrosine kinase inhibitors
    • P. Traxler, and P. Furet Strategies toward the design of novel and selective protein tyrosine kinase inhibitors Pharmacol. Ther. 82 1999 195 206
    • (1999) Pharmacol. Ther. , vol.82 , pp. 195-206
    • Traxler, P.1    Furet, P.2
  • 12
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • F. Meggio, and L.A. Pinna One-thousand-and-one substrates of protein kinase CK2? FASEB J. 17 2003 349 368
    • (2003) FASEB J. , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 13
    • 0038340907 scopus 로고    scopus 로고
    • The raison d'etre of constitutively active protein kinases: The lesson of CK2
    • L.A. Pinna The raison d'etre of constitutively active protein kinases: the lesson of CK2 Acc. Chem. Res. 36 2003 378 384
    • (2003) Acc. Chem. Res. , vol.36 , pp. 378-384
    • Pinna, L.A.1
  • 14
    • 0037107552 scopus 로고    scopus 로고
    • Protein kinase CK2: A challenge to canons
    • L.A. Pinna Protein kinase CK2: a challenge to canons J. Cell Sci. 115 2002 3873 3878
    • (2002) J. Cell Sci. , vol.115 , pp. 3873-3878
    • Pinna, L.A.1
  • 15
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase CK2: Structure, regulation and role in cellular decisions of life and death
    • D.W. Litchfield Protein kinase CK2: structure, regulation and role in cellular decisions of life and death Biochem. J. 369 2003 1 15
    • (2003) Biochem. J. , vol.369 , pp. 1-15
    • Litchfield, D.W.1
  • 16
    • 0035476623 scopus 로고    scopus 로고
    • Crystal structure of human protein kinase CK2: Insights into basic properties of the CK2 holoenzyme
    • K. Niefind, B. Guerra, I. Ermakowa, and O.G. Issinger Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme EMBO J. 20 2001 5320 5331
    • (2001) EMBO J. , vol.20 , pp. 5320-5331
    • Niefind, K.1    Guerra, B.2    Ermakowa, I.3    Issinger, O.G.4
  • 18
    • 0028985936 scopus 로고
    • Casein kinase II alpha transgene-induced murine lymphoma: Relation to theileriosis in cattle
    • D.C. Seldin, and P. Leder Casein kinase II alpha transgene-induced murine lymphoma: relation to theileriosis in cattle Science 267 1995 894 897
    • (1995) Science , vol.267 , pp. 894-897
    • Seldin, D.C.1    Leder, P.2
  • 19
    • 0029815976 scopus 로고    scopus 로고
    • Tal-1 induces T cell acute lymphoblastic leukemia accelerated by casein kinase IIalpha
    • M.A. Kelliher, D.C. Seldin, and P. Leder Tal-1 induces T cell acute lymphoblastic leukemia accelerated by casein kinase IIalpha EMBO J. 15 1996 5160 5166
    • (1996) EMBO J. , vol.15 , pp. 5160-5166
    • Kelliher, M.A.1    Seldin, D.C.2    Leder, P.3
  • 20
    • 0032516522 scopus 로고    scopus 로고
    • Protein kinase CK2alpha' is induced by serum as a delayed early gene and cooperates with Ha-ras in fibroblast transformation
    • M. Orlandini, F. Semplici, R. Ferruzzi, F. Meggio, L.A. Pinna, and S. Oliviero Protein kinase CK2alpha' is induced by serum as a delayed early gene and cooperates with Ha-ras in fibroblast transformation J. Biol. Chem. 273 1998 21291 21297
    • (1998) J. Biol. Chem. , vol.273 , pp. 21291-21297
    • Orlandini, M.1    Semplici, F.2    Ferruzzi, R.3    Meggio, F.4    Pinna, L.A.5    Oliviero, S.6
  • 21
    • 0032507966 scopus 로고    scopus 로고
    • P53 deficiency and misexpression of protein kinase CK2alpha collaborate in the development of thymic lymphomas in mice
    • E. Landesman-Bollag, P.L. Channavajhala, R.D. Cardiff, and D.C. Seldin p53 deficiency and misexpression of protein kinase CK2alpha collaborate in the development of thymic lymphomas in mice Oncogene 16 1998 2965 2974
    • (1998) Oncogene , vol.16 , pp. 2965-2974
    • Landesman-Bollag, E.1    Channavajhala, P.L.2    Cardiff, R.D.3    Seldin, D.C.4
  • 22
    • 22344454388 scopus 로고    scopus 로고
    • Modulation of death receptor-mediated apoptosis by CK2
    • G. Wang, K.A. Ahmad, and K. Ahmed Modulation of death receptor-mediated apoptosis by CK2 Mol. Cell. Biochem. 274 2005 201 205
    • (2005) Mol. Cell. Biochem. , vol.274 , pp. 201-205
    • Wang, G.1    Ahmad, K.A.2    Ahmed, K.3
  • 24
    • 0141791013 scopus 로고    scopus 로고
    • Biochemical and three-dimensional-structural study of the specific inhibition of protein kinase CK2 by [5-oxo-5,6-dihydroindolo-(1,2-a)quinazolin- 7-yl]acetic acid (IQA)
    • S. Sarno, E. de Moliner, M. Ruzzene, M.A. Pagano, R. Battistutta, J. Bain, D. Fabbro, J. Schoepfer, M. Elliott, and P. Furet Biochemical and three-dimensional-structural study of the specific inhibition of protein kinase CK2 by [5-oxo-5,6-dihydroindolo-(1,2-a)quinazolin-7-yl]acetic acid (IQA) Biochem. J. 374 2003 639 646
    • (2003) Biochem. J. , vol.374 , pp. 639-646
    • Sarno, S.1    De Moliner, E.2    Ruzzene, M.3    Pagano, M.A.4    Battistutta, R.5    Bain, J.6    Fabbro, D.7    Schoepfer, J.8    Elliott, M.9    Furet, P.10
  • 25
    • 0033060267 scopus 로고    scopus 로고
    • Emodin, an anthraquinone derivative isolated from the rhizomes of Rheum palmatum, selectively inhibits the activity of casein kinase II as a competitive inhibitor
    • H. Yim, Y.H. Lee, C.H. Lee, and S.K. Lee Emodin, an anthraquinone derivative isolated from the rhizomes of Rheum palmatum, selectively inhibits the activity of casein kinase II as a competitive inhibitor Planta Med. 65 1999 9 13
    • (1999) Planta Med. , vol.65 , pp. 9-13
    • Yim, H.1    Lee, Y.H.2    Lee, C.H.3    Lee, S.K.4
  • 28
    • 0022123704 scopus 로고
    • Stereospecific synthesis by the sodium salt glycosylation method of halogeno benzimidazole 2′-deoxyribose analogues of the inhibitor of hnRNA synthesis, 5,6-dichloro-1-(beta-D-ribofuranosyl)benzimidazole (DRB)
    • Z. Kazimierczuk, R. Stolarski, and D. Shugar Stereospecific synthesis by the sodium salt glycosylation method of halogeno benzimidazole 2′-deoxyribose analogues of the inhibitor of hnRNA synthesis, 5,6-dichloro-1-(beta-D-ribofuranosyl)benzimidazole (DRB) Z. Naturforsch. [C] 40 1985 715 720
    • (1985) Z. Naturforsch. [C] , vol.40 , pp. 715-720
    • Kazimierczuk, Z.1    Stolarski, R.2    Shugar, D.3
  • 29
    • 0023000520 scopus 로고
    • Casein kinase type II is involved in the inhibition by 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole of specific RNA polymerase II transcription
    • R. Zandomeni, M.C. Zandomeni, D. Shugar, and R. Weinmann Casein kinase type II is involved in the inhibition by 5,6-dichloro-1-beta-D- ribofuranosylbenzimidazole of specific RNA polymerase II transcription J. Biol. Chem. 261 1986 3414 3419
    • (1986) J. Biol. Chem. , vol.261 , pp. 3414-3419
    • Zandomeni, R.1    Zandomeni, M.C.2    Shugar, D.3    Weinmann, R.4
  • 30
    • 0035805108 scopus 로고    scopus 로고
    • Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 ('casein kinase-2')
    • S. Sarno, H. Reddy, F. Meggio, M. Ruzzene, S.P. Davies, A. Donella Deana, D. Shugar, and L.A. Pinna Selectivity of 4,5,6,7-tetrabromobenzotriazole, an ATP site-directed inhibitor of protein kinase CK2 ('casein kinase-2') FEBS Lett. 496 2001 44 48
    • (2001) FEBS Lett. , vol.496 , pp. 44-48
    • Sarno, S.1    Reddy, H.2    Meggio, F.3    Ruzzene, M.4    Davies, S.P.5    Donella Deana, A.6    Shugar, D.7    Pinna, L.A.8
  • 31
    • 0037093352 scopus 로고    scopus 로고
    • Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells
    • M. Ruzzene, D. Penzo, and L.A. Pinna Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells Biochem. J. 364 2002 41 47
    • (2002) Biochem. J. , vol.364 , pp. 41-47
    • Ruzzene, M.1    Penzo, D.2    Pinna, L.A.3
  • 33
    • 1942486312 scopus 로고    scopus 로고
    • CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37
    • Y. Miyata, and E. Nishida CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37 Mol. Cell. Biol. 24 2004 4065 4074
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4065-4074
    • Miyata, Y.1    Nishida, E.2
  • 37
    • 0034775155 scopus 로고    scopus 로고
    • Structural features underlying selective inhibition of protein kinase CK2 by ATP site-directed tetrabromo-2-benzotriazole
    • R. Battistutta, E. De Moliner, S. Sarno, G. Zanotti, and L.A. Pinna Structural features underlying selective inhibition of protein kinase CK2 by ATP site-directed tetrabromo-2-benzotriazole Protein Sci. 10 2001 2200 2206
    • (2001) Protein Sci. , vol.10 , pp. 2200-2206
    • Battistutta, R.1    De Moliner, E.2    Sarno, S.3    Zanotti, G.4    Pinna, L.A.5
  • 38
    • 0032854118 scopus 로고    scopus 로고
    • The structure-based design of ATP-site directed protein kinase inhibitors
    • L.M. Toledo, N.B. Lydon, and D. Elbaum The structure-based design of ATP-site directed protein kinase inhibitors Curr. Med. Chem. 6 1999 775 805
    • (1999) Curr. Med. Chem. , vol.6 , pp. 775-805
    • Toledo, L.M.1    Lydon, N.B.2    Elbaum, D.3
  • 39
    • 0036591874 scopus 로고    scopus 로고
    • Structural biology in drug design: Selective protein kinase inhibitors
    • G. Scapin Structural biology in drug design: selective protein kinase inhibitors Drug Discov. Today 7 2002 601 611
    • (2002) Drug Discov. Today , vol.7 , pp. 601-611
    • Scapin, G.1
  • 41
    • 0042591222 scopus 로고    scopus 로고
    • Polyhalogenobenzimidazoles: Synthesis and their inhibitory activity against casein kinases
    • M. Andrzejewska, M.A. Pagano, F. Meggio, A.M. Brunati, and Z. Kazimierczuk Polyhalogenobenzimidazoles: synthesis and their inhibitory activity against casein kinases Bioorg. Med. Chem. 11 2003 3997 4002
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 3997-4002
    • Andrzejewska, M.1    Pagano, M.A.2    Meggio, F.3    Brunati, A.M.4    Kazimierczuk, Z.5
  • 42
    • 0034703030 scopus 로고    scopus 로고
    • The replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2
    • R. Battistutta, S. Sarno, E. De Moliner, E. Papinutto, G. Zanotti, and L.A. Pinna The replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2 J. Biol. Chem. 275 2000 29618 29622
    • (2000) J. Biol. Chem. , vol.275 , pp. 29618-29622
    • Battistutta, R.1    Sarno, S.2    De Moliner, E.3    Papinutto, E.4    Zanotti, G.5    Pinna, L.A.6
  • 45
    • 0042769409 scopus 로고    scopus 로고
    • Alternative binding modes of an inhibitor to two different kinases
    • E. De Moliner, N.R. Brown, and L.N. Johnson Alternative binding modes of an inhibitor to two different kinases Eur. J. Biochem. 270 2003 3174 3181
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3174-3181
    • De Moliner, E.1    Brown, N.R.2    Johnson, L.N.3
  • 46
    • 0030567353 scopus 로고    scopus 로고
    • The nature and geometry of intermolecular interactions between halogens and oxygen or nitrogen
    • J.P.M. Lommerse, A.J. Stone, R. Taylor, and F.H. Allen The nature and geometry of intermolecular interactions between halogens and oxygen or nitrogen J. Am. Chem. Soc. 118 1996 3108 3116
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3108-3116
    • Lommerse, J.P.M.1    Stone, A.J.2    Taylor, R.3    Allen, F.H.4
  • 48
    • 17544377840 scopus 로고    scopus 로고
    • Protein kinase CK2 mutants defective in substrate recognition: Purification and kinetic analysis
    • S. Sarno, P. Vaglio, F. Meggio, O.G. Issinger, and L.A. Pinna Protein kinase CK2 mutants defective in substrate recognition: purification and kinetic analysis J. Biol. Chem. 271 1996 10595 10601
    • (1996) J. Biol. Chem. , vol.271 , pp. 10595-10601
    • Sarno, S.1    Vaglio, P.2    Meggio, F.3    Issinger, O.G.4    Pinna, L.A.5
  • 49
    • 0002414103 scopus 로고
    • Molecular data processing
    • D. Moras A.D. Podjarny J.P. Thierry Oxford University Press Oxford
    • A.G.W. Leslie Molecular data processing D. Moras A.D. Podjarny J.P. Thierry Crystallographic Computing V 1991 Oxford University Press Oxford 50 61
    • (1991) Crystallographic Computing V , pp. 50-61
    • Leslie, A.G.W.1
  • 50
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 The CCP4 suite: programs for protein crystallography Acta Crystallogr. D50 1994 760 763
    • (1994) Acta Crystallogr. , vol.50 , pp. 760-763
  • 53
    • 0032215320 scopus 로고    scopus 로고
    • Databases in protein crystallography
    • G.J. Kleywegt, and T.A. Jones Databases in protein crystallography Acta Crystallogr. D 54 1998 1119 1131
    • (1998) Acta Crystallogr. D , vol.54 , pp. 1119-1131
    • Kleywegt, G.J.1    Jones, T.A.2


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