메뉴 건너뛰기




Volumn 55, Issue 1, 2004, Pages 214-217

X-ray Structure of Human Gankyrin, the Product of a Gene Linked to Hepatocellular Carcinoma

Author keywords

[No Author keywords available]

Indexed keywords

GANKYRIN; GENE PRODUCT; ONCOPROTEIN; UNCLASSIFIED DRUG;

EID: 1442275579     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20028     Document Type: Article
Times cited : (24)

References (32)
  • 1
    • 0033978257 scopus 로고    scopus 로고
    • Reduced stability of retinoblastoma protein by gankyrin, an oncogenic ankyrin-repeat protein overexpressed in hepatomas
    • Higashitsuji H, Itoh K, Nagao T, Dawson S, Nonoguchi K, Kido T, Mayer RJ, Arii S, Fujita, J. Reduced stability of retinoblastoma protein by gankyrin, an oncogenic ankyrin-repeat protein overexpressed in hepatomas. Nat Med 2000;6:96-99.
    • (2000) Nat Med , vol.6 , pp. 96-99
    • Higashitsuji, H.1    Itoh, K.2    Nagao, T.3    Dawson, S.4    Nonoguchi, K.5    Kido, T.6    Mayer, R.J.7    Arii, S.8    Fujita, J.9
  • 2
    • 0037192842 scopus 로고    scopus 로고
    • Gankyrin is an ankyrin-repeat oncoprotein that interacts with CDK4 kinase and the S6 ATPase of the 26 S proteasome
    • Dawson S, Apcher S, Mee M, Higashitsuji H, Baker R, Uhle S, Dubiel W, Fujita J, Mayer RJ. Gankyrin is an ankyrin-repeat oncoprotein that interacts with CDK4 kinase and the S6 ATPase of the 26 S proteasome. J Biol Chem 2002;277:10893-10902.
    • (2002) J Biol Chem , vol.277 , pp. 10893-10902
    • Dawson, S.1    Apcher, S.2    Mee, M.3    Higashitsuji, H.4    Baker, R.5    Uhle, S.6    Dubiel, W.7    Fujita, J.8    Mayer, R.J.9
  • 5
    • 0029033861 scopus 로고
    • The retinoblastoma protein and cell cycle control
    • Weinberg RA. The retinoblastoma protein and cell cycle control. Cell 1995;81:323-330.
    • (1995) Cell , vol.81 , pp. 323-330
    • Weinberg, R.A.1
  • 6
    • 2642601106 scopus 로고    scopus 로고
    • Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7
    • Lee JO, Russo AA, Pavletich NP. Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7. Nature 1998:391;859-865.
    • (1998) Nature , vol.391 , pp. 859-865
    • Lee, J.O.1    Russo, A.A.2    Pavletich, N.P.3
  • 7
    • 0035863048 scopus 로고    scopus 로고
    • Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen
    • Kim HY, Ahn BY, Cho Y. Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen. EMBO J 2001:20;295-304.
    • (2001) EMBO J , vol.20 , pp. 295-304
    • Kim, H.Y.1    Ahn, B.Y.2    Cho, Y.3
  • 9
    • 0037177225 scopus 로고    scopus 로고
    • Novel insights into the INK4-CDK4/6-Rb pathway: Counter action of gankyrin against INK4 proteins regulates the CDK4-mediated phosphorylation of Rb
    • Li J, Tsai MD. Novel insights into the INK4-CDK4/6-Rb pathway: counter action of gankyrin against INK4 proteins regulates the CDK4-mediated phosphorylation of Rb. Biochemistry 2002;41:3977-3983.
    • (2002) Biochemistry , vol.41 , pp. 3977-3983
    • Li, J.1    Tsai, M.D.2
  • 10
    • 0037086294 scopus 로고    scopus 로고
    • The MAGE proteins: Emerging roles in cell cycle progression, apoptosis, and neurogenetic disease
    • Barker PA, Salehi A. The MAGE proteins: emerging roles in cell cycle progression, apoptosis, and neurogenetic disease. J Neurosci Res 2002;67:705-712.
    • (2002) J Neurosci Res , vol.67 , pp. 705-712
    • Barker, P.A.1    Salehi, A.2
  • 11
    • 0035879005 scopus 로고    scopus 로고
    • An overview of the MAGE gene family with the identification of all human members of the family
    • Chomez P, De Backer O, Bertrand M, De Plaen E, Boon T, Lucas S. An overview of the MAGE gene family with the identification of all human members of the family. Cancer Res 2001;61:5544-5551.
    • (2001) Cancer Res , vol.61 , pp. 5544-5551
    • Chomez, P.1    De Backer, O.2    Bertrand, M.3    De Plaen, E.4    Boon, T.5    Lucas, S.6
  • 14
    • 0036014796 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray diffraction analysis of yeast regulatory particle non-ATPase subunit 6 (Nas6p)
    • Adachi N, Padmanabhan B, Kataoka K, Kijima K, Yamaki M, Horikoshi M. Purification, crystallization and preliminary X-ray diffraction analysis of yeast regulatory particle non-ATPase subunit 6 (Nas6p). Acta Crystallogr D 2002;58:859-860.
    • (2002) Acta Crystallogr D , vol.58 , pp. 859-860
    • Adachi, N.1    Padmanabhan, B.2    Kataoka, K.3    Kijima, K.4    Yamaki, M.5    Horikoshi, M.6
  • 15
    • 0037349370 scopus 로고    scopus 로고
    • Facilities and methods for the high-throughput crystal structural analysis of human proteins
    • Heinemann U, Büssow K, Mueller U, Umbach P. Facilities and methods for the high-throughput crystal structural analysis of human proteins. Acc Chem Res 2003;36:157-163.
    • (2003) Acc Chem Res , vol.36 , pp. 157-163
    • Heinemann, U.1    Büssow, K.2    Mueller, U.3    Umbach, P.4
  • 18
    • 0034671563 scopus 로고    scopus 로고
    • Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitors
    • Jeffrey PD, Tong L, Pavletich NP. Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitors. Genes Dev 2000;14:3115-3125.
    • (2000) Genes Dev , vol.14 , pp. 3115-3125
    • Jeffrey, P.D.1    Tong, L.2    Pavletich, N.P.3
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 21
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • Vagin A, Teplyakov A. An approach to multi-copy search in molecular replacement. Acta Crystallogr D 2000;56;1622-1624.
    • (2000) Acta Crystallogr D , vol.56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 22
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, Peitsch MC. SWISS-MODEL: An automated protein homology-modeling server. Nucleic Acids Res 2003;31:3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 23
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 1997;53:240-255.
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 24
  • 26
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn MD, Isupov MN, Murshudov GN. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr D 2001;57:122-133.
    • (2001) Acta Crystallogr D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 27
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991;24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 28
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf RM. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr D 1999;55:938-940.
    • (1999) Acta Crystallogr D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 29
    • 0028057108 scopus 로고
    • Raster3d version 2.0-a program for photorealistic molecular graphics
    • Merritt EA, Murphy MEP. Raster3d version 2.0-a program for photorealistic molecular graphics. Acta Crystallogr D 1994;50:869-873.
    • (1994) Acta Crystallogr D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 30
    • 0037011104 scopus 로고    scopus 로고
    • Crystal structure of a 12 ANK repeat stack from human ankyrinR
    • Michaely P, Tomchick DR, Machius M, Anderson RGW. Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO J 2002;21:6387-6396.
    • (2002) EMBO J , vol.21 , pp. 6387-6396
    • Michaely, P.1    Tomchick, D.R.2    Machius, M.3    Anderson, R.G.W.4
  • 31
    • 0347093301 scopus 로고    scopus 로고
    • The crystal structure of gankyrin, an oncoprotein found in complexes with cyclin-dependent kinase 4, a 19 S proteasomal regulator, and the tumor suppressors Rb and p53
    • Krzywda S, Brzozowski AM, Higashitsuji H, Fujita J, Welchman R, Dawson S, Mayer RJ, Wilkinson AJ. The crystal structure of gankyrin, an oncoprotein found in complexes with cyclin-dependent kinase 4, a 19 S proteasomal regulator, and the tumor suppressors Rb and p53. J Biol Chem 2004;279:1541-1545.
    • (2004) J Biol Chem , vol.279 , pp. 1541-1545
    • Krzywda, S.1    Brzozowski, A.M.2    Higashitsuji, H.3    Fujita, J.4    Welchman, R.5    Dawson, S.6    Mayer, R.J.7    Wilkinson, A.J.8
  • 32
    • 0345832060 scopus 로고    scopus 로고
    • Crystal structure of the homolog of the oncoprotein gankyrin, an interactor of Rb and CDK4/6
    • Padmanabhan B, Adachi N, Kataoka K, Horikoshi M. Crystal structure of the homolog of the oncoprotein gankyrin, an interactor of Rb and CDK4/6. J Biol Chem 2004;279:1546-1552.
    • (2004) J Biol Chem , vol.279 , pp. 1546-1552
    • Padmanabhan, B.1    Adachi, N.2    Kataoka, K.3    Horikoshi, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.