메뉴 건너뛰기




Volumn 54, Issue 4, 2004, Pages 814-816

Crystal Structure of Human p120 Homologue Protein PH1374 from Pyrococcus horikoshii

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; PH1374 PROTEIN; PROTEIN P120; UNCLASSIFIED DRUG;

EID: 1542346449     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10645     Document Type: Article
Times cited : (10)

References (19)
  • 1
    • 0023870151 scopus 로고
    • Identification and characterization of a human proliferation-associated nucleolar antigen with a molecular weight of 120,000 expressed in early G1 phase
    • Freeman JW, Busch RK, Gyorkey F, Gyorkey P, Ross BE, Busch H. Identification and characterization of a human proliferation-associated nucleolar antigen with a molecular weight of 120,000 expressed in early G1 phase. Cancer Res 1988;48:1244-1251.
    • (1988) Cancer Res , vol.48 , pp. 1244-1251
    • Freeman, J.W.1    Busch, R.K.2    Gyorkey, F.3    Gyorkey, P.4    Ross, B.E.5    Busch, H.6
  • 2
    • 0028357246 scopus 로고
    • Prediction of an rRNA methyltransferase domain in human tumor-specific nucleolar protein P120
    • Koonin EV. Prediction of an rRNA methyltransferase domain in human tumor-specific nucleolar protein P120. Nucleic Acids Res 1994;22:2476-2478.
    • (1994) Nucleic Acids Res , vol.22 , pp. 2476-2478
    • Koonin, E.V.1
  • 3
    • 0033509092 scopus 로고    scopus 로고
    • Protein trans-acting factors involved in ribosome biogenesis in Saccharomyces cerevisiae
    • Kressler D, Linder P, de La Cruz J. Protein trans-acting factors involved in ribosome biogenesis in Saccharomyces cerevisiae. Mol Cell Biol 1999;19:7897-7912.
    • (1999) Mol Cell Biol , vol.19 , pp. 7897-7912
    • Kressler, D.1    Linder, P.2    De La Cruz, J.3
  • 4
    • 0033050006 scopus 로고    scopus 로고
    • Purification, cloning, and characterization of the 16S RNA m5C967 methyltransferase from Escherichia coli
    • Tscherne JS, Nurse K, Popienick P, Michel H, Sochacki M, Ofengand J. Purification, cloning, and characterization of the 16S RNA m5C967 methyltransferase from Escherichia coli. Biochemistry 1999;38:1884-1892.
    • (1999) Biochemistry , vol.38 , pp. 1884-1892
    • Tscherne, J.S.1    Nurse, K.2    Popienick, P.3    Michel, H.4    Sochacki, M.5    Ofengand, J.6
  • 5
    • 0001445292 scopus 로고    scopus 로고
    • Identification of the 16S rRNA m5C967 methyltransferase from Escherichia coli
    • Gu XR, Gustafsson C, Ku J, Yu M, Santi DV. Identification of the 16S rRNA m5C967 methyltransferase from Escherichia coli. Biochemistry 1999;38:4053-4057.
    • (1999) Biochemistry , vol.38 , pp. 4053-4057
    • Gu, X.R.1    Gustafsson, C.2    Ku, J.3    Yu, M.4    Santi, D.V.5
  • 6
    • 0032959714 scopus 로고    scopus 로고
    • A conserved motif in the yeast nucleolar protein Nop2p contains an essential cysteine residue
    • King M, Ton D, Redman KL. A conserved motif in the yeast nucleolar protein Nop2p contains an essential cysteine residue. Biochem J 1999;337:29-35.
    • (1999) Biochem J , vol.337 , pp. 29-35
    • King, M.1    Ton, D.2    Redman, K.L.3
  • 7
    • 0034682446 scopus 로고    scopus 로고
    • m5C RNA and m5C DNA methyl transferases use different cysteine residues as catalysts
    • Liu Y, Santi DV. m5C RNA and m5C DNA methyl transferases use different cysteine residues as catalysts. Proc Natl Acad Sci USA 2000;97:8263-8265.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8263-8265
    • Liu, Y.1    Santi, D.V.2
  • 8
    • 0037125961 scopus 로고    scopus 로고
    • RNA methyltransferases utilize two cysteine residues in the formation of 5-methylcytosine
    • King MY, Redman KL. RNA methyltransferases utilize two cysteine residues in the formation of 5-methylcytosine. Biochemistry 2002;41:11218-11225.
    • (2002) Biochemistry , vol.41 , pp. 11218-11225
    • King, M.Y.1    Redman, K.L.2
  • 10
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project, No. 4. The CCP4 Suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 12
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • La Fortelle E de, Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol 1997;276:472-494.
    • (1997) Methods Enzymol , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 13
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams JP, Leslie AGW. Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr D Biol Crystallogr 1996;52:30-42.
    • (1996) Acta Crystallogr D Biol Crystallogr , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 16
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou J-Y, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 17
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L, Sandler C. Mapping the protein universe. Science 1996;273:595-602.
    • (1996) Science , vol.273 , pp. 595-602
    • Holm, L.1    Sandler, C.2
  • 18
    • 0028956315 scopus 로고
    • Universal catalytic domain structure of AdoMet-dependent methyltransferases
    • Schluckebier G, O'Gara M, Saenger W, Cheng X. Universal catalytic domain structure of AdoMet-dependent methyltransferases. J Mol Biol 1995;247:16-20.
    • (1995) J Mol Biol , vol.247 , pp. 16-20
    • Schluckebier, G.1    O'Gara, M.2    Saenger, W.3    Cheng, X.4
  • 19
    • 0035883736 scopus 로고    scopus 로고
    • AdoMet-dependent methylation, DNA methyltransferases and base flipping
    • Cheng X, Roberts RJ. AdoMet-dependent methylation, DNA methyltransferases and base flipping. Nucleic Acids Res 2001;29:3784-3795.
    • (2001) Nucleic Acids Res , vol.29 , pp. 3784-3795
    • Cheng, X.1    Roberts, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.