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Volumn 334, Issue 3, 2003, Pages 595-603

Glucocorticoid receptor-like Zn(Cys)4 motifs in BslI restriction endonuclease

Author keywords

EXAFS; MicroPIXE; REMS PCR; Restriction endonuclease; Zn motif

Indexed keywords

AMINO ACID; CYSTEINE; DIMER; DNA; DNA BINDING PROTEIN; GLUCOCORTICOID RECEPTOR; PROTEIN SUBUNIT; PROTON; RESTRICTION ENDONUCLEASE; ZINC;

EID: 0242662176     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.09.043     Document Type: Article
Times cited : (8)

References (28)
  • 1
    • 0035883723 scopus 로고    scopus 로고
    • Structure and function of type II restriction endonucleases
    • Pingoud A., Jeltsch A. Structure and function of type II restriction endonucleases. Nucl. Acids Res. 29:2001;3705-3727.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 3705-3727
    • Pingoud, A.1    Jeltsch, A.2
  • 2
    • 0033984761 scopus 로고    scopus 로고
    • Cloning, expression, and purification of a thermostable nonhomodimeric restriction enzyme, BslI
    • Hsieh P.C., Xiao J.P., O'Loane D., Xu S.Y. Cloning, expression, and purification of a thermostable nonhomodimeric restriction enzyme, BslI. J. Bacteriol. 182:2000;949-955.
    • (2000) J. Bacteriol. , vol.182 , pp. 949-955
    • Hsieh, P.C.1    Xiao, J.P.2    O'loane, D.3    Xu, S.Y.4
  • 3
    • 0034113440 scopus 로고    scopus 로고
    • Detection of rare mutant alleles by restriction endonuclease-mediated selective-PCR: Assay design and optimization
    • Fuery C.J., Impey H.L., Roberts N.J., Applegate T.L., Ward R.L., Hawkins N.J., et al. Detection of rare mutant alleles by restriction endonuclease-mediated selective-PCR: assay design and optimization. Clin. Chem. 46:2000;620-624.
    • (2000) Clin. Chem. , vol.46 , pp. 620-624
    • Fuery, C.J.1    Impey, H.L.2    Roberts, N.J.3    Applegate, T.L.4    Ward, R.L.5    Hawkins, N.J.6
  • 4
    • 0024292722 scopus 로고
    • Most human carcinomas of the exocrine pancreas contain mutant c-K-ras genes
    • Almoguera C., Shibata D., Forrester K., Martin J., Arnheim N., Perucho M. Most human carcinomas of the exocrine pancreas contain mutant c-K-ras genes. Cell. 53:1988;549-554.
    • (1988) Cell , vol.53 , pp. 549-554
    • Almoguera, C.1    Shibata, D.2    Forrester, K.3    Martin, J.4    Arnheim, N.5    Perucho, M.6
  • 5
    • 0024376173 scopus 로고
    • Ras oncogenes in human cancer: A review
    • Bos J.L. ras oncogenes in human cancer: a review. Cancer Res. 49:1989;4682-4689.
    • (1989) Cancer Res. , vol.49 , pp. 4682-4689
    • Bos, J.L.1
  • 7
    • 0033572720 scopus 로고    scopus 로고
    • Leaving no element of doubt: Analysis of proteins using microPIXE
    • Garman E. Leaving no element of doubt: analysis of proteins using microPIXE. Struct. Fold. Des. 7:1999;R291-R299.
    • (1999) Struct. Fold. Des. , vol.7
    • Garman, E.1
  • 8
    • 0026547747 scopus 로고
    • DNA recognition by GAL4: Structure of a protein-DNA complex
    • Marmorstein R., Carey M., Ptashne M., Harrison S.C. DNA recognition by GAL4: structure of a protein-DNA complex. Nature. 356:1992;408-414.
    • (1992) Nature , vol.356 , pp. 408-414
    • Marmorstein, R.1    Carey, M.2    Ptashne, M.3    Harrison, S.C.4
  • 10
    • 0035150384 scopus 로고    scopus 로고
    • Polyphyletic evolution of type II restriction enzymes revisited: Two independent sources of second-hand folds revealed
    • Bujnicki J.M., Radlinska M., Rychlewski L. Polyphyletic evolution of type II restriction enzymes revisited: two independent sources of second-hand folds revealed. Trends Biochem. Sci. 26:2001;9-11.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 9-11
    • Bujnicki, J.M.1    Radlinska, M.2    Rychlewski, L.3
  • 11
    • 0035253047 scopus 로고    scopus 로고
    • Zinc finger proteins: New insights into structural and functional diversity
    • Laity J.H., Lee B.M., Wright P.E. Zinc finger proteins: new insights into structural and functional diversity. Curr. Opin. Struct. Biol. 11:2001;39-46.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 39-46
    • Laity, J.H.1    Lee, B.M.2    Wright, P.E.3
  • 13
    • 0035369335 scopus 로고    scopus 로고
    • Nuclear-receptor interactions on DNA-response elements
    • Khorasanizadeh S., Rastinejad F. Nuclear-receptor interactions on DNA-response elements. Trends Biochem. Sci. 26:2001;384-390.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 384-390
    • Khorasanizadeh, S.1    Rastinejad, F.2
  • 15
    • 0032474760 scopus 로고    scopus 로고
    • DNA binding and cleavage by the nuclear intron-encoded homing endonuclease I-PpoI
    • Flick K.E., Jurica M.S., Monnat R.J. Jr, Stoddard B.L. DNA binding and cleavage by the nuclear intron-encoded homing endonuclease I-PpoI. Nature. 394:1998;96-101.
    • (1998) Nature , vol.394 , pp. 96-101
    • Flick, K.E.1    Jurica, M.S.2    Monnat Jr., R.J.3    Stoddard, B.L.4
  • 16
    • 0035898540 scopus 로고    scopus 로고
    • Intertwined structure of the DNA-binding domain of intron endonuclease I-TevI with its substrate
    • Van Roey P., Waddling C.A., Fox K.M., Belfort M., Derbyshire V. Intertwined structure of the DNA-binding domain of intron endonuclease I-TevI with its substrate. EMBO J. 20:2001;3631-3637.
    • (2001) EMBO J. , vol.20 , pp. 3631-3637
    • Van Roey, P.1    Waddling, C.A.2    Fox, K.M.3    Belfort, M.4    Derbyshire, V.5
  • 18
    • 0033529716 scopus 로고    scopus 로고
    • Structure of the DNA repair enzyme endonuclease IV and its DNA complex: Double-nucleotide flipping at abasic sites and three-metal-ion catalysis
    • Hosfield D.J., Guan Y., Haas B.J., Cunningham R.P., Tainer J.A. Structure of the DNA repair enzyme endonuclease IV and its DNA complex: double-nucleotide flipping at abasic sites and three-metal-ion catalysis. Cell. 98:1999;397-408.
    • (1999) Cell , vol.98 , pp. 397-408
    • Hosfield, D.J.1    Guan, Y.2    Haas, B.J.3    Cunningham, R.P.4    Tainer, J.A.5
  • 19
    • 0023769378 scopus 로고
    • The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain
    • Freedman L.P., Luisi B.F., Korszun Z.R., Basavappa R., Sigler P.B., Yamamoto K.R. The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain. Nature. 334:1988;543-546.
    • (1988) Nature , vol.334 , pp. 543-546
    • Freedman, L.P.1    Luisi, B.F.2    Korszun, Z.R.3    Basavappa, R.4    Sigler, P.B.5    Yamamoto, K.R.6
  • 20
    • 0025780755 scopus 로고
    • Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
    • Luisi B.F., Xu W.X., Otwinowski Z., Freedman L.P., Yamamoto K.R., Sigler P.B. Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature. 352:1991;497-505.
    • (1991) Nature , vol.352 , pp. 497-505
    • Luisi, B.F.1    Xu, W.X.2    Otwinowski, Z.3    Freedman, L.P.4    Yamamoto, K.R.5    Sigler, P.B.6
  • 22
    • 0027531860 scopus 로고
    • A PCR-based strategy for extensive mutagenesis of a target DNA sequence
    • Morrison H.G., Desrosiers R.C. A PCR-based strategy for extensive mutagenesis of a target DNA sequence. Biotechniques. 14:1993;454-457.
    • (1993) Biotechniques , vol.14 , pp. 454-457
    • Morrison, H.G.1    Desrosiers, R.C.2
  • 25
    • 0032370284 scopus 로고    scopus 로고
    • WinXAS: A program for X-ray absorption data analysis under MS-Windows
    • Ressler T. WinXAS: a program for X-ray absorption data analysis under MS-Windows. J. Synchrotron Rad. 5:1998;118-122.
    • (1998) J. Synchrotron Rad. , vol.5 , pp. 118-122
    • Ressler, T.1
  • 27
    • 11844260365 scopus 로고
    • High-order multiple-scattering calculations of X-ray-absorption fine structure
    • Rehr J.J., Albers R.C., Zabinsky S.I. High-order multiple-scattering calculations of X-ray-absorption fine structure. Phys. Rev. Letters. 69:1992;3397-3400.
    • (1992) Phys. Rev. Letters , vol.69 , pp. 3397-3400
    • Rehr, J.J.1    Albers, R.C.2    Zabinsky, S.I.3
  • 28
    • 0025773296 scopus 로고
    • Zinc finger-DNA recognition: Crystal structure of a Zif268-DNA complex at 2.1 Å
    • Pavletich N.P., Pabo C.O. Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 Å Science. 252:1991;809-817.
    • (1991) Science , vol.252 , pp. 809-817
    • Pavletich, N.P.1    Pabo, C.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.