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Volumn 48, Issue 21, 2009, Pages 4431-4439

The tandem zinc-finger region of human ZHX adopts a novel C2H2 zinc finger structure with a C-terminal extension

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION DOMAIN; C-TERMINAL EXTENSIONS; HISTIDINE RESIDUES; HOMOLOGOUS PROTEINS; HOMOLOGY MODELS; MUTUAL ORIENTATION; NUCLEAR FACTORS; NUCLEOSOME; SECONDARY STRUCTURE PREDICTION; SEQUENCE CONSERVATION; SINGLE DOMAINS; SOLUTION STRUCTURES; STRUCTURAL FEATURE; SURFACE CHARACTERISTICS; TRANSCRIPTION REGULATIONS; ZINC FINGER STRUCTURE; ZINC IONS;

EID: 66349117961     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9001997     Document Type: Article
Times cited : (11)

References (59)
  • 1
    • 0025278259 scopus 로고
    • Weight matrix descriptions of four eukaryotic RNA polymerase II promoter elements derived from 502 unrelated promoter sequences
    • Bucher, P. (1990) Weight matrix descriptions of four eukaryotic RNA polymerase II promoter elements derived from 502 unrelated promoter sequences. J. Mol. Biol. 212, 563-578.
    • (1990) J. Mol. Biol. , vol.212 , pp. 563-578
    • Bucher, P.1
  • 2
    • 0032030308 scopus 로고    scopus 로고
    • A survey of 178 NF-Y binding CCAAT boxes
    • DOI 10.1093/nar/26.5.1135
    • Mantovani, R. (1998) A survey of 178 NF-Y binding CCAAT boxes. Nucleic Acids Res. 26, 1135-1143. (Pubitemid 28291681)
    • (1998) Nucleic Acids Research , vol.26 , Issue.5 , pp. 1135-1143
    • Mantovani, R.1
  • 3
    • 0032851812 scopus 로고    scopus 로고
    • The molecular biology of the CCAAT-binding factor NF-Y
    • DOI 10.1016/S0378-1119(99)00368-6, PII S0378111999003686
    • Mantovani, R. (1999) The molecular biology of the CCAAT-binding factor NF-Y. Gene 239, 15-27. (Pubitemid 29462565)
    • (1999) Gene , vol.239 , Issue.1 , pp. 15-27
    • Mantovani, R.1
  • 4
    • 0029127222 scopus 로고
    • A variety of DNA-binding and multimeric proteins contain the histone fold motif
    • Baxevanis, A. D., Arents, G., Moudrianakis, E. N., and Landsman, D. (1995) A variety of DNA-binding and multimeric proteins contain the histone fold motif. Nucleic Acids Res. 23, 2685-2691.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2685-2691
    • Baxevanis, A.D.1    Arents, G.2    Moudrianakis, E.N.3    Landsman, D.4
  • 8
    • 0038343841 scopus 로고    scopus 로고
    • Analysis of zinc-fingers and homeoboxes (ZHX)-1-interacting proteins: Molecular cloning and characterization of a member of the ZHX family, ZHX3
    • Yamada, K., Kawata, H., Shou, Z., Hirano, S., Mizutani, T., Yazawa, T., Sekiguchi, T., Yoshino, M., Kajitani, T., and Miyamoto, K. (2003) Analysis of zinc-fingers and homeoboxes (ZHX)-1-interacting proteins: molecular cloning and characterization of a member of the ZHX family, ZHX3. Biochem. J. 373, 167-178.
    • (2003) Biochem. J. , vol.373 , pp. 167-178
    • Yamada, K.1    Kawata, H.2    Shou, Z.3    Hirano, S.4    Mizutani, T.5    Yazawa, T.6    Sekiguchi, T.7    Yoshino, M.8    Kajitani, T.9    Miyamoto, K.10
  • 9
    • 0344628550 scopus 로고    scopus 로고
    • The mouse zinc-fingers and homeoboxes (ZHX) family; ZHX2 forms a heterodimer with ZHX3
    • Kawata, H., Yamada, K., Shou, Z., Mizutani, T., and Miyamoto, K. (2003) The mouse zinc-fingers and homeoboxes (ZHX) family; ZHX2 forms a heterodimer with ZHX3. Gene 323, 133-140.
    • (2003) Gene , vol.323 , pp. 133-140
    • Kawata, H.1    Yamada, K.2    Shou, Z.3    Mizutani, T.4    Miyamoto, K.5
  • 10
    • 33845998580 scopus 로고    scopus 로고
    • ZHX proteins regulate podocyte gene expression during the development of nephrotic syndrome
    • Liu, G., Clement, L. C., Kanwar,Y. S., Avila-Casado, C., and Chugh, S. S. (2006) ZHX proteins regulate podocyte gene expression during the development of nephrotic syndrome. J. Biol. Chem. 281, 39681-39692.
    • (2006) J. Biol. Chem. , vol.281 , pp. 39681-39692
    • Liu, G.1    Clement, L.C.2    Kanwar, Y.S.3    Avila-Casado, C.4    Chugh, S.S.5
  • 11
    • 34247361596 scopus 로고    scopus 로고
    • Transcriptional regulation of podocyte disease
    • Chugh, S. S. (2007) Transcriptional regulation of podocyte disease. Transl. Res. 149, 237-242.
    • (2007) Transl. Res. , vol.149 , pp. 237-242
    • Chugh, S.S.1
  • 14
    • 20744437001 scopus 로고    scopus 로고
    • RONN: The bio-basis function neural network technique applied to the detection of natively disordered regions in proteins
    • DOI 10.1093/bioinformatics/bti534
    • Yang, Z. R., Thomson, R., McNeil, P., and Esnouf, R. M. (2005) RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins. Bioinformatics 21, 3369-3376. (Pubitemid 41222441)
    • (2005) Bioinformatics , vol.21 , Issue.16 , pp. 3369-3376
    • Yang, Z.R.1    Thomson, R.2    McNeil, P.3    Esnouf, R.M.4
  • 16
    • 0344688165 scopus 로고    scopus 로고
    • Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region
    • DOI 10.1016/S0888-7543(03)00235-0
    • Lehner, B., Semple, J. I., Brown, S. E., Counsell, D., Campbell, D., and Sanderson, C. M. (2004) Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region. Genomics 83, 153-167. (Pubitemid 37518270)
    • (2004) Genomics , vol.83 , Issue.1 , pp. 153-167
    • Lehner, B.1    Semple, J.I.2    Brown, S.E.3    Counsell, D.4    Campbell, R.D.5    Sanderson, C.M.6
  • 18
    • 34249824605 scopus 로고    scopus 로고
    • BS69, a corepressor interacting with ZHX1, is a bifunctional transcription factor
    • Ogata-Kawata, H., Yamada, K., Uesaka-Yoshino, M., Kagawa, N., and Miyamoto, K. (2007) BS69, a corepressor interacting with ZHX1, is a bifunctional transcription factor. Front. Biosci. 12, 1911-1926.
    • (2007) Front. Biosci. , vol.12 , pp. 1911-1926
    • Ogata-Kawata, H.1    Yamada, K.2    Uesaka-Yoshino, M.3    Kagawa, N.4    Miyamoto, K.5
  • 19
    • 33745223494 scopus 로고    scopus 로고
    • New insights into BS69 functions
    • Velasco, G., Grkovic, S., and Ansieau, S. (2006) New insights into BS69 functions. J. Biol. Chem. 281, 16546-16550.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16546-16550
    • Velasco, G.1    Grkovic, S.2    Ansieau, S.3
  • 20
    • 3543148406 scopus 로고    scopus 로고
    • Expression screening, protein purification and NMR analysis of human protein domains for structural genomics
    • Folkers, G. E., van Buuren, B. N., and Kaptein, R. (2004) Expression screening, protein purification and NMR analysis of human protein domains for structural genomics. J. Struct. Funct. Genomics 5, 119-131.
    • (2004) J. Struct. Funct. Genomics , vol.5 , pp. 119-131
    • Folkers, G.E.1    Van Buuren, B.N.2    Kaptein, R.3
  • 21
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 22
    • 0004040543 scopus 로고    scopus 로고
    • University of California, San Francisco, CA
    • Goddard, T. D., and Kneller, D. G., SPARKY 3, University of California, San Francisco, CA.
    • SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 24
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • DOI 10.1023/A:1008392405740
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302. (Pubitemid 29143535)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 25
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert, P., Mumenthaler, C., and Wüthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273, 283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 26
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T., Güntert, P., and Wüthrich, K. (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319, 209-227.
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 28
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 29
    • 0030047142 scopus 로고    scopus 로고
    • Errors in protein structures [3]
    • Hooft, R. W. W., Vriend, G., Sander, C., and Abola, E. E. (1996) Errors in protein structures. Nature (London) 381, 272-1272 (Pubitemid 26000124)
    • (1996) Nature , vol.381 , Issue.6580 , pp. 272
    • Hooft, R.W.W.1    Vriend, G.2    Sander, C.3    Abola, E.E.4
  • 32
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 51-55; 29-32. (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 36
    • 4544348855 scopus 로고    scopus 로고
    • Zinc Finger Proteins
    • (Bertini, I., Sigel, A., and Sigel, H., Eds.) M. Dekker, New York
    • Folkers, G. E., Hanzawa, H., and Boelens, R. (2001) Zinc Finger Proteins, in Handbook on Metalloproteins (Bertini, I., Sigel, A., and Sigel, H., Eds.) pp 961-1000, M. Dekker, New York.
    • (2001) Handbook on Metalloproteins , pp. 961-1000
    • Folkers, G.E.1    Hanzawa, H.2    Boelens, R.3
  • 38
    • 4143051195 scopus 로고    scopus 로고
    • Comparison of site-specific rate-inference methods: Bayesian methods are superior
    • Mayrose, I., Graur, D., Ben-Tal, N., and Pupko, T. (2004) Comparison of site-specific rate-inference methods: Bayesian methods are superior. Mol. Biol. Evol. 21, 1781-1791.
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 1781-1791
    • Mayrose, I.1    Graur, D.2    Ben-Tal, N.3    Pupko, T.4
  • 39
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • DOI 10.1093/nar/25.17.3389
    • Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J. (1997) Gapped BLAST and PSIBLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402. (Pubitemid 27359211)
    • (1997) Nucleic Acids Research , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 40
    • 0035878724 scopus 로고    scopus 로고
    • Improving the accuracy of PSI-BLAST protein database searches with composition-based statistics and other refinements
    • Schäffer, A. A., Aravind, L., Madden, T. L., Shavirin, S., Spouge, J. L.,Wolf,Y. I.,Koonin, E. V., and Altschul, S.F. (2001) Improving the accuracy of PSI-BLAST protein database searches with composition-based statistics and other refinements. Nucleic Acids Res. 29, 2994-3005. (Pubitemid 32685225)
    • (2001) Nucleic Acids Research , vol.29 , Issue.14 , pp. 2994-3005
    • Schaffer, A.A.1    Aravind, L.2    Madden, T.L.3    Shavirin, S.4    Spouge, J.L.5    Wolf, Y.I.6    Koonin, E.V.7    Altschul, S.F.8
  • 42
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E., and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr., Sect. D 60, 2256-2268.
    • (2004) Acta Crystallogr., Sect. , vol.D 60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 44
    • 0026684669 scopus 로고
    • High-resolution solution structure of the double Cys2His2 zinc fingers from the human enhancer binding protein MBP-1
    • Omichinski, J. G., Clore, G. M., Robien, M., Sakaguchi, K., Appella, E., and Gronenborn, A. M. (1992) High-resolution solution structure of the double Cys2His2 zinc fingers from the human enhancer binding protein MBP-1. Biochemistry 31, 3907-3917.
    • (1992) Biochemistry , vol.31 , pp. 3907-3917
    • Omichinski, J.G.1    Clore, G.M.2    Robien, M.3    Sakaguchi, K.4    Appella, E.5    Gronenborn, A.M.6
  • 45
    • 33644828992 scopus 로고    scopus 로고
    • Solution structure of a Zap1 zinc-responsive domain provides insights into metalloregulatory Transcriptional Repression in Saccharomyces cerevisiae
    • Wang, Z., Feng, L. S., Matskevich, V., Venkataraman, K., Parasuram, P., and Laity, J. H. (2006) Solution structure of a Zap1 zinc-responsive domain provides insights into metalloregulatory Transcriptional Repression in Saccharomyces cerevisiae. J. Mol. Biol. 357, 1167-1183.
    • (2006) J. Mol. Biol. , vol.357 , pp. 1167-1183
    • Wang, Z.1    Feng, L.S.2    Matskevich, V.3    Venkataraman, K.4    Parasuram, P.5    Laity, J.H.6
  • 46
    • 0027423758 scopus 로고
    • Crystal structure of a five-finger GLI-DNA complex: New perspectives on zinc fingers
    • Pavletich, N. P., and Pabo, C. O. (1993) Crystal structure of a five-finger GLI-DNA complex: new perspectives on zinc fingers. Science 261, 1701-1707. (Pubitemid 23332917)
    • (1993) Science , vol.261 , Issue.5129 , pp. 1701-1707
    • Pavletich, N.P.1    Pabo, C.O.2
  • 47
    • 0032539846 scopus 로고    scopus 로고
    • Differing roles for zinc fingers in DNA recognition: Structure of a six-finger transcription factor IIIA complex
    • Nolte, R. T., Conlin, R. M., Harrison, S. C., and Brown, R. S. (1998) Differing roles for zinc fingers in DNA recognition: structure of a six-finger transcription factor IIIA complex. Proc. Natl. Acad. Sci. U.S. A. 95, 2938-2943.
    • (1998) Proc. Natl. Acad. Sci. U.S. A. , vol.95 , pp. 2938-2943
    • Nolte, R.T.1    Conlin, R.M.2    Harrison, S.C.3    Brown, R.S.4
  • 48
    • 0025773296 scopus 로고
    • Zinc finger-DNA recognition: Crystal structure of a Zif268-DNA complex at 2.1 Å
    • Pavletich, N. P., and Pabo, C. O. (1991) Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 Å. Science 252, 809-817. (Pubitemid 121000517)
    • (1991) Science , vol.252 , Issue.5007 , pp. 809-817
    • Pavletich, N.P.1    Pabo, C.O.2
  • 49
    • 0030587774 scopus 로고    scopus 로고
    • Zif268 protein-DNAcomplex refined at 1.6Å: Amodel systemfor understanding zinc finger-DNA interactions
    • Elrod-Erickson, M., Rould, M. A., Nekludova, L., and Pabo, C. O. (1996) Zif268 protein-DNAcomplex refined at 1.6Å: amodel systemfor understanding zinc finger-DNA interactions. Structure 4, 1171-1180.
    • (1996) Structure , vol.4 , pp. 1171-1180
    • Elrod-Erickson, M.1    Rould, M.A.2    Nekludova, L.3    Pabo, C.O.4
  • 50
    • 0027222793 scopus 로고
    • Structure of the retinoid X receptor alpha DNA binding domain: A helix required for homodimeric DNA binding
    • Lee, M. S., Kliewer, S. A., Provencal, J., Wright, P. E., and Evans, R. M. (1993) Structure of the retinoid X receptor alpha DNA binding domain: a helix required for homodimeric DNA binding. Science 260, 1117-1121. (Pubitemid 23186785)
    • (1993) Science , vol.260 , Issue.5111 , pp. 1117-1121
    • Lee, M.S.1    Kliewer, S.A.2    Provencal, J.3    Wright, P.E.4    Evans, R.M.5
  • 51
    • 0028313996 scopus 로고
    • The dimerization interfaces formed between the DNA binding domains of RXR, RAR and TR determine the binding specificity and polarity of the full-length receptors to direct repeats
    • Zechel, C., Shen, X. Q., Chen, J. Y., Chen, Z. P., Chambon, P., and Gronemeyer, H. (1994) The dimerization interfaces formed between the DNA binding domains of RXR, RAR and TR determine the binding specificity and polarity of the full-length receptors to direct repeats. EMBO J. 13, 1425-1433.
    • (1994) EMBO J. , vol.13 , pp. 1425-1433
    • Zechel, C.1    Shen, X.Q.2    Chen, J.Y.3    Chen, Z.P.4    Chambon, P.5    Gronemeyer, H.6
  • 53
    • 39549098666 scopus 로고    scopus 로고
    • The solution structure of ZNF593 from Homo sapiens reveals a zinc finger in a predominantly unstructured protein
    • Hayes, P. L.,Lytle,B.L.,Volkman, B.F., and Peterson,F.C. (2008)The solution structure of ZNF593 from Homo sapiens reveals a zinc finger in a predominantly unstructured protein. Protein Sci. 17, 571-576.
    • (2008) Protein Sci. , vol.17 , pp. 571-576
    • Hayes, P.L.1    Lytle, B.L.2    Volkman, B.F.3    Peterson, F.C.4
  • 54
    • 23444460429 scopus 로고    scopus 로고
    • Solution structure of the N-terminal zinc fingers of the Xenopus laevis double-stranded RNA-binding protein ZFa
    • Möller, H. M., Martinez-Yamout, M. A., Dyson, H. J., and Wright, P. E. (2005) Solution structure of the N-terminal zinc fingers of the Xenopus laevis double-stranded RNA-binding protein ZFa. J. Mol. Biol. 351, 718-730.
    • (2005) J. Mol. Biol. , vol.351 , pp. 718-730
    • Möller, H.M.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 55
    • 0030585197 scopus 로고    scopus 로고
    • The solution structure of the first zinc finger domain of SW15: A novel structural extension to a common fold
    • Dutnall, R. N., Neuhaus, D., and Rhodes, D. (1996) The solution structure of the first zinc finger domain of SWI5: a novel structural extension to a common fold. Structure 4, 599-611. (Pubitemid 126657552)
    • (1996) Structure , vol.4 , Issue.5 , pp. 599-611
    • Dutnall, R.N.1    Neuhaus, D.2    Rhodes, D.3
  • 56
    • 0027749348 scopus 로고
    • The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition
    • DOI 10.1038/366483a0
    • Fairall, L., Schwabe, J. W., Chapman, L., Finch, J. T., and Rhodes, D. (1993) The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition. Nature (London) 366, 483-487 (Pubitemid 24013885)
    • (1993) Nature , vol.366 , Issue.6454 , pp. 483-487
    • Fairall, L.1    Schwabe, J.W.R.2    Chapman, L.3    Finch, J.T.4    Rhodes, D.5
  • 57
    • 22544441094 scopus 로고    scopus 로고
    • ProFunc: A server for predicting protein function from 3D structure
    • DOI 10.1093/nar/gki414
    • Laskowski, R. A., Watson, J. D., and Thornton, J. M. (2005) ProFunc: a server for predicting protein function from 3D structure. Nucleic Acids Res. 33(Web Server issue), W89-W93. (Pubitemid 44529886)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISS
    • Laskowski, R.A.1    Watson, J.D.2    Thornton, J.M.3
  • 58
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • DOI 10.1093/nar/26.1.316
    • Holm, L., and Sander, C. (1998) Touring protein fold space with Dali/FSSP. Nucleic Acids Res. 26, 316-319. (Pubitemid 28291549)
    • (1998) Nucleic Acids Research , vol.26 , Issue.1 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 59
    • 0028109545 scopus 로고
    • Three-dimensional solution structure of an immunoglobulin light chain-binding domain of Protein L. Comparison with the IgG-binding domains of Protein G
    • Wikström, M., Drakenberg, T., Forsén, S., Sjöbring, U.and Björck, L. (1994) Three-dimensional solution structure of an immunoglobulin light chain-binding domain of Protein L. Comparison with the IgG-binding domains of Protein G. Biochemistry 33, 14011-21417
    • (1994) Biochemistry , vol.33 , pp. 14011-21417
    • Wikström, M.1    Drakenberg, T.2    Forsén, S.3    Sjöbring, U.4    Björck, L.5


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