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Volumn 31, Issue 12, 2013, Pages 1467-1480

Understanding the role of domain-domain linkers in the spatial orientation of domains in multi-domain proteins

Author keywords

Inter domain linkers; Inter domain orientation; Interface constraints; Linker flexibility; Multi domain proteins

Indexed keywords

PROTEIN;

EID: 84887004419     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2012.743438     Document Type: Article
Times cited : (31)

References (75)
  • 2
    • 0028577684 scopus 로고
    • Conservation of polyproline II helices in homologous proteins: Implications for structure prediction by model building
    • Adzhubei, A. A., & Sternberg, M. J. (1994). Conservation of polyproline II helices in homologous proteins: Implications for structure prediction by model building. Protein Science, 3, 2395-2410.
    • (1994) Protein Science , vol.3 , pp. 2395-2410
    • Adzhubei, A.A.1    Sternberg, M.J.2
  • 3
    • 0008515583 scopus 로고
    • Automated conformational analysis from crystallographic data 4. Statistical descriptors for torsion angles
    • Allen, F. H., & Johnson, O. (1991). Automated conformational analysis from crystallographic data. 4. Statistical descriptors for torsion angles. Acta Crystallographica. Section B, Structural Science, 47, 62-67.
    • (1991) Acta Crystallographica. Section B, Structural Science , vol.47 , pp. 62-67
    • Allen, F.H.1    Johnson, O.2
  • 4
    • 0028181138 scopus 로고
    • Modulation of the enzymatic activity of papain by interdomain residues remote from the active site
    • Altschuh, D., Tessier, D. C., & Vernet, T. (1994). Modulation of the enzymatic activity of papain by interdomain residues remote from the active site. Protein Engineering, 7, 769-775. (Pubitemid 24188431)
    • (1994) Protein Engineering , vol.7 , Issue.6 , pp. 769-775
    • Altschuh, D.1    Tessier, D.C.2    Vernet, T.3
  • 5
    • 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., & Lipman, D. J. (1997). Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Research, 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
  • 6
    • 0034788744 scopus 로고    scopus 로고
    • Design of the linkers which effectively separate domains of a bifunctional fusion protein
    • Arai, R., Ueda, H., Kitayama, A., Kamiya, N., & Nagamune, T. (2001). Design of the linkers which effectively separate domains of a bifunctional fusion protein. Protein Engineering, 14, 529-532. (Pubitemid 32959476)
    • (2001) Protein Engineering , vol.14 , Issue.8 , pp. 529-532
    • Arai, R.1    Ueda, H.2    Kitayama, A.3    Kamiya, N.4    Nagamune, T.5
  • 7
    • 0032766134 scopus 로고    scopus 로고
    • The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins
    • DOI 10.1016/S0378-1097(99)00197-4, PII S0378109799001974
    • Aravind, L., & Ponting, C. P. (1999). The cytoplasmic helical linker domain of receptor histidine kinase and methylaccepting proteins is common to many prokaryotic signalling proteins. FEMS Microbiology Letters, 176, 111-116. (Pubitemid 29324608)
    • (1999) FEMS Microbiology Letters , vol.176 , Issue.1 , pp. 111-116
    • Aravind, L.1    Ponting, C.P.2
  • 8
    • 0036307754 scopus 로고    scopus 로고
    • The geometry of domain combination in proteins
    • DOI 10.1006/jmbi.2001.5288
    • Bashton, M., & Chothia, C. (2002). The geometry of domain combination in proteins. Journal of Molecular Biology, 315, 927-939. (Pubitemid 34729337)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.4 , pp. 927-939
    • Bashton, M.1    Chothia, C.2
  • 10
    • 0028077639 scopus 로고
    • Refined structure of monomeric diphtheria toxin at 2.3 A resolution
    • Bennett, M. J., & Eisenberg, D. (1994). Refined structure of monomeric diphtheria toxin at 2.3 A resolution. Protein Science, 3, 1464-1475. (Pubitemid 24314465)
    • (1994) Protein Science , vol.3 , Issue.9 , pp. 1464-1475
    • Bennett, M.J.1    Eisenberg, D.2
  • 11
    • 57749200715 scopus 로고    scopus 로고
    • Analyzing the sequence-structure relationship of a library of local structural prototypes
    • Benros, C., de Brevern, A. G., & Hazout, S. (2009). Analyzing the sequence-structure relationship of a library of local structural prototypes. Journal of Theoretical Biology, 256, 215-226.
    • (2009) Journal of Theoretical Biology , vol.256 , pp. 215-226
    • Benros, C.1    De Brevern, A.G.2    Hazout, S.3
  • 12
    • 0037542601 scopus 로고    scopus 로고
    • Discrete structure of van der Waals domains in globular proteins
    • Berezovsky, I. N. (2003). Discrete structure of van der Waals domains in globular proteins. Protein Engineering, 16, 161-167. (Pubitemid 36565630)
    • (2003) Protein Engineering , vol.16 , Issue.3 , pp. 161-167
    • Berezovsky, I.N.1
  • 13
    • 0034101680 scopus 로고    scopus 로고
    • Hierarchy of regions of amino acid sequence with respect to their role in the protein spatial structure
    • DOI 10.1089/10665270050081450
    • Berezovsky, I. N., Esipova, N. G., & Tumanyan, V. G. (2000). Hierarchy of regions of amino acid sequence with respect to their role in the protein spatial structure. Journal of Computational Biology, 7, 183-192. (Pubitemid 30412168)
    • (2000) Journal of Computational Biology , vol.7 , Issue.1-2 , pp. 183-192
    • Berezovsky, I.N.1    Esipova, N.G.2    Tumanyan, V.G.3
  • 14
    • 0033972919 scopus 로고    scopus 로고
    • Closed loops of nearly standard size: Common basic element of protein structure
    • DOI 10.1016/S0014-5793(00)01091-7, PII S0014579300010917
    • Berezovsky, I. N., Grosberg, A. Y., & Trifonov, E. N. (2000). Closed loops of nearly standard size: Common basic element of protein structure. FEBS Letters, 466, 283-286. (Pubitemid 30069842)
    • (2000) FEBS Letters , vol.466 , Issue.2-3 , pp. 283-286
    • Berezovsky, I.N.1    Grosberg, A.Y.2    Trifonov, E.N.3
  • 16
    • 0032845660 scopus 로고    scopus 로고
    • Hierarchy of the interaction energy distribution in the spatial structure of globular proteins and the problem of domain definition
    • Berezovsky, I. N., Namiot, V. A., Tumanyan, V. G., & Esipova, N. G. (1999). Hierarchy of the interaction energy distribution in the spatial structure of globular proteins and the problem of domain definition. Journal of Biomolecular Structure & Dynamics, 17, 133-155. (Pubitemid 29439458)
    • (1999) Journal of Biomolecular Structure and Dynamics , vol.17 , Issue.1 , pp. 133-155
    • Berezovsky, I.N.1    Namiot, V.A.2    Tumanyan, V.G.3    Esipova, N.G.4
  • 17
    • 0035853276 scopus 로고    scopus 로고
    • Van der Waals locks: Loop-n-lock structure of globular proteins
    • DOI 10.1006/jmbi.2001.4554
    • Berezovsky, I. N., & Trifonov, E. N. (2001). Van der Waals locks: Loop-n-lock structure of globular proteins. Journal of Molecular Biology, 307, 1419-1426. (Pubitemid 33027650)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.5 , pp. 1419-1426
    • Berezovsky, I.N.1    Trifonov, E.N.2
  • 18
    • 84857982668 scopus 로고    scopus 로고
    • The protein data bank at 40: Reflecting on the past to prepare for the future
    • Berman, H. M., Kleywegt, G. J., Nakamura, H., & Markley, J. L. (2012). The protein data bank at 40: Reflecting on the past to prepare for the future. Structure, 20, 391-396.
    • (2012) Structure , vol.20 , pp. 391-396
    • Berman, H.M.1    Kleywegt, G.J.2    Nakamura, H.3    Markley, J.L.4
  • 19
    • 84860170573 scopus 로고    scopus 로고
    • Stability of domain structures in multi-domain proteins
    • Bhaskara, R. M., & Srinivasan, N. (2011). Stability of domain structures in multi-domain proteins. Scientific Reports, 1, 40.
    • (2011) Scientific Reports , Issue.1 , pp. 40
    • Bhaskara, R.M.1    Srinivasan, N.2
  • 21
    • 84862682035 scopus 로고    scopus 로고
    • Combined bottom-up and top-down mass spectrometry analyses of the pattern of post-translational modifications of Drosophila melanogaster linker histone H1
    • Bonet-Costa, C., Vilaseca, M., Diema, C., Vujatovic, O., Vaquero, A., Omenaca, N., ? Azorin, F. (2012). Combined bottom-up and top-down mass spectrometry analyses of the pattern of post-translational modifications of Drosophila melanogaster linker histone H1. Journal of Proteomics, 75, 4124-4138.
    • (2012) Journal of Proteomics , vol.75 , pp. 4124-4138
    • Bonet-Costa, C.1    Vilaseca, M.2    Diema, C.3    Vujatovic, O.4    Vaquero, A.5    Omenaca, N.6    Azorin, F.7
  • 22
    • 0033543694 scopus 로고    scopus 로고
    • SH2-kinase linker mutations release Hck tyrosine kinase and transforming activities in Rat-2 fibroblasts
    • Briggs, S. D., & Smithgall, T. E. (1999). SH2-kinase linker mutations release Hck tyrosine kinase and transforming activities in Rat-2 fibroblasts. Journal of Biological Chemistry, 274, 26579-26583.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 26579-26583
    • Briggs, S.D.1    Smithgall, T.E.2
  • 23
    • 77956938868 scopus 로고    scopus 로고
    • DomSVR: Domain boundary prediction with support vector regression from sequence information alone
    • Chen, P., Liu, C., Burge, L., Li, J., Mohammad, M., Southerland, W., ? Wang, B. (2010). DomSVR: Domain boundary prediction with support vector regression from sequence information alone. Amino Acids, 39, 713-726.
    • (2010) Amino Acids , vol.39 , pp. 713-726
    • Chen, P.1    Liu, C.2    Burge, L.3    Li, J.4    Mohammad, M.5    Southerland, W.6    Wang, B.7
  • 24
    • 67349171544 scopus 로고    scopus 로고
    • Impact of linker strain and flexibility in the design of a fragment-based inhibitor
    • Chung, S., Parker, J. B., Bianchet, M., Amzel, L. M., & Stivers, J. T. (2009). Impact of linker strain and flexibility in the design of a fragment-based inhibitor. Nature Chemical Biology, 5, 407-413.
    • (2009) Nature Chemical Biology , vol.5 , pp. 407-413
    • Chung, S.1    Parker, J.B.2    Bianchet, M.3    Amzel, L.M.4    Stivers, J.T.5
  • 25
    • 84860833500 scopus 로고    scopus 로고
    • Reorganizing the protein space at the universal protein resource (uniprot)
    • Consortium
    • Consortium (2012). Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucleic Acids Research, 40, D71-D75.
    • (2012) Nucleic Acids Research , vol.40
  • 26
    • 23144437382 scopus 로고    scopus 로고
    • New assessment of a structural alphabet
    • de Brevern, A. G. (2005). New assessment of a structural alphabet. In Silico Biology, 5, 283-289.
    • (2005) Silico Biology , vol.5 , pp. 283-289
    • De Brevern, A.G.1
  • 27
    • 0034669774 scopus 로고    scopus 로고
    • Bayesian probabilistic approach for predicting backbone structures in terms of protein blocks
    • de Brevern, A. G., Etchebest, C., & Hazout, S. (2000). Bayesian probabilistic approach for predicting backbone structures in terms of protein blocks. Proteins, 41, 271-287.
    • (2000) Proteins , vol.41 , pp. 271-287
    • De Brevern, A.G.1    Etchebest, C.2    Hazout, S.3
  • 28
    • 0036893073 scopus 로고    scopus 로고
    • Extension of a local backbone description using a structural alphabet: A new approach to the sequence-structure relationship
    • DOI 10.1110/ps.0220502
    • de Brevern, A. G., Valadie, H., Hazout, S., & Etchebest, C. (2002). Extension of a local backbone description using a structural alphabet: A new approach to the sequence-structure relationship. Protein Science, 11, 2871-2886. (Pubitemid 35365253)
    • (2002) Protein Science , vol.11 , Issue.12 , pp. 2871-2886
    • De Brevern, A.G.1    Valadie, H.2    Hazout, S.3    Etchebest, C.4
  • 30
    • 33645879534 scopus 로고    scopus 로고
    • Domain boundary prediction based on profile domain linker propensity index
    • Dong, Q., Wang, X., Lin, L., & Xu, Z. (2006). Domain boundary prediction based on profile domain linker propensity index. Computational Biology and Chemistry, 30, 127-133.
    • (2006) Computational Biology and Chemistry , vol.30 , pp. 127-133
    • Dong, Q.1    Wang, X.2    Lin, L.3    Xu, Z.4
  • 32
    • 21744461895 scopus 로고    scopus 로고
    • Armadillo: Domain boundary prediction by amino acid composition
    • DOI 10.1016/j.jmb.2005.05.037, PII S0022283605005802
    • Dumontier, M., Yao, R., Feldman, H. J., & Hogue, C. W. (2005). Armadillo: Domain boundary prediction by amino acid composition. Journal of Molecular Biology, 350, 1061-1073. (Pubitemid 40943462)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.5 , pp. 1061-1073
    • Dumontier, M.1    Yao, R.2    Feldman, H.J.3    Hogue, C.W.V.4
  • 33
    • 60149103898 scopus 로고    scopus 로고
    • Loop-length-dependent SVM prediction of domain linkers for high-throughput structural proteomics
    • Ebina, T., Toh, H., & Kuroda, Y. (2009). Loop-length-dependent SVM prediction of domain linkers for high-throughput structural proteomics. Biopolymers, 92, 1-8.
    • (2009) Biopolymers , vol.92 , pp. 1-8
    • Ebina, T.1    Toh, H.2    Kuroda, Y.3
  • 34
    • 79351469227 scopus 로고    scopus 로고
    • DoBo: Protein domain boundary prediction by integrating evolutionary signals and machine learning
    • Eickholt, J., Deng, X., & Cheng, J. (2011). DoBo: Protein domain boundary prediction by integrating evolutionary signals and machine learning. BMC Bioinformatics, 12, 43.
    • (2011) BMC Bioinformatics , vol.12 , pp. 43
    • Eickholt, J.1    Deng, X.2    Cheng, J.3
  • 35
    • 74249108517 scopus 로고    scopus 로고
    • Assessment of domain boundary predictions and the prediction of intramolecular contacts in CASP8
    • Ezkurdia, I., Grana, O., Izarzugaza, J. M., & Tress, M. L. (2009). Assessment of domain boundary predictions and the prediction of intramolecular contacts in CASP8. Proteins, 77(Suppl. 9), 196-209.
    • (2009) Proteins , vol.77 , Issue.SUPPL. 9 , pp. 196-209
    • Ezkurdia, I.1    Grana, O.2    Izarzugaza, J.M.3    Tress, M.L.4
  • 36
    • 0242290326 scopus 로고    scopus 로고
    • Single Mutation in the Linker Domain Confers Protein Flexibility and Camptothecin Resistance to Human Topoisomerase I
    • DOI 10.1074/jbc.M303899200
    • Fiorani, P., Bruselles, A., Falconi, M., Chillemi, G., Desideri, A., & Benedetti, P. (2003). Single mutation in the linker domain confers protein flexibility and camptothecin resistance to human topoisomerase I. Journal of Biological Chemistry, 278, 43268-43275. (Pubitemid 37345947)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.44 , pp. 43268-43275
    • Fiorani, P.1    Bruselles, A.2    Falconi, M.3    Chillemi, G.4    Desideri, A.5    Benedetti, P.6
  • 37
    • 2942541294 scopus 로고    scopus 로고
    • Use of a structural alphabet for analysis of short loops connecting repetitive structures
    • Fourrier, L., Benros, C., & de Brevern, A. G. (2004). Use of a structural alphabet for analysis of short loops connecting repetitive structures. BMC Bioinformatics, 5, 58.
    • (2004) BMC Bioinformatics , vol.5 , pp. 58
    • Fourrier, L.1    Benros, C.2    De Brevern, A.G.3
  • 38
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • DOI 10.1002/prot.340230412
    • Frishman, D., & Argos, P. (1995). Knowledge-based protein secondary structure assignment. Proteins, 23, 566-579. (Pubitemid 26009520)
    • (1995) Proteins: Structure, Function and Genetics , vol.23 , Issue.4 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 39
    • 77956502131 scopus 로고    scopus 로고
    • IAlign: A method for the structural comparison of protein-protein interfaces
    • Gao, M., & Skolnick, J. (2010). IAlign: A method for the structural comparison of protein-protein interfaces. Bioinformatics, 26, 2259-2265.
    • (2010) Bioinformatics , vol.26 , pp. 2259-2265
    • Gao, M.1    Skolnick, J.2
  • 40
    • 79959981766 scopus 로고    scopus 로고
    • IPBA: A tool for protein structure comparison using sequence alignment strategies
    • Gelly, J. C., Joseph, A. P., Srinivasan, N., & de Brevern, A. G. (2011). IPBA: A tool for protein structure comparison using sequence alignment strategies. Nucleic Acids Research, 39, W18-W23.
    • (2011) Nucleic Acids Research , vol.39
    • Gelly, J.C.1    Joseph, A.P.2    Srinivasan, N.3    De Brevern, A.G.4
  • 41
    • 0036878154 scopus 로고    scopus 로고
    • An analysis of protein domain linkers: Their classification and role in protein folding
    • George, R. A., & Heringa, J. (2002). An analysis of protein domain linkers: Their classification and role in protein folding. Protein Engineering, 15, 871-879. (Pubitemid 36172724)
    • (2002) Protein Engineering , vol.15 , Issue.11 , pp. 871-879
    • George, R.A.1    Heringa, J.2
  • 42
    • 0033574768 scopus 로고    scopus 로고
    • Dissecting and exploiting intermodular communication in polyketide synthases
    • DOI 10.1126/science.284.5413.482
    • Gokhale, R. S., Tsuji, S. Y., Cane, D. E., & Khosla, C. (1999). Dissecting and exploiting intermodular communication in polyketide synthases. Science, 284, 482-485. (Pubitemid 29289620)
    • (1999) Science , vol.284 , Issue.5413 , pp. 482-485
    • Gokhale, R.S.1    Tsuji, S.Y.2    Cane, D.E.3    Khosla, C.4
  • 43
    • 33646475098 scopus 로고    scopus 로고
    • Divergence of interdomain geometry in two-domain proteins
    • Han, J. H., Kerrison, N., Chothia, C., & Teichmann, S. A. (2006). Divergence of interdomain geometry in two-domain proteins. Structure, 14, 935-945.
    • (2006) Structure , vol.14 , pp. 935-945
    • Han, J.H.1    Kerrison, N.2    Chothia, C.3    Teichmann, S.A.4
  • 44
    • 66549119395 scopus 로고    scopus 로고
    • Advances and pitfalls of protein structural alignment
    • Hasegawa, H., & Holm, L. (2009). Advances and pitfalls of protein structural alignment. Current Opinion in Structural Biology, 19, 341-348.
    • (2009) Current Opinion in Structural Biology , vol.19 , pp. 341-348
    • Hasegawa, H.1    Holm, L.2
  • 45
    • 3242887525 scopus 로고    scopus 로고
    • STRIDE: A web server for secondary structure assignment from known atomic coordinates of proteins
    • DOI 10.1093/nar/gkh429
    • Heinig, M., & Frishman, D. (2004). STRIDE: A web server for secondary structure assignment from known atomic coordinates of proteins. Nucleic Acids Research, 32, W500-W502. (Pubitemid 38997383)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Heinig, M.1    Frishman, D.2
  • 46
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • DOI 10.1093/nar/26.1.316
    • Holm, L., & Sander, C. (1998). Touring protein fold space with Dali/FSSP. Nucleic Acids Research, 26, 316-319. (Pubitemid 28291549)
    • (1998) Nucleic Acids Research , vol.26 , Issue.1 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 47
    • 0032504192 scopus 로고    scopus 로고
    • A hinge at the central helix of the regulatory light chain of myosin is critical for phosphorylation-dependent regulation of smooth muscle myosin motor activity
    • DOI 10.1074/jbc.273.28.17702
    • Ikebe, M. Kambara, T., Stafford, W. F., Sata, M., Katayama, E., & Ikebe, R. (1998). A hinge at the central helix of the regulatory light chain of myosin is critical for phosphorylation-dependent regulation of smooth muscle myosin motor activity. Journal of Biological Chemistry, 273, 17702-17707. (Pubitemid 28355110)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.28 , pp. 17702-17707
    • Ikebe, M.1    Kambara, T.2    Stafford, W.F.3    Sata, M.4    Katayama, E.5    Ikebe, R.6
  • 49
    • 48449099769 scopus 로고    scopus 로고
    • Domain hierarchy and closed loops (DHcL): A server for exploring hierarchy of protein domain structure
    • Koczyk, G., & Berezovsky, I. N. (2008). Domain hierarchy and closed loops (DHcL): A server for exploring hierarchy of protein domain structure. Nucleic Acids Research, 36, W239-W245.
    • (2008) Nucleic Acids Research , vol.36
    • Koczyk, G.1    Berezovsky, I.N.2
  • 50
    • 16644363065 scopus 로고    scopus 로고
    • Delineation of modular proteins: Domain boundary prediction from sequence information
    • Kong, L., & Ranganathan, S. (2004). Delineation of modular proteins: Domain boundary prediction from sequence information. Brief Bioinformatics, 5, 179-192.
    • (2004) Brief Bioinformatics , vol.5 , pp. 179-192
    • Kong, L.1    Ranganathan, S.2
  • 51
    • 70349789244 scopus 로고    scopus 로고
    • Structural basis for autoregulation of the zinc transporter YiiP
    • Lu, M., Chai, J., & Fu, D. (2009). Structural basis for autoregulation of the zinc transporter YiiP. Nature Structural & Molecular Biology, 16, 1063-1067.
    • (2009) Nature Structural & Molecular Biology , vol.16 , pp. 1063-1067
    • Lu, M.1    Chai, J.2    Fu, D.3
  • 52
    • 0030020483 scopus 로고    scopus 로고
    • Expression of a bifunctional chimeric protein A-Vargula hilgendorfii luciferase in mammalian cells
    • Maeda, Y., Ueda, H., Hara, T., Kazami, J., Kawano, G., Suzuki, E., & Nagamune, T. (1996). Expression of a bifunctional chimeric protein A-Vargula hilgendorfii luciferase in mammalian cells. BioTechniques, 20, 116-121. (Pubitemid 26023336)
    • (1996) BioTechniques , vol.20 , Issue.1 , pp. 116-121
    • Maeda, Y.1    Ueda, H.2    Hara, T.3    Kazami, J.4    Kawano, G.5    Suzuki, E.6    Nagamune, T.7
  • 54
    • 57649134962 scopus 로고    scopus 로고
    • Bimodal recognition of DNA geometry by human topoisomerase II alpha: Preferential relaxation of positively supercoiled DNA requires elements in the C-terminal domain
    • McClendon, A. K., Gentry, A. C., Dickey, J. S., Brinch, M., Bendsen, S., Andersen, A. H., & Osheroff, N. (2008). Bimodal recognition of DNA geometry by human topoisomerase II alpha: Preferential relaxation of positively supercoiled DNA requires elements in the C-terminal domain. Biochemistry, 47, 13169-13178.
    • (2008) Biochemistry , vol.47 , pp. 13169-13178
    • McClendon, A.K.1    Gentry, A.C.2    Dickey, J.S.3    Brinch, M.4    Bendsen, S.5    Andersen, A.H.6    Osheroff, N.7
  • 55
    • 0000009443 scopus 로고
    • Rapid comparison of protein structures
    • McLaclan, A. D. (1982). Rapid comparison of protein structures. Acta Crystallographica, 38, 871-873.
    • (1982) Acta Crystallographica , vol.38 , pp. 871-873
    • McLaclan, A.D.1
  • 56
    • 33747099239 scopus 로고    scopus 로고
    • Identification of putative domain linkers by a neural network application to a large sequence database
    • Miyazaki, S., Kuroda, Y., & Yokoyama, S. (2006). Identification of putative domain linkers by a neural network application to a large sequence database. BMC Bioinformatics, 7, 323.
    • (2006) BMC Bioinformatics , vol.7 , pp. 323
    • Miyazaki, S.1    Kuroda, Y.2    Yokoyama, S.3
  • 57
    • 84861005184 scopus 로고    scopus 로고
    • Corresponding functional dynamics across the Hsp90 Chaperone family: Insights from a multiscale analysis of MD simulations
    • Morra, G., Potestio, R., Micheletti, C., & Colombo, G. (2012). Corresponding functional dynamics across the Hsp90 Chaperone family: Insights from a multiscale analysis of MD simulations. PLoS Computational Biology, 8, e1002433.
    • (2012) PLoS Computational Biology , vol.8
    • Morra, G.1    Potestio, R.2    Micheletti, C.3    Colombo, G.4
  • 58
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A. G., Brenner, S. E., Hubbard, T., & Chothia, C. (1995). SCOP: A structural classification of proteins database for the investigation of sequences and structures. Journal of Molecular Biology, 247, 536-540.
    • (1995) Journal of Molecular Biology , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 59
    • 84857418823 scopus 로고    scopus 로고
    • Effects of DNA binding of the zinc finger and linkers for domain fusion on the catalytic activity of sequence-specific chimeric recombinases determined by a facile fluorescent system
    • Nomura, W., Masuda, A., Ohba, K., Urabe, A., Ito, N., Ryo, A., ? Tamamura, H. (2012). Effects of DNA binding of the zinc finger and linkers for domain fusion on the catalytic activity of sequence-specific chimeric recombinases determined by a facile fluorescent system. Biochemistry, 51, 1510-1517.
    • (2012) Biochemistry , vol.51 , pp. 1510-1517
    • Nomura, W.1    Masuda, A.2    Ohba, K.3    Urabe, A.4    Ito, N.5    Ryo, A.6    Tamamura, H.7
  • 62
    • 0027156880 scopus 로고
    • Site-directed alterations to the geometry of the aspartate transcarbamoylase zinc domain: Selective alteration to regulation by heterotropic ligands, isoelectric point, and stability in urea
    • Strang, C. J., Wales, M. E., Brown, D. M., & Wild, J. R. (1993). Site-directed alterations to the geometry of the aspartate transcarbamoylase zinc domain: Selective alteration to regulation by heterotropic ligands, isoelectric point, and stability in urea. Biochemistry, 32, 4156-4167. (Pubitemid 23137720)
    • (1993) Biochemistry , vol.32 , Issue.16 , pp. 4156-4167
    • Strang, C.J.1    Wales, M.E.2    Brown, D.M.3    Wild, J.R.4
  • 63
    • 80855123725 scopus 로고    scopus 로고
    • Regulation of the susceptibility of HIV-1 to a neutralizing antibody KD-247 by nonepitope mutations distant from its epitope
    • Takizawa, M., Miyauchi, K., Urano, E., Kusagawa, S., Kitamura, K., Naganawa, S., ? Komano, J. (2011). Regulation of the susceptibility of HIV-1 to a neutralizing antibody KD-247 by nonepitope mutations distant from its epitope. AIDS, 25, 2209-2216.
    • (2011) AIDS , vol.25 , pp. 2209-2216
    • Takizawa, M.1    Miyauchi, K.2    Urano, E.3    Kusagawa, S.4    Kitamura, K.5    Naganawa, S.6    Komano, J.7
  • 64
    • 0029955258 scopus 로고    scopus 로고
    • Selection of linkers for a catalytic single-chain antibody using phage display technology
    • DOI 10.1074/jbc.271.26.15682
    • Tang, Y., Jiang, N., Parakh, C., & Hilvert, D. (1996). Selection of linkers for a catalytic single-chain antibody using phage display technology. Journal of Biological Chemistry, 271, 15682-15686. (Pubitemid 26225345)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.26 , pp. 15682-15686
    • Tang, Y.1    Jiang, N.2    Parakh, C.3    Hilvert, D.4
  • 65
    • 0023683585 scopus 로고
    • Enzymes of nucleotide metabolism: The significance of subunit size and polymer size for biological function and regulatory properties
    • Traut, T. W. (1988). Enzymes of nucleotide metabolism: The significance of subunit size and polymer size for biological function and regulatory properties. CRC Critical Reviews in Biochemistry, 23, 121-169.
    • (1988) CRC Critical Reviews in Biochemistry , vol.23 , pp. 121-169
    • Traut, T.W.1
  • 68
    • 0030937754 scopus 로고    scopus 로고
    • Linker length and composition influence the flexibility of Oct-1 DNA binding
    • DOI 10.1093/emboj/16.8.2043
    • van Leeuwen, H. C., Strating, M. J., Rensen, M., de Laat, W., & van der Vliet, P. C. (1997). Linker length and composition influence the flexibility of Oct-1 DNA binding. EMBO Journal, 16, 2043-2053. (Pubitemid 27170965)
    • (1997) EMBO Journal , vol.16 , Issue.8 , pp. 2043-2053
    • Van Leeuwen, H.C.1    Strating, M.J.2    Rensen, M.3    De Laat, W.4    Van Der Vliet, P.C.5
  • 69
    • 0035856542 scopus 로고    scopus 로고
    • Investigation of the role of the domain linkers in separate site catalysis by clostridium symbiosum pyruvate phosphate dikinase
    • DOI 10.1021/bi0113061
    • Wei, M., Ye, D., & Dunaway-Mariano, D. (2001). Investigation of the role of the domain linkers in separate site catalysis by Clostridium symbiosum pyruvate phosphate dikinase. Biochemistry, 40, 13466-13473. (Pubitemid 33130774)
    • (2001) Biochemistry , vol.40 , Issue.45 , pp. 13466-13473
    • Wei, M.1    Ye, D.2    Dunaway-Mariano, D.3
  • 70
    • 0017359170 scopus 로고
    • Tomato bushy stunt virus at 5.5 A resolution
    • DOI 10.1038/265509a0
    • Winkler, F. K., Schutt, C. E., Harrison, S. C., & Bricogne, G. (1977). Tomato bushy stunt virus at 5.5-A resolution. Nature, 265, 509-513. (Pubitemid 8035719)
    • (1977) Nature , vol.265 , Issue.5594 , pp. 509-513
    • Winkler, F.K.1    Schutt, C.E.2    Harrison, S.C.3    Bricogne, G.4
  • 72
    • 45249093424 scopus 로고    scopus 로고
    • DomNet: Protein domain boundary prediction using enhanced general regression network and new profiles
    • DOI 10.1109/TNB.2008.2000747, 10
    • Yoo, P. D., Sikder, A. R., Taheri, J., Zhou, B. B., & Zomaya, A. Y. (2008). DomNet: Protein domain boundary prediction using enhanced general regression network and new profiles. IEEE Transactions on Nanobioscience, 7, 172-181. (Pubitemid 351835965)
    • (2008) IEEE Transactions on Nanobioscience , vol.7 , Issue.2 , pp. 172-181
    • Yoo, P.D.1    Sikder, A.R.2    Taheri, J.3    Zhou, B.B.4    Zomaya, A.Y.5
  • 73
    • 41949117705 scopus 로고    scopus 로고
    • Improved general regression network for protein domain boundary prediction
    • Yoo, P. D., Sikder, A. R., Zhou, B. B., & Zomaya, A. Y. (2008). Improved general regression network for protein domain boundary prediction. BMC Bioinformatics, 9(Suppl. 1), S12.
    • (2008) BMC Bioinformatics , vol.9 , Issue.SUPPL. 1
    • Yoo, P.D.1    Sikder, A.R.2    Zhou, B.B.3    Zomaya, A.Y.4
  • 74
    • 0042622381 scopus 로고    scopus 로고
    • LGA: A method for finding 3D similarities in protein structures
    • DOI 10.1093/nar/gkg571
    • Zemla, A. (2003). LGA: A method for finding 3D similarities in protein structures. Nucleic Acids Research, 31, 3370-3374. (Pubitemid 37442162)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3370-3374
    • Zemla, A.1
  • 75
    • 78751536327 scopus 로고    scopus 로고
    • An improved profile-level domain linker propensity index for protein domain boundary prediction
    • Zhang, Y., Liu, B., Dong, Q., & Jin, V. X. (2011). An improved profile-level domain linker propensity index for protein domain boundary prediction. Protein and Peptide Letters, 18, 7-16.
    • (2011) Protein and Peptide Letters , vol.18 , pp. 7-16
    • Zhang, Y.1    Liu, B.2    Dong, Q.3    Jin, V.X.4


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