메뉴 건너뛰기




Volumn 72, Issue , 2016, Pages 72-95

Protein stability: A crystallographer's perspective

Author keywords

crystallizability; protein crystallization; protein disorder; protein stability

Indexed keywords

PROTEIN;

EID: 84958046376     PISSN: None     EISSN: 2053230X     Source Type: Journal    
DOI: 10.1107/S2053230X15024619     Document Type: Review
Times cited : (202)

References (258)
  • 1
    • 0032848027 scopus 로고    scopus 로고
    • Insect cells as hosts for the expression of recombinant glycoproteins
    • Altmann, F., Staudacher, E., Wilson, I. B. & März, L. (1999). Insect cells as hosts for the expression of recombinant glycoproteins. Glycoconj. J. 16, 109-123.
    • (1999) Glycoconj. J. , vol.16 , pp. 109-123
    • Altmann, F.1    Staudacher, E.2    Wilson, I.B.3    März, L.4
  • 2
    • 84901362834 scopus 로고    scopus 로고
    • High-resolution microtubule structures reveal the structural transitions in αβ-tubulin upon GTP hydrolysis
    • Alushin, G. M., Lander, G. C., Kellogg, E. H., Zhang, R., Baker, D. & Nogales, E. (2014). High-resolution microtubule structures reveal the structural transitions in αβ-tubulin upon GTP hydrolysis. Cell, 157, 1117-1129.
    • (2014) Cell , vol.157 , pp. 1117-1129
    • Alushin, G.M.1    Lander, G.C.2    Kellogg, E.H.3    Zhang, R.4    Baker, D.5    Nogales, E.6
  • 3
    • 84940854603 scopus 로고    scopus 로고
    • The use of affinity tags to overcome obstacles in recombinant protein expression and purification
    • Amarasinghe, C. & Jin, J.-P. (2015). The use of affinity tags to overcome obstacles in recombinant protein expression and purification. Protein Pept. Lett. 22, 885-892.
    • (2015) Protein Pept. Lett. , vol.22 , pp. 885-892
    • Amarasinghe, C.1    Jin, J.-P.2
  • 4
    • 0036795652 scopus 로고    scopus 로고
    • An overview on 2-methyl-2,4-pentanediol in crystallization and in crystals of biological macromolecules
    • Anand, K., Pal, D. & Hilgenfeld, R. (2002). An overview on 2-methyl-2,4-pentanediol in crystallization and in crystals of biological macromolecules. Acta Cryst. D58, 1722-1728.
    • (2002) Acta Cryst. D , vol.58 , pp. 1722-1728
    • Anand, K.1    Pal, D.2    Hilgenfeld, R.3
  • 5
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C. B. (1973). Principles that govern the folding of protein chains. Science, 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 7
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., Finley, D. & Varshavsky, A. (1986). In vivo half-life of a protein is a function of its amino-terminal residue. Science, 234, 179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 8
    • 33847120307 scopus 로고    scopus 로고
    • The use of in situ proteolysis in the crystallization of murine CstF-77
    • Bai, Y., Auperin, T. C. & Tong, L. (2007). The use of in situ proteolysis in the crystallization of murine CstF-77. Acta Cryst. F63, 135-138.
    • (2007) Acta Cryst. F , vol.63 , pp. 135-138
    • Bai, Y.1    Auperin, T.C.2    Tong, L.3
  • 10
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • Barth, A. (2007). Infrared spectroscopy of proteins. Biochim. Biophys. Acta, 1767, 1073-1101.
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1073-1101
    • Barth, A.1
  • 11
    • 0033607292 scopus 로고    scopus 로고
    • Measures of residue density in protein structures
    • Baud, F. & Karlin, S. (1999). Measures of residue density in protein structures. Proc. Natl Acad. Sci. USA, 96, 12494-12499.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12494-12499
    • Baud, F.1    Karlin, S.2
  • 12
    • 79951931431 scopus 로고    scopus 로고
    • Macromolecular NMR spectroscopy for the nonspectroscopist: Beyond macromolecular solution structure determination
    • Bieri, M., Kwan, A. H., Mobli, M., King, G. F., Mackay, J. P. & Gooley, P. R. (2011). Macromolecular NMR spectroscopy for the nonspectroscopist: beyond macromolecular solution structure determination. FEBS J. 278, 704-715.
    • (2011) FEBS J. , vol.278 , pp. 704-715
    • Bieri, M.1    Kwan, A.H.2    Mobli, M.3    King, G.F.4    Mackay, J.P.5    Gooley, P.R.6
  • 13
    • 84883894803 scopus 로고    scopus 로고
    • Optimization of protein purification and characterization using Thermofluor screens
    • Boivin, S., Kozak, S. & Meijers, R. (2013). Optimization of protein purification and characterization using Thermofluor screens. Protein Expr. Purif. 91, 192-206.
    • (2013) Protein Expr. Purif. , vol.91 , pp. 192-206
    • Boivin, S.1    Kozak, S.2    Meijers, R.3
  • 14
    • 0035423934 scopus 로고    scopus 로고
    • Stabilizing membrane proteins
    • Bowie, J. U. (2001). Stabilizing membrane proteins. Curr. Opin. Struct. Biol. 11, 397-402.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 397-402
    • Bowie, J.U.1
  • 15
    • 34447316738 scopus 로고    scopus 로고
    • The LOV domain: A chromophore module servicing multiple photoreceptors
    • Briggs, W. R. (2007). The LOV domain: A chromophore module servicing multiple photoreceptors. J. Biomed. Sci. 14, 499-504.
    • (2007) J. Biomed. Sci. , vol.14 , pp. 499-504
    • Briggs, W.R.1
  • 16
    • 71549157111 scopus 로고    scopus 로고
    • Selecting an appropriate method for expressing a recombinant protein
    • Brondyk, W. H. (2009). Selecting an appropriate method for expressing a recombinant protein. Methods Enzymol. 463, 131-147.
    • (2009) Methods Enzymol. , vol.463 , pp. 131-147
    • Brondyk, W.H.1
  • 17
    • 84892819762 scopus 로고    scopus 로고
    • Variations on the theme: Allosteric control in hemoglobin
    • Brunori, M. (2014). Variations on the theme: allosteric control in hemoglobin. FEBS J. 281, 633-643.
    • (2014) FEBS J. , vol.281 , pp. 633-643
    • Brunori, M.1
  • 18
    • 84942079610 scopus 로고    scopus 로고
    • NMR methods for the study of instrinsically disordered proteins structure, dynamics, and interactions: General overview and practical guidelines
    • Brutscher, B., Felli, I. C., Gil-Caballero, S., Hošek, T., Kümmerle, R., Piai, A., Pierattelli, R. & Sólyom, Z. (2015). NMR methods for the study of instrinsically disordered proteins structure, dynamics, and interactions: general overview and practical guidelines. Adv. Exp. Med. Biol. 870, 49-122.
    • (2015) Adv. Exp. Med. Biol. , vol.870 , pp. 49-122
    • Brutscher, B.1    Felli, I.C.2    Gil-Caballero, S.3    Hošek, T.4    Kümmerle, R.5    Piai, A.6    Pierattelli, R.7    Sólyom, Z.8
  • 19
    • 22544442178 scopus 로고    scopus 로고
    • Differential scanning calorimetry in life science: Thermodynamics, stability, molecular recognition and application in drug design
    • Bruylants, G., Wouters, J. & Michaux, C. (2005). Differential scanning calorimetry in life science: thermodynamics, stability, molecular recognition and application in drug design. Curr. Med. Chem. 12, 2011-2020.
    • (2005) Curr. Med. Chem. , vol.12 , pp. 2011-2020
    • Bruylants, G.1    Wouters, J.2    Michaux, C.3
  • 21
    • 0036006255 scopus 로고    scopus 로고
    • Differential effects of short affinity tags on the crystallization of Pyrococcus furiosus maltodextrin-binding protein
    • Bucher, M. H., Evdokimov, A. G. & Waugh, D. S. (2002). Differential effects of short affinity tags on the crystallization of Pyrococcus furiosus maltodextrin-binding protein. Acta Cryst. D58, 392-397.
    • (2002) Acta Cryst. D , vol.58 , pp. 392-397
    • Bucher, M.H.1    Evdokimov, A.G.2    Waugh, D.S.3
  • 22
    • 84921891585 scopus 로고    scopus 로고
    • Design, synthesis, and study of fluorinated proteins
    • Buer, B. C. & Marsh, E. N. (2014). Design, synthesis, and study of fluorinated proteins. Methods Mol. Biol. 1216, 89-116.
    • (2014) Methods Mol. Biol. , vol.1216 , pp. 89-116
    • Buer, B.C.1    Marsh, E.N.2
  • 23
    • 84859465095 scopus 로고    scopus 로고
    • Structural basis for the enhanced stability of highly fluorinated proteins
    • Buer, B. C., Meagher, J. L., Stuckey, J. A. & Marsh, E. N. (2012). Structural basis for the enhanced stability of highly fluorinated proteins. Proc. Natl Acad. Sci. USA, 109, 4810-4815.
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 4810-4815
    • Buer, B.C.1    Meagher, J.L.2    Stuckey, J.A.3    Marsh, E.N.4
  • 24
    • 84879177985 scopus 로고    scopus 로고
    • New concepts and AIDS to facilitate crystallization
    • Bukowska, M. A. & Grütter, M. G. (2013). New concepts and aids to facilitate crystallization. Curr. Opin. Struct. Biol. 23, 409-416.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 409-416
    • Bukowska, M.A.1    Grütter, M.G.2
  • 26
    • 0030568996 scopus 로고    scopus 로고
    • High-level misincorporation of lysine for arginine at AGA codons in a fusion protein expressed in Escherichia coli
    • Calderone, T. L., Stevens, R. D. & Oas, T. G. (1996). High-level misincorporation of lysine for arginine at AGA codons in a fusion protein expressed in Escherichia coli. J. Mol. Biol. 262, 407-412.
    • (1996) J. Mol. Biol. , vol.262 , pp. 407-412
    • Calderone, T.L.1    Stevens, R.D.2    Oas, T.G.3
  • 27
    • 20144384268 scopus 로고    scopus 로고
    • Decrypting the biochemical function of an essential gene from Streptococcus pneumoniae using Thermofluor technology
    • Carver, T. E. et al. (2005). Decrypting the biochemical function of an essential gene from Streptococcus pneumoniae using Thermofluor technology. J. Biol. Chem. 280, 11704-11712.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11704-11712
    • Carver, T.E.1
  • 29
    • 84883364817 scopus 로고    scopus 로고
    • SCMCRYS: Predicting protein crystallization using an ensemble scoring card method with estimating propensity scores of P-collocated amino acid pairs
    • Charoenkwan, P., Shoombuatong, W., Lee, H.-C., Chaijaruwanich, J., Huang, H.-L. & Ho, S.-Y. (2013). SCMCRYS: predicting protein crystallization using an ensemble scoring card method with estimating propensity scores of P-collocated amino acid pairs. PLoS One, 8, e72368.
    • (2013) PLoS One , vol.8 , pp. e72368
    • Charoenkwan, P.1    Shoombuatong, W.2    Lee, H.-C.3    Chaijaruwanich, J.4    Huang, H.-L.5    Ho, S.-Y.6
  • 30
    • 0035666914 scopus 로고    scopus 로고
    • The GPI-anchor and protein sorting
    • Chatterjee, S. & Mayor, S. (2001). The GPI-anchor and protein sorting. Cell. Mol. Life Sci. 58, 1969-1987.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1969-1987
    • Chatterjee, S.1    Mayor, S.2
  • 32
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical,-sheet, and random coil regions calculated from proteins
    • Chou, P. Y. & Fasman, G. D. (1974). Conformational parameters for amino acids in helical,-sheet, and random coil regions calculated from proteins. Biochemistry, 13, 211-222.
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 33
    • 33846419564 scopus 로고    scopus 로고
    • The use of biophysical methods increases success in obtaining liganded crystal structures
    • Chung, C. (2007). The use of biophysical methods increases success in obtaining liganded crystal structures. Acta Cryst. D63, 62-71.
    • (2007) Acta Cryst. D , vol.63 , pp. 62-71
    • Chung, C.1
  • 35
    • 84929379135 scopus 로고    scopus 로고
    • A maltose-binding protein fusion construct yields a robust crystallography platform for MCL1
    • Clifton, M. C. et al. (2015). A maltose-binding protein fusion construct yields a robust crystallography platform for MCL1. PLoS One, 10, e0125010.
    • (2015) PLoS One , vol.10 , pp. e0125010
    • Clifton, M.C.1
  • 36
    • 84934911449 scopus 로고    scopus 로고
    • Post-expression strategies for structural investigations of membrane proteins
    • Columbus, L. (2015). Post-expression strategies for structural investigations of membrane proteins. Curr. Opin. Struct. Biol. 32, 131-138.
    • (2015) Curr. Opin. Struct. Biol. , vol.32 , pp. 131-138
    • Columbus, L.1
  • 37
    • 84889263238 scopus 로고    scopus 로고
    • Computational and theoretical methods for protein folding
    • Compiani, M. & Capriotti, E. (2013). Computational and theoretical methods for protein folding. Biochemistry, 52, 8601-8624.
    • (2013) Biochemistry , vol.52 , pp. 8601-8624
    • Compiani, M.1    Capriotti, E.2
  • 38
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Conte, L. L., Chothia, C. & Janin, J. (1999). The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285, 2177-2198.
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 40
    • 84888312300 scopus 로고    scopus 로고
    • Disulfide by Design 2.0: A web-based tool for disulfide engineering in proteins
    • Craig, D. B. & Dombkowski, A. A. (2013). Disulfide by Design 2.0: A web-based tool for disulfide engineering in proteins. BMC Bioinformatics, 14, 346.
    • (2013) BMC Bioinformatics , vol.14 , pp. 346
    • Craig, D.B.1    Dombkowski, A.A.2
  • 41
    • 1842526110 scopus 로고    scopus 로고
    • The impact of Lys!Arg surface mutations on the crystallization of the globular domain of RhoGDI
    • Czepas, J., Devedjiev, Y., Krowarsch, D., Derewenda, U., Otlewski, J. & Derewenda, Z. S. (2004). The impact of Lys!Arg surface mutations on the crystallization of the globular domain of RhoGDI. Acta Cryst. D60, 275-280.
    • (2004) Acta Cryst. D , vol.60 , pp. 275-280
    • Czepas, J.1    Devedjiev, Y.2    Krowarsch, D.3    Derewenda, U.4    Otlewski, J.5    Derewenda, Z.S.6
  • 42
    • 84959165530 scopus 로고    scopus 로고
    • ATGme: Open-source web application for rare codon identification and custom DNA sequence optimization
    • Daniel, E., Onwukwe, G. U., Wierenga, R. K., Quaggin, S. E., Vainio, S. J. & Krause, M. (2015). ATGme: open-source web application for rare codon identification and custom DNA sequence optimization. BMC Bioinformatics, 16, 303.
    • (2015) BMC Bioinformatics , vol.16 , pp. 303
    • Daniel, E.1    Onwukwe, G.U.2    Wierenga, R.K.3    Quaggin, S.E.4    Vainio, S.J.5    Krause, M.6
  • 43
    • 0000142773 scopus 로고
    • A correlation between amino acid composition and protein structure
    • Davies, D. R. (1964). A correlation between amino acid composition and protein structure. J. Mol. Biol. 9, 605-609.
    • (1964) J. Mol. Biol. , vol.9 , pp. 605-609
    • Davies, D.R.1
  • 45
    • 84906217605 scopus 로고    scopus 로고
    • Predicting aggregation-prone sequences in proteins
    • De Baets, G., Schymkowitz, J. & Rousseau, F. (2014). Predicting aggregation-prone sequences in proteins. Essays Biochem. 56, 41-52.
    • (2014) Essays Biochem. , vol.56 , pp. 41-52
    • De Baets, G.1    Schymkowitz, J.2    Rousseau, F.3
  • 46
    • 0027143565 scopus 로고
    • Val!Ala mutations selectively alter helix-helix packing in the transmembrane segment of phage M13 coat protein
    • Deber, C. M., Khan, A. R., Li, Z., Joensson, C., Glibowicka, M. & Wang, J. (1993). Val!Ala mutations selectively alter helix-helix packing in the transmembrane segment of phage M13 coat protein. Proc. Natl Acad. Sci. USA, 90, 11648-11652.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11648-11652
    • Deber, C.M.1    Khan, A.R.2    Li, Z.3    Joensson, C.4    Glibowicka, M.5    Wang, J.6
  • 47
    • 0025765288 scopus 로고
    • Xylose (glucose) isomerase gene from the thermophile Thermus thermophilus: Cloning, sequencing, and comparison with other thermostable xylose isomerases
    • Dekker, K., Yamagata, H., Sakaguchi, K. & Udaka, S. (1991). Xylose (glucose) isomerase gene from the thermophile Thermus thermophilus: cloning, sequencing, and comparison with other thermostable xylose isomerases. J. Bacteriol. 173, 3078-3083.
    • (1991) J. Bacteriol. , vol.173 , pp. 3078-3083
    • Dekker, K.1    Yamagata, H.2    Sakaguchi, K.3    Udaka, S.4
  • 49
    • 1842555070 scopus 로고    scopus 로고
    • Rational protein crystallization by mutational surface engineering
    • Derewenda, Z. S. (2004). Rational protein crystallization by mutational surface engineering. Structure, 12, 529-535.
    • (2004) Structure , vol.12 , pp. 529-535
    • Derewenda, Z.S.1
  • 50
    • 77952022366 scopus 로고    scopus 로고
    • Application of protein engineering to enhance crystallizability and improve crystal properties
    • Derewenda, Z. S. (2010). Application of protein engineering to enhance crystallizability and improve crystal properties. Acta Cryst. D66, 604-615.
    • (2010) Acta Cryst. D , vol.66 , pp. 604-615
    • Derewenda, Z.S.1
  • 51
    • 33644874674 scopus 로고    scopus 로고
    • Entropy and surface engineering in protein crystallization
    • Derewenda, Z. S. & Vekilov, P. G. (2006). Entropy and surface engineering in protein crystallization. Acta Cryst. D62, 116-124.
    • (2006) Acta Cryst. D , vol.62 , pp. 116-124
    • Derewenda, Z.S.1    Vekilov, P.G.2
  • 53
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. (1990). Dominant forces in protein folding. Biochemistry, 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 54
    • 84863518014 scopus 로고    scopus 로고
    • MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins
    • Disfani, F. M., Hsu, W.-L., Mizianty, M. J., Oldfield, C. J., Xue, B., Dunker, A. K., Uversky, V. N. & Kurgan, L. (2012). MoRFpred, a computational tool for sequence-based prediction and characterization of short disorder-to-order transitioning binding regions in proteins. Bioinformatics, 28, i75-i83.
    • (2012) Bioinformatics , vol.28 , pp. i75-i83
    • Disfani, F.M.1    Hsu, W.-L.2    Mizianty, M.J.3    Oldfield, C.J.4    Xue, B.5    Dunker, A.K.6    Uversky, V.N.7    Kurgan, L.8
  • 56
    • 36749034218 scopus 로고    scopus 로고
    • In situ proteolysis for protein crystallization and structure determination
    • Dong, A. et al. (2007). In situ proteolysis for protein crystallization and structure determination. Nature Methods, 4, 1019-1021.
    • (2007) Nature Methods , vol.4 , pp. 1019-1021
    • Dong, A.1
  • 57
    • 84942102408 scopus 로고    scopus 로고
    • Back to the future: Nuclear magnetic resonance and bioinformatics studies on intrinsically disordered proteins
    • Dunker, A. K. & Oldfield, C. J. (2015). Back to the future: nuclear magnetic resonance and bioinformatics studies on intrinsically disordered proteins. Adv. Exp. Med. Biol. 870, 1-34.
    • (2015) Adv. Exp. Med. Biol. , vol.870 , pp. 1-34
    • Dunker, A.K.1    Oldfield, C.J.2
  • 58
    • 80955136787 scopus 로고    scopus 로고
    • A thermal stability assay can help to estimate the crystallization likelihood of biological samples
    • Dupeux, F., Röwer, M., Seroul, G., Blot, D. & Márquez, J. A. (2011). A thermal stability assay can help to estimate the crystallization likelihood of biological samples. Acta Cryst. D67, 915-919.
    • (2011) Acta Cryst. D , vol.67 , pp. 915-919
    • Dupeux, F.1    Röwer, M.2    Seroul, G.3    Blot, D.4    Márquez, J.A.5
  • 59
    • 0023159808 scopus 로고
    • Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains
    • Elbein, A. D. (1987). Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains. Annu. Rev. Biochem. 56, 497-534.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 497-534
    • Elbein, A.D.1
  • 60
    • 33750320427 scopus 로고    scopus 로고
    • Hydrogen exchange and mass spectrometry: A historical perspective
    • Englander, S.W. (2006). Hydrogen exchange and mass spectrometry: A historical perspective. J. Am. Soc. Mass Spectrom. 17, 1481-1489.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1481-1489
    • Englander, S.W.1
  • 61
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander, S.W. & Kallenbach, N. R. (1983). Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q. Rev. Biophys. 16, 521-655.
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 62
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • Ericsson, U. B., Hallberg, B. M., DeTitta, G. T., Dekker, N. & Nordlund, P. (2006). Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal. Biochem. 357, 289-298.
    • (2006) Anal. Biochem. , vol.357 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    DeTitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 63
    • 33846215584 scopus 로고    scopus 로고
    • Serendipitous discovery of novel bacterial methionine aminopeptidase inhibitors
    • Evdokimov, A. G. et al. (2007). Serendipitous discovery of novel bacterial methionine aminopeptidase inhibitors. Proteins, 66, 538-546.
    • (2007) Proteins , vol.66 , pp. 538-546
    • Evdokimov, A.G.1
  • 64
    • 10344236053 scopus 로고    scopus 로고
    • Protein stabilization by osmolytes from hyperthermophiles: Effect of mannosylglycerate on the thermal unfolding of recombinant nuclease A from Staphylococcus aureus studied by picosecond timeresolved fluorescence and calorimetry
    • Faria, T. Q., Lima, J. C., Bastos, M., Maçanita, A. L. & Santos, H. (2004). Protein stabilization by osmolytes from hyperthermophiles: effect of mannosylglycerate on the thermal unfolding of recombinant nuclease A from Staphylococcus aureus studied by picosecond timeresolved fluorescence and calorimetry. J. Biol. Chem. 279, 48680-48691.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48680-48691
    • Faria, T.Q.1    Lima, J.C.2    Bastos, M.3    Maçanita, A.L.4    Santos, H.5
  • 65
    • 84946235568 scopus 로고    scopus 로고
    • Adaptations of protein structure and function to temperature: There is more than one way to 'skin a cat'
    • Fields, P. A., Dong, Y., Meng, X. & Somero, G. N. (2015). Adaptations of protein structure and function to temperature: there is more than one way to 'skin a cat'. J. Exp. Biol. 218, 1801-1811.
    • (2015) J. Exp. Biol. , vol.218 , pp. 1801-1811
    • Fields, P.A.1    Dong, Y.2    Meng, X.3    Somero, G.N.4
  • 66
    • 84949032232 scopus 로고    scopus 로고
    • The art of CHO cell engineering: A comprehensive retrospect and future perspectives
    • Fischer, S., Handrick, R. & Otte, K. (2015). The art of CHO cell engineering: A comprehensive retrospect and future perspectives. Biotechnol. Adv. 33, 1878-1896.
    • (2015) Biotechnol. Adv. , vol.33 , pp. 1878-1896
    • Fischer, S.1    Handrick, R.2    Otte, K.3
  • 68
    • 78650808679 scopus 로고    scopus 로고
    • Synthetic symmetrization in the crystallization and structure determination of CelA from Thermotoga maritima
    • Forse, G. J., Ram, N., Banatao, D. R., Cascio, D., Sawaya, M. R., Klock, H. E., Lesley, S. A. & Yeates, T. O. (2011). Synthetic symmetrization in the crystallization and structure determination of CelA from Thermotoga maritima. Protein Sci. 20, 168-178.
    • (2011) Protein Sci. , vol.20 , pp. 168-178
    • Forse, G.J.1    Ram, N.2    Banatao, D.R.3    Cascio, D.4    Sawaya, M.R.5    Klock, H.E.6    Lesley, S.A.7    Yeates, T.O.8
  • 69
    • 84872475055 scopus 로고    scopus 로고
    • Structure, function and biosynthesis of O2-tolerant hydrogenases
    • Fritsch, J., Lenz, O. & Friedrich, B. (2013). Structure, function and biosynthesis of O2-tolerant hydrogenases. Nature Rev. Microbiol. 11, 106-114.
    • (2013) Nature Rev. Microbiol. , vol.11 , pp. 106-114
    • Fritsch, J.1    Lenz, O.2    Friedrich, B.3
  • 70
    • 34547407784 scopus 로고    scopus 로고
    • 5-Aminolevulinate production with recombinant Escherichia coli using a rare codon optimizer host strain
    • Fu, W., Lin, J. & Cen, P. (2007). 5-Aminolevulinate production with recombinant Escherichia coli using a rare codon optimizer host strain. Appl. Microbiol. Biotechnol. 75, 777-782.
    • (2007) Appl. Microbiol. Biotechnol. , vol.75 , pp. 777-782
    • Fu, W.1    Lin, J.2    Cen, P.3
  • 71
    • 77956873612 scopus 로고    scopus 로고
    • Mass spectrometry guided in situ proteolysis to obtain crystals for X-ray structure determination
    • Gheyi, T., Rodgers, L., Romero, R., Sauder, J. M. & Burley, S. K. (2010). Mass spectrometry guided in situ proteolysis to obtain crystals for X-ray structure determination. J. Am. Soc. Mass Spectrom. 21, 1795-1801.
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1795-1801
    • Gheyi, T.1    Rodgers, L.2    Romero, R.3    Sauder, J.M.4    Burley, S.K.5
  • 72
    • 84910596652 scopus 로고    scopus 로고
    • Stabilization of protein-protein interactions by small molecules
    • Giordanetto, F., Schäfer, A. & Ottmann, C. (2014). Stabilization of protein-protein interactions by small molecules. Drug Discov. Today, 19, 1812-1821.
    • (2014) Drug Discov. Today , vol.19 , pp. 1812-1821
    • Giordanetto, F.1    Schäfer, A.2    Ottmann, C.3
  • 73
    • 34547566008 scopus 로고    scopus 로고
    • Toward rational protein crystallization: A web server for the design of crystallizable protein variants
    • Goldschmidt, L., Cooper, D. R., Derewenda, Z. S. & Eisenberg, D. (2007). Toward rational protein crystallization: A web server for the design of crystallizable protein variants. Protein Sci. 16, 1569-1576.
    • (2007) Protein Sci. , vol.16 , pp. 1569-1576
    • Goldschmidt, L.1    Cooper, D.R.2    Derewenda, Z.S.3    Eisenberg, D.4
  • 74
    • 84907938815 scopus 로고    scopus 로고
    • Salvage or recovery of failed targets by mutagenesis to reduce surface entropy
    • Goldschmidt, L., Eisenberg, D. & Derewenda, Z. S. (2014). Salvage or recovery of failed targets by mutagenesis to reduce surface entropy. Methods Mol. Biol. 1140, 201-209.
    • (2014) Methods Mol. Biol. , vol.1140 , pp. 201-209
    • Goldschmidt, L.1    Eisenberg, D.2    Derewenda, Z.S.3
  • 75
    • 84958603157 scopus 로고    scopus 로고
    • Insoluble protein characterization by circular dichroism (CD) spectroscopy and nuclear magnetic resonance (NMR)
    • Goyal, S., Qin, H., Lim, L. & Song, J. (2015). Insoluble protein characterization by circular dichroism (CD) spectroscopy and nuclear magnetic resonance (NMR). Methods Mol. Biol. 1258, 371-385.
    • (2015) Methods Mol. Biol. , vol.1258 , pp. 371-385
    • Goyal, S.1    Qin, H.2    Lim, L.3    Song, J.4
  • 77
    • 84937398926 scopus 로고    scopus 로고
    • Biostructural science inspired by next-generation X-ray sources
    • Gruner, S. M. & Lattman, E. E. (2015). Biostructural science inspired by next-generation X-ray sources. Annu. Rev. Biophys. 44, 33-51.
    • (2015) Annu. Rev. Biophys. , vol.44 , pp. 33-51
    • Gruner, S.M.1    Lattman, E.E.2
  • 78
    • 84865066445 scopus 로고    scopus 로고
    • Solution structure, conformational dynamics, and CD4-induced activation in full-length, glycosylated, monomeric HIV gp120
    • Guttman, M., Kahn, M., Garcia, N. K., Hu, S.-L. & Lee, K. K. (2012). Solution structure, conformational dynamics, and CD4-induced activation in full-length, glycosylated, monomeric HIV gp120. J. Virol. 86, 8750-8764.
    • (2012) J. Virol. , vol.86 , pp. 8750-8764
    • Guttman, M.1    Kahn, M.2    Garcia, N.K.3    Hu, S.-L.4    Lee, K.K.5
  • 79
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., Belin, D., Carson, M. J. & Beckwith, J. (1995). Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177, 4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 80
    • 0013817874 scopus 로고
    • The influence of amino acid sequence on protein structure
    • Guzzo, A. V. (1965). The influence of amino acid sequence on protein structure. Biophys. J. 5, 809-822.
    • (1965) Biophys. J. , vol.5 , pp. 809-822
    • Guzzo, A.V.1
  • 81
    • 84926311802 scopus 로고    scopus 로고
    • Biotransformation and in vivo stability of protein biotherapeutics: Impact on candidate selection and pharmacokinetic profiling
    • Hall, M. P. (2014). Biotransformation and in vivo stability of protein biotherapeutics: impact on candidate selection and pharmacokinetic profiling. Drug Metab. Dispos. 42, 1873-1880.
    • (2014) Drug Metab. Dispos. , vol.42 , pp. 1873-1880
    • Hall, M.P.1
  • 82
    • 33846460839 scopus 로고    scopus 로고
    • Crystallization of protein-ligand complexes
    • Hassell, A. M. et al. (2007). Crystallization of protein-ligand complexes. Acta Cryst. D63, 72-79.
    • (2007) Acta Cryst. D , vol.63 , pp. 72-79
    • Hassell, A.M.1
  • 83
    • 15944406765 scopus 로고    scopus 로고
    • SUMO
    • Hay, R. T. (2005). SUMO. Mol. Cell, 18, 1-12.
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 84
    • 0028158008 scopus 로고
    • Rapid crystallization of T4 lysozyme by intermolecular disulfide cross-linking
    • Heinz, D. W. & Matthews, B. W. (1994). Rapid crystallization of T4 lysozyme by intermolecular disulfide cross-linking. Protein Eng. Des. Sel. 7, 301-307.
    • (1994) Protein Eng. Des. Sel. , vol.7 , pp. 301-307
    • Heinz, D.W.1    Matthews, B.W.2
  • 85
    • 0026748637 scopus 로고
    • Differential helix propensity of small apolar side chains studied by molecular dynamics simulations
    • Hermans, J., Anderson, A. G. & Yun, R. H. (1992). Differential helix propensity of small apolar side chains studied by molecular dynamics simulations. Biochemistry, 31, 5646-5653.
    • (1992) Biochemistry , vol.31 , pp. 5646-5653
    • Hermans, J.1    Anderson, A.G.2    Yun, R.H.3
  • 86
    • 0025240361 scopus 로고
    • Molecular structure of a gene, VMA1, encoding the catalytic subunit of H+-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae
    • Hirata, R., Ohsumk, Y., Nakano, A., Kawasaki, H., Suzuki, K. & Anraku, Y. (1990). Molecular structure of a gene, VMA1, encoding the catalytic subunit of H+-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae. J. Biol. Chem. 265, 6726-6733.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6726-6733
    • Hirata, R.1    Ohsumk, Y.2    Nakano, A.3    Kawasaki, H.4    Suzuki, K.5    Anraku, Y.6
  • 87
    • 0037126026 scopus 로고    scopus 로고
    • Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes
    • Huai, Q., Kim, H.-Y., Liu, Y., Zhao, Y., Mondragon, A., Liu, J. O. & Ke, H. (2002). Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Proc. Natl Acad. Sci. USA, 99, 12037-12042.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12037-12042
    • Huai, Q.1    Kim, H.-Y.2    Liu, Y.3    Zhao, Y.4    Mondragon, A.5    Liu, J.O.6    Ke, H.7
  • 88
    • 84934436140 scopus 로고    scopus 로고
    • DisMeta: A meta server for construct design and optimization
    • Huang, Y. J., Acton, T. B. & Montelione, G. T. (2014). DisMeta: A meta server for construct design and optimization. Methods Mol. Biol. 1091, 3-16.
    • (2014) Methods Mol. Biol. , vol.1091 , pp. 3-16
    • Huang, Y.J.1    Acton, T.B.2    Montelione, G.T.3
  • 90
    • 84896792916 scopus 로고    scopus 로고
    • Improving the chances of successful protein structure determination with a random forest classifier
    • Jahandideh, S., Jaroszewski, L. & Godzik, A. (2014). Improving the chances of successful protein structure determination with a random forest classifier. Acta Cryst. D70, 627-635.
    • (2014) Acta Cryst. D , vol.70 , pp. 627-635
    • Jahandideh, S.1    Jaroszewski, L.2    Godzik, A.3
  • 91
    • 84861008426 scopus 로고    scopus 로고
    • RFCRYS: Sequence-based protein crystallization propensity prediction by means of random forest
    • Jahandideh, S. & Mahdavi, A. (2012). RFCRYS: sequence-based protein crystallization propensity prediction by means of random forest. J. Theor. Biol. 306, 115-119.
    • (2012) J. Theor. Biol. , vol.306 , pp. 115-119
    • Jahandideh, S.1    Mahdavi, A.2
  • 92
    • 71549150895 scopus 로고    scopus 로고
    • Baculovirus-insect cell expression systems
    • Jarvis, D. L. (2009). Baculovirus-insect cell expression systems. Methods Enzymol. 463, 191-222.
    • (2009) Methods Enzymol. , vol.463 , pp. 191-222
    • Jarvis, D.L.1
  • 93
    • 84922154903 scopus 로고    scopus 로고
    • Design of monomeric water-soluble-hairpin and-sheet peptides
    • Jiménez, M. A. (2014). Design of monomeric water-soluble-hairpin and-sheet peptides. Methods Mol. Biol. 1216, 15-52.
    • (2014) Methods Mol. Biol. , vol.1216 , pp. 15-52
    • Jiménez, M.A.1
  • 94
    • 84942856317 scopus 로고    scopus 로고
    • Design and structure of two HIV-1 clade C SOSIP.664 trimers that increase the arsenal of native-like Env immunogens
    • Julien, J.-P. et al. (2015). Design and structure of two HIV-1 clade C SOSIP.664 trimers that increase the arsenal of native-like Env immunogens. Proc. Natl Acad. Sci. USA, 112, 11947-11952.
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 11947-11952
    • Julien, J.-P.1
  • 95
    • 77950100747 scopus 로고    scopus 로고
    • SVMCRYS: An SVM approach for the prediction of protein crystallization propensity from protein sequence
    • Kandaswamy, K. K., Pugalenthi, G., Suganthan, P. N. & Gangal, R. (2010). SVMCRYS: an SVM approach for the prediction of protein crystallization propensity from protein sequence. Protein Pept. Lett. 17, 423-430.
    • (2010) Protein Pept. Lett. , vol.17 , pp. 423-430
    • Kandaswamy, K.K.1    Pugalenthi, G.2    Suganthan, P.N.3    Gangal, R.4
  • 96
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • Kane, J. F. (1995). Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr. Opin. Biotechnol. 6, 494-500.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 97
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust, R. B. & Waugh, D. S. (1999). Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8, 1668-1674.
    • (1999) Protein Sci. , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 98
    • 0037305746 scopus 로고    scopus 로고
    • Insights into binding cooperativity of MATa1/MAT2 from the crystal structure of a MATa1 homeodomain-maltose binding protein chimera
    • Ke, A. & Wolberger, C. (2003). Insights into binding cooperativity of MATa1/MAT2 from the crystal structure of a MATa1 homeodomain-maltose binding protein chimera. Protein Sci. 12, 306-312.
    • (2003) Protein Sci. , vol.12 , pp. 306-312
    • Ke, A.1    Wolberger, C.2
  • 99
    • 0028984985 scopus 로고
    • Aminolevulinate increases heme saturation and yield of human cystathionine-synthase expressed in Escherichia coli
    • Kery, V., Elleder, D. & Kraus, J. P. (1995).-Aminolevulinate increases heme saturation and yield of human cystathionine-synthase expressed in Escherichia coli. Arch. Biochem. Biophys. 316, 24-29.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 24-29
    • Kery, V.1    Elleder, D.2    Kraus, J.P.3
  • 100
    • 84910679144 scopus 로고    scopus 로고
    • Proteome-wide post-translational modification statistics: Frequency analysis and curation of the Swiss-Prot database
    • Khoury, G. A., Baliban, R. C. & Floudas, C. A. (2011). Proteome-wide post-translational modification statistics: frequency analysis and curation of the Swiss-Prot database. Sci. Rep. 1, 90.
    • (2011) Sci. Rep. , vol.1 , pp. 90
    • Khoury, G.A.1    Baliban, R.C.2    Floudas, C.A.3
  • 101
    • 80051689337 scopus 로고    scopus 로고
    • Hydrogenases for biological hydrogen production
    • Kim, D.-H. & Kim, M.-S. (2011). Hydrogenases for biological hydrogen production. Bioresour. Technol. 102, 8423-8431.
    • (2011) Bioresour. Technol. , vol.102 , pp. 8423-8431
    • Kim, D.-H.1    Kim, M.-S.2
  • 102
    • 41149148236 scopus 로고    scopus 로고
    • Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts
    • Klock, H. E., Koesema, E. J., Knuth, M. W. & Lesley, S. A. (2008). Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts. Proteins, 71, 982-994.
    • (2008) Proteins , vol.71 , pp. 982-994
    • Klock, H.E.1    Koesema, E.J.2    Knuth, M.W.3    Lesley, S.A.4
  • 103
    • 84934438590 scopus 로고    scopus 로고
    • The polymerase incomplete primer extension (PIPE) method applied to high-throughput cloning and site-directed mutagenesis
    • Klock, H. E. & Lesley, S. A. (2009). The polymerase incomplete primer extension (PIPE) method applied to high-throughput cloning and site-directed mutagenesis. Methods Mol. Biol. 498, 91-103.
    • (2009) Methods Mol. Biol. , vol.498 , pp. 91-103
    • Klock, H.E.1    Lesley, S.A.2
  • 104
    • 0033551053 scopus 로고    scopus 로고
    • Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins
    • Kobe, B., Center, R. J., Kemp, B. E. & Poumbourios, P. (1999). Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins. Proc. Natl Acad. Sci. USA, 96, 4319-4324.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4319-4324
    • Kobe, B.1    Center, R.J.2    Kemp, B.E.3    Poumbourios, P.4
  • 106
    • 79951887389 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for studying protein structure and dynamics
    • Konermann, L., Pan, J. & Liu, Y.-H. (2011). Hydrogen exchange mass spectrometry for studying protein structure and dynamics. Chem. Soc. Rev. 40, 1224-1234.
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 1224-1234
    • Konermann, L.1    Pan, J.2    Liu, Y.-H.3
  • 108
    • 77956819789 scopus 로고    scopus 로고
    • Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/deuterium exchange
    • Kong, L., Huang, C.-C., Coales, S. J., Molnar, K. S., Skinner, J., Hamuro, Y. & Kwong, P. D. (2010). Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/deuterium exchange. J. Virol. 84, 10311-10321.
    • (2010) J. Virol. , vol.84 , pp. 10311-10321
    • Kong, L.1    Huang, C.-C.2    Coales, S.J.3    Molnar, K.S.4    Skinner, J.5    Hamuro, Y.6    Kwong, P.D.7
  • 109
    • 84926683003 scopus 로고    scopus 로고
    • HIV Glycans in Infection and Immunity, edited by R
    • New York: Springer
    • Kong, L., Stanfield, R. & Wilson, I. (2014). HIV Glycans in Infection and Immunity, edited by R. Pantophlet, pp. 117-141. New York: Springer.
    • (2014) Pantophlet , pp. 117-141
    • Kong, L.1    Stanfield, R.2    Wilson, I.3
  • 111
    • 33745727013 scopus 로고    scopus 로고
    • The photochemistry of the light-, oxygen-, and voltage-sensitive domains in the algal blue light receptor phot
    • Kottke, T., Hegemann, P., Dick, B. & Heberle, J. (2006). The photochemistry of the light-, oxygen-, and voltage-sensitive domains in the algal blue light receptor phot. Biopolymers, 82, 373-378.
    • (2006) Biopolymers , vol.82 , pp. 373-378
    • Kottke, T.1    Hegemann, P.2    Dick, B.3    Heberle, J.4
  • 112
    • 77949358922 scopus 로고    scopus 로고
    • Sequence-specific NiII-dependent peptide bond hydrolysis for protein engineering. Combinatorial library determination of optimal sequences
    • Kręzel, A., Kopera, E., Protas, A. M., Poznański, J., Wysłouch-Cieszyńska, A. & Bal, W. (2010). Sequence-specific NiII-dependent peptide bond hydrolysis for protein engineering. Combinatorial library determination of optimal sequences. J. Am. Chem. Soc. 132, 3355-3366.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 3355-3366
    • Kręzel, A.1    Kopera, E.2    Protas, A.M.3    Poznański, J.4    Wysłouch-Cieszyńska, A.5    Bal, W.6
  • 113
    • 84856225222 scopus 로고    scopus 로고
    • X-ray structures of LeuT in substrate-free outward-open and apo inward-open states
    • Krishnamurthy, H. & Gouaux, E. (2012). X-ray structures of LeuT in substrate-free outward-open and apo inward-open states. Nature (London), 481, 469-474.
    • (2012) Nature (London) , vol.481 , pp. 469-474
    • Krishnamurthy, H.1    Gouaux, E.2
  • 114
    • 84991001273 scopus 로고    scopus 로고
    • Macromolecular structure determination: Comparison of X-ray crystallography and NMR spectroscopy
    • Krishnan, V. V. & Rupp, B. (2012). Macromolecular structure determination: comparison of X-ray crystallography and NMR spectroscopy. eLS, doi:10.1002/9780470015902.a0002716.pub2.
    • (2012) ELS
    • Krishnan, V.V.1    Rupp, B.2
  • 117
    • 79951919101 scopus 로고    scopus 로고
    • Macromolecular NMR spectroscopy for the non-spectroscopist
    • Kwan, A. H., Mobli, M., Gooley, P. R., King, G. F. & Mackay, J. P. (2011). Macromolecular NMR spectroscopy for the non-spectroscopist. FEBS J. 278, 687-703.
    • (2011) FEBS J. , vol.278 , pp. 687-703
    • Kwan, A.H.1    Mobli, M.2    Gooley, P.R.3    King, G.F.4    Mackay, J.P.5
  • 118
    • 84855959081 scopus 로고    scopus 로고
    • Heat-shock protein fusion vectors for improved expression of soluble recombinant proteins in Escherichia coli
    • Kyratsous, C. A. & Panagiotidis, C. A. (2012). Heat-shock protein fusion vectors for improved expression of soluble recombinant proteins in Escherichia coli. Methods Mol. Biol. 824, 109-129.
    • (2012) Methods Mol. Biol. , vol.824 , pp. 109-129
    • Kyratsous, C.A.1    Panagiotidis, C.A.2
  • 119
    • 67349207064 scopus 로고    scopus 로고
    • Chaperone-fusion expression plasmid vectors for improved solubility of recombinant proteins in Escherichia coli
    • Kyratsous, C. A., Silverstein, S. J., DeLong, C. R. & Panagiotidis, C. A. (2009). Chaperone-fusion expression plasmid vectors for improved solubility of recombinant proteins in Escherichia coli. Gene, 440, 9-15.
    • (2009) Gene , vol.440 , pp. 9-15
    • Kyratsous, C.A.1    Silverstein, S.J.2    DeLong, C.R.3    Panagiotidis, C.A.4
  • 121
    • 79960692993 scopus 로고    scopus 로고
    • Quantitation of protein-protein interactions by thermal stability shift analysis
    • Layton, C. J. & Hellinga, H. W. (2011). Quantitation of protein-protein interactions by thermal stability shift analysis. Protein Sci. 20, 1439-1450.
    • (2011) Protein Sci. , vol.20 , pp. 1439-1450
    • Layton, C.J.1    Hellinga, H.W.2
  • 122
    • 0037438567 scopus 로고    scopus 로고
    • Thermodynamics of protein folding: A microscopic view
    • Lazaridis, T. & Karplus, M. (2002). Thermodynamics of protein folding: A microscopic view. Biophys. Chem. 100, 367-395.
    • (2002) Biophys. Chem. , vol.100 , pp. 367-395
    • Lazaridis, T.1    Karplus, M.2
  • 123
    • 84871457453 scopus 로고    scopus 로고
    • Stabilizing additives added during cell lysis aid in the solubilization of recombinant proteins
    • Leibly, D. J., Nguyen, T. N., Kao, L. T., Hewitt, S. N., Barrett, L. K. & Van Voorhis, W. C. (2012). Stabilizing additives added during cell lysis aid in the solubilization of recombinant proteins. PLoS One, 7, e52482.
    • (2012) PLoS One , vol.7 , pp. e52482
    • Leibly, D.J.1    Nguyen, T.N.2    Kao, L.T.3    Hewitt, S.N.4    Barrett, L.K.5    Van Voorhis, W.C.6
  • 124
    • 0030015420 scopus 로고    scopus 로고
    • Helical, but not-sheet, propensity of proline is determined by peptide environment
    • Li, S.-C., Goto, N. K., Williams, K. A. & Deber, C. M. (1996).-Helical, but not-sheet, propensity of proline is determined by peptide environment. Proc. Natl Acad. Sci. USA, 93, 6676-6681.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6676-6681
    • Li, S.-C.1    Goto, N.K.2    Williams, K.A.3    Deber, C.M.4
  • 126
    • 84958669304 scopus 로고    scopus 로고
    • Cleavable selfaggregating tags (cSAT) for protein expression and purification
    • Lin, Z., Zhao, Q., Zhou, B., Xing, L. & Xu, W. (2015). Cleavable selfaggregating tags (cSAT) for protein expression and purification. Methods Mol. Biol. 1258, 65-78.
    • (2015) Methods Mol. Biol. , vol.1258 , pp. 65-78
    • Lin, Z.1    Zhao, Q.2    Zhou, B.3    Xing, L.4    Xu, W.5
  • 127
    • 71049135717 scopus 로고    scopus 로고
    • Insights into protein aggregation by NMR characterization of insoluble SH3 mutants solubilized in salt-free water
    • Liu, J. & Song, J. (2009). Insights into protein aggregation by NMR characterization of insoluble SH3 mutants solubilized in salt-free water. PLoS One, 4, e7805.
    • (2009) PLoS One , vol.4 , pp. e7805
    • Liu, J.1    Song, J.2
  • 129
    • 84901017485 scopus 로고    scopus 로고
    • Advantages of proteins being disordered
    • Liu, Z. & Huang, Y. (2014). Advantages of proteins being disordered. Protein Sci. 23, 539-550.
    • (2014) Protein Sci. , vol.23 , pp. 539-550
    • Liu, Z.1    Huang, Y.2
  • 130
    • 84896055636 scopus 로고    scopus 로고
    • Western blot: Technique, theory and trouble shooting
    • Liu, Z.-Q., Mahmood, T. & Yang, P.-C. (2014). Western blot: technique, theory and trouble shooting. N. Am. J. Med. Sci. 6, 160.
    • (2014) N. Am. J. Med. Sci. , vol.6 , pp. 160
    • Liu, Z.-Q.1    Mahmood, T.2    Yang, P.-C.3
  • 131
    • 0035024436 scopus 로고    scopus 로고
    • Protein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI
    • Longenecker, K. L., Garrard, S. M., Sheffield, P. J. & Derewenda, Z. S. (2001). Protein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI. Acta Cryst. D57, 679-688.
    • (2001) Acta Cryst. D , vol.57 , pp. 679-688
    • Longenecker, K.L.1    Garrard, S.M.2    Sheffield, P.J.3    Derewenda, Z.S.4
  • 134
    • 33749536025 scopus 로고    scopus 로고
    • A serendipitous discovery that in situ proteolysis is essential for the crystallization of yeast CPSF-100 (Ydh1p)
    • Mandel, C. R., Gebauer, D., Zhang, H. & Tong, L. (2006). A serendipitous discovery that in situ proteolysis is essential for the crystallization of yeast CPSF-100 (Ydh1p). Acta Cryst. F62, 1041-1045.
    • (2006) Acta Cryst. F , vol.62 , pp. 1041-1045
    • Mandel, C.R.1    Gebauer, D.2    Zhang, H.3    Tong, L.4
  • 135
    • 84908082308 scopus 로고    scopus 로고
    • Fluorinated proteins: From design and synthesis to structure and stability
    • Marsh, E. N. (2014). Fluorinated proteins: from design and synthesis to structure and stability. Acc. Chem. Res. 47, 2878-2886.
    • (2014) Acc. Chem. Res. , vol.47 , pp. 2878-2886
    • Marsh, E.N.1
  • 136
    • 0036900352 scopus 로고    scopus 로고
    • The impact of Glu!Ala and Glu!Asp mutations on the crystallization properties of RhoGDI: The structure of RhoGDI at 1.3 A resolution
    • Mateja, A., Devedjiev, Y., Krowarsch, D., Longenecker, K., Dauter, Z., Otlewski, J. & Derewenda, Z. S. (2002). The impact of Glu!Ala and Glu!Asp mutations on the crystallization properties of RhoGDI: The structure of RhoGDI at 1.3 A resolution. Acta Cryst. D58, 1983-1991.
    • (2002) Acta Cryst. D , vol.58 , pp. 1983-1991
    • Mateja, A.1    Devedjiev, Y.2    Krowarsch, D.3    Longenecker, K.4    Dauter, Z.5    Otlewski, J.6    Derewenda, Z.S.7
  • 138
    • 33751000441 scopus 로고    scopus 로고
    • Searching for silver bullets: An alternative strategy for crystallizing macromolecules
    • McPherson, A. & Cudney, B. (2006). Searching for silver bullets: an alternative strategy for crystallizing macromolecules. J. Struct. Biol. 156, 387-406.
    • (2006) J. Struct. Biol. , vol.156 , pp. 387-406
    • McPherson, A.1    Cudney, B.2
  • 139
    • 0017731504 scopus 로고
    • Reductive alkylation of amino groups
    • Means, G. E. (1977). Reductive alkylation of amino groups. Methods Enzymol. 47, 469-478.
    • (1977) Methods Enzymol. , vol.47 , pp. 469-478
    • Means, G.E.1
  • 140
    • 0032510739 scopus 로고    scopus 로고
    • The amino acid following an Asn-X-Ser/Thr sequon is an important determinant of N-linked core glycosylation efficiency
    • Mellquist, J. L., Kasturi, L., Spitalnik, S. L. & Shakin-Eshleman, S. H. (1998). The amino acid following an Asn-X-Ser/Thr sequon is an important determinant of N-linked core glycosylation efficiency. Biochemistry, 37, 6833-6837.
    • (1998) Biochemistry , vol.37 , pp. 6833-6837
    • Mellquist, J.L.1    Kasturi, L.2    Spitalnik, S.L.3    Shakin-Eshleman, S.H.4
  • 141
    • 84901468888 scopus 로고    scopus 로고
    • Protein splicing: How inteins escape from precursor proteins
    • Mills, K. V., Johnson, M. A. & Perler, F. B. (2014). Protein splicing: how inteins escape from precursor proteins. J. Biol. Chem. 289, 14498-14505.
    • (2014) J. Biol. Chem. , vol.289 , pp. 14498-14505
    • Mills, K.V.1    Johnson, M.A.2    Perler, F.B.3
  • 142
    • 70349964409 scopus 로고    scopus 로고
    • Meta prediction of protein crystallization propensity
    • Mizianty, M. J. & Kurgan, L. (2009). Meta prediction of protein crystallization propensity. Biochem. Biophys. Res. Commun. 390, 10-15.
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 10-15
    • Mizianty, M.J.1    Kurgan, L.2
  • 143
    • 84907882545 scopus 로고    scopus 로고
    • Prediction of intrinsic disorder in proteins using MFDp2
    • Mizianty, M. J., Uversky, V. & Kurgan, L. (2014). Prediction of intrinsic disorder in proteins using MFDp2. Methods Mol. Biol. 1137, 147-162.
    • (2014) Methods Mol. Biol. , vol.1137 , pp. 147-162
    • Mizianty, M.J.1    Uversky, V.2    Kurgan, L.3
  • 144
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J. & Changeux, J.-P. (1965). On the nature of allosteric transitions: A plausible model. J. Mol. Biol. 12, 88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 145
    • 77951587361 scopus 로고    scopus 로고
    • A synergistic approach to protein crystallization: Combination of a fixed-arm carrier with surface entropy reduction
    • Moon, A. F., Mueller, G. A., Zhong, X. & Pedersen, L. C. (2010). A synergistic approach to protein crystallization: combination of a fixed-arm carrier with surface entropy reduction. Protein Sci. 19, 901-913.
    • (2010) Protein Sci. , vol.19 , pp. 901-913
    • Moon, A.F.1    Mueller, G.A.2    Zhong, X.3    Pedersen, L.C.4
  • 146
    • 84958055228 scopus 로고    scopus 로고
    • Differential scanning calorimetry (DSC) for biopharmaceutical development: Old concepts, new applications
    • Morar-Mitrica, S., Nesta, D. & Crotts, G. (2013). Differential scanning calorimetry (DSC) for biopharmaceutical development: old concepts, new applications. BioPharma Asia, 2(4), 44-55.
    • (2013) BioPharma Asia , vol.2 , Issue.4 , pp. 44-55
    • Morar-Mitrica, S.1    Nesta, D.2    Crotts, G.3
  • 147
    • 84943791270 scopus 로고    scopus 로고
    • Preparation of crystalline samples of amyloid fibrils and oligomers
    • Moshe, A., Landau, M. & Eisenberg, D. (2016). Preparation of crystalline samples of amyloid fibrils and oligomers. Methods Mol. Biol. 1345, 201-210.
    • (2016) Methods Mol. Biol. , vol.1345 , pp. 201-210
    • Moshe, A.1    Landau, M.2    Eisenberg, D.3
  • 153
    • 84867743209 scopus 로고    scopus 로고
    • Time-resolved structural studies at synchrotrons and X-ray free electron lasers: Opportunities and challenges
    • Neutze, R. & Moffat, K. (2012). Time-resolved structural studies at synchrotrons and X-ray free electron lasers: opportunities and challenges. Curr. Opin. Struct. Biol. 22, 651-659.
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 651-659
    • Neutze, R.1    Moffat, K.2
  • 154
    • 84901468696 scopus 로고    scopus 로고
    • Enigmatic distribution, evolution, and function of inteins
    • Novikova, O., Topilina, N. & Belfort, M. (2014). Enigmatic distribution, evolution, and function of inteins. J. Biol. Chem. 289, 14490-14497.
    • (2014) J. Biol. Chem. , vol.289 , pp. 14490-14497
    • Novikova, O.1    Topilina, N.2    Belfort, M.3
  • 155
    • 40949117264 scopus 로고    scopus 로고
    • Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners
    • Oldfield, C. J., Meng, J., Yang, J. Y., Yang, M. Q., Uversky, V. N. & Dunker, A. K. (2008). Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners. BMC Genomics, 9, S1.
    • (2008) BMC Genomics , vol.9 , pp. S1
    • Oldfield, C.J.1    Meng, J.2    Yang, J.Y.3    Yang, M.Q.4    Uversky, V.N.5    Dunker, A.K.6
  • 157
    • 20444486559 scopus 로고    scopus 로고
    • An inhibitor of Bcl-2 family proteins induces regression of solid tumours
    • Oltersdorf, T. et al. (2005). An inhibitor of Bcl-2 family proteins induces regression of solid tumours. Nature (London), 435, 677-681.
    • (2005) Nature (London) , vol.435 , pp. 677-681
    • Oltersdorf, T.1
  • 158
    • 41349121172 scopus 로고    scopus 로고
    • ParCrys: A Parzen window density estimation approach to protein crystallization propensity prediction
    • Overton, I. M., Padovani, G., Girolami, M. A. & Barton, G. J. (2008). ParCrys: A Parzen window density estimation approach to protein crystallization propensity prediction. Bioinformatics, 24, 901-907.
    • (2008) Bioinformatics , vol.24 , pp. 901-907
    • Overton, I.M.1    Padovani, G.2    Girolami, M.A.3    Barton, G.J.4
  • 159
    • 79952488138 scopus 로고    scopus 로고
    • XANNpred: Neural nets that predict the propensity of a protein to yield diffraction-quality crystals
    • Overton, I. M., van Niekerk, C. A. & Barton, G. J. (2011). XANNpred: neural nets that predict the propensity of a protein to yield diffraction-quality crystals. Proteins, 79, 1027-1033.
    • (2011) Proteins , vol.79 , pp. 1027-1033
    • Overton, I.M.1    Van Niekerk, C.A.2    Barton, G.J.3
  • 161
    • 84901012002 scopus 로고    scopus 로고
    • Contribution of hydrogen bonds to protein stability
    • Pace, C. N., Fu, H. et al. (2014). Contribution of hydrogen bonds to protein stability. Protein Sci. 23, 652-661.
    • (2014) Protein Sci. , vol.23 , pp. 652-661
    • Pace, C.N.1    Et, Al. F.H.2
  • 164
    • 1642514905 scopus 로고    scopus 로고
    • Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange MS
    • Pantazatos, D., Kim, J. S., Klock, H. E., Stevens, R. C., Wilson, I. A., Lesley, S. A. & Woods, V. L. Jr (2004). Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange MS. Proc. Natl Acad. Sci. USA, 101, 751-756.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 751-756
    • Pantazatos, D.1    Kim, J.S.2    Klock, H.E.3    Stevens, R.C.4    Wilson, I.A.5    Lesley, S.A.6    Woods, V.L.7
  • 165
    • 84888323401 scopus 로고    scopus 로고
    • Statistical approaches to maximize recombinant protein expression in Escherichia coli: A general review
    • Papaneophytou, C. P. & Kontopidis, G. (2014). Statistical approaches to maximize recombinant protein expression in Escherichia coli: A general review. Protein Expr. Purif. 94, 22-32.
    • (2014) Protein Expr. Purif. , vol.94 , pp. 22-32
    • Papaneophytou, C.P.1    Kontopidis, G.2
  • 166
    • 77953039922 scopus 로고    scopus 로고
    • Functional significance of eIF5A and its hypusine modification in eukaryotes
    • Park, M. H., Nishimura, K., Zanelli, C. F. & Valentini, S. R. (2010). Functional significance of eIF5A and its hypusine modification in eukaryotes. Amino Acids, 38, 491-500.
    • (2010) Amino Acids , vol.38 , pp. 491-500
    • Park, M.H.1    Nishimura, K.2    Zanelli, C.F.3    Valentini, S.R.4
  • 167
    • 76549252207 scopus 로고
    • The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain
    • Pauling, L., Corey, R. B. & Branson, H. R. (1951). The structure of proteins: two hydrogen-bonded helical configurations of the polypeptide chain. Proc. Natl Acad. Sci. USA, 37, 205-211.
    • (1951) Proc. Natl Acad. Sci. USA , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 168
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • Paulus, H. (2000). Protein splicing and related forms of protein autoprocessing. Annu. Rev. Biochem. 69, 447-496.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 447-496
    • Paulus, H.1
  • 169
    • 0034650323 scopus 로고    scopus 로고
    • Spectroscopic methods for analysis of protein secondary structure
    • Pelton, J. T. & McLean, L. R. (2000). Spectroscopic methods for analysis of protein secondary structure. Anal. Biochem. 277, 167-176.
    • (2000) Anal. Biochem. , vol.277 , pp. 167-176
    • Pelton, J.T.1    McLean, L.R.2
  • 170
    • 33846637900 scopus 로고    scopus 로고
    • Microcalorimetry of biological macromolecules
    • Privalov, P. L. & Dragan, A. I. (2007). Microcalorimetry of biological macromolecules. Biophys. Chem. 126, 16-24.
    • (2007) Biophys. Chem. , vol.126 , pp. 16-24
    • Privalov, P.L.1    Dragan, A.I.2
  • 171
    • 0013905904 scopus 로고
    • Correlation between the distribution of amino acids and alpha helices
    • Prothero, J. W. (1966). Correlation between the distribution of amino acids and alpha helices. Biophys. J. 6, 367-370.
    • (1966) Biophys. J. , vol.6 , pp. 367-370
    • Prothero, J.W.1
  • 172
    • 84923172318 scopus 로고    scopus 로고
    • A native-like SOSIP.664 trimer based on an HIV-1 subtype B env gene
    • Pugach, P. et al. (2015). A native-like SOSIP.664 trimer based on an HIV-1 subtype B env gene. J. Virol. 89, 3380-3395.
    • (2015) J. Virol. , vol.89 , pp. 3380-3395
    • Pugach, P.1
  • 173
    • 0029965591 scopus 로고    scopus 로고
    • Glycosylation defect in Lec1 Chinese hamster ovary mutant is due to a point mutation in N-acetylglucosaminyltransferase i gene
    • Puthalakath, H., Burke, J. & Gleeson, P. A. (1996). Glycosylation defect in Lec1 Chinese hamster ovary mutant is due to a point mutation in N-acetylglucosaminyltransferase I gene. J. Biol. Chem. 271, 27818-27822.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27818-27822
    • Puthalakath, H.1    Burke, J.2    Gleeson, P.A.3
  • 175
    • 84908636980 scopus 로고    scopus 로고
    • A disulfide polymerized protein crystal
    • Quistgaard, E. M. (2014). A disulfide polymerized protein crystal. Chem. Commun. 50, 14995-14997.
    • (2014) Chem. Commun. , vol.50 , pp. 14995-14997
    • Quistgaard, E.M.1
  • 176
    • 53249154203 scopus 로고    scopus 로고
    • Function and regulation of protein neddylation
    • Rabut, G. & Peter, M. (2008). Function and regulation of protein neddylation. EMBO Rep. 9, 969-976.
    • (2008) EMBO Rep. , vol.9 , pp. 969-976
    • Rabut, G.1    Peter, M.2
  • 178
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves, P. J., Callewaert, N., Contreras, R. & Khorana, H. G. (2002). Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc. Natl Acad. Sci. USA, 99, 13419-13424.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 179
    • 0036899405 scopus 로고    scopus 로고
    • Application of NMR in structural proteomics: Screening for proteins amenable to structural analysis
    • Rehm, T., Huber, R. & Holak, T. A. (2002). Application of NMR in structural proteomics: screening for proteins amenable to structural analysis. Structure, 10, 1613-1618.
    • (2002) Structure , vol.10 , pp. 1613-1618
    • Rehm, T.1    Huber, R.2    Holak, T.A.3
  • 183
    • 0017375309 scopus 로고
    • Stabilization of bovine trypsin by reductive methylation
    • Rice, R. H., Means, G. E. & Brown, W. D. (1977). Stabilization of bovine trypsin by reductive methylation. Biochim. Biophys. Acta, 492, 316-321.
    • (1977) Biochim. Biophys. Acta , vol.492 , pp. 316-321
    • Rice, R.H.1    Means, G.E.2    Brown, W.D.3
  • 184
    • 0030690394 scopus 로고    scopus 로고
    • Protein stability: Still an unsolved problem
    • Richards, F. M. (1997). Protein stability: still an unsolved problem. Cell. Mol. Life Sci. 53, 790-802.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 790-802
    • Richards, F.M.1
  • 185
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J. S. (1981). The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34, 167-339.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 186
    • 84944182881 scopus 로고    scopus 로고
    • Formulation screening by differential scanning fluorimetry: How often does it work?
    • Ristic, M., Rosa, N., Seabrook, S. A. & Newman, J. (2015). Formulation screening by differential scanning fluorimetry: how often does it work? Acta Cryst. F71, 1359-1364.
    • (2015) Acta Cryst. F , vol.71 , pp. 1359-1364
    • Ristic, M.1    Rosa, N.2    Seabrook, S.A.3    Newman, J.4
  • 187
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers, S., Wells, R. & Rechsteiner, M. (1986). Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis. Science, 234, 364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 188
    • 84884658112 scopus 로고    scopus 로고
    • Tertiary and quaternary effects in the allosteric regulation of animal hemoglobins
    • Ronda, L., Bruno, S. & Bettati, S. (2013). Tertiary and quaternary effects in the allosteric regulation of animal hemoglobins. Biochim. Biophys. Acta, 1834, 1860-1872.
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 1860-1872
    • Ronda, L.1    Bruno, S.2    Bettati, S.3
  • 189
    • 84937821831 scopus 로고    scopus 로고
    • Meltdown: A tool to help in the interpretation of thermal melt curves acquired by differential scanning fluorimetry
    • Rosa, N., Ristic, M., Seabrook, S. A., Lovell, D., Lucent, D. & Newman, J. (2015). Meltdown: A tool to help in the interpretation of thermal melt curves acquired by differential scanning fluorimetry. J. Biomol. Screen. 20, 898-905.
    • (2015) J. Biomol. Screen. , vol.20 , pp. 898-905
    • Rosa, N.1    Ristic, M.2    Seabrook, S.A.3    Lovell, D.4    Lucent, D.5    Newman, J.6
  • 190
    • 84863769912 scopus 로고    scopus 로고
    • Enhanced crystallizability by protein engineering approaches: A general overview
    • Ruggiero, A., Smaldone, G., Squeglia, F. & Berisio, R. (2012). Enhanced crystallizability by protein engineering approaches: A general overview. Protein Pept. Lett. 19, 732-742.
    • (2012) Protein Pept. Lett. , vol.19 , pp. 732-742
    • Ruggiero, A.1    Smaldone, G.2    Squeglia, F.3    Berisio, R.4
  • 191
    • 84924678731 scopus 로고    scopus 로고
    • Origin and use of crystallization phase diagrams
    • Rupp, B. (2015). Origin and use of crystallization phase diagrams. Acta Cryst. F71, 247-260.
    • (2015) Acta Cryst. F , vol.71 , pp. 247-260
    • Rupp, B.1
  • 192
    • 0029203156 scopus 로고
    • Differential scanning calorimetry of proteins
    • Sanchez-Ruiz, J. M. (1995). Differential scanning calorimetry of proteins. Subcell. Biochem. 24, 133-176.
    • (1995) Subcell. Biochem. , vol.24 , pp. 133-176
    • Sanchez-Ruiz, J.M.1
  • 195
    • 67349208429 scopus 로고    scopus 로고
    • The threedimensional structure of a mycobacterial DapD provides insights into DapD diversity and reveals unexpected particulars about the enzymatic mechanism
    • Schuldt, L., Weyand, S., Kefala, G. & Weiss, M. S. (2009). The threedimensional structure of a mycobacterial DapD provides insights into DapD diversity and reveals unexpected particulars about the enzymatic mechanism. J. Mol. Biol. 389, 863-879.
    • (2009) J. Mol. Biol. , vol.389 , pp. 863-879
    • Schuldt, L.1    Weyand, S.2    Kefala, G.3    Weiss, M.S.4
  • 196
    • 84881486856 scopus 로고    scopus 로고
    • High-throughput thermal scanning for protein stability: Making a good technique more robust
    • Seabrook, S. A. & Newman, J. (2013). High-throughput thermal scanning for protein stability: making a good technique more robust. ACS Comb. Sci. 15, 387-392.
    • (2013) ACS Comb. Sci. , vol.15 , pp. 387-392
    • Seabrook, S.A.1    Newman, J.2
  • 197
    • 79953655080 scopus 로고    scopus 로고
    • Recent advances in the therapeutic perspectives of nutlin-3
    • Secchiero, P., Bosco, R., Celeghini, C. & Zauli, G. (2011). Recent advances in the therapeutic perspectives of nutlin-3. Curr. Pharm. Des. 17, 569-577.
    • (2011) Curr. Pharm. Des. , vol.17 , pp. 569-577
    • Secchiero, P.1    Bosco, R.2    Celeghini, C.3    Zauli, G.4
  • 198
    • 84947751326 scopus 로고    scopus 로고
    • Hepatitis B virus core protein phosphorylation sites affect capsid stability and transient exposure of the C-terminal domain
    • Selzer, L., Kant, R., Wang, J. C., Bothner, B. & Zlotnick, A. (2015). Hepatitis B virus core protein phosphorylation sites affect capsid stability and transient exposure of the C-terminal domain. J. Biol. Chem. 290, 28584-28593
    • (2015) J. Biol. Chem. , vol.290 , pp. 28584-28593
    • Selzer, L.1    Kant, R.2    Wang, J.C.3    Bothner, B.4    Zlotnick, A.5
  • 199
  • 200
    • 35648936537 scopus 로고    scopus 로고
    • A structural hypothesis for the transition between bent and extended conformations of the leukocyte 2 integrins
    • Shi,M., Foo, S. Y., Tan, S.-M., Mitchell, E. P., Law, S. K. A. & Lescar, J. (2007). A structural hypothesis for the transition between bent and extended conformations of the leukocyte 2 integrins. J. Biol. Chem. 282, 30198-30206.
    • (2007) J. Biol. Chem. , vol.282 , pp. 30198-30206
    • Shi, M.1    Foo, S.Y.2    Tan, S.-M.3    Mitchell, E.P.4    Law, S.K.A.5    Lescar, J.6
  • 201
    • 84907873312 scopus 로고    scopus 로고
    • POODLE: Tools predicting intrinsically disordered regions of amino acid sequence
    • Shimizu, K. (2014). POODLE: tools predicting intrinsically disordered regions of amino acid sequence. Methods Mol. Biol. 1137, 131-145.
    • (2014) Methods Mol. Biol. , vol.1137 , pp. 131-145
    • Shimizu, K.1
  • 202
    • 0033595636 scopus 로고    scopus 로고
    • The PEST domain of IB is necessary and sufficient for in vitro degradation by-calpain
    • Shumway, S. D., Maki, M. & Miyamoto, S. (1999). The PEST domain of IB is necessary and sufficient for in vitro degradation by-calpain. J. Biol. Chem. 274, 30874-30881.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30874-30881
    • Shumway, S.D.1    Maki, M.2    Miyamoto, S.3
  • 203
    • 78149234277 scopus 로고    scopus 로고
    • CARON-average RMSD of NMR structure ensembles
    • Sikic, K. & Carugo, O. (2009). CARON-average RMSD of NMR structure ensembles. Bioinformation, 4, 132-133.
    • (2009) Bioinformation , vol.4 , pp. 132-133
    • Sikic, K.1    Carugo, O.2
  • 205
    • 77953984062 scopus 로고    scopus 로고
    • New surface contacts formed upon reductive lysine methylation: Improving the probability of protein crystallization
    • Sledz, P., Zheng, H., Murzyn, K., Chruszcz, M., Zimmerman, M. D., Chordia, M. D., Joachimiak, A. & Minor, W. (2010). New surface contacts formed upon reductive lysine methylation: improving the probability of protein crystallization. Protein Sci. 19, 1395-1404.
    • (2010) Protein Sci. , vol.19 , pp. 1395-1404
    • Sledz, P.1    Zheng, H.2    Murzyn, K.3    Chruszcz, M.4    Zimmerman, M.D.5    Chordia, M.D.6    Joachimiak, A.7    Minor, W.8
  • 206
    • 77958477970 scopus 로고    scopus 로고
    • Modulation of integrin activation by an entropic spring in the-knee
    • Smagghe, B. J., Huang, P.-S., Ban, Y.-E. A., Baker, D. & Springer, T. A. (2010). Modulation of integrin activation by an entropic spring in the-knee. J. Biol. Chem. 285, 32954-32966.
    • (2010) J. Biol. Chem. , vol.285 , pp. 32954-32966
    • Smagghe, B.J.1    Huang, P.-S.2    Ban, Y.-E.A.3    Baker, D.4    Springer, T.A.5
  • 208
    • 0028175780 scopus 로고
    • A thermodynamic scale for the-sheet forming tendencies of the amino acids
    • Smith, C. K., Withka, J. M. & Regan, L. (1994). A thermodynamic scale for the-sheet forming tendencies of the amino acids. Biochemistry, 33, 5510-5517.
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 209
    • 0035836456 scopus 로고    scopus 로고
    • The binding of bis-ANS to the isolated GroEL apical domain fragment induces the formation of a folding intermediate with increased hydrophobic surface not observed in tetradecameric GroEL
    • Smoot, A. L., Panda, M., Brazil, B. T., Buckle, A. M., Fersht, A. R. & Horowitz, P. M. (2001). The binding of bis-ANS to the isolated GroEL apical domain fragment induces the formation of a folding intermediate with increased hydrophobic surface not observed in tetradecameric GroEL. Biochemistry, 40, 4484-4492.
    • (2001) Biochemistry , vol.40 , pp. 4484-4492
    • Smoot, A.L.1    Panda, M.2    Brazil, B.T.3    Buckle, A.M.4    Fersht, A.R.5    Horowitz, P.M.6
  • 211
    • 8444219763 scopus 로고    scopus 로고
    • Adaptation of enzymes to temperature: Searching for basic 'strategies'
    • Somero, G. N. (2004). Adaptation of enzymes to temperature: searching for basic 'strategies'. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 139, 321-333.
    • (2004) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.139 , pp. 321-333
    • Somero, G.N.1
  • 212
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • Sørensen, H. P. & Mortensen, K. K. (2005). Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotechnol. 115, 113-128.
    • (2005) J. Biotechnol. , vol.115 , pp. 113-128
    • Sørensen, H.P.1    Mortensen, K.K.2
  • 213
    • 84866315674 scopus 로고    scopus 로고
    • X-ray lasers for structural and dynamic biology
    • Spence, J. C.,Weierstall, U. & Chapman, H. N. (2012). X-ray lasers for structural and dynamic biology. Rep. Prog. Phys. 75, 102601.
    • (2012) Rep. Prog. Phys. , vol.75 , pp. 102601
    • Spence, J.C.1    Weierstall, U.2    Chapman, H.N.3
  • 214
    • 4344691452 scopus 로고    scopus 로고
    • NPDC-1, a novel regulator of neuronal proliferation, is degraded by the ubiquitin/proteasome system through a PEST degradation motif
    • Spencer, M. L., Theodosiou, M. & Noonan, D. J. (2004). NPDC-1, a novel regulator of neuronal proliferation, is degraded by the ubiquitin/proteasome system through a PEST degradation motif. J. Biol. Chem. 279, 37069-37078.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37069-37078
    • Spencer, M.L.1    Theodosiou, M.2    Noonan, D.J.3
  • 216
    • 9344256689 scopus 로고    scopus 로고
    • On the use of DXMS to produce more crystallizable proteins: Structures of the T. Maritima proteins TM0160 and TM1171
    • Spraggon, G., Pantazatos, D., Klock, H. E.,Wilson, I. A.,Woods, V. L. Jr & Lesley, S. A. (2004). On the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171. Protein Sci. 13, 3187-3199.
    • (2004) Protein Sci. , vol.13 , pp. 3187-3199
    • Spraggon, G.1    Pantazatos, D.2    Klock, H.E.3    Wilson, I.A.4    Woods, V.L.5    Lesley, S.A.6
  • 218
  • 219
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier, F.W. (1991). Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J. Mol. Biol. 219, 37-44.
    • (1991) J. Mol. Biol. , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 220
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • Sugase, K., Dyson, H. J. & Wright, P. E. (2007). Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature (London), 447, 1021-1025.
    • (2007) Nature (London) , vol.447 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 221
    • 84913558113 scopus 로고    scopus 로고
    • Comparative studies on detergent-assisted apocytochrome b6 reconstitution into liposomal bilayers monitored by zetasizer instruments
    • Surma, M. A., Szczepaniak, A. & Króliczewski, J. (2014). Comparative studies on detergent-assisted apocytochrome b6 reconstitution into liposomal bilayers monitored by zetasizer instruments. PLoS One, 9, e111341.
    • (2014) PLoS One , vol.9 , pp. e111341
    • Surma, M.A.1    Szczepaniak, A.2    Króliczewski, J.3
  • 222
    • 84907933127 scopus 로고    scopus 로고
    • Salvage of failed protein targets by reductive alkylation
    • Tan, K. et al. (2014). Salvage of failed protein targets by reductive alkylation. Methods Mol. Biol. 1140, 189-200.
    • (2014) Methods Mol. Biol. , vol.1140 , pp. 189-200
    • Tan, K.1
  • 223
    • 0029936488 scopus 로고    scopus 로고
    • Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus d-glyceraldehyde-3-phosphate dehydrogenase at 2.5 A resolution
    • Tanner, J. J., Hecht, R. M. & Krause, K. L. (1996). Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus d-glyceraldehyde-3-phosphate dehydrogenase at 2.5 A resolution. Biochemistry, 35, 2597-2609.
    • (1996) Biochemistry , vol.35 , pp. 2597-2609
    • Tanner, J.J.1    Hecht, R.M.2    Krause, K.L.3
  • 224
    • 70449525585 scopus 로고    scopus 로고
    • Increased levels of recombinant human proteins with the Escherichia coli strain Rosetta(DE3)
    • Tegel, H., Tourle, S., Ottosson, J. & Persson, A. (2010). Increased levels of recombinant human proteins with the Escherichia coli strain Rosetta(DE3). Protein Expr. Purif. 69, 159-167.
    • (2010) Protein Expr. Purif. , vol.69 , pp. 159-167
    • Tegel, H.1    Tourle, S.2    Ottosson, J.3    Persson, A.4
  • 225
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA, 76, 4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 226
    • 84984876870 scopus 로고    scopus 로고
    • Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals
    • Uervirojnangkoorn, M., Zeldin, O. B., Lyubimov, A. Y., Hattne, J., Brewster, A. S., Sauter, N. K., Brunger, A. T. & Weis, W. I. (2015). Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals. Elife, 4, e05421.
    • (2015) Elife , vol.4 , pp. e05421
    • Uervirojnangkoorn, M.1    Zeldin, O.B.2    Lyubimov, A.Y.3    Hattne, J.4    Brewster, A.S.5    Sauter, N.K.6    Brunger, A.T.7    Weis, W.I.8
  • 227
    • 77949916296 scopus 로고    scopus 로고
    • Understanding protein nonfolding
    • Uversky, V. N. & Dunker, A. K. (2010). Understanding protein nonfolding. Biochim. Biophys. Acta, 1804, 1231-1264.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1231-1264
    • Uversky, V.N.1    Dunker, A.K.2
  • 228
    • 0031105876 scopus 로고    scopus 로고
    • Expression of aggregation-prone recombinant proteins at low temperatures: A comparative study of the Escherichia coli cspA and tac promoter systems
    • Vasina, J. A. & Baneyx, F. (1997). Expression of aggregation-prone recombinant proteins at low temperatures: A comparative study of the Escherichia coli cspA and tac promoter systems. Protein Expr. Purif. 9, 211-218.
    • (1997) Protein Expr. Purif. , vol.9 , pp. 211-218
    • Vasina, J.A.1    Baneyx, F.2
  • 229
    • 77957907731 scopus 로고    scopus 로고
    • Protein trans-splicing and its use in structural biology: Opportunities and limitations
    • Volkmann, G. & Iwaï, H. (2010). Protein trans-splicing and its use in structural biology: opportunities and limitations. Mol. Biosyst. 6, 2110-2121.
    • (2010) Mol. Biosyst. , vol.6 , pp. 2110-2121
    • Volkmann, G.1    Iwaï, H.2
  • 230
    • 84940502220 scopus 로고    scopus 로고
    • edited by E. Jaeschke, S. Khan, J. R. Schneider & J. B. Hastings. New York: Springer. In the press
    • Wakatsuki, S. (2016). In Synchrotron Light Sources and Free-Electron Lasers, edited by E. Jaeschke, S. Khan, J. R. Schneider & J. B. Hastings. New York: Springer. In the press.
    • (2016) Synchrotron Light Sources and Free-Electron Lasers
    • Wakatsuki, S.1
  • 231
    • 0035896551 scopus 로고    scopus 로고
    • On a potential global role for Vitamin K-dependent-carboxylation in animal systems: Evidence for a-glutamyl carboxylase in Drosophila
    • Walker, C. S., Shetty, R. P., Clark, K., Kazuko, S. G., Letsou, A., Olivera, B. M. & Bandyopadhyay, P. K. (2001). On a potential global role for vitamin K-dependent-carboxylation in animal systems: evidence for a-glutamyl carboxylase in Drosophila. J. Biol. Chem. 276, 7769-7774.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7769-7774
    • Walker, C.S.1    Shetty, R.P.2    Clark, K.3    Kazuko, S.G.4    Letsou, A.5    Olivera, B.M.6    Bandyopadhyay, P.K.7
  • 232
    • 77952363935 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism (SRCD) spectroscopy: An enhanced method for examining protein conformations and protein interactions
    • Wallace, B. A. & Janes, R. W. (2010). Synchrotron radiation circular dichroism (SRCD) spectroscopy: an enhanced method for examining protein conformations and protein interactions. Biochem. Soc. Trans. 38, 861-873.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 861-873
    • Wallace, B.A.1    Janes, R.W.2
  • 233
    • 79952200480 scopus 로고    scopus 로고
    • Tagging recombinant proteins to enhance solubility and aid purification
    • Walls, D. & Loughran, S. T. (2011). Tagging recombinant proteins to enhance solubility and aid purification. Methods Mol. Biol. 681, 151-175.
    • (2011) Methods Mol. Biol. , vol.681 , pp. 151-175
    • Walls, D.1    Loughran, S.T.2
  • 235
    • 79957846007 scopus 로고    scopus 로고
    • Novel strategies for drug discovery based on intrinsically disordered proteins (IDPs)
    • Wang, J., Cao, Z., Zhao, L. & Li, S. (2011). Novel strategies for drug discovery based on intrinsically disordered proteins (IDPs). Int. J. Mol. Sci. 12, 3205-3219.
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 3205-3219
    • Wang, J.1    Cao, Z.2    Zhao, L.3    Li, S.4
  • 237
    • 84940928861 scopus 로고    scopus 로고
    • The potential of future light sources to explore the structure and function of matter
    • Weckert, E. (2015). The potential of future light sources to explore the structure and function of matter. IUCrJ, 2, 230-245.
    • (2015) IUCrJ , vol.2 , pp. 230-245
    • Weckert, E.1
  • 238
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells, J. A. & McClendon, C. L. (2007). Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature (London), 450, 1001-1009.
    • (2007) Nature (London) , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 239
    • 64549153594 scopus 로고    scopus 로고
    • In situ proteolysis to generate crystals for structure determination: An update
    • Wernimont, A. & Edwards, A. (2009). In situ proteolysis to generate crystals for structure determination: an update. PLoS One, 4, e5094.
    • (2009) PLoS One , vol.4 , pp. e5094
    • Wernimont, A.1    Edwards, A.2
  • 240
    • 34447095724 scopus 로고    scopus 로고
    • Molecular gymnastics: Serpin structure, folding and misfolding
    • Whisstock, J. C. & Bottomley, S. P. (2006). Molecular gymnastics: serpin structure, folding and misfolding. Curr. Opin. Struct. Biol. 16, 761-768.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 761-768
    • Whisstock, J.C.1    Bottomley, S.P.2
  • 241
    • 0034681281 scopus 로고    scopus 로고
    • Conformational changes in serpins. I. The native and cleaved conformations of 1-antitrypsin
    • Whisstock, J. C., Skinner, R., Carrell, R. W. & Lesk, A. M. (2000). Conformational changes in serpins. I. The native and cleaved conformations of 1-antitrypsin. J. Mol. Biol. 296, 685-699.
    • (2000) J. Mol. Biol. , vol.296 , pp. 685-699
    • Whisstock, J.C.1    Skinner, R.2    Carrell, R.W.3    Lesk, A.M.4
  • 242
    • 0024414072 scopus 로고
    • Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolaminephosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha
    • Whiteheart, S. W., Shenbagamurthi, P., Chen, L., Cotter, R. J. & Hart, G. W. (1989). Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolaminephosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha. J. Biol. Chem. 264, 14334-14341.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14334-14341
    • Whiteheart, S.W.1    Shenbagamurthi, P.2    Chen, L.3    Cotter, R.J.4    Hart, G.W.5
  • 243
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore, L. & Wallace, B. A. (2008). Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers, 89, 392-400.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 244
    • 78651324803 scopus 로고    scopus 로고
    • PCDDB: The Protein Circular Dichroism Data Bank, a repository for circular dichroism spectral and metadata
    • Whitmore, L., Woollett, B., Miles, A. J., Klose, D. P., Janes, R. W. & Wallace, B. A. (2011). PCDDB: The Protein Circular Dichroism Data Bank, a repository for circular dichroism spectral and metadata. Nucleic Acids Res. 39, D480-D486.
    • (2011) Nucleic Acids Res. , vol.39 , pp. D480-D486
    • Whitmore, L.1    Woollett, B.2    Miles, A.J.3    Klose, D.P.4    Janes, R.W.5    Wallace, B.A.6
  • 246
    • 84901035269 scopus 로고    scopus 로고
    • New trends and affinity tag designs for recombinant protein purification
    • Wood, D. W. (2014). New trends and affinity tag designs for recombinant protein purification. Curr. Opin. Struct. Biol. 26, 54-61.
    • (2014) Curr. Opin. Struct. Biol. , vol.26 , pp. 54-61
    • Wood, D.W.1
  • 247
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P. E. & Dyson, H. J. (1999). Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293, 321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 248
    • 0028787430 scopus 로고
    • Why protein crystals favour some space groups over others
    • Wukovitz, S. W. & Yeates, T. O. (1995). Why protein crystals favour some space groups over others. Nature Struct. Mol. Biol. 2, 1062-1067.
    • (1995) Nature Struct. Mol. Biol. , vol.2 , pp. 1062-1067
    • Wukovitz, S.W.1    Yeates, T.O.2
  • 250
    • 55249111481 scopus 로고    scopus 로고
    • Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization
    • Yamasaki, M., Li, W., Johnson, D. J. & Huntington, J. A. (2008). Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Nature (London), 455, 1255-1258.
    • (2008) Nature (London) , vol.455 , pp. 1255-1258
    • Yamasaki, M.1    Li, W.2    Johnson, D.J.3    Huntington, J.A.4
  • 251
    • 33646252015 scopus 로고    scopus 로고
    • Rapid and simple protein-stability screens: Application to membrane proteins
    • Yeh, A. P.,McMillan, A. & Stowell,M. H. B. (2006). Rapid and simple protein-stability screens: application to membrane proteins. Acta Cryst. D62, 451-457.
    • (2006) Acta Cryst. D , vol.62 , pp. 451-457
    • Yeh, A.P.1    McMillan, A.2    Stowell, M.H.B.3
  • 252
    • 77956185960 scopus 로고    scopus 로고
    • ESPRIT: An automated, library-based method for mapping and soluble expression of protein domains from challenging targets
    • Yumerefendi, H., Tarendeau, F., Mas, P. J. & Hart, D. J. (2010). ESPRIT: an automated, library-based method for mapping and soluble expression of protein domains from challenging targets. J. Struct. Biol. 172, 66-74.
    • (2010) J. Struct. Biol. , vol.172 , pp. 66-74
    • Yumerefendi, H.1    Tarendeau, F.2    Mas, P.J.3    Hart, D.J.4
  • 253
    • 0025996871 scopus 로고
    • Proline in-helix: Stability and conformation studied by dynamics simulation
    • Yun, R. H., Anderson, A. & Hermans, J. (1991). Proline in-helix: stability and conformation studied by dynamics simulation. Proteins, 10, 219-228.
    • (1991) Proteins , vol.10 , pp. 219-228
    • Yun, R.H.1    Anderson, A.2    Hermans, J.3
  • 254
    • 84860903741 scopus 로고    scopus 로고
    • The ebola virus interferon antagonist VP24 directly binds STAT1 and has a novel, pyramidal fold
    • Zhang, A. P., Bornholdt, Z. A., Liu, T., Abelson, D. M., Lee, D. E., Li, S., Woods, V. L. Jr & Saphire, E. O. (2012). The ebola virus interferon antagonist VP24 directly binds STAT1 and has a novel, pyramidal fold. PLoS Pathog. 8, e1002550.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002550
    • Zhang, A.P.1    Bornholdt, Z.A.2    Liu, T.3    Abelson, D.M.4    Lee, D.E.5    Li, S.6    Woods, V.L.7    Saphire, E.O.8
  • 256
    • 84940928578 scopus 로고    scopus 로고
    • Architecture of the synaptotagmin-SNARE machinery for neuronal exocytosis
    • Zhou, Q. et al. (2015). Architecture of the synaptotagmin-SNARE machinery for neuronal exocytosis. Nature (London), 525, 62-67.
    • (2015) Nature (London) , vol.525 , pp. 62-67
    • Zhou, Q.1
  • 257
    • 38149111171 scopus 로고    scopus 로고
    • Differences in amino acids composition and coupling patterns between mesophilic and thermophilic proteins
    • Zhou, X.-X., Wang, Y.-B., Pan, Y.-J. & Li, W.-F. (2008). Differences in amino acids composition and coupling patterns between mesophilic and thermophilic proteins. Amino Acids, 34, 25-33.
    • (2008) Amino Acids , vol.34 , pp. 25-33
    • Zhou, X.-X.1    Wang, Y.-B.2    Pan, Y.-J.3    Li, W.-F.4
  • 258
    • 84867131783 scopus 로고    scopus 로고
    • N-Terminal T4 lysozyme fusion facilitates crystallization of a G protein coupled receptor
    • Zou, Y.,Weis, W. I. & Kobilka, B. K. (2012). N-Terminal T4 lysozyme fusion facilitates crystallization of a G protein coupled receptor. PLoS One, 7, e46039.
    • (2012) PLoS One , vol.7 , pp. e46039
    • Zou, Y.1    Weis, W.I.2    Kobilka, B.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.