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Volumn 24, Issue 22, 2014, Pages 2643-2651

A comprehensive biophysical description of pairwise epistasis throughout an entire protein domain

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; IGG FC-BINDING PROTEIN, STREPTOCOCCUS;

EID: 84923249936     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2014.09.072     Document Type: Article
Times cited : (230)

References (68)
  • 2
    • 0025912824 scopus 로고
    • Recent development of the neutral theory viewed from the Wrightian tradition of theoretical population genetics
    • Kimura, M. (1991). Recent development of the neutral theory viewed from the Wrightian tradition of theoretical population genetics. Proc. Natl. Acad. Sci. USA 88, 5969-5973.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5969-5973
    • Kimura, M.1
  • 3
    • 21044435697 scopus 로고    scopus 로고
    • Perspective: Sign epistasis and genetic constraint on evolutionary trajectories
    • Weinreich, D.M., Watson, R.A., and Chao, L. (2005). Perspective: sign epistasis and genetic constraint on evolutionary trajectories. Evolution 59, 1165-1174.
    • (2005) Evolution , vol.59 , pp. 1165-1174
    • Weinreich, D.M.1    Watson, R.A.2    Chao, L.3
  • 4
    • 77953718211 scopus 로고    scopus 로고
    • Sequence space and the ongoing expansion of the protein universe
    • Povolotskaya, I.S., and Kondrashov, F.A. (2010). Sequence space and the ongoing expansion of the protein universe. Nature 465, 922-926.
    • (2010) Nature , vol.465 , pp. 922-926
    • Povolotskaya, I.S.1    Kondrashov, F.A.2
  • 5
    • 84880862788 scopus 로고    scopus 로고
    • Evolutionary biochemistry: Revealing the historical and physical causes of protein properties
    • Harms, M.J., and Thornton, J.W. (2013). Evolutionary biochemistry: revealing the historical and physical causes of protein properties. Nat. Rev. Genet. 14, 559-571.
    • (2013) Nat. Rev. Genet , vol.14 , pp. 559-571
    • Harms, M.J.1    Thornton, J.W.2
  • 6
    • 70349464621 scopus 로고    scopus 로고
    • An epistatic ratchet constrains the direction of glucocorticoid receptor evolution
    • Bridgham, J.T., Ortlund, E.A., and Thornton, J.W. (2009). An epistatic ratchet constrains the direction of glucocorticoid receptor evolution. Nature 461, 515-519.
    • (2009) Nature , vol.461 , pp. 515-519
    • Bridgham, J.T.1    Ortlund, E.A.2    Thornton, J.W.3
  • 8
    • 33645666942 scopus 로고    scopus 로고
    • Darwinian evolution can follow only very few mutational paths to fitter proteins
    • Weinreich, D.M., Delaney, N.F., Depristo, M.A., and Hartl, D.L. (2006). Darwinian evolution can follow only very few mutational paths to fitter proteins. Science 312, 111-114.
    • (2006) Science , vol.312 , pp. 111-114
    • Weinreich, D.M.1    Delaney, N.F.2    Depristo, M.A.3    Hartl, D.L.4
  • 9
    • 79952270576 scopus 로고    scopus 로고
    • Prevalence of epistasis in the evolution of influenza A surface proteins
    • Kryazhimskiy, S., Dushoff, J., Bazykin, G.A., and Plotkin, J.B. (2011). Prevalence of epistasis in the evolution of influenza A surface proteins. PLoS Genet. 7, e1001301.
    • (2011) PLoS Genet , vol.7
    • Kryazhimskiy, S.1    Dushoff, J.2    Bazykin, G.A.3    Plotkin, J.B.4
  • 10
    • 84879064073 scopus 로고    scopus 로고
    • Stability-mediated epistasis constrains the evolution of an influenza protein
    • Gong, L.I., Suchard, M.A., and Bloom, J.D. (2013). Stability-mediated epistasis constrains the evolution of an influenza protein. Elife 2, e00631.
    • (2013) Elife , vol.2
    • Gong, L.I.1    Suchard, M.A.2    Bloom, J.D.3
  • 11
    • 33846515095 scopus 로고    scopus 로고
    • Thermodynamics of neutral protein evolution
    • Bloom, J.D., Raval, A., and Wilke, C.O. (2007). Thermodynamics of neutral protein evolution. Genetics 175, 255-266.
    • (2007) Genetics , vol.175 , pp. 255-266
    • Bloom, J.D.1    Raval, A.2    Wilke, C.O.3
  • 12
    • 34248674895 scopus 로고    scopus 로고
    • The stability effects of protein mutations appear to be universally distributed
    • Tokuriki, N., Stricher, F., Schymkowitz, J., Serrano, L., and Tawfik, D.S. (2007). The stability effects of protein mutations appear to be universally distributed. J. Mol. Biol. 369, 1318-1332.
    • (2007) J. Mol. Biol , vol.369 , pp. 1318-1332
    • Tokuriki, N.1    Stricher, F.2    Schymkowitz, J.3    Serrano, L.4    Tawfik, D.S.5
  • 13
    • 70450242805 scopus 로고    scopus 로고
    • Exploring protein fitness landscapes by directed evolution
    • Romero, P.A., and Arnold, F.H. (2009). Exploring protein fitness landscapes by directed evolution. Nat. Rev. Mol. Cell Biol. 10, 866-876.
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 866-876
    • Romero, P.A.1    Arnold, F.H.2
  • 14
    • 78449233935 scopus 로고    scopus 로고
    • Pervasive cryptic epistasis in molecular evolution
    • Lunzer, M., Golding, G.B., and Dean, A.M. (2010). Pervasive cryptic epistasis in molecular evolution. PLoS Genet. 6, e1001162.
    • (2010) PLoS Genet , vol.6
    • Lunzer, M.1    Golding, G.B.2    Dean, A.M.3
  • 15
    • 0025082684 scopus 로고
    • Additivity of mutational effects in proteins
    • Wells, J.A. (1990). Additivity of mutational effects in proteins. Biochemistry 29, 8509-8517.
    • (1990) Biochemistry , vol.29 , pp. 8509-8517
    • Wells, J.A.1
  • 16
    • 0027248706 scopus 로고
    • Engineering multiple properties of a protein by combinatorial mutagenesis
    • Sandberg, W.S., and Terwilliger, T.C. (1993). Engineering multiple properties of a protein by combinatorial mutagenesis. Proc. Natl. Acad. Sci. USA 90, 8367-8371.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8367-8371
    • Sandberg, W.S.1    Terwilliger, T.C.2
  • 17
    • 0027211894 scopus 로고
    • Additivity of mutant effects assessed by binomial mutagenesis
    • Gregoret, L.M., and Sauer, R.T. (1993). Additivity of mutant effects assessed by binomial mutagenesis. Proc. Natl. Acad. Sci. USA 90, 4246-4250.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4246-4250
    • Gregoret, L.M.1    Sauer, R.T.2
  • 18
    • 0028965496 scopus 로고
    • Long-range, small magnitude nonadditivity of mutational effects in proteins
    • LiCata, V.J., and Ackers, G.K. (1995). Long-range, small magnitude nonadditivity of mutational effects in proteins. Biochemistry 34, 3133-3139.
    • (1995) Biochemistry , vol.34 , pp. 3133-3139
    • Licata, V.J.1    Ackers, G.K.2
  • 19
    • 84867644046 scopus 로고    scopus 로고
    • A fundamental protein property, thermodynamic stability, revealed solely from large-scale measurements of protein function
    • Araya, C.L., Fowler, D.M., Chen, W.,Muniez, I., Kelly, J.W., and Fields, S. (2012). A fundamental protein property, thermodynamic stability, revealed solely from large-scale measurements of protein function. Proc. Natl. Acad. Sci. USA 109, 16858-16863.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 16858-16863
    • Araya, C.L.1    Fowler, D.M.2    Chen, W.3    Muniez, I.4    Kelly, J.W.5    Fields, S.6
  • 20
    • 84886037483 scopus 로고    scopus 로고
    • Deep mutational scanning of an RRM domain of the Saccharomyces cerevisiae poly(A)-binding protein
    • Melamed, D., Young, D.L., Gamble, C.E., Miller, C.R., and Fields, S. (2013). Deep mutational scanning of an RRM domain of the Saccharomyces cerevisiae poly(A)-binding protein. RNA 19, 1537-1551.
    • (2013) RNA , vol.19 , pp. 1537-1551
    • Melamed, D.1    Young, D.L.2    Gamble, C.E.3    Miller, C.R.4    Fields, S.5
  • 21
    • 0029644247 scopus 로고
    • Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG
    • Sauer-Eriksson, A.E., Kleywegt, G.J., Uhlén, M., and Jones, T.A. (1995). Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG. Structure 3, 265-278.
    • (1995) Structure , vol.3 , pp. 265-278
    • Sauer-Eriksson, A.E.1    Kleywegt, G.J.2    Uhlén, M.3    Jones, T.A.4
  • 22
    • 0033871567 scopus 로고    scopus 로고
    • Critical role of betahairpin formation in protein G folding
    • McCallister, E.L., Alm, E., and Baker, D. (2000). Critical role of betahairpin formation in protein G folding. Nat. Struct. Biol. 7, 669-673.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 669-673
    • McCallister, E.L.1    Alm, E.2    Baker, D.3
  • 23
    • 0031779918 scopus 로고    scopus 로고
    • Design, structure and stability of a hyperthermophilic protein variant
    • Malakauskas, S.M., and Mayo, S.L. (1998). Design, structure and stability of a hyperthermophilic protein variant. Nat. Struct. Biol. 5, 470-475.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 470-475
    • Malakauskas, S.M.1    Mayo, S.L.2
  • 24
    • 34748819310 scopus 로고    scopus 로고
    • Optimization of the gbeta1 domain by computational design and by in vitro evolution: Structural and energetic basis of stabilization
    • Wunderlich, M., Max, K.E., Roske, Y., Mueller, U., Heinemann, U., and Schmid, F.X. (2007). Optimization of the gbeta1 domain by computational design and by in vitro evolution: structural and energetic basis of stabilization. J. Mol. Biol. 373, 775-784.
    • (2007) J. Mol. Biol , vol.373 , pp. 775-784
    • Wunderlich, M.1    Max, K.E.2    Roske, Y.3    Mueller, U.4    Heinemann, U.5    Schmid, F.X.6
  • 26
    • 33845864966 scopus 로고    scopus 로고
    • Robustness-epistasis link shapes the fitness landscape of a randomly drifting protein
    • Bershtein, S., Segal, M., Bekerman, R., Tokuriki, N., and Tawfik, D.S. (2006). Robustness-epistasis link shapes the fitness landscape of a randomly drifting protein. Nature 444, 929-932.
    • (2006) Nature , vol.444 , pp. 929-932
    • Bershtein, S.1    Segal, M.2    Bekerman, R.3    Tokuriki, N.4    Tawfik, D.S.5
  • 27
    • 70349901079 scopus 로고    scopus 로고
    • Stability effects of mutations and protein evolvability
    • Tokuriki, N., and Tawfik, D.S. (2009). Stability effects of mutations and protein evolvability. Curr. Opin. Struct. Biol. 19, 596-604.
    • (2009) Curr. Opin. Struct. Biol , vol.19 , pp. 596-604
    • Tokuriki, N.1    Tawfik, D.S.2
  • 28
    • 33746799726 scopus 로고    scopus 로고
    • Comprehensive and quantitative mapping of energy landscapes for protein-protein interactions by rapid combinatorial scanning
    • Pál, G., Kouadio, J.L., Artis, D.R., Kossiakoff, A.A., and Sidhu, S.S. (2006). Comprehensive and quantitative mapping of energy landscapes for protein-protein interactions by rapid combinatorial scanning. J. Biol. Chem. 281, 22378-22385.
    • (2006) J. Biol. Chem , vol.281 , pp. 22378-22385
    • Pál, G.1    Kouadio, J.L.2    Artis, D.R.3    Kossiakoff, A.A.4    Sidhu, S.S.5
  • 31
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusions for the in vitro selection of peptides and proteins
    • Roberts, R.W., and Szostak, J.W. (1997). RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc. Natl. Acad. Sci. USA 94, 12297-12302.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2
  • 33
    • 77954743785 scopus 로고    scopus 로고
    • Mutational effects and the evolution of new protein functions
    • Soskine, M., and Tawfik, D.S. (2010). Mutational effects and the evolution of new protein functions. Nat. Rev. Genet. 11, 572-582.
    • (2010) Nat. Rev. Genet , vol.11 , pp. 572-582
    • Soskine, M.1    Tawfik, D.S.2
  • 34
    • 84901408859 scopus 로고    scopus 로고
    • A comprehensive, high-resolution map of a gene's fitness landscape
    • Firnberg, E., Labonte, J.W., Gray, J.J., and Ostermeier, M. (2014). A comprehensive, high-resolution map of a gene's fitness landscape. Mol. Biol. Evol. 31, 1581-1592.
    • (2014) Mol. Biol. Evol , vol.31 , pp. 1581-1592
    • Firnberg, E.1    Labonte, J.W.2    Gray, J.J.3    Ostermeier, M.4
  • 35
    • 84858611541 scopus 로고    scopus 로고
    • Mechanisms of host receptor adaptation by severe acute respiratory syndrome coronavirus
    • Wu, K., Peng, G., Wilken, M., Geraghty, R.J., and Li, F. (2012). Mechanisms of host receptor adaptation by severe acute respiratory syndrome coronavirus. J. Biol. Chem. 287, 8904-8911.
    • (2012) J. Biol. Chem , vol.287 , pp. 8904-8911
    • Wu, K.1    Peng, G.2    Wilken, M.3    Geraghty, R.J.4    Li, F.5
  • 36
    • 0028354429 scopus 로고
    • Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR
    • Gallagher, T., Alexander, P., Bryan, P., and Gilliland, G.L. (1994). Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR. Biochemistry 33, 4721-4729.
    • (1994) Biochemistry , vol.33 , pp. 4721-4729
    • Gallagher, T.1    Alexander, P.2    Bryan, P.3    Gilliland, G.L.4
  • 37
    • 0019332167 scopus 로고
    • How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globins
    • Lesk, A.M., and Chothia, C. (1980). How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins. J. Mol. Biol. 136, 225-270.
    • (1980) J. Mol. Biol , vol.136 , pp. 225-270
    • Lesk, A.M.1    Chothia, C.2
  • 38
    • 0141750578 scopus 로고    scopus 로고
    • The relationship between conservation, thermodynamic stability, and function in the SH3 domain hydrophobic core
    • Di Nardo, A.A., Larson, S.M., and Davidson, A.R. (2003). The relationship between conservation, thermodynamic stability, and function in the SH3 domain hydrophobic core. J. Mol. Biol. 333, 641-655.
    • (2003) J. Mol. Biol , vol.333 , pp. 641-655
    • Di Nardo, A.A.1    Larson, S.M.2    Davidson, A.R.3
  • 39
    • 0031893269 scopus 로고    scopus 로고
    • The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect
    • Xu, J., Baase, W.A., Baldwin, E., and Matthews, B.W. (1998). The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. Protein Sci. 7, 158-177.
    • (1998) Protein Sci , vol.7 , pp. 158-177
    • Xu, J.1    Baase, W.A.2    Baldwin, E.3    Matthews, B.W.4
  • 40
    • 0032777649 scopus 로고    scopus 로고
    • Dissection of the protein G B1 domain binding site for human IgG Fc fragment
    • Sloan, D.J., and Hellinga, H.W. (1999). Dissection of the protein G B1 domain binding site for human IgG Fc fragment. Protein Sci. 8, 1643-1648.
    • (1999) Protein Sci , vol.8 , pp. 1643-1648
    • Sloan, D.J.1    Hellinga, H.W.2
  • 42
    • 84875703570 scopus 로고    scopus 로고
    • Analyses of the effects of all ubiquitin point mutants on yeast growth rate
    • Roscoe, B.P., Thayer, K.M., Zeldovich, K.B., Fushman, D., and Bolon, D.N. (2013). Analyses of the effects of all ubiquitin point mutants on yeast growth rate. J. Mol. Biol. 425, 1363-1377.
    • (2013) J. Mol. Biol , vol.425 , pp. 1363-1377
    • Roscoe, B.P.1    Thayer, K.M.2    Zeldovich, K.B.3    Fushman, D.4    Bolon, D.N.5
  • 44
    • 84901378315 scopus 로고    scopus 로고
    • A quantitative high-resolution genetic profile rapidly identifies sequence determinants of hepatitis C viral fitness and drug sensitivity
    • Qi, H., Olson, C.A., Wu, N.C., Ke, R., Loverdo, C., Chu, V., Truong, S., Remenyi, R., Chen, Z., Du, Y., et al. (2014). A quantitative high-resolution genetic profile rapidly identifies sequence determinants of hepatitis C viral fitness and drug sensitivity. PLoS Pathog. 10, e1004064.
    • (2014) PLoS Pathog , vol.10
    • Qi, H.1    Olson, C.A.2    Wu, N.C.3    Ke, R.4    Loverdo, C.5    Chu, V.6    Truong, S.7    Remenyi, R.8    Chen, Z.9    Du, Y.10
  • 45
    • 34447546660 scopus 로고    scopus 로고
    • The distribution of fitness effects of new mutations
    • Eyre-Walker, A., and Keightley, P.D. (2007). The distribution of fitness effects of new mutations. Nat. Rev. Genet. 8, 610-618.
    • (2007) Nat. Rev. Genet , vol.8 , pp. 610-618
    • Eyre-Walker, A.1    Keightley, P.D.2
  • 46
    • 79957948242 scopus 로고    scopus 로고
    • Negative epistasis between beneficial mutations in an evolving bacterial population
    • Khan, A.I., Dinh, D.M., Schneider, D., Lenski, R.E., and Cooper, T.F. (2011). Negative epistasis between beneficial mutations in an evolving bacterial population. Science 332, 1193-1196.
    • (2011) Science , vol.332 , pp. 1193-1196
    • Khan, A.I.1    Dinh, D.M.2    Schneider, D.3    Lenski, R.E.4    Cooper, T.F.5
  • 48
    • 0028500779 scopus 로고
    • A short linear peptide that folds into a native stable beta-hairpin in aqueous solution
    • Blanco, F.J., Rivas, G., and Serrano, L. (1994). A short linear peptide that folds into a native stable beta-hairpin in aqueous solution. Nat. Struct. Biol. 1, 584-590.
    • (1994) Nat. Struct. Biol , vol.1 , pp. 584-590
    • Blanco, F.J.1    Rivas, G.2    Serrano, L.3
  • 49
    • 74549207309 scopus 로고    scopus 로고
    • Assessing computational methods for predicting protein stability upon mutation: Good on average but not in the details
    • Potapov, V., Cohen, M., and Schreiber, G. (2009). Assessing computational methods for predicting protein stability upon mutation: good on average but not in the details. Protein Eng. Des. Sel. 22, 553-560.
    • (2009) Protein Eng. Des. Sel , vol.22 , pp. 553-560
    • Potapov, V.1    Cohen, M.2    Schreiber, G.3
  • 52
    • 34247500337 scopus 로고    scopus 로고
    • Exploring multiple timescale motions in protein GB3 using accelerated molecular dynamics and NMR spectroscopy
    • Markwick, P.R., Bouvignies, G., and Blackledge, M. (2007). Exploring multiple timescale motions in protein GB3 using accelerated molecular dynamics and NMR spectroscopy. J. Am. Chem. Soc. 129, 4724-4730.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 4724-4730
    • Markwick, P.R.1    Bouvignies, G.2    Blackledge, M.3
  • 53
    • 4143079167 scopus 로고    scopus 로고
    • Amplitudes of protein backbone dynamics and correlated motions in a small alpha/beta protein: Correspondence of dipolar coupling and heteronuclear relaxation measurements
    • Clore, G.M., and Schwieters, C.D. (2004). Amplitudes of protein backbone dynamics and correlated motions in a small alpha/beta protein: correspondence of dipolar coupling and heteronuclear relaxation measurements. Biochemistry 43, 10678-10691.
    • (2004) Biochemistry , vol.43 , pp. 10678-10691
    • Clore, G.M.1    Schwieters, C.D.2
  • 54
    • 20444424211 scopus 로고    scopus 로고
    • Molecular dynamics simulations of protein G challenge NMR-derived correlated backbone motions
    • Lange, O.F., Grubmüller, H., and de Groot, B.L. (2005). Molecular dynamics simulations of protein G challenge NMR-derived correlated backbone motions. Angew. Chem. Int. Ed. Engl. 44, 3394-3399.
    • (2005) Angew. Chem. Int. Ed. Engl , vol.44 , pp. 3394-3399
    • Lange, O.F.1    Grubmüller, H.2    De Groot, B.L.3
  • 55
    • 79551470095 scopus 로고    scopus 로고
    • Role of conformational sampling in computing mutation-induced changes in protein structure and stability
    • Kellogg, E.H., Leaver-Fay, A., and Baker, D. (2011). Role of conformational sampling in computing mutation-induced changes in protein structure and stability. Proteins 79, 830-838.
    • (2011) Proteins , vol.79 , pp. 830-838
    • Kellogg, E.H.1    Leaver-Fay, A.2    Baker, D.3
  • 57
    • 84869080668 scopus 로고    scopus 로고
    • Deep sequencing of systematic combinatorial libraries reveals b-lactamase sequence constraints at high resolution
    • Deng, Z., Huang, W., Bakkalbasi, E., Brown, N.G., Adamski, C.J., Rice, K., Muzny, D., Gibbs, R.A., and Palzkill, T. (2012). Deep sequencing of systematic combinatorial libraries reveals b-lactamase sequence constraints at high resolution. J. Mol. Biol. 424, 150-167.
    • (2012) J. Mol. Biol , vol.424 , pp. 150-167
    • Deng, Z.1    Huang, W.2    Bakkalbasi, E.3    Brown, N.G.4    Adamski, C.J.5    Rice, K.6    Muzny, D.7    Gibbs, R.A.8    Palzkill, T.9
  • 58
    • 84905197658 scopus 로고    scopus 로고
    • The inherent mutational tolerance and antigenic evolvability of influenza hemagglutinin
    • Thyagarajan, B., and Bloom, J.D. (2014). The inherent mutational tolerance and antigenic evolvability of influenza hemagglutinin. Elife 3, e03300.
    • (2014) Elife , vol.3
    • Thyagarajan, B.1    Bloom, J.D.2
  • 59
    • 84867069553 scopus 로고    scopus 로고
    • Construction of a stability landscape of the CH3 domain of human IgG1 by combining directed evolution with high throughput sequencing
    • Traxlmayr, M.W., Hasenhindl, C., Hackl, M., Stadlmayr, G., Rybka, J.D., Borth, N., Grillari, J., Rüker, F., and Obinger, C. (2012). Construction of a stability landscape of the CH3 domain of human IgG1 by combining directed evolution with high throughput sequencing. J. Mol. Biol. 423, 397-412.
    • (2012) J. Mol. Biol , vol.423 , pp. 397-412
    • Traxlmayr, M.W.1    Hasenhindl, C.2    Hackl, M.3    Stadlmayr, G.4    Rybka, J.D.5    Borth, N.6    Grillari, J.7    Rüker, F.8    Obinger, C.9
  • 61
    • 0028774340 scopus 로고
    • Stability and function: Two constraints in the evolution of barstar and other proteins
    • Schreiber, G., Buckle, A.M., and Fersht, A.R. (1994). Stability and function: two constraints in the evolution of barstar and other proteins. Structure 2, 945-951.
    • (1994) Structure , vol.2 , pp. 945-951
    • Schreiber, G.1    Buckle, A.M.2    Fersht, A.R.3
  • 62
    • 34547113538 scopus 로고    scopus 로고
    • Group G streptococcal IgG binding molecules FOG and protein G have different impacts on opsonization by C1q
    • Nitsche-Schmitz, D.P., Johansson, H.M., Sastalla, I., Reissmann, S., Frick, I.M., and Chhatwal, G.S. (2007). Group G streptococcal IgG binding molecules FOG and protein G have different impacts on opsonization by C1q. J. Biol. Chem. 282, 17530-17536.
    • (2007) J. Biol. Chem , vol.282 , pp. 17530-17536
    • Nitsche-Schmitz, D.P.1    Johansson, H.M.2    Sastalla, I.3    Reissmann, S.4    Frick, I.M.5    Chhatwal, G.S.6
  • 63
    • 84892475033 scopus 로고    scopus 로고
    • Comparing protein folding in vitro and in vivo: Foldability meets the fitness challenge
    • Hingorani, K.S., and Gierasch, L.M. (2014). Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge. Curr. Opin. Struct. Biol. 24, 81-90.
    • (2014) Curr. Opin. Struct. Biol , vol.24 , pp. 81-90
    • Hingorani, K.S.1    Gierasch, L.M.2
  • 64
    • 34547687667 scopus 로고    scopus 로고
    • Correlation of levels of folded recombinant p53 in escherichia coli with thermodynamic stability in vitro
    • Mayer, S., Rüdiger, S., Ang, H.C., Joerger, A.C., and Fersht, A.R. (2007). Correlation of levels of folded recombinant p53 in escherichia coli with thermodynamic stability in vitro. J. Mol. Biol. 372, 268-276.
    • (2007) J. Mol. Biol , vol.372 , pp. 268-276
    • Mayer, S.1    Rüdiger, S.2    Ang, H.C.3    Joerger, A.C.4    Fersht, A.R.5
  • 65
    • 79961006047 scopus 로고    scopus 로고
    • Sequence-specific long range networks in PSD-95/discs large/ZO-1 (PDZ) domains tune their binding selectivity
    • Gianni, S., Haq, S.R., Montemiglio, L.C., Jürgens, M.C., Engström, A., Chi, C.N., Brunori, M., and Jemth, P. (2011). Sequence-specific long range networks in PSD-95/discs large/ZO-1 (PDZ) domains tune their binding selectivity. J. Biol. Chem. 286, 27167-27175.
    • (2011) J. Biol. Chem , vol.286 , pp. 27167-27175
    • Gianni, S.1    Haq, S.R.2    Montemiglio, L.C.3    Jürgens, M.C.4    Engström, A.5    Chi, C.N.6    Brunori, M.7    Jemth, P.8
  • 67
    • 84455167671 scopus 로고    scopus 로고
    • Hot spots for allosteric regulation on protein surfaces
    • Reynolds, K.A., McLaughlin, R.N., and Ranganathan, R. (2011). Hot spots for allosteric regulation on protein surfaces. Cell 147, 1564-1575.
    • (2011) Cell , vol.147 , pp. 1564-1575
    • Reynolds, K.A.1    McLaughlin, R.N.2    Ranganathan, R.3
  • 68
    • 6344219895 scopus 로고    scopus 로고
    • Is allostery an intrinsic property of all dynamic proteins?
    • Gunasekaran, K., Ma, B., and Nussinov, R. (2004). Is allostery an intrinsic property of all dynamic proteins? Proteins 57, 433-443.
    • (2004) Proteins , vol.57 , pp. 433-443
    • Gunasekaran, K.1    Ma, B.2    Nussinov, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.