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Volumn 105, Issue 4, 2013, Pages 1027-1036

Investigating models of protein function and allostery with a widespread mutational analysis of a light-activated protein

Author keywords

[No Author keywords available]

Indexed keywords

VEGETABLE PROTEIN;

EID: 84882982790     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.07.010     Document Type: Article
Times cited : (43)

References (63)
  • 1
    • 61649112657 scopus 로고    scopus 로고
    • Domain-based and family-specific sequence identity thresholds increase the levels of reliable protein function transfer
    • S. Addou, and R. Rentzsch C.A. Orengo Domain-based and family-specific sequence identity thresholds increase the levels of reliable protein function transfer J. Mol. Biol. 387 2009 416 430
    • (2009) J. Mol. Biol. , vol.387 , pp. 416-430
    • Addou, S.1    Rentzsch, R.2    Orengo, C.A.3
  • 2
    • 0026071374 scopus 로고
    • Multiple sequence alignment of protein families showing low sequence homology: A methodological approach using database pattern-matching discriminators for G-protein-linked receptors
    • T.K. Attwood, E.E. Eliopoulos, and J.B. Findlay Multiple sequence alignment of protein families showing low sequence homology: a methodological approach using database pattern-matching discriminators for G-protein-linked receptors Gene 98 1991 153 159
    • (1991) Gene , vol.98 , pp. 153-159
    • Attwood, T.K.1    Eliopoulos, E.E.2    Findlay, J.B.3
  • 3
    • 0242490786 scopus 로고    scopus 로고
    • Functionality of system components: Conservation of protein function in protein feature space
    • L.J. Jensen, D.W. Ussery, and S. Brunak Functionality of system components: conservation of protein function in protein feature space Genome Res. 13 2003 2444 2449
    • (2003) Genome Res. , vol.13 , pp. 2444-2449
    • Jensen, L.J.1    Ussery, D.W.2    Brunak, S.3
  • 4
    • 47049105753 scopus 로고    scopus 로고
    • A dominant conformational role for amino acid diversity in minimalist protein-protein interfaces
    • R.N. Gilbreth, and K. Esaki S. Koide A dominant conformational role for amino acid diversity in minimalist protein-protein interfaces J. Mol. Biol. 381 2008 407 418
    • (2008) J. Mol. Biol. , vol.381 , pp. 407-418
    • Gilbreth, R.N.1    Esaki, K.2    Koide, S.3
  • 5
    • 34249852867 scopus 로고    scopus 로고
    • High-affinity single-domain binding proteins with a binary-code interface
    • A. Koide, and R.N. Gilbreth S. Koide High-affinity single-domain binding proteins with a binary-code interface Proc. Natl. Acad. Sci. USA 104 2007 6632 6637
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 6632-6637
    • Koide, A.1    Gilbreth, R.N.2    Koide, S.3
  • 6
    • 77950502609 scopus 로고    scopus 로고
    • A potent and highly specific FN3 monobody inhibitor of the Abl SH2 domain
    • J. Wojcik, and O. Hantschel S. Koide A potent and highly specific FN3 monobody inhibitor of the Abl SH2 domain Nat. Struct. Mol. Biol. 17 2010 519 527
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 519-527
    • Wojcik, J.1    Hantschel, O.2    Koide, S.3
  • 7
    • 80055066238 scopus 로고    scopus 로고
    • Change in allosteric network affects binding affinities of PDZ domains: Analysis through perturbation response scanning
    • Z.N. Gerek, and S.B. Ozkan Change in allosteric network affects binding affinities of PDZ domains: analysis through perturbation response scanning PLoS Comput. Biol. 7 2011 e1002154
    • (2011) PLoS Comput. Biol. , vol.7 , pp. 1002154
    • Gerek, Z.N.1    Ozkan, S.B.2
  • 10
    • 27544516094 scopus 로고    scopus 로고
    • Ubiquitin - Conserved protein or selfish gene?
    • A. Catic, and H.L. Ploegh Ubiquitin - conserved protein or selfish gene? Trends Biochem. Sci. 30 2005 600 604
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 600-604
    • Catic, A.1    Ploegh, H.L.2
  • 11
    • 77955794751 scopus 로고    scopus 로고
    • The evolutionary history of histone H3 suggests a deep eukaryotic root of chromatin modifying mechanisms
    • J. Postberg, and S. Forcob H.J. Lipps The evolutionary history of histone H3 suggests a deep eukaryotic root of chromatin modifying mechanisms BMC Evol. Biol. 10 2010 259
    • (2010) BMC Evol. Biol. , vol.10 , pp. 259
    • Postberg, J.1    Forcob, S.2    Lipps, H.J.3
  • 12
    • 84872835595 scopus 로고    scopus 로고
    • Impact of mutations on the allosteric conformational equilibrium
    • P. Weinkam, and Y.C. Chen A. Sali Impact of mutations on the allosteric conformational equilibrium J. Mol. Biol. 425 2013 647 661
    • (2013) J. Mol. Biol. , vol.425 , pp. 647-661
    • Weinkam, P.1    Chen, Y.C.2    Sali, A.3
  • 13
    • 77956338533 scopus 로고    scopus 로고
    • High-resolution mapping of protein sequence-function relationships
    • D.M. Fowler, and C.L. Araya S. Fields High-resolution mapping of protein sequence-function relationships Nat. Methods 7 2010 741 746
    • (2010) Nat. Methods , vol.7 , pp. 741-746
    • Fowler, D.M.1    Araya, C.L.2    Fields, S.3
  • 14
    • 70350635776 scopus 로고    scopus 로고
    • Exploitation of binding energy for catalysis and design
    • S.B. Thyme, and J. Jarjour D. Baker Exploitation of binding energy for catalysis and design Nature 461 2009 1300 1304
    • (2009) Nature , vol.461 , pp. 1300-1304
    • Thyme, S.B.1    Jarjour, J.2    Baker, D.3
  • 15
    • 3042681604 scopus 로고    scopus 로고
    • Protein tolerance to random amino acid change
    • H.H. Guo, J. Choe, and L.A. Loeb Protein tolerance to random amino acid change Proc. Natl. Acad. Sci. USA 101 2004 9205 9210
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9205-9210
    • Guo, H.H.1    Choe, J.2    Loeb, L.A.3
  • 16
    • 56749170877 scopus 로고    scopus 로고
    • Catalytic mechanism and performance of computationally designed enzymes for Kemp elimination
    • A.N. Alexandrova, and D. Röthlisberger W.L. Jorgensen Catalytic mechanism and performance of computationally designed enzymes for Kemp elimination J. Am. Chem. Soc. 130 2008 15907 15915
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15907-15915
    • Alexandrova, A.N.1    Röthlisberger, D.2    Jorgensen, W.L.3
  • 17
    • 78149272906 scopus 로고    scopus 로고
    • Robustness and evolvability in the functional anatomy of a PER-ARNT-SIM (PAS) domain
    • A.F. Philip, M. Kumauchi, and W.D. Hoff Robustness and evolvability in the functional anatomy of a PER-ARNT-SIM (PAS) domain Proc. Natl. Acad. Sci. USA 107 2010 17986 17991
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17986-17991
    • Philip, A.F.1    Kumauchi, M.2    Hoff, W.D.3
  • 18
    • 0029962946 scopus 로고    scopus 로고
    • Amino acid sequence determinants of beta-lactamase structure and activity
    • W. Huang, and J. Petrosino T. Palzkill Amino acid sequence determinants of beta-lactamase structure and activity J. Mol. Biol. 258 1996 688 703
    • (1996) J. Mol. Biol. , vol.258 , pp. 688-703
    • Huang, W.1    Petrosino, J.2    Palzkill, T.3
  • 19
    • 68749107059 scopus 로고    scopus 로고
    • Protein sectors: Evolutionary units of three-dimensional structure
    • N. Halabi, and O. Rivoire R. Ranganathan Protein sectors: evolutionary units of three-dimensional structure Cell 138 2009 774 786
    • (2009) Cell , vol.138 , pp. 774-786
    • Halabi, N.1    Rivoire, O.2    Ranganathan, R.3
  • 20
    • 84455167671 scopus 로고    scopus 로고
    • Hot spots for allosteric regulation on protein surfaces
    • K.A. Reynolds, R.N. McLaughlin, and R. Ranganathan Hot spots for allosteric regulation on protein surfaces Cell 147 2011 1564 1575
    • (2011) Cell , vol.147 , pp. 1564-1575
    • Reynolds, K.A.1    McLaughlin, R.N.2    Ranganathan, R.3
  • 21
    • 34249080375 scopus 로고    scopus 로고
    • Conformational switching in the fungal light sensor Vivid
    • B.D. Zoltowski, and C. Schwerdtfeger B.R. Crane Conformational switching in the fungal light sensor Vivid Science 316 2007 1054 1057
    • (2007) Science , vol.316 , pp. 1054-1057
    • Zoltowski, B.D.1    Schwerdtfeger, C.2    Crane, B.R.3
  • 23
    • 77957933198 scopus 로고    scopus 로고
    • Bacterial sensor kinases: Diversity in the recognition of environmental signals
    • T. Krell, and J. Lacal J.L. Ramos Bacterial sensor kinases: diversity in the recognition of environmental signals Annu. Rev. Microbiol. 64 2010 539 559
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 539-559
    • Krell, T.1    Lacal, J.2    Ramos, J.L.3
  • 24
    • 80053291460 scopus 로고    scopus 로고
    • Ligand-binding PAS domains in a genomic, cellular, and structural context
    • J.T. Henry, and S. Crosson Ligand-binding PAS domains in a genomic, cellular, and structural context Annu. Rev. Microbiol. 65 2011 261 286
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 261-286
    • Henry, J.T.1    Crosson, S.2
  • 25
    • 0032567106 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the HERG potassium channel N terminus: A eukaryotic PAS domain
    • J.H. Morais Cabral, and A. Lee R. Mackinnon Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain Cell 95 1998 649 655
    • (1998) Cell , vol.95 , pp. 649-655
    • Morais Cabral, J.H.1    Lee, A.2    Mackinnon, R.3
  • 26
    • 1642274684 scopus 로고    scopus 로고
    • The PAS fold. A redefinition of the PAS domain based upon structural prediction
    • M.H. Hefti, and K.-J. Françoijs J. Vervoort The PAS fold. A redefinition of the PAS domain based upon structural prediction Eur. J. Biochem. 271 2004 1198 1208
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1198-1208
    • Hefti, M.H.1    Françoijs, K.-J.2    Vervoort, J.3
  • 27
    • 70349777587 scopus 로고    scopus 로고
    • Structure and signaling mechanism of Per-ARNT-Sim domains
    • A. Möglich, R.A. Ayers, and K. Moffat Structure and signaling mechanism of Per-ARNT-Sim domains Structure 17 2009 1282 1294
    • (2009) Structure , vol.17 , pp. 1282-1294
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 28
    • 0034911722 scopus 로고    scopus 로고
    • Amino acids in the N-terminal region regulate the photocycle of photoactive yellow protein
    • M. Harigai, and S. Yasuda M. Kataoka Amino acids in the N-terminal region regulate the photocycle of photoactive yellow protein J. Biochem. 130 2001 51 56
    • (2001) J. Biochem. , vol.130 , pp. 51-56
    • Harigai, M.1    Yasuda, S.2    Kataoka, M.3
  • 29
    • 79251559440 scopus 로고    scopus 로고
    • The N-terminal tail of hERG contains an amphipathic α-helix that regulates channel deactivation
    • C.A. Ng, and M.J. Hunter J.I. Vandenberg The N-terminal tail of hERG contains an amphipathic α-helix that regulates channel deactivation PLoS ONE 6 2011 e16191
    • (2011) PLoS ONE , vol.6 , pp. 16191
    • Ng, C.A.1    Hunter, M.J.2    Vandenberg, J.I.3
  • 30
    • 84860285055 scopus 로고    scopus 로고
    • The amino-terminal helix modulates light-activated conformational changes in AsLOV2
    • J.P. Zayner, C. Antoniou, and T.R. Sosnick The amino-terminal helix modulates light-activated conformational changes in AsLOV2 J. Mol. Biol. 419 2012 61 74
    • (2012) J. Mol. Biol. , vol.419 , pp. 61-74
    • Zayner, J.P.1    Antoniou, C.2    Sosnick, T.R.3
  • 31
    • 37049002915 scopus 로고    scopus 로고
    • N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa
    • A.S. Halavaty, and K. Moffat N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa Biochemistry 46 2007 14001 14009
    • (2007) Biochemistry , vol.46 , pp. 14001-14009
    • Halavaty, A.S.1    Moffat, K.2
  • 32
    • 11144344967 scopus 로고    scopus 로고
    • Disruption of the LOV-Jalpha helix interaction activates phototropin kinase activity
    • S.M. Harper, J.M. Christie, and K.H. Gardner Disruption of the LOV-Jalpha helix interaction activates phototropin kinase activity Biochemistry 43 2004 16184 16192
    • (2004) Biochemistry , vol.43 , pp. 16184-16192
    • Harper, S.M.1    Christie, J.M.2    Gardner, K.H.3
  • 33
    • 70350340730 scopus 로고    scopus 로고
    • Mechanism-based tuning of a LOV domain photoreceptor
    • B.D. Zoltowski, B. Vaccaro, and B.R. Crane Mechanism-based tuning of a LOV domain photoreceptor Nat. Chem. Biol. 5 2009 827 834
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 827-834
    • Zoltowski, B.D.1    Vaccaro, B.2    Crane, B.R.3
  • 34
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • F. Delaglio, and S. Grzesiek A. Bax NMRPipe: a multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6 1995 277 293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Bax, A.3
  • 35
    • 4544297801 scopus 로고
    • UCSF Sparky: An NMR display, annotation and assignment tool
    • D.G. Kneller, and I.D. Kuntz UCSF Sparky: an NMR display, annotation and assignment tool J. Cell. Biochem. 53 1993 254
    • (1993) J. Cell. Biochem. , vol.53 , pp. 254
    • Kneller, D.G.1    Kuntz, I.D.2
  • 36
  • 37
    • 27544491192 scopus 로고    scopus 로고
    • ROCR: Visualizing classifier performance in R
    • T. Sing, and O. Sander T. Lengauer ROCR: visualizing classifier performance in R Bioinformatics 21 2005 3940 3941
    • (2005) Bioinformatics , vol.21 , pp. 3940-3941
    • Sing, T.1    Sander, O.2    Lengauer, T.3
  • 38
    • 58849158421 scopus 로고    scopus 로고
    • A conserved glutamine plays a central role in LOV domain signal transmission and its duration
    • A.I. Nash, and W.-H. Ko K.H. Gardner A conserved glutamine plays a central role in LOV domain signal transmission and its duration Biochemistry 47 2008 13842 13849
    • (2008) Biochemistry , vol.47 , pp. 13842-13849
    • Nash, A.I.1    Ko, W.-H.2    Gardner, K.H.3
  • 39
    • 33947377466 scopus 로고    scopus 로고
    • A base-catalyzed mechanism for dark state recovery in the Avena sativa phototropin-1 LOV2 domain
    • M.T.A. Alexandre, and J.C. Arents J.T.M. Kennis A base-catalyzed mechanism for dark state recovery in the Avena sativa phototropin-1 LOV2 domain Biochemistry 46 2007 3129 3137
    • (2007) Biochemistry , vol.46 , pp. 3129-3137
    • Alexandre, M.T.A.1    Arents, J.C.2    Kennis, J.T.M.3
  • 40
    • 0035983657 scopus 로고    scopus 로고
    • Photochemical properties of the flavin mononucleotide-binding domains of the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii
    • M. Kasahara, and T.E. Swartz W.R. Briggs Photochemical properties of the flavin mononucleotide-binding domains of the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii Plant Physiol. 129 2002 762 773
    • (2002) Plant Physiol. , vol.129 , pp. 762-773
    • Kasahara, M.1    Swartz, T.E.2    Briggs, W.R.3
  • 41
    • 0035912211 scopus 로고    scopus 로고
    • Phototropin-related NPL1 controls chloroplast relocation induced by blue light
    • J.A. Jarillo, and H. Gabrys A.R. Cashmore Phototropin-related NPL1 controls chloroplast relocation induced by blue light Nature 410 2001 952 954
    • (2001) Nature , vol.410 , pp. 952-954
    • Jarillo, J.A.1    Gabrys, H.2    Cashmore, A.R.3
  • 42
    • 0035896393 scopus 로고    scopus 로고
    • Arabidopsis NPL1: A phototropin homolog controlling the chloroplast high-light avoidance response
    • T. Kagawa, and T. Sakai M. Wada Arabidopsis NPL1: a phototropin homolog controlling the chloroplast high-light avoidance response Science 291 2001 2138 2141
    • (2001) Science , vol.291 , pp. 2138-2141
    • Kagawa, T.1    Sakai, T.2    Wada, M.3
  • 43
    • 0029278701 scopus 로고
    • Mutations in the NPH1 locus of Arabidopsis disrupt the perception of phototropic stimuli
    • E. Liscum, and W.R. Briggs Mutations in the NPH1 locus of Arabidopsis disrupt the perception of phototropic stimuli Plant Cell 7 1995 473 485
    • (1995) Plant Cell , vol.7 , pp. 473-485
    • Liscum, E.1    Briggs, W.R.2
  • 44
    • 77955170460 scopus 로고    scopus 로고
    • Rationally improving LOV domain-based photoswitches
    • D. Strickland, and X. Yao T.R. Sosnick Rationally improving LOV domain-based photoswitches Nat. Methods 7 2010 623 626
    • (2010) Nat. Methods , vol.7 , pp. 623-626
    • Strickland, D.1    Yao, X.2    Sosnick, T.R.3
  • 45
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • S. Henikoff, and J.G. Henikoff Amino acid substitution matrices from protein blocks Proc. Natl. Acad. Sci. USA 89 1992 10915 10919
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 46
    • 0043122919 scopus 로고    scopus 로고
    • SIFT: Predicting amino acid changes that affect protein function
    • P.C. Ng, and S. Henikoff SIFT: predicting amino acid changes that affect protein function Nucleic Acids Res. 31 2003 3812 3814
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3812-3814
    • Ng, P.C.1    Henikoff, S.2
  • 47
    • 34548546911 scopus 로고    scopus 로고
    • Structural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA
    • A. Möglich, and K. Moffat Structural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA J. Mol. Biol. 373 2007 112 126
    • (2007) J. Mol. Biol. , vol.373 , pp. 112-126
    • Möglich, A.1    Moffat, K.2
  • 48
    • 0345268673 scopus 로고    scopus 로고
    • Primary reactions of the LOV2 domain of phototropin, a plant blue-light photoreceptor
    • J.T.M. Kennis, and S. Crosson R. van Grondelle Primary reactions of the LOV2 domain of phototropin, a plant blue-light photoreceptor Biochemistry 42 2003 3385 3392
    • (2003) Biochemistry , vol.42 , pp. 3385-3392
    • Kennis, J.T.M.1    Crosson, S.2    Van Grondelle, R.3
  • 49
    • 84858952820 scopus 로고    scopus 로고
    • Mutations in N-terminal flanking region of blue light-sensing light-oxygen and voltage 2 (LOV2) domain disrupt its repressive activity on kinase domain in the Chlamydomonas phototropin
    • Y. Aihara, and T. Yamamoto A. Nagatani Mutations in N-terminal flanking region of blue light-sensing light-oxygen and voltage 2 (LOV2) domain disrupt its repressive activity on kinase domain in the Chlamydomonas phototropin J. Biol. Chem. 287 2012 9901 9909
    • (2012) J. Biol. Chem. , vol.287 , pp. 9901-9909
    • Aihara, Y.1    Yamamoto, T.2    Nagatani, A.3
  • 50
    • 84855290528 scopus 로고    scopus 로고
    • Divergence and convergence in enzyme evolution
    • M.Y. Galperin, and E.V. Koonin Divergence and convergence in enzyme evolution J. Biol. Chem. 287 2012 21 28
    • (2012) J. Biol. Chem. , vol.287 , pp. 21-28
    • Galperin, M.Y.1    Koonin, E.V.2
  • 51
    • 78650058676 scopus 로고    scopus 로고
    • Mechanism of signal transduction of the LOV2-Jα photosensor from Avena sativa
    • E. Peter, B. Dick, and S.A. Baeurle Mechanism of signal transduction of the LOV2-Jα photosensor from Avena sativa Nat Commun 1 2010 122
    • (2010) Nat Commun , vol.1 , pp. 122
    • Peter, E.1    Dick, B.2    Baeurle, S.A.3
  • 52
    • 84883025863 scopus 로고    scopus 로고
    • Signaling mechanisms of LOV domains: New insights from molecular dynamics studies
    • P.L. Freddolino, K.H. Gardner, and K. Schulten Signaling mechanisms of LOV domains: new insights from molecular dynamics studies Photochem. Photobiol. Sci. 12 2013 1158 1170
    • (2013) Photochem. Photobiol. Sci. , vol.12 , pp. 1158-1170
    • Freddolino, P.L.1    Gardner, K.H.2    Schulten, K.3
  • 53
  • 54
    • 0345040873 scopus 로고    scopus 로고
    • Classification and regression by randomForest
    • A. Liaw, and M. Wiener Classification and regression by randomForest R News. 2 2002 18 22
    • (2002) R News. , vol.2 , pp. 18-22
    • Liaw, A.1    Wiener, M.2
  • 55
    • 84867539303 scopus 로고    scopus 로고
    • PROTS-RF: A robust model for predicting mutation-induced protein stability changes
    • Y. Li, and J. Fang PROTS-RF: a robust model for predicting mutation-induced protein stability changes PLoS ONE 7 2012 e47247
    • (2012) PLoS ONE , vol.7 , pp. 47247
    • Li, Y.1    Fang, J.2
  • 56
    • 46649102221 scopus 로고    scopus 로고
    • Selectional and mutational scope of peptides sequestering the Jun-Fos coiled-coil domain
    • U.B. Hagemann, and J.M. Mason K.M. Arndt Selectional and mutational scope of peptides sequestering the Jun-Fos coiled-coil domain J. Mol. Biol. 381 2008 73 88
    • (2008) J. Mol. Biol. , vol.381 , pp. 73-88
    • Hagemann, U.B.1    Mason, J.M.2    Arndt, K.M.3
  • 57
    • 44349104094 scopus 로고    scopus 로고
    • Design of protein function leaps by directed domain interface evolution
    • J. Huang, and A. Koide S. Koide Design of protein function leaps by directed domain interface evolution Proc. Natl. Acad. Sci. USA 105 2008 6578 6583
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 6578-6583
    • Huang, J.1    Koide, A.2    Koide, S.3
  • 58
    • 0005876924 scopus 로고
    • Bacteriophage lambda cro mutations: Effects on activity and intracellular degradation
    • A.A. Pakula, V.B. Young, and R.T. Sauer Bacteriophage lambda cro mutations: effects on activity and intracellular degradation Proc. Natl. Acad. Sci. USA 83 1986 8829 8833
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8829-8833
    • Pakula, A.A.1    Young, V.B.2    Sauer, R.T.3
  • 59
    • 0025363984 scopus 로고
    • Deciphering the message in protein sequences: Tolerance to amino acid substitutions
    • J.U. Bowie, and J.F. Reidhaar-Olson R.T. Sauer Deciphering the message in protein sequences: tolerance to amino acid substitutions Science 247 1990 1306 1310
    • (1990) Science , vol.247 , pp. 1306-1310
    • Bowie, J.U.1    Reidhaar-Olson, J.F.2    Sauer, R.T.3
  • 60
    • 0028076771 scopus 로고
    • Genetic studies of the lac repressor. XIV. Analysis of 4000 altered Escherichia coli lac repressors reveals essential and non-essential residues, as well as "spacers" which do not require a specific sequence
    • P. Markiewicz, and L.G. Kleina J.H. Miller Genetic studies of the lac repressor. XIV. Analysis of 4000 altered Escherichia coli lac repressors reveals essential and non-essential residues, as well as "spacers" which do not require a specific sequence J. Mol. Biol. 240 1994 421 433
    • (1994) J. Mol. Biol. , vol.240 , pp. 421-433
    • Markiewicz, P.1    Kleina, L.G.2    Miller, J.H.3
  • 61
    • 0025955349 scopus 로고
    • Systematic mutation of bacteriophage T4 lysozyme
    • D. Rennell, and S.E. Bouvier A.R. Poteete Systematic mutation of bacteriophage T4 lysozyme J. Mol. Biol. 222 1991 67 88
    • (1991) J. Mol. Biol. , vol.222 , pp. 67-88
    • Rennell, D.1    Bouvier, S.E.2    Poteete, A.R.3
  • 62
    • 0028197601 scopus 로고
    • In vivo characterization of mutants of the bacteriophage f1 gene v protein isolated by saturation mutagenesis
    • T.C. Terwilliger, and H.B. Zabin P.M. Schlunk In vivo characterization of mutants of the bacteriophage f1 gene V protein isolated by saturation mutagenesis J. Mol. Biol. 236 1994 556 571
    • (1994) J. Mol. Biol. , vol.236 , pp. 556-571
    • Terwilliger, T.C.1    Zabin, H.B.2    Schlunk, P.M.3
  • 63
    • 84863337761 scopus 로고    scopus 로고
    • Comparison of random mutagenesis and semi-rational designed libraries for improved cytochrome P450 BM3-catalyzed hydroxylation of small alkanes
    • M.M.Y. Chen, and C.D. Snow F.H. Arnold Comparison of random mutagenesis and semi-rational designed libraries for improved cytochrome P450 BM3-catalyzed hydroxylation of small alkanes Protein Eng. Des. Sel. 25 2012 171 178
    • (2012) Protein Eng. Des. Sel. , vol.25 , pp. 171-178
    • Chen, M.M.Y.1    Snow, C.D.2    Arnold, F.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.