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Volumn 7, Issue 3, 2015, Pages 330-341

Rational protein design: Developing next-generation biological therapeutics and nanobiotechnological tools

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINS; RECOMBINANT PROTEINS;

EID: 84927158354     PISSN: 19395116     EISSN: 19390041     Source Type: Journal    
DOI: 10.1002/wnan.1310     Document Type: Review
Times cited : (11)

References (64)
  • 1
    • 37749004225 scopus 로고    scopus 로고
    • Protein therapeutics: a summary and pharmacological classification
    • Leader B, Baca QJ, Golan DE. Protein therapeutics: a summary and pharmacological classification. Nat Rev Drug Discov 2008, 7:21-39.
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 21-39
    • Leader, B.1    Baca, Q.J.2    Golan, D.E.3
  • 2
    • 24944493938 scopus 로고    scopus 로고
    • Toward high-resolution de novo structure prediction for small proteins
    • Bradley P, Misura KMS, Baker D. Toward high-resolution de novo structure prediction for small proteins. Science 2005, 309:1868-1871.
    • (2005) Science , vol.309 , pp. 1868-1871
    • Bradley, P.1    Misura, K.M.S.2    Baker, D.3
  • 3
    • 0343742614 scopus 로고    scopus 로고
    • Automated design of the surface positions of protein helices
    • Dahiyat BI, Gordon DB, Mayo SL. Automated design of the surface positions of protein helices. Protein Sci 1997, 6:1333-1337.
    • (1997) Protein Sci , vol.6 , pp. 1333-1337
    • Dahiyat, B.I.1    Gordon, D.B.2    Mayo, S.L.3
  • 4
    • 0029920337 scopus 로고    scopus 로고
    • Protein design automation
    • Dahiyat BI, Mayo SL. Protein design automation. Protein Sci 1996, 5:895-903.
    • (1996) Protein Sci , vol.5 , pp. 895-903
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 5
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: fully automated sequence selection
    • Dahiyat BI, Mayo SL. De novo protein design: fully automated sequence selection. Science 1997, 278:82-87.
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 6
    • 0030987610 scopus 로고    scopus 로고
    • Probing the role of packing specificity in protein design
    • Dahiyat BI, Mayo SL. Probing the role of packing specificity in protein design. Proc Natl Acad Sci USA 1997, 94:10172-10177.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10172-10177
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 7
    • 0002807377 scopus 로고    scopus 로고
    • Site-specific modification of α-helical peptides with electron donors and acceptors
    • Dahiyat BI, Meade TJ, Mayo SL. Site-specific modification of α-helical peptides with electron donors and acceptors. Inorg Chim Acta 1996, 243:207-212.
    • (1996) Inorg Chim Acta , vol.243 , pp. 207-212
    • Dahiyat, B.I.1    Meade, T.J.2    Mayo, S.L.3
  • 8
    • 0031558762 scopus 로고    scopus 로고
    • De novo protein design: towards fully automated sequence selection
    • Dahiyat BI, Sarisky CA, Mayo SL. De novo protein design: towards fully automated sequence selection. J Mol Biol 1997, 273:789-796.
    • (1997) J Mol Biol , vol.273 , pp. 789-796
    • Dahiyat, B.I.1    Sarisky, C.A.2    Mayo, S.L.3
  • 13
    • 84893786232 scopus 로고    scopus 로고
    • Understanding thermal adaptation of enzymes through the multistate rational design and stability prediction of 100 adenylate kinases
    • Howell SC, Inampudi KK, Bean DP, Wilson CJ. Understanding thermal adaptation of enzymes through the multistate rational design and stability prediction of 100 adenylate kinases. Structure 2014, 22:218-229.
    • (2014) Structure , vol.22 , pp. 218-229
    • Howell, S.C.1    Inampudi, K.K.2    Bean, D.P.3    Wilson, C.J.4
  • 14
    • 84874033495 scopus 로고    scopus 로고
    • Role of lysine during protein modification by HOCl and HOBr: halogen-transfer agent or sacrificial antioxidant?
    • Sivey JD, Howell SC, Bean DJ, McCurry DL, Mitch WA, Wilson CJ. Role of lysine during protein modification by HOCl and HOBr: halogen-transfer agent or sacrificial antioxidant? Biochemistry 2013, 52:1260-1271.
    • (2013) Biochemistry , vol.52 , pp. 1260-1271
    • Sivey, J.D.1    Howell, S.C.2    Bean, D.J.3    McCurry, D.L.4    Mitch, W.A.5    Wilson, C.J.6
  • 20
    • 0031939630 scopus 로고    scopus 로고
    • A preliminary study on delayed vestibulocerebellar effects of Tokyo subway sarin poisoning in relation to gender difference: frequency analysis of postural sway
    • Yokoyama K, Araki S, Murata K, Nishikitani M, Okumura T, Ishimatsu S, Takasu N. A preliminary study on delayed vestibulocerebellar effects of Tokyo subway sarin poisoning in relation to gender difference: frequency analysis of postural sway. J Occup Environ Med 1998, 40:17-21.
    • (1998) J Occup Environ Med , vol.40 , pp. 17-21
    • Yokoyama, K.1    Araki, S.2    Murata, K.3    Nishikitani, M.4    Okumura, T.5    Ishimatsu, S.6    Takasu, N.7
  • 21
    • 33846247849 scopus 로고    scopus 로고
    • Nerve agents
    • Newmark J. Nerve agents. Neurologist 2007, 13:20-32.
    • (2007) Neurologist , vol.13 , pp. 20-32
    • Newmark, J.1
  • 22
    • 0032488593 scopus 로고    scopus 로고
    • Organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase: synergy results in a somanase
    • Millard CB, Lockridge O, Broomfield CA. Organophosphorus acid anhydride hydrolase activity in human butyrylcholinesterase: synergy results in a somanase. Biochemistry 1998, 37:237-247.
    • (1998) Biochemistry , vol.37 , pp. 237-247
    • Millard, C.B.1    Lockridge, O.2    Broomfield, C.A.3
  • 23
    • 40349083695 scopus 로고    scopus 로고
    • The global distribution of fatal pesticide self-poisoning: systematic review
    • Gunnell D, Eddleston M, Phillips MR, Konradsen F. The global distribution of fatal pesticide self-poisoning: systematic review. BMC Public Health 2007, 7:357.
    • (2007) BMC Public Health , vol.7 , pp. 357
    • Gunnell, D.1    Eddleston, M.2    Phillips, M.R.3    Konradsen, F.4
  • 24
    • 0021601290 scopus 로고
    • Design and structure-activity-relationships of antidotes to organo-phosphorus anticholinesterase agents
    • Gray AP. Design and structure-activity-relationships of antidotes to organo-phosphorus anticholinesterase agents. Drug Metab Rev 1984, 15:557-589.
    • (1984) Drug Metab Rev , vol.15 , pp. 557-589
    • Gray, A.P.1
  • 25
    • 28744449011 scopus 로고    scopus 로고
    • Bioscavengers for the protection of humans against organophosphate toxicity
    • Doctor BP, Saxena A. Bioscavengers for the protection of humans against organophosphate toxicity. Chem Biol Interact 2005, 157:167-171.
    • (2005) Chem Biol Interact , vol.157 , pp. 167-171
    • Doctor, B.P.1    Saxena, A.2
  • 27
    • 14644422580 scopus 로고    scopus 로고
    • Mammalian carboxylesterases: from drug targets to protein therapeutics
    • Redinbo MR, Potter PM. Mammalian carboxylesterases: from drug targets to protein therapeutics. Drug Discov Today 2005, 10:313-325.
    • (2005) Drug Discov Today , vol.10 , pp. 313-325
    • Redinbo, M.R.1    Potter, P.M.2
  • 29
    • 80051814341 scopus 로고    scopus 로고
    • In vitro detoxification of cyclosarin in human blood pre-incubated ex vivo with recombinant serum paraoxonases
    • Ashani Y, Goldsmith M, Leader H, Silman I, Sussman JL, Tawfik DS. In vitro detoxification of cyclosarin in human blood pre-incubated ex vivo with recombinant serum paraoxonases. Toxicol Lett 2011, 206:24-28.
    • (2011) Toxicol Lett , vol.206 , pp. 24-28
    • Ashani, Y.1    Goldsmith, M.2    Leader, H.3    Silman, I.4    Sussman, J.L.5    Tawfik, D.S.6
  • 30
    • 0036715684 scopus 로고    scopus 로고
    • Coeliac disease: dissecting a complex inflammatory disorder
    • Sollid LM. Coeliac disease: dissecting a complex inflammatory disorder. Nat Rev Immunol 2002, 2:647-655.
    • (2002) Nat Rev Immunol , vol.2 , pp. 647-655
    • Sollid, L.M.1
  • 31
    • 0028919608 scopus 로고
    • Induction of homologous recombination in mammalian chromosomes by using the I-SceI system of Saccharomyces cerevisiae
    • Choulika A, Perrin A, Dujon B, Nicolas JF. Induction of homologous recombination in mammalian chromosomes by using the I-SceI system of Saccharomyces cerevisiae. Mol Cell Biol 1995, 15:1968-1973.
    • (1995) Mol Cell Biol , vol.15 , pp. 1968-1973
    • Choulika, A.1    Perrin, A.2    Dujon, B.3    Nicolas, J.F.4
  • 33
    • 0031863007 scopus 로고    scopus 로고
    • Analysis of gene targeting and intrachromosomal homologous recombination stimulated by genomic double-strand breaks in mouse embryonic stem cells
    • Donoho G, Jasin M, Berg P. Analysis of gene targeting and intrachromosomal homologous recombination stimulated by genomic double-strand breaks in mouse embryonic stem cells. Mol Cell Biol 1998, 18:4070-4078.
    • (1998) Mol Cell Biol , vol.18 , pp. 4070-4078
    • Donoho, G.1    Jasin, M.2    Berg, P.3
  • 34
    • 0029598505 scopus 로고
    • Double-strand breaks at the target locus stimulate gene targeting in embryonic stem cells
    • Smih F, Rouet P, Romanienko PJ, Jasin M. Double-strand breaks at the target locus stimulate gene targeting in embryonic stem cells. Nucleic Acids Res 1995, 23:5012-5019.
    • (1995) Nucleic Acids Res , vol.23 , pp. 5012-5019
    • Smih, F.1    Rouet, P.2    Romanienko, P.J.3    Jasin, M.4
  • 36
    • 0037510038 scopus 로고    scopus 로고
    • Enhancing gene targeting with designed zinc finger nucleases
    • Bibikova M, Beumer K, Trautman JK, Carroll D. Enhancing gene targeting with designed zinc finger nucleases. Science 2003, 300:764.
    • (2003) Science , vol.300 , pp. 764
    • Bibikova, M.1    Beumer, K.2    Trautman, J.K.3    Carroll, D.4
  • 40
    • 79960034141 scopus 로고    scopus 로고
    • Modularly assembled designer TAL effector nucleases for targeted gene knockout and gene replacement in eukaryotes
    • Li T, Huang S, Zhao X, Wright DA, Carpenter S, Spalding MH, Weeks DP, Yang B. Modularly assembled designer TAL effector nucleases for targeted gene knockout and gene replacement in eukaryotes. Nucleic Acids Res 2011, 39:6315-6325.
    • (2011) Nucleic Acids Res , vol.39 , pp. 6315-6325
    • Li, T.1    Huang, S.2    Zhao, X.3    Wright, D.A.4    Carpenter, S.5    Spalding, M.H.6    Weeks, D.P.7    Yang, B.8
  • 42
    • 67651235292 scopus 로고    scopus 로고
    • Examination of enzymatic H-tunneling through kinetics and dynamics
    • Bandaria JN, Cheatum CM, Kohen A. Examination of enzymatic H-tunneling through kinetics and dynamics. J Am Chem Soc 2009, 131:10151-10155.
    • (2009) J Am Chem Soc , vol.131 , pp. 10151-10155
    • Bandaria, J.N.1    Cheatum, C.M.2    Kohen, A.3
  • 43
    • 0034973280 scopus 로고    scopus 로고
    • Review: protein function at thermal extremes: balancing stability and flexibility
    • Fields PA. Review: protein function at thermal extremes: balancing stability and flexibility. Comp Biochem Phys A 2001, 129:417-431.
    • (2001) Comp Biochem Phys A , vol.129 , pp. 417-431
    • Fields, P.A.1
  • 44
    • 36849039429 scopus 로고    scopus 로고
    • A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
    • Henzler-Wildman KA, Lei M, Thai V, Kerns SJ, Karplus M, Kern D. A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature 2007, 450:913-927.
    • (2007) Nature , vol.450 , pp. 913-927
    • Henzler-Wildman, K.A.1    Lei, M.2    Thai, V.3    Kerns, S.J.4    Karplus, M.5    Kern, D.6
  • 45
    • 77955670221 scopus 로고    scopus 로고
    • Evolutionary fates within a microbial population highlight an essential role for protein folding during natural selection
    • Pena MI, Davlieva M, Bennett MR, Olson JS, Shamoo Y. Evolutionary fates within a microbial population highlight an essential role for protein folding during natural selection. Mol Syst Biol 2010, 6:1-11.
    • (2010) Mol Syst Biol , vol.6 , pp. 1-11
    • Pena, M.I.1    Davlieva, M.2    Bennett, M.R.3    Olson, J.S.4    Shamoo, Y.5
  • 47
    • 84899846059 scopus 로고    scopus 로고
    • Effect of chemical oxidation on the sorption tendency of dissolved organic matter to a model hydrophobic surface
    • Zeng T, Wilson CJ, Mitch WA. Effect of chemical oxidation on the sorption tendency of dissolved organic matter to a model hydrophobic surface. Environ Sci Technol 2014, 48:5118-5126.
    • (2014) Environ Sci Technol , vol.48 , pp. 5118-5126
    • Zeng, T.1    Wilson, C.J.2    Mitch, W.A.3
  • 49
    • 84877899298 scopus 로고    scopus 로고
    • Immune suppression in cynomolgus monkeys by XPro9523: an improved CTLA4-Ig fusion with enhanced binding to CD80, CD86 and neonatal Fc receptor FcRn
    • Bernett MJ, Chu SY, Leung I, Moore GL, Lee SH, Pong E, Chen H, Phung S, Muchhal US, Horton HM, et al. Immune suppression in cynomolgus monkeys by XPro9523: an improved CTLA4-Ig fusion with enhanced binding to CD80, CD86 and neonatal Fc receptor FcRn. MAbs 2013, 5:384-396.
    • (2013) MAbs , vol.5 , pp. 384-396
    • Bernett, M.J.1    Chu, S.Y.2    Leung, I.3    Moore, G.L.4    Lee, S.H.5    Pong, E.6    Chen, H.7    Phung, S.8    Muchhal, U.S.9    Horton, H.M.10
  • 50
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: the neonatal Fc receptor comes of age
    • Roopenian DC, Akilesh S. FcRn: the neonatal Fc receptor comes of age. Nat Rev Immunology 2007, 7:715-725.
    • (2007) Nat Rev Immunology , vol.7 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 52
    • 34247572895 scopus 로고    scopus 로고
    • New developments in FcepsilonRI regulation, function and inhibition
    • Kraft S, Kinet JP. New developments in FcepsilonRI regulation, function and inhibition. Nat Rev Immunol 2007, 7:365-378.
    • (2007) Nat Rev Immunol , vol.7 , pp. 365-378
    • Kraft, S.1    Kinet, J.P.2
  • 56
    • 22344449105 scopus 로고    scopus 로고
    • A new strategy to counter allergy
    • Kinet JP. A new strategy to counter allergy. N Engl J Med 2005, 353:310-312.
    • (2005) N Engl J Med , vol.353 , pp. 310-312
    • Kinet, J.P.1
  • 57
    • 17644388057 scopus 로고    scopus 로고
    • A chimeric human-cat fusion protein blocks cat-induced allergy
    • Zhu D, Kepley CL, Zhang K, Terada T, Yamada T, Saxon A. A chimeric human-cat fusion protein blocks cat-induced allergy. Nat Med 2005, 11:446-449.
    • (2005) Nat Med , vol.11 , pp. 446-449
    • Zhu, D.1    Kepley, C.L.2    Zhang, K.3    Terada, T.4    Yamada, T.5    Saxon, A.6
  • 58
    • 84858864276 scopus 로고    scopus 로고
    • Suppression of mast cell degranulation through a dual-targeting tandem IgE-IgG Fc domain biologic engineered to bind with high affinity to FcγRIIb
    • Cemerski S, Chu SY, Moore GL, Muchhal US, Desjarlais JR, Szymkowski DE. Suppression of mast cell degranulation through a dual-targeting tandem IgE-IgG Fc domain biologic engineered to bind with high affinity to FcγRIIb. Immunol Lett 2012, 143:34-43.
    • (2012) Immunol Lett , vol.143 , pp. 34-43
    • Cemerski, S.1    Chu, S.Y.2    Moore, G.L.3    Muchhal, U.S.4    Desjarlais, J.R.5    Szymkowski, D.E.6
  • 64
    • 84893816638 scopus 로고    scopus 로고
    • Examining photoinduced energy transfer in Pseudomonas aeruginosa azurin
    • Tobin PH, Wilson CJ. Examining photoinduced energy transfer in Pseudomonas aeruginosa azurin. J Am Chem Soc 2014, 136:1793-1802.
    • (2014) J Am Chem Soc , vol.136 , pp. 1793-1802
    • Tobin, P.H.1    Wilson, C.J.2


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