메뉴 건너뛰기




Volumn 7, Issue 11, 2012, Pages

Genetic PEGylation

Author keywords

[No Author keywords available]

Indexed keywords

LIGASE; MACROGOL; THIOREDOXIN; TRANSFER RNA;

EID: 84869047111     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0049235     Document Type: Article
Times cited : (14)

References (52)
  • 1
    • 0032938527 scopus 로고    scopus 로고
    • Enzyme modification by polymers with solubilities that change in response to photoirradiation in organic media
    • Ito Y, Sugimura N, Kwon OH, Imanishi Y, (1999) Enzyme modification by polymers with solubilities that change in response to photoirradiation in organic media. Nature Biotechnol 17: 73-75.
    • (1999) Nature Biotechnol , vol.17 , pp. 73-75
    • Ito, Y.1    Sugimura, N.2    Kwon, O.H.3    Imanishi, Y.4
  • 2
    • 0000026335 scopus 로고    scopus 로고
    • Catalytic activity and conformation of chemically modified subtilisin Carlsberg in organic media
    • Kwon OH, Imanishi Y, Ito Y, (1999) Catalytic activity and conformation of chemically modified subtilisin Carlsberg in organic media. Biotechnol Bioeng 66: 265-270.
    • (1999) Biotechnol Bioeng , vol.66 , pp. 265-270
    • Kwon, O.H.1    Imanishi, Y.2    Ito, Y.3
  • 3
    • 13644256398 scopus 로고    scopus 로고
    • Protein-polymer nano-machines. Towards synthetic control of biological processes
    • Pennadam S, Firman K, Alexander C, Gorecki D, (2004) Protein-polymer nano-machines. Towards synthetic control of biological processes. J Nanotechnol 2: 1-7.
    • (2004) J Nanotechnol , vol.2 , pp. 1-7
    • Pennadam, S.1    Firman, K.2    Alexander, C.3    Gorecki, D.4
  • 5
    • 33847050891 scopus 로고    scopus 로고
    • Biosynthetic-synthetic polymer conjugates
    • Hest JCM, (2007) Biosynthetic-synthetic polymer conjugates. J Macromol Sci Part C Polym Rev 47: 63-92.
    • (2007) J Macromol Sci Part C Polym Rev , vol.47 , pp. 63-92
    • Hest, J.C.M.1
  • 6
    • 79751479008 scopus 로고    scopus 로고
    • Emerging synthetic approaches for protein-polymer conjugations, Chem Commun
    • Broyer RM, Grover GN, Maynard HD, (2011) Emerging synthetic approaches for protein-polymer conjugations, Chem Commun. 47: 2212-2226.
    • (2011) , vol.47 , pp. 2212-2226
    • Broyer, R.M.1    Grover, G.N.2    Maynard, H.D.3
  • 7
    • 70449397517 scopus 로고    scopus 로고
    • Peptide/protein-polymer conjugates: Quo Vadis
    • Klok H-A, (2009) Peptide/protein-polymer conjugates: Quo Vadis. Macromolecules 42: 7990-8000.
    • (2009) Macromolecules , vol.42 , pp. 7990-8000
    • Klok, H.-A.1
  • 9
    • 77950363877 scopus 로고    scopus 로고
    • Protein- and peptide-modified synthetic polymeric biomaterials
    • Krishna OD, Kiick KL, (2010) Protein- and peptide-modified synthetic polymeric biomaterials. Biopolymers (Pep Sci) 94: 32-48.
    • (2010) Biopolymers (Pep Sci) , vol.94 , pp. 32-48
    • Krishna, O.D.1    Kiick, K.L.2
  • 10
    • 78649707326 scopus 로고    scopus 로고
    • Protein-polymer amphiphilic chimeras: recent advances and future challenges
    • Velonia K, (2010) Protein-polymer amphiphilic chimeras: recent advances and future challenges. Polym Chem 1: 944-952.
    • (2010) Polym Chem , vol.1 , pp. 944-952
    • Velonia, K.1
  • 11
    • 51549092094 scopus 로고    scopus 로고
    • The impact of PEGylation on biological therapies
    • Veronese FM, Mero A, (2008) The impact of PEGylation on biological therapies. Biodrugs 22: 315-329.
    • (2008) Biodrugs , vol.22 , pp. 315-329
    • Veronese, F.M.1    Mero, A.2
  • 12
    • 76949103845 scopus 로고    scopus 로고
    • PEGylated polymers for medicine: from conjugation to self-assembled systems
    • Joralemon MJ, McRae S, Emrick T, (2010) PEGylated polymers for medicine: from conjugation to self-assembled systems. Chem Commun 46: 1377-1393.
    • (2010) Chem Commun , vol.46 , pp. 1377-1393
    • Joralemon, M.J.1    McRae, S.2    Emrick, T.3
  • 13
    • 0017701219 scopus 로고
    • Alteration of immunological properties of bovine serum by covalent attachment of polyethylene glycol
    • Abuchowsky A, Van Es T, Palczuk NC, Davis FF, (1977) Alteration of immunological properties of bovine serum by covalent attachment of polyethylene glycol. J Biol Chem 251: 3578-3581.
    • (1977) J Biol Chem , vol.251 , pp. 3578-3581
    • Abuchowsky, A.1    van Es, T.2    Palczuk, N.C.3    Davis, F.F.4
  • 14
    • 0017388651 scopus 로고
    • Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase
    • Abuchowsky A, McCoy TJR, Palczuk NC, Van Es T, Davis FF, (1977) Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase. J Biol Chem 251: 3578-3581.
    • (1977) J Biol Chem , vol.251 , pp. 3578-3581
    • Abuchowsky, A.1    McCoy, T.J.R.2    Palczuk, N.C.3    van Es, T.4    Davis, F.F.5
  • 15
    • 0037362655 scopus 로고    scopus 로고
    • Effect of PEGylation on pharmaceuticals
    • Harris JM, Chess RB, (2003) Effect of PEGylation on pharmaceuticals. Nat Rev Drug Discovery 2: 214-221.
    • (2003) Nat Rev Drug Discovery , vol.2 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 16
    • 37549023093 scopus 로고    scopus 로고
    • Effect of PEG modification on subtilisin Carsberg activity, enantioselectivity, and structural dynamics in 1,4-dioxane
    • Catillo B, Sola RJ, Ferrer A, Barletta G, Griebenow K, (2007) Effect of PEG modification on subtilisin Carsberg activity, enantioselectivity, and structural dynamics in 1,4-dioxane. Biotechnol Bioeng 99: 9-17.
    • (2007) Biotechnol Bioeng , vol.99 , pp. 9-17
    • Catillo, B.1    Sola, R.J.2    Ferrer, A.3    Barletta, G.4    Griebenow, K.5
  • 18
  • 19
    • 1942484412 scopus 로고    scopus 로고
    • Site-directed PEGylation of trichostanthin retained its anti-HIV activity with reduced potency in vitro
    • Wang JH, Tam SC, Huang H, Ouyang DY, Wang YY, et al. (2004) Site-directed PEGylation of trichostanthin retained its anti-HIV activity with reduced potency in vitro. Biochim Biophys Res Comm 3317: 965-971.
    • (2004) Biochim Biophys Res Comm , vol.3317 , pp. 965-971
    • Wang, J.H.1    Tam, S.C.2    Huang, H.3    Ouyang, D.Y.4    Wang, Y.Y.5
  • 20
    • 25444439806 scopus 로고    scopus 로고
    • Site-specific PEGylation of engineered cysteine analogues of recombinant human granulocyte-macrophage colony-stimulating factor
    • Doherty DH, Rosendahl MS, Smith DJ, Hughes JM, Chlipala EA, et al. (2005) Site-specific PEGylation of engineered cysteine analogues of recombinant human granulocyte-macrophage colony-stimulating factor. Bioconjug Chem 16: 1291-1298.
    • (2005) Bioconjug Chem , vol.16 , pp. 1291-1298
    • Doherty, D.H.1    Rosendahl, M.S.2    Smith, D.J.3    Hughes, J.M.4    Chlipala, E.A.5
  • 21
    • 0037124507 scopus 로고    scopus 로고
    • Enzymatic procedure for site-specific pegylation of proteins
    • Sato H, (2002) Enzymatic procedure for site-specific pegylation of proteins. Adv Drug Delivery 54: 487-504.
    • (2002) Adv Drug Delivery , vol.54 , pp. 487-504
    • Sato, H.1
  • 22
    • 52949097799 scopus 로고    scopus 로고
    • Precisely defined protein-polymer conjugates: Construction of synthetic DNA binding domains on proteins by using multivalent dendrons
    • Kostiainen MA, Szilvay GR, Lehtinen J, Smith DK, Linder MB, et al. (2007) Precisely defined protein-polymer conjugates: Construction of synthetic DNA binding domains on proteins by using multivalent dendrons. ACS Nano 1: 103-113.
    • (2007) ACS Nano , vol.1 , pp. 103-113
    • Kostiainen, M.A.1    Szilvay, G.R.2    Lehtinen, J.3    Smith, D.K.4    Linder, M.B.5
  • 23
    • 57049092249 scopus 로고    scopus 로고
    • Single-site cys-substituting mutation of human lectin galectin-2: Modulating solubility in recombinant production, reducing long-term aggregation, and enabling site-specific monoPEGylation
    • Wang H, He L, Lensch M, Gabius H-J, Fee CJ, et al. (2008) Single-site cys-substituting mutation of human lectin galectin-2: Modulating solubility in recombinant production, reducing long-term aggregation, and enabling site-specific monoPEGylation. Biomacromolecules. 9: 3223-3230.
    • (2008) Biomacromolecules , vol.9 , pp. 3223-3230
    • Wang, H.1    He, L.2    Lensch, M.3    Gabius, H.-J.4    Fee, C.J.5
  • 24
    • 77958183695 scopus 로고    scopus 로고
    • Site-specific PEGylation of bone morphogenetic protein-2 cysteine analogues
    • Hu J, Duppatla V, Harth S, Schmitz W, Sebald W, (2010) Site-specific PEGylation of bone morphogenetic protein-2 cysteine analogues. Bioconjug Chem 21: 1762-1772.
    • (2010) Bioconjug Chem , vol.21 , pp. 1762-1772
    • Hu, J.1    Duppatla, V.2    Harth, S.3    Schmitz, W.4    Sebald, W.5
  • 25
    • 79951709244 scopus 로고    scopus 로고
    • In situ maleimide bridging of disulfides and a new approach to protein PEGylation
    • Schumacher FF, Nobles M, Ryan CP, Smith MEB, Tinker A, et al. (2011) In situ maleimide bridging of disulfides and a new approach to protein PEGylation. Bioconjug Chem 22: 132-136.
    • (2011) Bioconjug Chem , vol.22 , pp. 132-136
    • Schumacher, F.F.1    Nobles, M.2    Ryan, C.P.3    Smith, M.E.B.4    Tinker, A.5
  • 26
    • 10344251551 scopus 로고    scopus 로고
    • A three-component Mannich-type reaction for selective tyrosine bioconjugation
    • Joshi NS, Whitaker LR, Francis MB, (2004) A three-component Mannich-type reaction for selective tyrosine bioconjugation. J Am Chem Soc 126: 15942-15943.
    • (2004) J Am Chem Soc , vol.126 , pp. 15942-15943
    • Joshi, N.S.1    Whitaker, L.R.2    Francis, M.B.3
  • 27
    • 31944445245 scopus 로고    scopus 로고
    • Tyrosine-selective protein alkylation using p-palladium complexes
    • Tilley SD, Francis MB, (2006) Tyrosine-selective protein alkylation using p-palladium complexes. J Am Chem Soc 128: 1080-1081.
    • (2006) J Am Chem Soc , vol.128 , pp. 1080-1081
    • Tilley, S.D.1    Francis, M.B.2
  • 28
    • 4644256655 scopus 로고    scopus 로고
    • C-Terminal site-specific PEGylation of a truncated thrombomodulin mutant with retention of full bioactivity
    • Cazalis CS, Haller CA, Sease-Cargo L, Chaikof EL, (2004) C-Terminal site-specific PEGylation of a truncated thrombomodulin mutant with retention of full bioactivity. Bioconjug Chem 15: 1005-1009.
    • (2004) Bioconjug Chem , vol.15 , pp. 1005-1009
    • Cazalis, C.S.1    Haller, C.A.2    Sease-Cargo, L.3    Chaikof, E.L.4
  • 30
    • 0037423148 scopus 로고    scopus 로고
    • Design and chemical synthesis of homogeneous polymer-modified erythropoiesis protein
    • Kochendoerfer GG, Chen SY, Mao F, Cressman S, Traviglia S, et al. (2003) Design and chemical synthesis of homogeneous polymer-modified erythropoiesis protein. Science 299: 884-887.
    • (2003) Science , vol.299 , pp. 884-887
    • Kochendoerfer, G.G.1    Chen, S.Y.2    Mao, F.3    Cressman, S.4    Traviglia, S.5
  • 31
    • 20144371341 scopus 로고    scopus 로고
    • Synthetic erythropoietic proteins: tuning biological performance by site-specific polymer attachment
    • Chen SY, Cressman S, Mao F, Shao H, Low DW, et al. (2005) Synthetic erythropoietic proteins: tuning biological performance by site-specific polymer attachment. Chem Biol 12: 371-383.
    • (2005) Chem Biol , vol.12 , pp. 371-383
    • Chen, S.Y.1    Cressman, S.2    Mao, F.3    Shao, H.4    Low, D.W.5
  • 32
    • 70349917806 scopus 로고    scopus 로고
    • Bioorthogonal chemistry: fishing for selectivity in a sea of functionality
    • Sletten EM, Bertozzi CR, (2009) Bioorthogonal chemistry: fishing for selectivity in a sea of functionality. Angew Chem Int Ed Engl 48: 6974-6998.
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 6974-6998
    • Sletten, E.M.1    Bertozzi, C.R.2
  • 33
    • 77949341762 scopus 로고    scopus 로고
    • Advances in bioconjugation
    • Kalia J, Raines T, (2010) Advances in bioconjugation. Curr Org Chem 14: 138-147.
    • (2010) Curr Org Chem , vol.14 , pp. 138-147
    • Kalia, J.1    Raines, T.2
  • 34
    • 79960987250 scopus 로고    scopus 로고
    • Bridging chemistry to life
    • Boyce M, Bertozzi CR, (2011) Bridging chemistry to life. Nat Meth 8: 638-642.
    • (2011) Nat Meth , vol.8 , pp. 638-642
    • Boyce, M.1    Bertozzi, C.R.2
  • 35
    • 80053010069 scopus 로고    scopus 로고
    • Guest Editorial A decade of bioorthogonal chemistry
    • Berzozzi CR, (2011) Guest Editorial A decade of bioorthogonal chemistry. Acc Chem Res 44: 651-653.
    • (2011) Acc Chem Res , vol.44 , pp. 651-653
    • Berzozzi, C.R.1
  • 36
    • 81355139629 scopus 로고    scopus 로고
    • Choosing an effective protein bioconjugation strategy
    • Stephanopoulos N, Francis MB, (2011) Choosing an effective protein bioconjugation strategy. Nat Chem Biol 7: 876-884.
    • (2011) Nat Chem Biol , vol.7 , pp. 876-884
    • Stephanopoulos, N.1    Francis, M.B.2
  • 37
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • Noren CJ, Anthony-Cahill SJ, Griffith MC, Schultz PG, (1989) A general method for site-specific incorporation of unnatural amino acids into proteins. Science 244: 182-188.
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 38
    • 0000652848 scopus 로고
    • Biosynthetic site-specific incorporation of a non-natural amino acid into a polypeptide
    • Bain JD, Glabe CG, Dix TA, Chamberlin AR, Diala ES, (1989) Biosynthetic site-specific incorporation of a non-natural amino acid into a polypeptide. J Am Chem Soc 111: 8013-8014.
    • (1989) J Am Chem Soc , vol.111 , pp. 8013-8014
    • Bain, J.D.1    Glabe, C.G.2    Dix, T.A.3    Chamberlin, A.R.4    Diala, E.S.5
  • 39
  • 41
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu CC, Schultz PG, (2010) Adding new chemistries to the genetic code. Annu Rev Biochem 79: 413-444.
    • (2010) Annu Rev Biochem , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 42
    • 77951236321 scopus 로고    scopus 로고
    • Beyoud the canonical 20 amino acids: Expanding the genetic lexicon
    • Young TS, Schults PG, (2010) Beyoud the canonical 20 amino acids: Expanding the genetic lexicon. J Biol Chem 285: 11039-11044.
    • (2010) J Biol Chem , vol.285 , pp. 11039-11044
    • Young, T.S.1    Schults, P.G.2
  • 43
    • 77949625552 scopus 로고    scopus 로고
    • Genetic incorporation of unnatural amino acids into proteins in Mycobacterium tuberculosis
    • Wang F, Robbins S, Guo J, Shen W, Schults PG, (2010) Genetic incorporation of unnatural amino acids into proteins in Mycobacterium tuberculosis. PLoS ONE 5: e9354.
    • (2010) PLoS ONE , vol.5
    • Wang, F.1    Robbins, S.2    Guo, J.3    Shen, W.4    Schults, P.G.5
  • 45
    • 80054854782 scopus 로고    scopus 로고
    • RF1 knockout allows ribosomal incorporation of unnatural amino acids at multiple sites
    • Johnson DB, Xu J, Shen Z, Takimoto JK, Schultz MD, et al. (2011) RF1 knockout allows ribosomal incorporation of unnatural amino acids at multiple sites. Nat Chem Biol 7: 779-786.
    • (2011) Nat Chem Biol , vol.7 , pp. 779-786
    • Johnson, D.B.1    Xu, J.2    Shen, Z.3    Takimoto, J.K.4    Schultz, M.D.5
  • 46
    • 0029968958 scopus 로고    scopus 로고
    • Incorporation of non-natural amino acids into streptavidin through in vitro frame-shift suppression
    • Hohsaka T, Ashizuka Y, Murakami H, Sisido M, (1996) Incorporation of non-natural amino acids into streptavidin through in vitro frame-shift suppression. J Am Chem Soc 118: 9778-9779.
    • (1996) J Am Chem Soc , vol.118 , pp. 9778-9779
    • Hohsaka, T.1    Ashizuka, Y.2    Murakami, H.3    Sisido, M.4
  • 47
    • 68349127052 scopus 로고    scopus 로고
    • Site-specific incorporation of PEGylated amino acids into proteins using nonnatural amino acid mutagenesis
    • Shozen N, Iijima I, Hohsaka T, (2009) Site-specific incorporation of PEGylated amino acids into proteins using nonnatural amino acid mutagenesis. Bioorg Med Chem Lett 19: 4909-4911.
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 4909-4911
    • Shozen, N.1    Iijima, I.2    Hohsaka, T.3
  • 48
    • 0033550501 scopus 로고    scopus 로고
    • Efficient incorporation of nonnatural amino acids with large aromatic groups into streptavidin in in vitro protein synthesizing systems
    • Hohsaka T, Kajihara D, Ashizuka Y, Murakami H, Sisido M, (1999) Efficient incorporation of nonnatural amino acids with large aromatic groups into streptavidin in in vitro protein synthesizing systems. J Am Chem Soc 121: 34-40.
    • (1999) J Am Chem Soc , vol.121 , pp. 34-40
    • Hohsaka, T.1    Kajihara, D.2    Ashizuka, Y.3    Murakami, H.4    Sisido, M.5
  • 49
    • 33750324246 scopus 로고    scopus 로고
    • FRET analysis of protein conformational change through position-specific incorporation of fluorescent amino acids
    • Kajihara D, Abe R, Iijima I, Komiyama C, Sisido M, et al. (2006) FRET analysis of protein conformational change through position-specific incorporation of fluorescent amino acids. Nat Methods 3: 923-929.
    • (2006) Nat Methods , vol.3 , pp. 923-929
    • Kajihara, D.1    Abe, R.2    Iijima, I.3    Komiyama, C.4    Sisido, M.5
  • 50
    • 34547775169 scopus 로고    scopus 로고
    • Position-specific incorporation of biotinylated non-natural amino acids into a protein in a cell-free translation system
    • Watanabe T, Muranaka N, Iijima I, Hohsaka T, (2007) Position-specific incorporation of biotinylated non-natural amino acids into a protein in a cell-free translation system. Biochem Biophys Res Commun 361: 794-799.
    • (2007) Biochem Biophys Res Commun , vol.361 , pp. 794-799
    • Watanabe, T.1    Muranaka, N.2    Iijima, I.3    Hohsaka, T.4
  • 51
    • 77953123601 scopus 로고    scopus 로고
    • Incorporation of fluorescent non-natural amino acids into N-terminal tag of proteins in cell-free translation and dependence of position and neighboring codons
    • Abe R, Shiraga K, Ebisu S, Takagi H, Hohsaka T, (2010) Incorporation of fluorescent non-natural amino acids into N-terminal tag of proteins in cell-free translation and dependence of position and neighboring codons. J Biosci Bioeng 110: 32-38.
    • (2010) J Biosci Bioeng , vol.110 , pp. 32-38
    • Abe, R.1    Shiraga, K.2    Ebisu, S.3    Takagi, H.4    Hohsaka, T.5
  • 52
    • 77049113819 scopus 로고    scopus 로고
    • Site-specific incorporation of p-propargyloxyphenylalanine in a cell-free environment for direct protein-protein click conjugation
    • Bundy BC, Swartz JR, (2010) Site-specific incorporation of p-propargyloxyphenylalanine in a cell-free environment for direct protein-protein click conjugation. Bioconjug Chem 21: 255-263.
    • (2010) Bioconjug Chem , vol.21 , pp. 255-263
    • Bundy, B.C.1    Swartz, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.