메뉴 건너뛰기




Volumn 462, Issue , 2009, Pages 77-96

Chapter 4 Semisynthesis of Proteins Using Split Inteins

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; INTEIN; PEPTIDE; BETA LACTAMASE; PROTEIN; THIOREDOXIN;

EID: 67651017997     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(09)62004-8     Document Type: Review
Times cited : (13)

References (68)
  • 1
    • 36649015993 scopus 로고    scopus 로고
    • Construction of a small-molecule-integrated semisynthetic split intein for in vivo protein ligation
    • Ando T., et al. Construction of a small-molecule-integrated semisynthetic split intein for in vivo protein ligation. Chem. Commun. (Camb) (2007) 4995-4997
    • (2007) Chem. Commun. (Camb) , pp. 4995-4997
    • Ando, T.1
  • 2
    • 0025778670 scopus 로고
    • Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives
    • Bartolome B., et al. Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives. Gene 102 (1991) 75-78
    • (1991) Gene , vol.102 , pp. 75-78
    • Bartolome, B.1
  • 3
    • 36749028242 scopus 로고    scopus 로고
    • Copper-free click chemistry for dynamic in vivo imaging
    • Baskin J.M., et al. Copper-free click chemistry for dynamic in vivo imaging. Proc. Natl. Acad. Sci. USA 104 (2007) 16793-16797
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 16793-16797
    • Baskin, J.M.1
  • 4
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett D., et al. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci. 8 (1999) 921-929
    • (1999) Protein Sci. , vol.8 , pp. 921-929
    • Beckett, D.1
  • 5
    • 32344433372 scopus 로고    scopus 로고
    • Engineering artificially split inteins for applications in protein chemistry: Biochemical characterization of the split Ssp DnaB intein and comparison to the split Sce VMA intein
    • Brenzel S., Kurpiers T., and Mootz H.D. Engineering artificially split inteins for applications in protein chemistry: Biochemical characterization of the split Ssp DnaB intein and comparison to the split Sce VMA intein. Biochemistry 45 (2006) 1571-1578
    • (2006) Biochemistry , vol.45 , pp. 1571-1578
    • Brenzel, S.1    Kurpiers, T.2    Mootz, H.D.3
  • 6
    • 8344222343 scopus 로고    scopus 로고
    • Prolegomena to future experimental efforts on genetic code engineering by expanding its amino acid repertoire
    • Budisa N. Prolegomena to future experimental efforts on genetic code engineering by expanding its amino acid repertoire. Angew. Chem. Int. Ed. Engl. 43 (2004) 6426-6463
    • (2004) Angew. Chem. Int. Ed. Engl. , vol.43 , pp. 6426-6463
    • Budisa, N.1
  • 7
    • 34249076359 scopus 로고    scopus 로고
    • Introducing genetically encoded aldehydes into proteins
    • Carrico I.S., et al. Introducing genetically encoded aldehydes into proteins. Nat. Chem. Biol. 3 (2007) 321-322
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 321-322
    • Carrico, I.S.1
  • 8
    • 0347517763 scopus 로고    scopus 로고
    • Distribution of split DnaE inteins in cyanobacteria
    • Caspi J., et al. Distribution of split DnaE inteins in cyanobacteria. Mol. Microbiol. 50 (2003) 1569-1577
    • (2003) Mol. Microbiol. , vol.50 , pp. 1569-1577
    • Caspi, J.1
  • 9
    • 32044468517 scopus 로고    scopus 로고
    • Protein trans-splicing and characterization of a split family B-type DNA polymerase from the hyperthermophilic archaeal parasite Nanoarchaeum equitans
    • Choi J.J., et al. Protein trans-splicing and characterization of a split family B-type DNA polymerase from the hyperthermophilic archaeal parasite Nanoarchaeum equitans. J. Mol. Biol. 356 (2006) 1093-1106
    • (2006) J. Mol. Biol. , vol.356 , pp. 1093-1106
    • Choi, J.J.1
  • 10
    • 17744415288 scopus 로고    scopus 로고
    • Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element
    • Chong S., et al. Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element. Gene 192 (1997) 271-281
    • (1997) Gene , vol.192 , pp. 271-281
    • Chong, S.1
  • 11
    • 0032562685 scopus 로고    scopus 로고
    • Modulation of protein splicing of the Saccharomyces cerevisiae vacuolar membrane ATPase intein
    • Chong S., et al. Modulation of protein splicing of the Saccharomyces cerevisiae vacuolar membrane ATPase intein. J. Biol. Chem. 273 (1998) 10567-10577
    • (1998) J. Biol. Chem. , vol.273 , pp. 10567-10577
    • Chong, S.1
  • 12
    • 33846072572 scopus 로고    scopus 로고
    • Trans protein splicing of cyanobacterial split inteins in endogenous and exogenous combinations
    • Dassa B., et al. Trans protein splicing of cyanobacterial split inteins in endogenous and exogenous combinations. Biochemistry 46 (2007) 322-330
    • (2007) Biochemistry , vol.46 , pp. 322-330
    • Dassa, B.1
  • 13
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • Dawson P.E., and Kent S.B. Synthesis of native proteins by chemical ligation. Annu. Rev. Biochem. 69 (2000) 923-960
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 923-960
    • Dawson, P.E.1    Kent, S.B.2
  • 14
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson P.E., et al. Synthesis of proteins by native chemical ligation. Science 266 (1994) 776-779
    • (1994) Science , vol.266 , pp. 776-779
    • Dawson, P.E.1
  • 15
    • 33747157139 scopus 로고    scopus 로고
    • Diels-Alder ligation of peptides and proteins
    • de Araujo A.D., et al. Diels-Alder ligation of peptides and proteins. Chemistry 12 (2006) 6095-6109
    • (2006) Chemistry , vol.12 , pp. 6095-6109
    • de Araujo, A.D.1
  • 16
    • 0141755113 scopus 로고    scopus 로고
    • Crystal structure of a mini-intein reveals a conserved catalytic module involved in side chain cyclization of asparagine during protein splicing
    • Ding Y., et al. Crystal structure of a mini-intein reveals a conserved catalytic module involved in side chain cyclization of asparagine during protein splicing. J. Biol. Chem. 278 (2003) 39133-39142
    • (2003) J. Biol. Chem. , vol.278 , pp. 39133-39142
    • Ding, Y.1
  • 17
    • 33845191735 scopus 로고    scopus 로고
    • Nucleophilic catalysis of oxime ligation
    • Dirksen A., et al. Nucleophilic catalysis of oxime ligation. Angew. Chem. Int. Ed. Engl. 45 (2006) 7581-7584
    • (2006) Angew. Chem. Int. Ed. Engl. , vol.45 , pp. 7581-7584
    • Dirksen, A.1
  • 18
    • 27944433008 scopus 로고    scopus 로고
    • Protein semisynthesis: New proteins for functional and structural studies
    • Durek T., and Becker C.F. Protein semisynthesis: New proteins for functional and structural studies. Biomol. Eng. 22 (2005) 153-172
    • (2005) Biomol. Eng. , vol.22 , pp. 153-172
    • Durek, T.1    Becker, C.F.2
  • 19
    • 0030482408 scopus 로고    scopus 로고
    • The leucine zipper domain controls the orientation of AP-1 in the NFAT.AP-1.DNA complex
    • Erlanson D.A., et al. The leucine zipper domain controls the orientation of AP-1 in the NFAT.AP-1.DNA complex. Chem. Biol. 3 (1996) 981-991
    • (1996) Chem. Biol. , vol.3 , pp. 981-991
    • Erlanson, D.A.1
  • 20
    • 0344351815 scopus 로고    scopus 로고
    • Semisynthesis of cytotoxic proteins using a modified protein splicing element
    • Evans Jr. T.C., et al. Semisynthesis of cytotoxic proteins using a modified protein splicing element. Protein Sci. 7 (1998) 2256-2264
    • (1998) Protein Sci. , vol.7 , pp. 2256-2264
    • Evans Jr., T.C.1
  • 21
    • 0040187857 scopus 로고    scopus 로고
    • Protein trans-splicing and cyclization by a naturally split intein from the dnaE gene of Synechocystis species PCC6803
    • Evans Jr. T.C., et al. Protein trans-splicing and cyclization by a naturally split intein from the dnaE gene of Synechocystis species PCC6803. J. Biol. Chem. 275 (2000) 9091-9094
    • (2000) J. Biol. Chem. , vol.275 , pp. 9091-9094
    • Evans Jr., T.C.1
  • 22
    • 36849084059 scopus 로고    scopus 로고
    • Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes
    • Fernandez-Suarez M., et al. Redirecting lipoic acid ligase for cell surface protein labeling with small-molecule probes. Nat. Biotechnol. 25 (2007) 1483-1487
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1483-1487
    • Fernandez-Suarez, M.1
  • 23
    • 0037774580 scopus 로고    scopus 로고
    • Protein semisynthesis in living cells
    • Giriat I., and Muir T.W. Protein semisynthesis in living cells. J. Am. Chem. Soc. 125 (2003) 7180-7181
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7180-7181
    • Giriat, I.1    Muir, T.W.2
  • 24
    • 0035238173 scopus 로고    scopus 로고
    • Protein splicing and its applications
    • Giriat I., et al. Protein splicing and its applications. Genet. Eng. (NY) 23 (2001) 171-199
    • (2001) Genet. Eng. (NY) , vol.23 , pp. 171-199
    • Giriat, I.1
  • 25
    • 0034581376 scopus 로고    scopus 로고
    • Fluorescent labeling of recombinant proteins in living cells with FlAsH
    • Griffin B.A., et al. Fluorescent labeling of recombinant proteins in living cells with FlAsH. Methods Enzymol. 327 (2000) 565-578
    • (2000) Methods Enzymol. , vol.327 , pp. 565-578
    • Griffin, B.A.1
  • 26
    • 0342813091 scopus 로고    scopus 로고
    • Crystal structure of a Hedgehog autoprocessing domain: Homology between Hedgehog and self-splicing proteins
    • Hall T.M., et al. Crystal structure of a Hedgehog autoprocessing domain: Homology between Hedgehog and self-splicing proteins. Cell 91 (1997) 85-97
    • (1997) Cell , vol.91 , pp. 85-97
    • Hall, T.M.1
  • 28
    • 0018723651 scopus 로고
    • Thioredoxin Catalyzes the Reduction of Insulin Disulfides by Dithiothreitol and Dihydrolipoamide
    • Holmgren. Thioredoxin Catalyzes the Reduction of Insulin Disulfides by Dithiothreitol and Dihydrolipoamide. JBC 254 (1979) 9627-9632
    • (1979) JBC , vol.254 , pp. 9627-9632
    • Holmgren1
  • 29
    • 33644912308 scopus 로고    scopus 로고
    • Highly efficient protein trans-splicing by a naturally split DnaE intein from Nostoc punctiforme
    • Iwai H., et al. Highly efficient protein trans-splicing by a naturally split DnaE intein from Nostoc punctiforme. FEBS Lett. 580 (2006) 1853-1858
    • (2006) FEBS Lett. , vol.580 , pp. 1853-1858
    • Iwai, H.1
  • 30
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • Keppler A., et al. A general method for the covalent labeling of fusion proteins with small molecules in vivo. Nat. Biotechnol. 21 (2003) 86-89
    • (2003) Nat. Biotechnol. , vol.21 , pp. 86-89
    • Keppler, A.1
  • 31
    • 0037020080 scopus 로고    scopus 로고
    • Retrovirally delivered random cyclic Peptide libraries yield inhibitors of interleukin-4 signaling in human B cells
    • Kinsella T.M., et al. Retrovirally delivered random cyclic Peptide libraries yield inhibitors of interleukin-4 signaling in human B cells. J. Biol. Chem. 277 (2002) 37512-37518
    • (2002) J. Biol. Chem. , vol.277 , pp. 37512-37518
    • Kinsella, T.M.1
  • 32
    • 34447329908 scopus 로고    scopus 로고
    • Regioselective cysteine bioconjugation by appending a labeled cystein tag to a protein by using protein splicing in trans
    • Kurpiers T., and Mootz H.D. Regioselective cysteine bioconjugation by appending a labeled cystein tag to a protein by using protein splicing in trans. Angew. Chem. Int. Ed. Engl. 46 (2007) 5234-5237
    • (2007) Angew. Chem. Int. Ed. Engl. , vol.46 , pp. 5234-5237
    • Kurpiers, T.1    Mootz, H.D.2
  • 33
    • 54349101831 scopus 로고    scopus 로고
    • Site-Specific Chemical Modification of Proteins with a Prelabelled Cysteine Tag Using the Artificially Split Mxe GyrA Intein
    • Kurpiers T., and Mootz H.D. Site-Specific Chemical Modification of Proteins with a Prelabelled Cysteine Tag Using the Artificially Split Mxe GyrA Intein. Chembiochem 9 (2008) 2317-2325
    • (2008) Chembiochem , vol.9 , pp. 2317-2325
    • Kurpiers, T.1    Mootz, H.D.2
  • 34
    • 33746311225 scopus 로고    scopus 로고
    • Selective immobilization of proteins onto solid supports through split-intein-mediated protein trans-splicing
    • Kwon Y., et al. Selective immobilization of proteins onto solid supports through split-intein-mediated protein trans-splicing. Angew. Chem. Int. Ed. Engl. 45 (2006) 1726-1729
    • (2006) Angew. Chem. Int. Ed. Engl. , vol.45 , pp. 1726-1729
    • Kwon, Y.1
  • 35
    • 0032569012 scopus 로고    scopus 로고
    • Protein splicing in vitro with a semisynthetic two-component minimal intein
    • Lew B.M., et al. Protein splicing in vitro with a semisynthetic two-component minimal intein. J. Biol. Chem. 273 (1998) 15887-15890
    • (1998) J. Biol. Chem. , vol.273 , pp. 15887-15890
    • Lew, B.M.1
  • 36
    • 0033492884 scopus 로고    scopus 로고
    • Characteristics of protein splicing in trans mediated by a semisynthetic split intein
    • Lew B.M., et al. Characteristics of protein splicing in trans mediated by a semisynthetic split intein. Biopolymers 51 (1999) 355-362
    • (1999) Biopolymers , vol.51 , pp. 355-362
    • Lew, B.M.1
  • 37
    • 33747321396 scopus 로고    scopus 로고
    • Ligation of a synthetic peptide to the N terminus of a recombinant protein using semisynthetic protein trans-splicing
    • Ludwig C., et al. Ligation of a synthetic peptide to the N terminus of a recombinant protein using semisynthetic protein trans-splicing. Angew. Chem. Int. Ed. Engl. 45 (2006) 5218-5221
    • (2006) Angew. Chem. Int. Ed. Engl. , vol.45 , pp. 5218-5221
    • Ludwig, C.1
  • 38
    • 54449093009 scopus 로고    scopus 로고
    • Interaction studies and alanine scanning analysis of a semi-synthetic split intein reveal thiazoline ring formation from an intermediate of the protein splicing reaction
    • Ludwig C., et al. Interaction studies and alanine scanning analysis of a semi-synthetic split intein reveal thiazoline ring formation from an intermediate of the protein splicing reaction. J. Biol. Chem. 283 (2008) 25264-25272
    • (2008) J. Biol. Chem. , vol.283 , pp. 25264-25272
    • Ludwig, C.1
  • 39
    • 0033614484 scopus 로고    scopus 로고
    • Characterization of a self-splicing mini-intein and its conversion into autocatalytic N- and C-terminal cleavage elements: Facile production of protein building blocks for protein ligation
    • Mathys S., et al. Characterization of a self-splicing mini-intein and its conversion into autocatalytic N- and C-terminal cleavage elements: Facile production of protein building blocks for protein ligation. Gene 231 (1999) 1-13
    • (1999) Gene , vol.231 , pp. 1-13
    • Mathys, S.1
  • 40
    • 0032584098 scopus 로고    scopus 로고
    • Protein splicing in trans by purified N- and C-terminal fragments of the Mycobacterium tuberculosis RecA intein
    • Mills K.V., et al. Protein splicing in trans by purified N- and C-terminal fragments of the Mycobacterium tuberculosis RecA intein. Proc. Natl. Acad. Sci. USA 95 (1998) 3543-3548
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3543-3548
    • Mills, K.V.1
  • 41
    • 0037548053 scopus 로고    scopus 로고
    • Semisynthesis of proteins by expressed protein ligation
    • Muir T.W. Semisynthesis of proteins by expressed protein ligation. Annu. Rev. Biochem. 72 (2003) 249-289
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 249-289
    • Muir, T.W.1
  • 42
    • 0032499752 scopus 로고    scopus 로고
    • Expressed protein ligation: A general method for protein engineering
    • Muir T.W., et al. Expressed protein ligation: A general method for protein engineering. Proc. Natl. Acad. Sci. USA 95 (1998) 6705-6710
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6705-6710
    • Muir, T.W.1
  • 43
    • 34247876268 scopus 로고    scopus 로고
    • Exploiting the substrate tolerance of farnesyltransferase for site-selective protein derivatization
    • Nguyen U.T., et al. Exploiting the substrate tolerance of farnesyltransferase for site-selective protein derivatization. Chembiochem 8 (2007) 408-423
    • (2007) Chembiochem , vol.8 , pp. 408-423
    • Nguyen, U.T.1
  • 45
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • Noren C.J., et al. A general method for site-specific incorporation of unnatural amino acids into proteins. Science 244 (1989) 182-188
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1
  • 46
    • 0034602984 scopus 로고    scopus 로고
    • Dissecting the Chemistry of Protein Splicing and Its Applications
    • Noren C.J., et al. Dissecting the Chemistry of Protein Splicing and Its Applications. Angew. Chem. Int. Ed. Engl. 39 (2000) 450-466
    • (2000) Angew. Chem. Int. Ed. Engl. , vol.39 , pp. 450-466
    • Noren, C.J.1
  • 47
    • 0015327122 scopus 로고
    • Novel method for detection of beta-lactamases by using a chromogenic cephalosporin substrate
    • O'Callaghan C.H., et al. Novel method for detection of beta-lactamases by using a chromogenic cephalosporin substrate. Antimicrob. Agents Chemother. 1 (1972) 283-288
    • (1972) Antimicrob. Agents Chemother. , vol.1 , pp. 283-288
    • O'Callaghan, C.H.1
  • 48
    • 34548604645 scopus 로고    scopus 로고
    • Semisynthetic murine prion protein equipped with a GPI anchor mimic incorporates into cellular membranes
    • Olschewski D., et al. Semisynthetic murine prion protein equipped with a GPI anchor mimic incorporates into cellular membranes. Chem. Biol. 14 (2007) 994-1006
    • (2007) Chem. Biol. , vol.14 , pp. 994-1006
    • Olschewski, D.1
  • 49
    • 0037338277 scopus 로고    scopus 로고
    • A genetic approach to identifying mitochondrial proteins
    • Ozawa T., et al. A genetic approach to identifying mitochondrial proteins. Nat. Biotechnol. 21 (2003) 287-293
    • (2003) Nat. Biotechnol. , vol.21 , pp. 287-293
    • Ozawa, T.1
  • 50
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • Paulus H. Protein splicing and related forms of protein autoprocessing. Annu. Rev. Biochem. 69 (2000) 447-496
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 447-496
    • Paulus, H.1
  • 51
    • 0036084146 scopus 로고    scopus 로고
    • InBase: The Intein Database
    • Perler F.B. InBase: The Intein Database. Nucleic Acids Res. 30 (2002) 383-384
    • (2002) Nucleic Acids Res. , vol.30 , pp. 383-384
    • Perler, F.B.1
  • 52
    • 35349018481 scopus 로고    scopus 로고
    • Sortagging: A versatile method for protein labeling
    • Popp M.W., et al. Sortagging: A versatile method for protein labeling. Nat. Chem. Biol. 3 (2007) 707-708
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 707-708
    • Popp, M.W.1
  • 54
    • 0034643993 scopus 로고    scopus 로고
    • A "traceless" Staudinger ligation for the chemoselective synthesis of amide bonds
    • Saxon E., et al. A "traceless" Staudinger ligation for the chemoselective synthesis of amide bonds. Org. Lett. 2 (2000) 2141-2143
    • (2000) Org. Lett. , vol.2 , pp. 2141-2143
    • Saxon, E.1
  • 55
    • 42249110717 scopus 로고    scopus 로고
    • A photoinducible 1,3-dipolar cycloaddition reaction for rapid, selective modification of tetrazole-containing proteins
    • Song W., et al. A photoinducible 1,3-dipolar cycloaddition reaction for rapid, selective modification of tetrazole-containing proteins. Angew. Chem. Int. Ed. Engl. 47 (2008) 2832-2835
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 2832-2835
    • Song, W.1
  • 56
    • 0032481347 scopus 로고    scopus 로고
    • Control of protein splicing by intein fragment reassembly
    • Southworth M.W., et al. Control of protein splicing by intein fragment reassembly. EMBO J. 17 (1998) 918-926
    • (1998) EMBO J. , vol.17 , pp. 918-926
    • Southworth, M.W.1
  • 57
    • 0032988320 scopus 로고    scopus 로고
    • Purification of proteins fused to either the amino or carboxy terminus of the Mycobacterium xenopi gyrase A intein
    • 116, 118-120
    • Southworth M.W., et al. Purification of proteins fused to either the amino or carboxy terminus of the Mycobacterium xenopi gyrase A intein. Biotechniques 27 (1999) 110-114 116, 118-120
    • (1999) Biotechniques , vol.27 , pp. 110-114
    • Southworth, M.W.1
  • 59
    • 4143058067 scopus 로고    scopus 로고
    • Synthetic Two-piece and Three-piece Split Inteins for Protein trans-Splicing
    • Sun W., et al. Synthetic Two-piece and Three-piece Split Inteins for Protein trans-Splicing. J. Biological Chemistry 279 (2004) 35281-35286
    • (2004) J. Biological Chemistry , vol.279 , pp. 35281-35286
    • Sun, W.1
  • 60
    • 34447342528 scopus 로고    scopus 로고
    • Evolved orthogonal ribosomes enhance the efficiency of synthetic genetic code expansion
    • Wang K., et al. Evolved orthogonal ribosomes enhance the efficiency of synthetic genetic code expansion. Nat. Biotechnol. 25 (2007) 770-777
    • (2007) Nat. Biotechnol. , vol.25 , pp. 770-777
    • Wang, K.1
  • 61
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang L., et al. Expanding the genetic code of Escherichia coli. Science 292 (2001) 498-500
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1
  • 63
    • 0038288767 scopus 로고    scopus 로고
    • Reverse proteolysis promoted by in situ generated peptide ester fragments
    • Wehofsky N., et al. Reverse proteolysis promoted by in situ generated peptide ester fragments. J. Am. Chem. Soc. 125 (2003) 6126-6133
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6126-6133
    • Wehofsky, N.1
  • 64
    • 0032483013 scopus 로고    scopus 로고
    • Protein trans-splicing by a split intein encoded in a split DnaE gene of Synechocystis sp
    • Wu H., et al. Protein trans-splicing by a split intein encoded in a split DnaE gene of Synechocystis sp. PCC6803. Proc. Natl. Acad. Sci. USA 95 (1998) 9226-9231
    • (1998) PCC6803. Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9226-9231
    • Wu, H.1
  • 65
    • 33749019097 scopus 로고    scopus 로고
    • A chemical toolkit for proteins--an expanded genetic code
    • Xie J., and Schultz P.G. A chemical toolkit for proteins--an expanded genetic code. Nat. Rev. Mol. Cell. Biol. 7 (2006) 775-782
    • (2006) Nat. Rev. Mol. Cell. Biol. , vol.7 , pp. 775-782
    • Xie, J.1    Schultz, P.G.2
  • 66
    • 0033814098 scopus 로고    scopus 로고
    • Fusions to self-splicing inteins for protein purification
    • Xu M.Q., et al. Fusions to self-splicing inteins for protein purification. Methods Enzymol. 326 (2000) 376-418
    • (2000) Methods Enzymol. , vol.326 , pp. 376-418
    • Xu, M.Q.1
  • 67
    • 0032503612 scopus 로고    scopus 로고
    • Segmental Isotope Labeling for Protein NMR Using Peptide Splicing
    • Yamazaki T. Segmental Isotope Labeling for Protein NMR Using Peptide Splicing. J. Am. Chem. Soc. 120 (1998) 5591-5592
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 5591-5592
    • Yamazaki, T.1
  • 68
    • 27644508250 scopus 로고    scopus 로고
    • Genetically encoded short peptide tag for versatile protein labeling by Sfp phosphopantetheinyl transferase
    • Yin J., et al. Genetically encoded short peptide tag for versatile protein labeling by Sfp phosphopantetheinyl transferase. Proc. Natl. Acad. Sci. USA 102 (2005) 15815-15820
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15815-15820
    • Yin, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.