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Volumn 271, Issue 4, 2004, Pages 663-677

Expressed protein ligation: Method and applications

Author keywords

Expressed protein ligation; IMPACT system; Intein; Native chemical ligation

Indexed keywords

ENDONUCLEASE; INTEIN; NANOPARTICLE; THIOESTER;

EID: 1342301482     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.03978.x     Document Type: Review
Times cited : (128)

References (117)
  • 1
    • 0032111031 scopus 로고    scopus 로고
    • A new general method for the biosynthesis of stable isotope-enriched peptides using a decahistidine-tagged ubiquitin fusion system: An application to the production of mastoparan-X uniformly enriched with 15N and 15N/13C
    • Kohno, T., Kusunoki, H., Sato, K. & Wakamatsu, K. (1998) A new general method for the biosynthesis of stable isotope-enriched peptides using a decahistidine-tagged ubiquitin fusion system: an application to the production of mastoparan-X uniformly enriched with 15N and 15N/13C. J. Biomol. NMR 12, 109-121.
    • (1998) J. Biomol. NMR , vol.12 , pp. 109-121
    • Kohno, T.1    Kusunoki, H.2    Sato, K.3    Wakamatsu, K.4
  • 2
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • Marley, J., Lu, M. & Bracken, C. (2001) A method for efficient isotopic labeling of recombinant proteins. J. Biomol. NMR 20, 71-75.
    • (2001) J. Biomol. NMR , vol.20 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 6
    • 0029102380 scopus 로고
    • Peptide ligation and semisynthesis
    • Wallace, C.J. (1995) Peptide ligation and semisynthesis. Curr. Opin. Biotechnol. 6, 403-410.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 403-410
    • Wallace, C.J.1
  • 7
    • 0028223433 scopus 로고
    • Peptide segment ligation strategy without use of protecting groups
    • Liu, C.-F. & Tam, J.P. (1994) Peptide segment ligation strategy without use of protecting groups. Proc. Natl Acad. Sci. USA 91, 6584-6588.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6584-6588
    • Liu, C.-F.1    Tam, J.P.2
  • 8
    • 0001385018 scopus 로고
    • Synthesis of a 39-peptide and a 25-peptide by thiol capture ligations: Observation of a 40-fold rate acceleration of the intramolecular O,N-acyl-transfer reaction between peptide fragments bearing only cysteine protective groups
    • Kemp, D.S. & Carey, R.I. (1993) Synthesis of a 39-peptide and a 25-peptide by thiol capture ligations: observation of a 40-fold rate acceleration of the intramolecular O,N-acyl-transfer reaction between peptide fragments bearing only cysteine protective groups. J. Org. Chem. 58, 2216-2222.
    • (1993) J. Org. Chem. , vol.58 , pp. 2216-2222
    • Kemp, D.S.1    Carey, R.I.2
  • 9
    • 0015983977 scopus 로고
    • Spontaneous re-formation of a broken peptide chain
    • Dyckes, D.F., Creighton, T. & Sheppard, R.C. (1974) Spontaneous re-formation of a broken peptide chain. Nature 247, 202-204.
    • (1974) Nature , vol.247 , pp. 202-204
    • Dyckes, D.F.1    Creighton, T.2    Sheppard, R.C.3
  • 10
    • 0027419150 scopus 로고
    • Understanding cytochrome c function: Engineering protein structure by semisynthesis
    • Wallace, C.J. (1993) Understanding cytochrome c function: engineering protein structure by semisynthesis. FASEB J. 7, 505-515.
    • (1993) FASEB J. , vol.7 , pp. 505-515
    • Wallace, C.J.1
  • 11
    • 0037628610 scopus 로고    scopus 로고
    • Total chemical synthesis of a functional interacting protein pair: The protooncogene H-Ras and the Ras-binding domain of its effector c-Raf1
    • Becker, C.F., Hunter, C.L., Seidel, R., Kent, S.B., Goody, R.S. & Engelhard, M. (2003) Total chemical synthesis of a functional interacting protein pair: the protooncogene H-Ras and the Ras-binding domain of its effector c-Raf1. Proc. Natl Acad. Sci. USA 100, 5075-5080.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5075-5080
    • Becker, C.F.1    Hunter, C.L.2    Seidel, R.3    Kent, S.B.4    Goody, R.S.5    Engelhard, M.6
  • 12
    • 0032499752 scopus 로고    scopus 로고
    • Expressed protein ligation: A general method for protein engineering
    • Muir, T.W., Sondhi, D. & Cole, P.A. (1998) Expressed protein ligation: a general method for protein engineering. Proc. Natl Acad. Sci. USA 95, 6705-6710.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6705-6710
    • Muir, T.W.1    Sondhi, D.2    Cole, P.A.3
  • 13
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson, P.E., Muir, T.W., Clark-Lewis, I. & Kent, S.B. (1994) Synthesis of proteins by native chemical ligation. Science 266, 776-779.
    • (1994) Science , vol.266 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.4
  • 14
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • Dawson, P.E. & Kent, S.B. (2000) Synthesis of native proteins by chemical ligation. Annu. Rev. Biochem. 69, 923-960.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 923-960
    • Dawson, P.E.1    Kent, S.B.2
  • 15
    • 84939246733 scopus 로고
    • Bildung von S-haltigen Peptiden durch intramolekulare Wanderung von Aminoacylresten
    • Wieland, T., Bokelmann, E., Bauer, L., Lang, H.U. & Lau, H. (1953) Bildung von S-haltigen Peptiden durch intramolekulare Wanderung von Aminoacylresten. Annalen Chemie 583, 129-149.
    • (1953) Annalen Chemie , vol.583 , pp. 129-149
    • Wieland, T.1    Bokelmann, E.2    Bauer, L.3    Lang, H.U.4    Lau, H.5
  • 16
    • 0035685801 scopus 로고    scopus 로고
    • Methods and strategies of peptide ligation
    • Tam, J.P., Xu, J. & Eom, K.D. (2001) Methods and strategies of peptide ligation. Biopolymers 60, 194-205.
    • (2001) Biopolymers , vol.60 , pp. 194-205
    • Tam, J.P.1    Xu, J.2    Eom, K.D.3
  • 17
    • 0029559773 scopus 로고
    • Peptide synthesis using unprotected peptides through orthogonal coupling methods
    • Tam, J.P., Lu, Y.A., Liu, C.F. & Shao, J. (1995) Peptide synthesis using unprotected peptides through orthogonal coupling methods. Proc. Natl Acad. Sci. USA 92, 12485-12489.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12485-12489
    • Tam, J.P.1    Lu, Y.A.2    Liu, C.F.3    Shao, J.4
  • 18
    • 0001153517 scopus 로고
    • Selective reduction of disulfides by tris (2-carboxyethyl) phosphine
    • Burns, J.A., Butler, J.C., Moran, J. & Whitesides, G.M. (1991) Selective reduction of disulfides by tris (2-carboxyethyl) phosphine. J. Org. Chem. 56, 2648-2650.
    • (1991) J. Org. Chem. , vol.56 , pp. 2648-2650
    • Burns, J.A.1    Butler, J.C.2    Moran, J.3    Whitesides, G.M.4
  • 19
    • 0030973396 scopus 로고    scopus 로고
    • Modulation of reactivity in native chemical ligation through the use of thiol additives
    • Dawson, P.E., Churchill, M., Ghadiri, M.R. & Kent, S.B.H. (1997) Modulation of reactivity in native chemical ligation through the use of thiol additives. J. Am. Chem. Soc. 119, 4325-4329.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 4325-4329
    • Dawson, P.E.1    Churchill, M.2    Ghadiri, M.R.3    Kent, S.B.H.4
  • 20
    • 0033621158 scopus 로고    scopus 로고
    • Protein synthesis by native chemical ligation: Expanded scope by using straightforward methodology
    • Hackeng, T.M., Griffin, J.H. & Dawson, P.E. (1999) Protein synthesis by native chemical ligation: expanded scope by using straightforward methodology. Proc. Natl Acad. Sci. USA 96, 10068-10073.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10068-10073
    • Hackeng, T.M.1    Griffin, J.H.2    Dawson, P.E.3
  • 21
    • 0041783935 scopus 로고    scopus 로고
    • Native chemical ligation with aspartic and glutamic acids as C-terminal residues: Scope and limitations
    • Villain, M., Gaertner, H. & Botti, P. (2003) Native chemical ligation with aspartic and glutamic acids as C-terminal residues: Scope and limitations. Eur. J. Org. Chem. 3267-3272.
    • (2003) Eur. J. Org. Chem. , pp. 3267-3272
    • Villain, M.1    Gaertner, H.2    Botti, P.3
  • 22
    • 0033615313 scopus 로고    scopus 로고
    • Chemical protein synthesis by solid phase ligation of unprotected peptide segments
    • Canne, L.E., Botti, P., Simon, R.J., Chen, Y., Dennis, E.A. & Kent, S.B.H. (1999) Chemical protein synthesis by solid phase ligation of unprotected peptide segments. J. Am. Chem. Soc. 121, 8720-8727.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8720-8727
    • Canne, L.E.1    Botti, P.2    Simon, R.J.3    Chen, Y.4    Dennis, E.A.5    Kent, S.B.H.6
  • 23
    • 0035701972 scopus 로고    scopus 로고
    • Tandem peptide ligation for synthetic and natural biologicals
    • Tam, J.P., Yu, Q. & Lu, Y.A. (2001) Tandem peptide ligation for synthetic and natural biologicals. Biologicals 29, 189-196.
    • (2001) Biologicals , vol.29 , pp. 189-196
    • Tam, J.P.1    Yu, Q.2    Lu, Y.A.3
  • 24
    • 0037425576 scopus 로고    scopus 로고
    • Tandem ligation of multipartite peptides with cell-permeable activity
    • Eom, K.D., Miao, Z., Yang, J.L. & Tam, J.P. (2003) Tandem ligation of multipartite peptides with cell-permeable activity. J. Am. Chem. Soc. 125, 73-82.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 73-82
    • Eom, K.D.1    Miao, Z.2    Yang, J.L.3    Tam, J.P.4
  • 25
    • 0034808792 scopus 로고    scopus 로고
    • Selenocysteine in native chemical ligation and expressed protein ligation
    • Hondal, R.J., Nilsson, B.L. & Raines, R.T. (2001) Selenocysteine in native chemical ligation and expressed protein ligation. J. Am. Chem. Soc. 123, 5140-5141.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5140-5141
    • Hondal, R.J.1    Nilsson, B.L.2    Raines, R.T.3
  • 26
    • 0037981629 scopus 로고    scopus 로고
    • Incorporation of selenomethionine into proteins through selenohomocysteine-mediated ligation
    • Roelfes, G. & Hilvert, D. (2003) Incorporation of selenomethionine into proteins through selenohomocysteine-mediated ligation. Angew. Chem. Int. Ed. Engl. 42, 2275-2277.
    • (2003) Angew. Chem. Int. Ed. Engl. , vol.42 , pp. 2275-2277
    • Roelfes, G.1    Hilvert, D.2
  • 27
    • 0034023981 scopus 로고    scopus 로고
    • Peptide thioester preparation by Fmoc solid phase peptide synthesis for use in native chemical ligation
    • Clippingdale, A.B., Barrow, C.J. & Wade, J.D. (2000) Peptide thioester preparation by Fmoc solid phase peptide synthesis for use in native chemical ligation. J. Pept. Sci. 6, 225-234.
    • (2000) J. Pept. Sci. , vol.6 , pp. 225-234
    • Clippingdale, A.B.1    Barrow, C.J.2    Wade, J.D.3
  • 28
    • 0032548051 scopus 로고    scopus 로고
    • Direct preparation of peptide thioesters using an Fmoc solid-phase method
    • Li, X., Kawakami, T. & Aimoto, S. (1998) Direct preparation of peptide thioesters using an Fmoc solid-phase method. Tetrahedron Lett. 39, 8669-8672.
    • (1998) Tetrahedron Lett. , vol.39 , pp. 8669-8672
    • Li, X.1    Kawakami, T.2    Aimoto, S.3
  • 29
    • 0037170594 scopus 로고    scopus 로고
    • An improved deblocking agent for direct Fmoc solid-phase synthesis of peptide thioesters
    • Bu, X., Xie, G., Law, C.W. & Guo, Z. (2002) An improved deblocking agent for direct Fmoc solid-phase synthesis of peptide thioesters. Tetrahedron Lett. 43, 2419-2422.
    • (2002) Tetrahedron Lett. , vol.43 , pp. 2419-2422
    • Bu, X.1    Xie, G.2    Law, C.W.3    Guo, Z.4
  • 30
    • 0001176887 scopus 로고    scopus 로고
    • Activation method to prepare a highly reactive acylsulfonamide 'safety-catch' linker for solid-phase synthesis
    • Backes, B.J., Virgilio, A.A. & Ellman, J.A. (1996) Activation method to prepare a highly reactive acylsulfonamide 'safety-catch' linker for solid-phase synthesis. J. Am. Chem. Soc. 118, 3055-3056.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3055-3056
    • Backes, B.J.1    Virgilio, A.A.2    Ellman, J.A.3
  • 31
    • 0033596308 scopus 로고    scopus 로고
    • Fmoc-based synthesis of peptide-alpha thioesters: Application to the total chemical synthesis of a glycoprotein by native chemical ligation
    • Shin, Y., Winans, K.A., Backes, B.J., Kent, S.B.H., Ellman, J.A. & Bertozzi, C.R. (1999) Fmoc-based synthesis of peptide-alpha thioesters: Application to the total chemical synthesis of a glycoprotein by native chemical ligation. J. Am. Chem. Soc. 121, 11684-11689.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11684-11689
    • Shin, Y.1    Winans, K.A.2    Backes, B.J.3    Kent, S.B.H.4    Ellman, J.A.5    Bertozzi, C.R.6
  • 32
    • 0033572729 scopus 로고    scopus 로고
    • Solid phase synthesis of peptide C-terminal thioesters by Fmoc/t-Bu chemistry
    • Ingenito, R., Bianchi, E., Fattori, D. & Pessi, A. (1999) Solid phase synthesis of peptide C-terminal thioesters by Fmoc/t-Bu chemistry. J. Am. Chem. Soc. 121, 11369-11374.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11369-11374
    • Ingenito, R.1    Bianchi, E.2    Fattori, D.3    Pessi, A.4
  • 33
    • 0033607759 scopus 로고    scopus 로고
    • Backbone amide linker (BAL) strategy for N (alpha)- fluorenylmethoxycarbonyl (Fmoc) solid-phase synthesis of unprotected peptide p-nitroanilides and thioesters
    • Alsina, J., Yokum, T.S., Albericio, F. & Barany, G. (1999) Backbone amide linker (BAL) strategy for N (alpha)-fluorenylmethoxycarbonyl (Fmoc) solid-phase synthesis of unprotected peptide p-nitroanilides and thioesters. J. Org. Chem. 64, 8761-8769.
    • (1999) J. Org. Chem. , vol.64 , pp. 8761-8769
    • Alsina, J.1    Yokum, T.S.2    Albericio, F.3    Barany, G.4
  • 34
    • 0034632429 scopus 로고    scopus 로고
    • Facile, Fmoc-compatible solid-phase synthesis of peptide C-terminal thioesters
    • Swinnen, D. & Hilvert, D. (2000) Facile, Fmoc-compatible solid-phase synthesis of peptide C-terminal thioesters. Org. Lett. 2, 2439-2442.
    • (2000) Org. Lett. , vol.2 , pp. 2439-2442
    • Swinnen, D.1    Hilvert, D.2
  • 35
    • 0035903684 scopus 로고    scopus 로고
    • Fmoc-compatible solid-phase peptide synthesis of long C-terminal peptide thioesters
    • Sewing, A. & Hilvert, D. (2001) Fmoc-compatible solid-phase peptide synthesis of long C-terminal peptide thioesters. Angew. Chem. Int. Ed. Engl. 40, 3395-3396.
    • (2001) Angew. Chem. Int. Ed. Engl. , vol.40 , pp. 3395-3396
    • Sewing, A.1    Hilvert, D.2
  • 36
    • 0030802865 scopus 로고    scopus 로고
    • Preparation of peptide thioesters using Fmoc-solid-phase peptide synthesis and its application to the construction of a template-assembled synthetic protein (TASP)
    • Futaki, S., Sogawa, K., Maruyama, J., Asahara, T. & Niwa, M. (1997) Preparation of peptide thioesters using Fmoc-solid-phase peptide synthesis and its application to the construction of a template-assembled synthetic protein (TASP). Tetrahedron Lett. 38, 6237-6240.
    • (1997) Tetrahedron Lett. , vol.38 , pp. 6237-6240
    • Futaki, S.1    Sogawa, K.2    Maruyama, J.3    Asahara, T.4    Niwa, M.5
  • 39
    • 0023733049 scopus 로고
    • A dominant trifluoperazine resistance gene from Saccharomyces cerevisiae has homology with F0F1 ATP synthase and confers calcium-sensitive growth
    • Shih, C.K., Wagner, R., Feinstein, S., Kanik-Ennulat, C. & Neff, N. (1988) A dominant trifluoperazine resistance gene from Saccharomyces cerevisiae has homology with F0F1 ATP synthase and confers calcium-sensitive growth. Mol. Cell. Biol. 8, 3094-3103.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3094-3103
    • Shih, C.K.1    Wagner, R.2    Feinstein, S.3    Kanik-Ennulat, C.4    Neff, N.5
  • 40
    • 0033963173 scopus 로고    scopus 로고
    • InBase, the intein database
    • Perler, F.B. (2000) InBase, the intein database. Nucleic Acids Res. 28, 344-345.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 344-345
    • Perler, F.B.1
  • 41
    • 0035479142 scopus 로고    scopus 로고
    • Deletional bias and the evolution of bacterial genomes
    • Mira, A., Ochman, H. & Moran, N.A. (2001) Deletional bias and the evolution of bacterial genomes. Trends Genet. 11, 589-596.
    • (2001) Trends Genet. , vol.11 , pp. 589-596
    • Mira, A.1    Ochman, H.2    Moran, N.A.3
  • 42
    • 0027373712 scopus 로고
    • Protein splicing: Selfish genes invade cellular proteins
    • Neff, N.F. (1993) Protein splicing: Selfish genes invade cellular proteins. Curr. Opin. Cell Biol. 5, 971-976.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 971-976
    • Neff, N.F.1
  • 43
    • 0033598755 scopus 로고    scopus 로고
    • Recurrent invasion and extinction of a selfish gene
    • Goddard, M.R. & Burt, A. (1999) Recurrent invasion and extinction of a selfish gene. Proc. Natl Acad. Sci. USA 96, 13880-13885.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13880-13885
    • Goddard, M.R.1    Burt, A.2
  • 44
    • 0035425040 scopus 로고    scopus 로고
    • Intein spread and extinction in evolution
    • Pietrokovski, S. (2001) Intein spread and extinction in evolution. Trends Genet. 17, 465-472.
    • (2001) Trends Genet. , vol.17 , pp. 465-472
    • Pietrokovski, S.1
  • 45
    • 0036882402 scopus 로고    scopus 로고
    • Mechanistic and kinetic considerations of protein splicing
    • Evans, T.C. Jr & Xu, M.-Q. (2002) Mechanistic and kinetic considerations of protein splicing. Chem. Rev. 102, 4869-4883.
    • (2002) Chem. Rev. , vol.102 , pp. 4869-4883
    • Evans Jr., T.C.1    Xu, M.-Q.2
  • 46
    • 0342470656 scopus 로고    scopus 로고
    • Intein-mediated protein ligation: Harnessing nature's escape artists
    • Evans, T.C. Jr & Xu, M.-Q. (2000) Intein-mediated protein ligation: harnessing nature's escape artists. Biopolymers 51, 333-342.
    • (2000) Biopolymers , vol.51 , pp. 333-342
    • Evans Jr., T.C.1    Xu, M.-Q.2
  • 47
    • 0029838842 scopus 로고    scopus 로고
    • The mechanism of protein splicing and its modulation by mutation
    • Xu, M.Q. & Perler, F.B. (1996) The mechanism of protein splicing and its modulation by mutation. EMBO J. 15, 5146-5153.
    • (1996) EMBO J. , vol.15 , pp. 5146-5153
    • Xu, M.Q.1    Perler, F.B.2
  • 48
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • Paulus, H. (2000) Protein splicing and related forms of protein autoprocessing. Annu. Rev. Biochem. 69, 447-496.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 447-496
    • Paulus, H.1
  • 49
    • 0034602984 scopus 로고    scopus 로고
    • Dissecting the chemistry of protein splicing and its applications
    • Noren, C.J., Wang, J. & Perler, F.B. (2000) Dissecting the chemistry of protein splicing and its applications. Angew. Chem. Int. Ed. Engl. 39, 450-466.
    • (2000) Angew. Chem. Int. Ed. Engl. , vol.39 , pp. 450-466
    • Noren, C.J.1    Wang, J.2    Perler, F.B.3
  • 50
    • 0037548053 scopus 로고    scopus 로고
    • Semisynthesis of proteins by expressed protein ligation
    • Muir, T.W. (2003) Semisynthesis of proteins by expressed protein ligation. Annu. Rev. Biochem. 72, 249-289.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 249-289
    • Muir, T.W.1
  • 51
    • 0031975772 scopus 로고    scopus 로고
    • Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing
    • Klabunde, T., Sharma, S., Telenti, A., Jacobs, W.R. Jr & Sacchettini, J.C. (1998) Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing. Nat. Struct. Biol. 5, 31-36.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 31-36
    • Klabunde, T.1    Sharma, S.2    Telenti, A.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5
  • 52
    • 0034617214 scopus 로고    scopus 로고
    • Protein splicing in the absence of an intein penultimate histidine
    • Chen, L., Benner, J. & Perler, F.B. (2000) Protein splicing in the absence of an intein penultimate histidine. J. Biol. Chem. 275, 20431-20435.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20431-20435
    • Chen, L.1    Benner, J.2    Perler, F.B.3
  • 53
    • 0036295886 scopus 로고    scopus 로고
    • Protein-splicing reaction via a thiazolidine intermediate: Crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides
    • Mizutani, R., Nogami, S., Kawasaki, M., Ohya, Y., Anraku, Y. & Satow, Y. (2002) Protein-splicing reaction via a thiazolidine intermediate: crystal structure of the VMA1-derived endonuclease bearing the N and C-terminal propeptides. J. Mol Biol. 316, 919-929.
    • (2002) J. Mol. Biol. , vol.316 , pp. 919-929
    • Mizutani, R.1    Nogami, S.2    Kawasaki, M.3    Ohya, Y.4    Anraku, Y.5    Satow, Y.6
  • 54
    • 0030952831 scopus 로고    scopus 로고
    • Identification of three core regions essential for protein splicing of the yeast VMA1 protozyme. A random mutagenesis study of the entire VMA1-derived endonuclease sequence
    • Kawasaki, M., Nogami, S., Satow, Y., Ohya, Y. & Anraku, Y. (1997) Identification of three core regions essential for protein splicing of the yeast VMA1 protozyme. A random mutagenesis study of the entire VMA1-derived endonuclease sequence. J. Biol. Chem. 272, 15668-15674.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15668-15674
    • Kawasaki, M.1    Nogami, S.2    Satow, Y.3    Ohya, Y.4    Anraku, Y.5
  • 55
    • 0030611387 scopus 로고    scopus 로고
    • Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity
    • Duan, X., Gimble, F.S. & Quiocho, F.A. (1997) Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity. Cell 89, 555-564.
    • (1997) Cell , vol.89 , pp. 555-564
    • Duan, X.1    Gimble, F.S.2    Quiocho, F.A.3
  • 56
    • 0036786717 scopus 로고    scopus 로고
    • Crystal structure of the intein homing endonuclease PI-SceI bound to its recognition sequence
    • Moure, C.M., Gimble, F.S. & Quiocho, F.A. (2002) Crystal structure of the intein homing endonuclease PI-SceI bound to its recognition sequence. Nat. Struct. Biol. 9, 764-770.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 764-770
    • Moure, C.M.1    Gimble, F.S.2    Quiocho, F.A.3
  • 57
    • 0034595699 scopus 로고    scopus 로고
    • Structural insights into the protein splicing mechanism of PI-SceI
    • Poland, B.W., Xu, M.Q. & Quiocho, F.A. (2000) Structural insights into the protein splicing mechanism of PI-SceI. J. Biol. Chem. 275, 16408-16413.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16408-16413
    • Poland, B.W.1    Xu, M.Q.2    Quiocho, F.A.3
  • 58
    • 0035968177 scopus 로고    scopus 로고
    • Zinc inhibition of protein trans-splicing and identification of regions essential for splicing and association of a split intein*
    • Ghosh, I., Sun, L. & Xu, M.Q. (2001) Zinc inhibition of protein trans-splicing and identification of regions essential for splicing and association of a split intein*. J. Biol. Chem. 276, 24051-24058.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24051-24058
    • Ghosh, I.1    Sun, L.2    Xu, M.Q.3
  • 59
    • 0035815658 scopus 로고    scopus 로고
    • Reversible inhibition of protein splicing by zinc ion
    • Mills, K.V. & Paulus, H. (2001) Reversible inhibition of protein splicing by zinc ion. J. Biol. Chem. 276, 10832-10838.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10832-10838
    • Mills, K.V.1    Paulus, H.2
  • 60
    • 0034723273 scopus 로고    scopus 로고
    • Probing the structure of the PI-SceI-DNA complex by affinity cleavage and affinity photocross-linking
    • Hu, D., Crist, M., Duan, X., Quiocho, F.A. & Gimble, F.S. (2000) Probing the structure of the PI-SceI-DNA complex by affinity cleavage and affinity photocross-linking. J. Biol. Chem. 275, 2705-2712.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2705-2712
    • Hu, D.1    Crist, M.2    Duan, X.3    Quiocho, F.A.4    Gimble, F.S.5
  • 61
    • 0032498234 scopus 로고    scopus 로고
    • Protein splicing of inteins and hedgehog autoproteolysis: Structure, function, and evolution
    • Perler, F.B. (1998) Protein splicing of inteins and hedgehog autoproteolysis: structure, function, and evolution. Cell 92, 1-4.
    • (1998) Cell , vol.92 , pp. 1-4
    • Perler, F.B.1
  • 63
    • 0344351815 scopus 로고    scopus 로고
    • Semisynthesis of cytotoxic proteins using a modified protein splicing element
    • Evans, T.C. Jr, Benner, J. & Xu, M.Q. (1998) Semisynthesis of cytotoxic proteins using a modified protein splicing element. Protein. Sci. 7, 2256-2264.
    • (1998) Protein. Sci. , vol.7 , pp. 2256-2264
    • Evans Jr., T.C.1    Benner, J.2    Xu, M.Q.3
  • 64
    • 0032988320 scopus 로고    scopus 로고
    • Purification of proteins fused to either the amino or carboxy terminus of the Mycobacterium xenopi gyrase A intein
    • Southworth, M.W., Amaya, K., Evans, T.C., Xu, M.Q. & Perler, F.B. (1999) Purification of proteins fused to either the amino or carboxy terminus of the Mycobacterium xenopi gyrase A intein. Biotechniques 27, 110-114,116,118-20.
    • (1999) Biotechniques , vol.27 , pp. 110-114
    • Southworth, M.W.1    Amaya, K.2    Evans, T.C.3    Xu, M.Q.4    Perler, F.B.5
  • 65
    • 0032568924 scopus 로고    scopus 로고
    • Expressed protein ligation, a novel method for studying protein-protein interactions in transcription
    • Severinov, K. & Muir, T.W. (1998) Expressed protein ligation, a novel method for studying protein-protein interactions in transcription. J. Biol. Chem. 273, 16205-16209.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16205-16209
    • Severinov, K.1    Muir, T.W.2
  • 66
    • 0036669566 scopus 로고    scopus 로고
    • Recent advances in the application of expressed protein ligation to protein engineering
    • Hofmann, R.M. & Muir, T.W. (2002) Recent advances in the application of expressed protein ligation to protein engineering. Curr. Opin. Biotechnol. 13, 297-303.
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 297-303
    • Hofmann, R.M.1    Muir, T.W.2
  • 67
    • 0035913759 scopus 로고    scopus 로고
    • Protein tyrosine kinase Csk-catalyzed phosphorylation of Src containing unnatural tyrosine analogues
    • Wang, D. & Cole, P.A. (2001) Protein tyrosine kinase Csk-catalyzed phosphorylation of Src containing unnatural tyrosine analogues. J. Am. Chem. Soc. 123, 8883-8886.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8883-8886
    • Wang, D.1    Cole, P.A.2
  • 68
    • 0034758469 scopus 로고    scopus 로고
    • Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling
    • Lu, W., Gong, D., Bar-Sagi, D. & Cole, P.A. (2001) Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling. Mol. Cell. 8, 759-769.
    • (2001) Mol. Cell , vol.8 , pp. 759-769
    • Lu, W.1    Gong, D.2    Bar-Sagi, D.3    Cole, P.A.4
  • 70
    • 0035904886 scopus 로고    scopus 로고
    • Fluorescent monitoring of kinase activity in real time: Development of a robust fluorescence-based assay for AbI tyrosine kinase activity
    • Hofmann, R.M., Cotton, G.J., Chang, E.J., Vidal, E., Veach, D., Bornmann, W. & Muir, T.W. (2001) Fluorescent monitoring of kinase activity in real time: development of a robust fluorescence-based assay for AbI tyrosine kinase activity. Bioorg. Med. Chem. Lett. 11, 3091-3094.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 3091-3094
    • Hofmann, R.M.1    Cotton, G.J.2    Chang, E.J.3    Vidal, E.4    Veach, D.5    Bornmann, W.6    Muir, T.W.7
  • 71
    • 0033506586 scopus 로고    scopus 로고
    • Introduction of unnatural amino acids into proteins using expressed protein ligation
    • Ayers, B., Blaschke, U.K., Camarero, J.A., Cotton, G.J., Holford, M. & Muir, T.W. (1999) Introduction of unnatural amino acids into proteins using expressed protein ligation. Biopolymers 51, 343-354.
    • (1999) Biopolymers , vol.51 , pp. 343-354
    • Ayers, B.1    Blaschke, U.K.2    Camarero, J.A.3    Cotton, G.J.4    Holford, M.5    Muir, T.W.6
  • 72
    • 0033540665 scopus 로고    scopus 로고
    • Insertion of a synthetic peptide into a recombinant protein framework: A protein biosensor
    • Cotton, G.J., Ayers, B., Xu, R. & Muir, T.W. (1999) Insertion of a synthetic peptide into a recombinant protein framework: a protein biosensor. J. Am. Chem. Soc. 121, 1100-1101.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 1100-1101
    • Cotton, G.J.1    Ayers, B.2    Xu, R.3    Muir, T.W.4
  • 73
    • 0034177596 scopus 로고    scopus 로고
    • Generation of a dual-labeled fluorescence biosensor for Crk-II phosphorylation using solid-phase expressed protein ligation
    • Cotton, G.J. & Muir, T.W. (2000) Generation of a dual-labeled fluorescence biosensor for Crk-II phosphorylation using solid-phase expressed protein ligation. Chem. Biol. 7, 253-261.
    • (2000) Chem. Biol. , vol.7 , pp. 253-261
    • Cotton, G.J.1    Muir, T.W.2
  • 74
    • 0037936779 scopus 로고    scopus 로고
    • Merging fluorescence resonance energy transfer and expressed protein ligation to analyze protein-protein interactions
    • Scheibner, K.A., Zhang, Z. & Cole, P.A. (2003) Merging fluorescence resonance energy transfer and expressed protein ligation to analyze protein-protein interactions. Anal. Biochem. 317, 226-232.
    • (2003) Anal. Biochem. , vol.317 , pp. 226-232
    • Scheibner, K.A.1    Zhang, Z.2    Cole, P.A.3
  • 76
    • 0347358980 scopus 로고    scopus 로고
    • Semisynthesis and application of carboxyfluorescein-labelled biologically active human interleukin-8
    • David, R., Machova, Z. & Beck-Sickinger, A.G. (2003) Semisynthesis and application of carboxyfluorescein-labelled biologically active human interleukin-8. Biol. Chem. 384, 1619-1630.
    • (2003) Biol. Chem. , vol.384 , pp. 1619-1630
    • David, R.1    Machova, Z.2    Beck-Sickinger, A.G.3
  • 77
    • 0034123154 scopus 로고    scopus 로고
    • Site-specific independent double labeling of proteins with reporter atoms
    • Wallace, C.J.A. & Clark-Lewis, I. (2000) Site-specific independent double labeling of proteins with reporter atoms. Bioch. Cell Biol. 78, 79-86.
    • (2000) Bioch. Cell Biol. , vol.78 , pp. 79-86
    • Wallace, C.J.A.1    Clark-Lewis, I.2
  • 78
    • 0035478478 scopus 로고    scopus 로고
    • Detection of protein-protein interactions in vivo based on protein splicing
    • Ozawa, T. & Umezawa, Y. (2001) Detection of protein-protein interactions in vivo based on protein splicing. Curr. Opin. Chem. Biol. 5, 578-583.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 578-583
    • Ozawa, T.1    Umezawa, Y.2
  • 79
    • 0033492884 scopus 로고    scopus 로고
    • Characteristics of protein splicing in trans mediated by a semisynthetic split intein
    • Lew, B.M., Mills, K.V. & Paulus, H. (1999) Characteristics of protein splicing in trans mediated by a semisynthetic split intein. Biopolymers 51, 355-362.
    • (1999) Biopolymers , vol.51 , pp. 355-362
    • Lew, B.M.1    Mills, K.V.2    Paulus, H.3
  • 80
    • 0035894271 scopus 로고    scopus 로고
    • Protein splicing-based reconstitution of split green fluorescent protein for monitoring protein-protein interactions in bacteria: Improved sensitivity and reduced screening time
    • Ozawa, T., Takeuchi, T.M., Kaihara, A., Sato, M. & Umezawa, Y. (2001) Protein splicing-based reconstitution of split green fluorescent protein for monitoring protein-protein interactions in bacteria: improved sensitivity and reduced screening time. Anal. Chem. 73, 5866-5874.
    • (2001) Anal. Chem. , vol.73 , pp. 5866-5874
    • Ozawa, T.1    Takeuchi, T.M.2    Kaihara, A.3    Sato, M.4    Umezawa, Y.5
  • 81
    • 0034329620 scopus 로고    scopus 로고
    • A fluorescent indicator for detecting protein-protein interactions in vivo based on protein splicing
    • Ozawa, T., Nogami, S., Sato, M., Ohya, Y. & Umezawa, Y. (2000) A fluorescent indicator for detecting protein-protein interactions in vivo based on protein splicing. Anal. Chem. 72, 5151-5157.
    • (2000) Anal. Chem. , vol.72 , pp. 5151-5157
    • Ozawa, T.1    Nogami, S.2    Sato, M.3    Ohya, Y.4    Umezawa, Y.5
  • 82
    • 0035356577 scopus 로고    scopus 로고
    • Split luciferase as an optical probe for detecting protein-protein interactions in mammalian cells based on protein splicing
    • Ozawa, T., Kaihara, A., Sato, M., Tachihara, K. & Umezawa, Y. (2001) Split luciferase as an optical probe for detecting protein-protein interactions in mammalian cells based on protein splicing. Anal. Chem. 73, 2516-2521.
    • (2001) Anal. Chem. , vol.73 , pp. 2516-2521
    • Ozawa, T.1    Kaihara, A.2    Sato, M.3    Tachihara, K.4    Umezawa, Y.5
  • 83
    • 0041854719 scopus 로고    scopus 로고
    • Conditional protein splicing: A new tool to control protein structure and function in vitro and in vivo
    • Mootz, H.D., Blum, E.S., Tyszkiewicz, A.B. & Muir, T.W. (2003) Conditional protein splicing: a new tool to control protein structure and function in vitro and in vivo. J. Am. Chem. Soc. 125, 10561-10569.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10561-10569
    • Mootz, H.D.1    Blum, E.S.2    Tyszkiewicz, A.B.3    Muir, T.W.4
  • 84
    • 0037036791 scopus 로고    scopus 로고
    • Protein splicing triggered by a small molecule
    • Mootz, H.D. & Muir, T.W. (2002) Protein splicing triggered by a small molecule. J. Am. Chem. Soc. 124, 9044-9045.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9044-9045
    • Mootz, H.D.1    Muir, T.W.2
  • 85
    • 0037774580 scopus 로고    scopus 로고
    • Protein semi-synthesis in living cells
    • Giriat, I. & Muir, T.W. (2003) Protein semi-synthesis in living cells. J. Am. Chem. Soc. 125, 7180-7181.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7180-7181
    • Giriat, I.1    Muir, T.W.2
  • 86
    • 0036902328 scopus 로고    scopus 로고
    • Cellular internalization of enhanced green fluorescent protein ligated to a human calcitonin-based carrier peptide
    • Machova, Z., Mühle, C., Krauss, U., Trehin, R., Koch, A., Merkle, H.P. & Beck-Sickinger, A.G. (2002) Cellular internalization of enhanced green fluorescent protein ligated to a human calcitonin-based carrier peptide. Chembiochemistry 3, 672-677.
    • (2002) Chembiochemistry , vol.3 , pp. 672-677
    • Machova, Z.1    Mühle, C.2    Krauss, U.3    Trehin, R.4    Koch, A.5    Merkle, H.P.6    Beck-Sickinger, A.G.7
  • 87
    • 0034854231 scopus 로고    scopus 로고
    • Intein-mediated ligation and cyclization of expressed proteins
    • Xu, M.Q. & Evans, T.C. Jr (2001) Intein-mediated ligation and cyclization of expressed proteins. Methods 24, 257-277.
    • (2001) Methods , vol.24 , pp. 257-277
    • Xu, M.Q.1    Evans Jr., T.C.2
  • 88
    • 0040559903 scopus 로고    scopus 로고
    • The cyclization and polymerization of bacterially expressed proteins using modified self-splicing inteins
    • Evans, T.C. Jr, Benner, J. & Xu, M.Q. (1999) The cyclization and polymerization of bacterially expressed proteins using modified self-splicing inteins. J. Biol. Chem. 274, 18359-18363.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18359-18363
    • Evans Jr., T.C.1    Benner, J.2    Xu, M.Q.3
  • 90
    • 0034865023 scopus 로고    scopus 로고
    • Structural requirements for the biosynthesis of backbone cyclic peptide libraries
    • Scott, C.P., Abel-Santos, E., Jones, A.D. & Benkovic, S.J. (2001) Structural requirements for the biosynthesis of backbone cyclic peptide libraries. Chem. Biol. 8, 801-815.
    • (2001) Chem. Biol. , vol.8 , pp. 801-815
    • Scott, C.P.1    Abel-Santos, E.2    Jones, A.D.3    Benkovic, S.J.4
  • 91
    • 0040187857 scopus 로고    scopus 로고
    • Protein trans-splicing and cyclization by a naturally split intein from the dnaE gene of Synechocystis species PCC6803
    • Evans, T.C. Jr, Martin, D., Kolly, R., Panne, D., Sun, L., Ghosh, I., Chen, L., Benner, J., Liu, X.Q. & Xu, M.Q. (2000) Protein trans-splicing and cyclization by a naturally split intein from the dnaE gene of Synechocystis species PCC6803. J. Biol. Chem. 275, 9091-9094.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9091-9094
    • Evans Jr., T.C.1    Martin, D.2    Kolly, R.3    Panne, D.4    Sun, L.5    Ghosh, I.6    Chen, L.7    Benner, J.8    Liu, X.Q.9    Xu, M.Q.10
  • 92
    • 0035844128 scopus 로고    scopus 로고
    • Cyclic green fluorescent protein produced in vivo using an artificially split PI-PfuI intein from Pyrococcus furiosus
    • Iwai, H., Lingel, A. & Pluckthun, A. (2001) Cyclic green fluorescent protein produced in vivo using an artificially split PI-PfuI intein from Pyrococcus furiosus. J. Biol. Chem. 276, 16548-16554.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16548-16554
    • Iwai, H.1    Lingel, A.2    Pluckthun, A.3
  • 93
    • 0034828385 scopus 로고    scopus 로고
    • Peptide chemical ligation inside living cells: In vivo generation of a circular protein domain
    • Camarero, J.A., Fushman, D., Cowburn, D. & Muir, T.W. (2001) Peptide chemical ligation inside living cells: in vivo generation of a circular protein domain. Bioorgan. Med. Chem. 9, 2479-2484.
    • (2001) Bioorgan. Med. Chem. , vol.9 , pp. 2479-2484
    • Camarero, J.A.1    Fushman, D.2    Cowburn, D.3    Muir, T.W.4
  • 94
    • 0037112699 scopus 로고    scopus 로고
    • Intein-mediated purification of cytotoxic endonuclease I-TevI by insertional inactivation and pH-controllable splicing
    • Wu, W., Wood, D.W., Belfort, G., Derbyshire, V. & Belfort, M. (2002) Intein-mediated purification of cytotoxic endonuclease I-TevI by insertional inactivation and pH-controllable splicing. Nucleic Acids Res. 30, 4864-4871.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4864-4871
    • Wu, W.1    Wood, D.W.2    Belfort, G.3    Derbyshire, V.4    Belfort, M.5
  • 95
    • 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., Lew, B.M., Jiang, S. & Paulus, H. (1998) Protein splicing in trans by purified N-and C-terminal fragments of the Mycobacterium tuberculosis RecA intein. Proc. Natl Acad. Sci. USA 95, 3543-3548.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3543-3548
    • Mills, K.V.1    Lew, B.M.2    Jiang, S.3    Paulus, H.4
  • 96
    • 0034711374 scopus 로고    scopus 로고
    • Synthesis of multi-domain proteins using expressed protein ligation: Strategies for segmental isotopic labeling of internal regions
    • Blaschke, U.K. Cotton, G.J. & Muir, T.W. (2000) Synthesis of multi-domain proteins using expressed protein ligation: strategies for segmental isotopic labeling of internal regions. Tetrahedron 56, 9461-9470.
    • (2000) Tetrahedron , vol.56 , pp. 9461-9470
    • Blaschke, U.K.1    Cotton, G.J.2    Muir, T.W.3
  • 97
    • 0041999612 scopus 로고    scopus 로고
    • Segmental isotopic labeling: Prospects for a new tool to study the structure-function relationships in multi-domain proteins
    • Ottesen, J.J., Blaschke, U.K., Cowburn, D. & Muir, T.W. (2003) Segmental isotopic labeling: prospects for a new tool to study the structure-function relationships in multi-domain proteins. Biol. Magnetic Resonance 20, 35-51.
    • (2003) Biol. Magnetic Resonance , vol.20 , pp. 35-51
    • Ottesen, J.J.1    Blaschke, U.K.2    Cowburn, D.3    Muir, T.W.4
  • 98
    • 0034884817 scopus 로고    scopus 로고
    • The use of Trosy for detection and suppression of conformational exchange NMR line broadening in biological macromolecules
    • Pervushin, K. (2001) The use of Trosy for detection and suppression of conformational exchange NMR line broadening in biological macromolecules. J. Biomol. NMR 20, 275-285.
    • (2001) J. Biomol. NMR , vol.20 , pp. 275-285
    • Pervushin, K.1
  • 100
    • 0033582287 scopus 로고    scopus 로고
    • Chemical ligation of folded recombinant proteins: Segmental isotopic labeling of domains for NMR studies
    • Xu, R., Ayers, B., Cowburn, D. & Muir, T.W. (1999) Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies. Proc. Natl. Acad. Sci. USA 96, 388-393.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 388-393
    • Xu, R.1    Ayers, B.2    Cowburn, D.3    Muir, T.W.4
  • 102
    • 0033534179 scopus 로고    scopus 로고
    • NMR observation of selected segments in a larger protein: Central-segment isotope labeling through intein-mediated ligation
    • Otomo, T., Ito, N., Kyogoku, Y. & Yamazaki, T. (1999) NMR observation of selected segments in a larger protein: central-segment isotope labeling through intein-mediated ligation. Biochemistry 38, 16040-16044.
    • (1999) Biochemistry , vol.38 , pp. 16040-16044
    • Otomo, T.1    Ito, N.2    Kyogoku, Y.3    Yamazaki, T.4
  • 103
    • 0033038793 scopus 로고    scopus 로고
    • Improved segmental isotope labeling of proteins and application to a larger protein
    • Otomo, T., Teruya, K., Uegaki, K., Yamazaki, T. & Kyogoku, Y. (1999) Improved segmental isotope labeling of proteins and application to a larger protein. J. Biomol. NMR 14, 105-114.
    • (1999) J. Biomol. NMR , vol.14 , pp. 105-114
    • Otomo, T.1    Teruya, K.2    Uegaki, K.3    Yamazaki, T.4    Kyogoku, Y.5
  • 104
    • 0030037155 scopus 로고    scopus 로고
    • Extending the applicability of native chemical ligation
    • Canne, L.E., Bark, S.J. & Kent, S.B.H. (1996) Extending the applicability of native chemical ligation. J. Am. Chem. Soc. 118, 5891-5896.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5891-5896
    • Canne, L.E.1    Bark, S.J.2    Kent, S.B.H.3
  • 105
    • 0035977638 scopus 로고    scopus 로고
    • Synthesis of peptides and proteins without cysteine residues by native chemical ligation combined with desulfurization
    • Yan, L.Z. & Dawson, P.E. (2001) Synthesis of peptides and proteins without cysteine residues by native chemical ligation combined with desulfurization. J. Am. Chem. Soc. 123, 526-533.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 526-533
    • Yan, L.Z.1    Dawson, P.E.2
  • 106
    • 0034729576 scopus 로고    scopus 로고
    • Staudinger ligation: A peptide from a thioester and azide
    • Nilsson, B.L., Kiessling, L.L. & Raines, R.T. (2000) Staudinger ligation: a peptide from a thioester and azide. Org. Lett. 2, 1939-1941.
    • (2000) Org. Lett. , vol.2 , pp. 1939-1941
    • Nilsson, B.L.1    Kiessling, L.L.2    Raines, R.T.3
  • 107
    • 0035843279 scopus 로고    scopus 로고
    • High-yielding Staudinger ligation of a phosphinothioester and azide to form a peptide
    • Nilsson, B.L., Kiessling, L.L. & Raines, R.T. (2001) High-yielding Staudinger ligation of a phosphinothioester and azide to form a peptide. Org. Lett. 3, 9-12.
    • (2001) Org. Lett. , vol.3 , pp. 9-12
    • Nilsson, B.L.1    Kiessling, L.L.2    Raines, R.T.3
  • 108
    • 0036882398 scopus 로고    scopus 로고
    • Proteases in organic synthesis
    • Bordusa, F. (2002) Proteases in organic synthesis. Chem. Rev. 102, 4817-4868.
    • (2002) Chem. Rev. , vol.102 , pp. 4817-4868
    • Bordusa, F.1
  • 109
    • 0034036068 scopus 로고    scopus 로고
    • Protease-catalyzed fragment condensation via substrate mimetic strategy: A useful combination of solid-phase peptide synthesis with enzymatic methods
    • Cerovsky, V. & Bordusa, F. (2000) Protease-catalyzed fragment condensation via substrate mimetic strategy: a useful combination of solid-phase peptide synthesis with enzymatic methods. J. Pept. Res. 55, 325-329.
    • (2000) J. Pept. Res. , vol.55 , pp. 325-329
    • Cerovsky, V.1    Bordusa, F.2
  • 111
    • 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., Evans, T.C., Chute, I.C., Wu, H., Chong, S., Benner, J., Liu, X.Q. & Xu, M.Q. (1999) 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, 1-13.
    • (1999) Gene , vol.231 , pp. 1-13
    • Mathys, S.1    Evans, T.C.2    Chute, I.C.3    Wu, H.4    Chong, S.5    Benner, J.6    Liu, X.Q.7    Xu, M.Q.8
  • 112
    • 0032534048 scopus 로고    scopus 로고
    • Utilizing the C-terminal cleavage activity of a protein splicing element to purify recombinant proteins in a single chromatographic step
    • Chong, S., Montello, G.E., Zhang, A., Cantor, E.J., Liao, W., Xu, M.Q. & Benner, J. (1998) Utilizing the C-terminal cleavage activity of a protein splicing element to purify recombinant proteins in a single chromatographic step. Nucleic Acids Res. 26, 5109-5115.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5109-5115
    • Chong, S.1    Montello, G.E.2    Zhang, A.3    Cantor, E.J.4    Liao, W.5    Xu, M.Q.6    Benner, J.7
  • 113
  • 116
    • 0033575092 scopus 로고    scopus 로고
    • Biosynthesis of a head-to-tail cyclized protein with improved biological activity
    • Camarero, J.A. & Muir, T.W. (1999) Biosynthesis of a head-to-tail cyclized protein with improved biological activity. J. Am. Chem. Soc. 121, 5597-5598.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 5597-5598
    • Camarero, J.A.1    Muir, T.W.2
  • 117
    • 0037953089 scopus 로고    scopus 로고
    • An in vitro screening system for protein splicing inhibitors based on green fluorescent protein as an indicator
    • Gangopadhyay, J.P., Jiang, S.-q. & Paulus, H. (2003) An in vitro screening system for protein splicing inhibitors based on green fluorescent protein as an indicator. Anal. Chem. 75, 2456-2462.
    • (2003) Anal. Chem. , vol.75 , pp. 2456-2462
    • Gangopadhyay, J.P.1    Jiang, S.-Q.2    Paulus, H.3


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