메뉴 건너뛰기




Volumn 6, Issue 8, 1998, Pages 951-956

Adding 'splice' to protein engineering

Author keywords

[No Author keywords available]

Indexed keywords

SACCHAROMYCES CEREVISIAE;

EID: 0032528873     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00097-5     Document Type: Article
Times cited : (11)

References (47)
  • 1
    • 10544223268 scopus 로고    scopus 로고
    • Synergy in protein engineering: Mutagenic manipulation of protein structure to simplify semisynthesis
    • Woods, A.C., Guillemette, J.G., Pasrrish, J.C., Smith, M. & Wallace, C.J.A. (1996). Synergy in protein engineering: mutagenic manipulation of protein structure to simplify semisynthesis. J. Biol. Chem. 271, 32008-32015.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32008-32015
    • Woods, A.C.1    Guillemette, J.G.2    Pasrrish, J.C.3    Smith, M.4    Wallace, C.J.A.5
  • 2
    • 0029108642 scopus 로고
    • Probing protein structure and function with an expanded genetic code
    • Cornish, V.W., Mendel, D. & Schultz, P.G. (1995). Probing protein structure and function with an expanded genetic code. Angew. Chem. Int. Ed. Engl. 34, 621-633.
    • (1995) Angew. Chem. Int. Ed. Engl. , vol.34 , pp. 621-633
    • Cornish, V.W.1    Mendel, D.2    Schultz, P.G.3
  • 3
    • 0026857064 scopus 로고
    • Construction of protein analogues by site-specific condensation of unprotected peptides
    • Gaertner, H.F., Rose, K., Cotton, R., Timms, D., Gamble R. & Offord, R.E. (1992). Construction of protein analogues by site-specific condensation of unprotected peptides. Bioconjugate Chem. 3, 262-268.
    • (1992) Bioconjugate Chem. , vol.3 , pp. 262-268
    • Gaertner, H.F.1    Rose, K.2    Cotton, R.3    Timms, D.4    Gamble, R.5    Offord, R.E.6
  • 4
    • 0026674590 scopus 로고
    • Functional role of heme ligation in cytochrome c
    • Wallace, C.J.A. & Clark-Lewis, I. (1992). Functional role of heme ligation in cytochrome c. J. Biol. Chem. 267, 3852-3861.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3852-3861
    • Wallace, C.J.A.1    Clark-Lewis, I.2
  • 5
    • 0026525457 scopus 로고
    • Constructing proteins by dovetailing unprotected synthetic peptides: Backbone-engineered HIV protease
    • Schnölzer, M. & Kent, S.B.H. (1992). Constructing proteins by dovetailing unprotected synthetic peptides: backbone-engineered HIV protease. Science 256, 221-225.
    • (1992) Science , vol.256 , pp. 221-225
    • Schnölzer, M.1    Kent, S.B.H.2
  • 6
    • 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 protecting 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 protecting groups. J. Org. Chem. 58, 2216-2222.
    • (1993) J. Org. Chem. , vol.58 , pp. 2216-2222
    • Kemp, D.S.1    Carey, R.I.2
  • 7
    • 0028231302 scopus 로고
    • Facile synthesis of homogeneous artificial proteins
    • Rose, K. (1994). Facile synthesis of homogeneous artificial proteins. J. Am. Chem. Soc. 116, 30-33.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 30-33
    • Rose, K.1
  • 8
    • 12044253737 scopus 로고
    • Chemical ligation approach to form a peptide bond between unprotected peptide segments. Concept and model study
    • Liu, C.-F. &Tam, J.P. (1994). Chemical ligation approach to form a peptide bond between unprotected peptide segments. Concept and model study. J. Am. Chem. Soc. 116, 4149-4153.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4149-4153
    • Liu, C.-F.1    Tam, J.P.2
  • 9
    • 0028831838 scopus 로고
    • Chemoselective ligation of multifunctional peptides to topological templates via thioether formation for TASP synthesis
    • Nefzi, A., Sun, X. & Mutter, M. (1995). Chemoselective ligation of multifunctional peptides to topological templates via thioether formation for TASP synthesis. Tetrahedron Lett. 36, 229-230.
    • (1995) Tetrahedron Lett. , vol.36 , pp. 229-230
    • Nefzi, A.1    Sun, X.2    Mutter, M.3
  • 11
    • 0028518514 scopus 로고
    • A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues
    • Jackson, D.Y., Burnier, J., Quan, C., Stanley, M., Tom, J. & Wells, J.A. (1994). A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues. Science 266, 243-247.
    • (1994) Science , vol.266 , pp. 243-247
    • Jackson, D.Y.1    Burnier, J.2    Quan, C.3    Stanley, M.4    Tom, J.5    Wells, J.A.6
  • 13
    • 0030936614 scopus 로고    scopus 로고
    • Enzymatic glycoprotein synthesis: Preparation of ribonuclease glycoforms via enzymatic glycopeptide condensation and glycosylation
    • Witte, K., Sears, P., Martin, R. & Wong, C.H. (1997). Enzymatic glycoprotein synthesis: preparation of ribonuclease glycoforms via enzymatic glycopeptide condensation and glycosylation. J. Am. Chem. Soc. 119, 2114-2118.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2114-2118
    • Witte, K.1    Sears, P.2    Martin, R.3    Wong, C.H.4
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0344351815 scopus 로고    scopus 로고
    • Semi-synthesis of cytotoxic proteins using a modified protein splicing element
    • in press
    • Evans, T.C.Jr, Benner, J. & Xu, M.-Q. (1998). Semi-synthesis of cytotoxic proteins using a modified protein splicing element. Protein Sci. in press.
    • (1998) Protein Sci.
    • Evans Jr., T.C.1    Benner, J.2    Xu, M.-Q.3
  • 17
    • 0031244525 scopus 로고    scopus 로고
    • Protein splicing and autoproteolysis mechanisms
    • Perler, F.B., Xu, M.-Q. & Paulus, H. (1997). Protein splicing and autoproteolysis mechanisms. Curr. Opin. Chem. Biol. 1, 292-299.
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 292-299
    • Perler, F.B.1    Xu, M.-Q.2    Paulus, H.3
  • 18
    • 0023889559 scopus 로고
    • Chemical synthesis of peptides and proteins
    • Kent, S.B.H. (1988). Chemical synthesis of peptides and proteins. Annu. Rev. Biochem. 57, 957-989.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 957-989
    • Kent, S.B.H.1
  • 19
    • 0029645122 scopus 로고
    • A chemical approach to the construction of multimeric protein assemblies
    • Muir, T.W. (1995). A chemical approach to the construction of multimeric protein assemblies. Structure 3, 649-652.
    • (1995) Structure , vol.3 , pp. 649-652
    • Muir, T.W.1
  • 21
    • 0027373903 scopus 로고
    • Convergent solid-phase peptide synthesis
    • Lloyd-Williams, P., Albericio, F. & E. Giralt, (1993). Convergent solid-phase peptide synthesis. Tetrahedron 48, 11065-11133.
    • (1993) Tetrahedron , vol.48 , pp. 11065-11133
    • Lloyd-Williams, P.1    Albericio, F.2    Giralt, E.3
  • 22
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson, P.E., Muir, T.W., Clark-Lewis, I. & Kent, S.B.H. (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.H.4
  • 23
    • 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
  • 25
    • 0030973396 scopus 로고    scopus 로고
    • Modulation in native chemical ligation through the use of thiol additives
    • Dawson, P.E., Churchill, M.J., Ghadiri, M.R. & Kent, S.B.H. (1997). Modulation 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.J.2    Ghadiri, M.R.3    Kent, S.B.H.4
  • 26
    • 0029847275 scopus 로고    scopus 로고
    • Comparative total synthesis of turkey ovomucoid third domain by both stepwise solid phase synthesis and native chemical ligation
    • Lu, W., Qasim, M.A. & Kent, S.B.H. (1996). Comparative total synthesis of turkey ovomucoid third domain by both stepwise solid phase synthesis and native chemical ligation. J. Am. Chem. Soc. 118, 8518-8523.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8518-8523
    • Lu, W.1    Qasim, M.A.2    Kent, S.B.H.3
  • 27
    • 0031894588 scopus 로고    scopus 로고
    • Chemical ligation of unprotected peptides directly from a solid support
    • Camarero, J.A., Cotton, G.C., Adeva, A. & Muir, T.W. (1998). Chemical ligation of unprotected peptides directly from a solid support. J. Peptide Res. 51, 303-316.
    • (1998) J. Peptide Res. , vol.51 , pp. 303-316
    • Camarero, J.A.1    Cotton, G.C.2    Adeva, A.3    Muir, T.W.4
  • 28
    • 0030482408 scopus 로고    scopus 로고
    • The leucine zipper domain controls the orientation of AP-1 in the NFAT·AP-1·DNA complex
    • Erlandson, D.A., Chytil, M. & Verdine, G.L. (1996). The leucine zipper domain controls the orientation of AP-1 in the NFAT·AP-1·DNA complex. Chem. Biol. 3, 981-991.
    • (1996) Chem. Biol. , vol.3 , pp. 981-991
    • Erlandson, D.A.1    Chytil, M.2    Verdine, G.L.3
  • 29
    • 0025226104 scopus 로고
    • Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H+-adenosine triphosphatase
    • Kane, P.M., Yamashiro, C.T., Wolczyk, D.F., Neff, N., Goebl, M. & Stevens, T.H. (1990). Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H+-adenosine triphosphatase. Science 250, 651-657.
    • (1990) Science , vol.250 , pp. 651-657
    • Kane, P.M.1    Yamashiro, C.T.2    Wolczyk, D.F.3    Neff, N.4    Goebl, M.5    Stevens, T.H.6
  • 30
    • 0028214350 scopus 로고
    • Protein splicing elements: Inteins and exteins - A definition of terms and recommended nomenclature
    • Perler, F.B., et al., & Belford, M. (1994). Protein splicing elements: inteins and exteins - a definition of terms and recommended nomenclature. Nucleic Acids Res. 22, 1125-1127.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1125-1127
    • Perler, F.B.1    Belford, M.2
  • 31
    • 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
  • 32
    • 0030012109 scopus 로고    scopus 로고
    • Protein splicing: Evidence of an N-O acyl rearrangement as the initial step in the splicing process
    • Shao, Y., Xu, M.-Q. & Paulus, H. (1996). Protein splicing: evidence of an N-O acyl rearrangement as the initial step in the splicing process. Biochemistry 35, 3810-3815.
    • (1996) Biochemistry , vol.35 , pp. 3810-3815
    • Shao, Y.1    Xu, M.-Q.2    Paulus, H.3
  • 33
    • 0029834656 scopus 로고    scopus 로고
    • Protein splicing involving the Saccharomyces cerevisiae VMA intein: The steps in the splicing pathway, side reactions leading to protein cleavage, and establishment of an in vitro splicing system
    • Chong, S., Shao, Y., Paulus, H., Benner, J., Perler, F.B. & Xu, M.-Q. (1996). Protein splicing involving the Saccharomyces cerevisiae VMA intein: the steps in the splicing pathway, side reactions leading to protein cleavage, and establishment of an in vitro splicing system. J. Biol. Chem. 271, 22159-22168.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22159-22168
    • Chong, S.1    Shao, Y.2    Paulus, H.3    Benner, J.4    Perler, F.B.5    Xu, M.-Q.6
  • 34
    • 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
  • 35
    • 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., & Xu, M.-Q. (1997). Single column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element. Gene 192, 271-281.
    • (1997) Gene , vol.192 , pp. 271-281
    • Chong, S.1    Xu, M.-Q.2
  • 36
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri, F., Moarefi, I. & Kuriyan, J. (1997). Crystal structure of the Src family tyrosine kinase Hck. Nature 385, 602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 37
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., Harrison, S.C. & Eck, M.J. (1997). Three-dimensional structure of the tyrosine kinase c-Src. Nature 385, 595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 39
    • 0032579457 scopus 로고    scopus 로고
    • Molecular dissection of the Mycobacterium tuberculosis RecA intein: Design of a minimal intein and of a trans-splicing system involving two intein fragments
    • Shingledecker, K., Jiang, S.-Q. & Paulus, H. (1998). Molecular dissection of the Mycobacterium tuberculosis RecA intein: design of a minimal intein and of a trans-splicing system involving two intein fragments. Gene 207, 187-195.
    • (1998) Gene , vol.207 , pp. 187-195
    • Shingledecker, K.1    Jiang, S.-Q.2    Paulus, H.3
  • 40
    • 0032584098 scopus 로고    scopus 로고
    • Protein slicing in trans by purified N- and C-terminal fragments of the Mycobacterium tuberculosis RecA intein
    • Mills, K.V., Lew, B.M., Jiang, S.-Q. & Paulus, H. (1998). Protein slicing in trans by purified N- and C-terminal fragments of the Mycobacterium tuberculosis RecA intein. Proc. Natl Acad. Sci. USA 95, 3343-3548.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3343-3548
    • Mills, K.V.1    Lew, B.M.2    Jiang, S.-Q.3    Paulus, H.4
  • 41
    • 0032503612 scopus 로고    scopus 로고
    • Segmental isotope labeling for protein NMR using peptide splicing
    • Yamazaki, T., et al., & Nakamura, H. (1998). Segmental isotope labeling for protein NMR using peptide splicing. J. Am. Chem. Soc. 120, 5591-5592.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 5591-5592
    • Yamazaki, T.1    Nakamura, H.2
  • 42
    • 0030210936 scopus 로고    scopus 로고
    • A new intein in cyanobacteria and its influence for the spread of inteins
    • Pietrokovski, S., (1996). A new intein in cyanobacteria and its influence for the spread of inteins. Trends Genet. 12, 287-288.
    • (1996) Trends Genet. , vol.12 , pp. 287-288
    • Pietrokovski, S.1
  • 43
    • 0030761813 scopus 로고    scopus 로고
    • The Mycobacterium xenopt GyrA protein splicing element: Characterization of a minimal intein
    • Telenti, A., Southworth, M., Alcaide, F., Daugelat, S., Jacobs, W.R.Jr. & Perler, F.B. (1997). The Mycobacterium xenopt GyrA protein splicing element: characterization of a minimal intein. J. Bacteriol. 179, 6378-6382.
    • (1997) J. Bacteriol. , vol.179 , pp. 6378-6382
    • Telenti, A.1    Southworth, M.2    Alcaide, F.3    Daugelat, S.4    Jacobs Jr., W.R.5    Perler, F.B.6
  • 44
    • 0030711495 scopus 로고    scopus 로고
    • Protein synthesis by chemical ligation of unprotected peptides in aqueous solution
    • Muir, T.W., Dawson, P.E. & Kent, S.B.H. (1997). Protein synthesis by chemical ligation of unprotected peptides in aqueous solution. Methods Enzymol. 289, 266-298.
    • (1997) Methods Enzymol. , vol.289 , pp. 266-298
    • Muir, T.W.1    Dawson, P.E.2    Kent, S.B.H.3
  • 45
    • 0030897311 scopus 로고    scopus 로고
    • Synthesis and application of unprotected cyclic peptides as building blocks for peptide dendrimers
    • Zhang, L. & Tam, J.P. (1997). Synthesis and application of unprotected cyclic peptides as building blocks for peptide dendrimers. J. Am. Chem. Soc. 119, 2363-2370.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2363-2370
    • Zhang, L.1    Tam, J.P.2
  • 46
    • 1542468131 scopus 로고    scopus 로고
    • Chemoselective backbone cyclization of unprotected peptides
    • Camarero, J.A. & Muir, T.W. (1997). Chemoselective backbone cyclization of unprotected peptides. J. Chem. Soc. Chem. Commun. 1369-1370.
    • (1997) J. Chem. Soc. Chem. Commun. , pp. 1369-1370
    • Camarero, J.A.1    Muir, T.W.2
  • 47
    • 0032536553 scopus 로고    scopus 로고
    • Chemical synthesis of a circular protein domain: Evidence for folding-assisted cyclization
    • Camarero, J.A., Pavel, J. & Muir, T.W. (1998). Chemical synthesis of a circular protein domain: evidence for folding-assisted cyclization. Angew. Chem. Int. Ed. 37, 347-349.
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 347-349
    • Camarero, J.A.1    Pavel, J.2    Muir, T.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.