메뉴 건너뛰기




Volumn 3, Issue 5, 1998, Pages 321-328

Proteolytic selection for protein folding using filamentous bacteriophages

Author keywords

Phage display; Protein folding; Proteolytic cleavage

Indexed keywords

COAT PROTEIN; LIGAND; PEPTIDE; PROTEIN; PROTEINASE; TRYPSIN; VILLIN;

EID: 0031759422     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(98)00044-3     Document Type: Article
Times cited : (247)

References (50)
  • 1
    • 0002983608 scopus 로고    scopus 로고
    • Protein folding from a combinatorial perspective
    • Sauer, R.T. (1996). Protein folding from a combinatorial perspective. Fold. Des. 1, R27-R30.
    • (1996) Fold. Des. , vol.1
    • Sauer, R.T.1
  • 2
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • Zhao, H., Giver, L, Shao, Z., Affholter, J.A. & Arnold, F.H. (1998). Molecular evolution by staggered extension process (StEP) in vitro recombination. Nature Biotechnol. 16, 258-261.
    • (1998) Nature Biotechnol. , vol.16 , pp. 258-261
    • Zhao, H.1    Giver, L.2    Shao, Z.3    Affholter, J.A.4    Arnold, F.H.5
  • 3
    • 0030057864 scopus 로고    scopus 로고
    • What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties
    • Munson, M., et al., & Regan, L (1996). What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties. Protein Sci. 5, 1584-1593.
    • (1996) Protein Sci. , vol.5 , pp. 1584-1593
    • Munson, M.1    Regan, L.2
  • 4
    • 0031558762 scopus 로고    scopus 로고
    • De novo protein design: Towards fully automated sequence selection
    • Dahiyat, B.I., Sarisky, C.A. & Mayo, S.L. (1997). De novo protein design: towards fully automated sequence selection. J. Mol. Biol. 273, 789-796.
    • (1997) J. Mol. Biol. , vol.273 , pp. 789-796
    • Dahiyat, B.I.1    Sarisky, C.A.2    Mayo, S.L.3
  • 5
    • 23444436172 scopus 로고
    • Protein design by binary patterning of polar and nonpolar amino acids
    • Kamtekar, S., Schiffer, J.M., Xiong, H., Babik, J.M. & Hecht, M.H. (1993). Protein design by binary patterning of polar and nonpolar amino acids. Science 262, 1680-1685.
    • (1993) Science , vol.262 , pp. 1680-1685
    • Kamtekar, S.1    Schiffer, J.M.2    Xiong, H.3    Babik, J.M.4    Hecht, M.H.5
  • 6
    • 0028218304 scopus 로고
    • Folded proteins occur frequently in libraries of random amino acid sequences
    • Davidson, A.R. & Sauer, R.T. (1994). Folded proteins occur frequently in libraries of random amino acid sequences. Proc. Natl Acad. Sci. USA 91, 2146-2150.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 2146-2150
    • Davidson, A.R.1    Sauer, R.T.2
  • 7
    • 0029120253 scopus 로고
    • Cooperatively folded proteins in random sequence libraries
    • Davidson, A.R., Lumb, K.J. & Sauer, R.T. (1995). Cooperatively folded proteins in random sequence libraries. Nat. Struct. Biol. 2, 856-864.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 856-864
    • Davidson, A.R.1    Lumb, K.J.2    Sauer, R.T.3
  • 8
    • 0026673067 scopus 로고
    • By-passing immunisation. Human antibodies from synthetic repertoires of germline VH gene segments rearranged in vitro
    • Hoogenboom, H.R. & Winter, G. (1992). By-passing immunisation. Human antibodies from synthetic repertoires of germline VH gene segments rearranged in vitro. J. Mol. Biol. 227, 381-388.
    • (1992) J. Mol. Biol. , vol.227 , pp. 381-388
    • Hoogenboom, H.R.1    Winter, G.2
  • 10
    • 0028291823 scopus 로고
    • Isolation of high affinity human antibodies directly from large synthetic repertoires
    • Griffiths, A.D., et al., & Winter, G. (1994). Isolation of high affinity human antibodies directly from large synthetic repertoires. EMBO J. 13, 3245-3260.
    • (1994) EMBO J. , vol.13 , pp. 3245-3260
    • Griffiths, A.D.1    Winter, G.2
  • 11
    • 0029904435 scopus 로고    scopus 로고
    • Minimizing a binding domain from protein a
    • Braisted, A.C. & Wells, J.A. (1996). Minimizing a binding domain from protein A. Proc. Natl Acad. Sci. USA 93, 5688-5692.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5688-5692
    • Braisted, A.C.1    Wells, J.A.2
  • 12
    • 0030852463 scopus 로고    scopus 로고
    • Functional rapidly folding proteins from simplified amino acid sequences
    • Riddle, D.S., et al., & Baker, D. (1997). Functional rapidly folding proteins from simplified amino acid sequences. Nat. Struct. Biol. 4, 805-809.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 805-809
    • Riddle, D.S.1    Baker, D.2
  • 13
    • 0028821194 scopus 로고
    • Thermodynamic genetics of the folding of the B1 immunoglobulinbinding domain from streptococcal protein G
    • O'Neil, K.T., Hoess, R.H., Raleigh, D.P. & DeGrado, W.F. (1995). Thermodynamic genetics of the folding of the B1 immunoglobulinbinding domain from streptococcal protein G. Proteins 21, 11-21.
    • (1995) Proteins , vol.21 , pp. 11-21
    • O'Neil, K.T.1    Hoess, R.H.2    Raleigh, D.P.3    DeGrado, W.F.4
  • 14
    • 0029004982 scopus 로고
    • A phage display system for studying the sequence determinants of protein folding
    • Gu, H., et al., & Baker, D. (1995). A phage display system for studying the sequence determinants of protein folding. Protein Sci. 4, 1108-1117.
    • (1995) Protein Sci. , vol.4 , pp. 1108-1117
    • Gu, H.1    Baker, D.2
  • 15
    • 0028336661 scopus 로고
    • Modeling studies of the change in conformation required for cleavage of limited proteolytic sites
    • Hubbard, S.J., Eisenmenger, F. & Thornton, J.M. (1994). Modeling studies of the change in conformation required for cleavage of limited proteolytic sites. Protein Sci. 3, 757-768.
    • (1994) Protein Sci. , vol.3 , pp. 757-768
    • Hubbard, S.J.1    Eisenmenger, F.2    Thornton, J.M.3
  • 17
    • 0027316004 scopus 로고
    • Substrate phage: Selection of protease substrates by monovalent phage display
    • Matthews, D.J. & Wells, J.A. (1993). Substrate phage: selection of protease substrates by monovalent phage display. Science 260, 1113-1117.
    • (1993) Science , vol.260 , pp. 1113-1117
    • Matthews, D.J.1    Wells, J.A.2
  • 18
    • 0030797114 scopus 로고    scopus 로고
    • The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. coll
    • Riechmann, L. & Holliger, P. (1997). The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. coll. Cell 90, 351-360.
    • (1997) Cell , vol.90 , pp. 351-360
    • Riechmann, L.1    Holliger, P.2
  • 19
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • Smith, G.P. (1985). Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228, 1315-1317.
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 20
    • 0031560775 scopus 로고    scopus 로고
    • Selectively-infective phage (SIP): A mechanistic dissection of a novel in vivo selection for protein-ligand interactions
    • Krebber, C., et al., & Plückthun, A. (1997). Selectively-infective phage (SIP): a mechanistic dissection of a novel in vivo selection for protein-ligand interactions. J. Mol. Biol. 268, 607-618.
    • (1997) J. Mol. Biol. , vol.268 , pp. 607-618
    • Krebber, C.1    Plückthun, A.2
  • 21
    • 0025273561 scopus 로고
    • Dissection of functional domains in phage fd adsorption protein. Discrimination between attachment and penetration
    • Stengele, I., Brass, P., Garces, X., Giray, J. & Rasched, I. (1990). Dissection of functional domains in phage fd adsorption protein. Discrimination between attachment and penetration. J. Mol. Biol. 212, 143-149.
    • (1990) J. Mol. Biol. , vol.212 , pp. 143-149
    • Stengele, I.1    Brass, P.2    Garces, X.3    Giray, J.4    Rasched, I.5
  • 22
    • 0019461994 scopus 로고
    • Adsorption complex of Filamentous fd virus
    • Gray, C.W., Brown, R.S. & Marvin, D.A. (1981). Adsorption complex of Filamentous fd virus. J. Mol. Biol. 146, 621-627.
    • (1981) J. Mol. Biol. , vol.146 , pp. 621-627
    • Gray, C.W.1    Brown, R.S.2    Marvin, D.A.3
  • 23
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom, H.R., et al., & Winter, G. (1991). Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res. 19, 4133-4137.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1    Winter, G.2
  • 24
    • 0025678186 scopus 로고
    • Hormone phage: An enrichment method for variant proteins with altered binding properties
    • Bass, S., Greene, R. & Wells, J.A. (1990). Hormone phage: an enrichment method for variant proteins with altered binding properties. Proteins 8, 309-314.
    • (1990) Proteins , vol.8 , pp. 309-314
    • Bass, S.1    Greene, R.2    Wells, J.A.3
  • 25
    • 0028006072 scopus 로고
    • Antibody fragments from a "single pot" phage display library as immunochemical reagents
    • Nissim, A., et al., & Winter, G. (1994). Antibody fragments from a "single pot" phage display library as immunochemical reagents. EMBOJ. 13, 692-698.
    • (1994) EMBOJ. , vol.13 , pp. 692-698
    • Nissim, A.1    Winter, G.2
  • 26
    • 0031031766 scopus 로고    scopus 로고
    • Extending filamentous phage host range by the grafting of a heterologous receptor binding domain
    • Marzari, R., Sblattero, D., Righi, M. & Bradbury, A. (1997). Extending filamentous phage host range by the grafting of a heterologous receptor binding domain. Gene 185, 27-33.
    • (1997) Gene , vol.185 , pp. 27-33
    • Marzari, R.1    Sblattero, D.2    Righi, M.3    Bradbury, A.4
  • 27
    • 0027163998 scopus 로고
    • Protein folding and stability: The pathway of folding of barnase
    • Fersht, A.R. (1993). Protein folding and stability: the pathway of folding of barnase. FEBS Lett. 325, 5-16.
    • (1993) FEBS Lett. , vol.325 , pp. 5-16
    • Fersht, A.R.1
  • 28
    • 0024501923 scopus 로고
    • Kinetic characterisation of the recombinant ribonuclease from bacillus amyloliquefaciens (Barnase) and investigation of key residues in catalysis by site-directed mutagenesis
    • Mossakowska, D.E., Nyberg, K. & Fersht, A.R. (1989). Kinetic characterisation of the recombinant ribonuclease from bacillus amyloliquefaciens (Barnase) and investigation of key residues in catalysis by site-directed mutagenesis. Biochemistry 28, 3843-3850.
    • (1989) Biochemistry , vol.28 , pp. 3843-3850
    • Mossakowska, D.E.1    Nyberg, K.2    Fersht, A.R.3
  • 29
    • 0026723477 scopus 로고
    • Effect of active site residues in barnase on activity and stability
    • Meiering, E.M., Serrano, L & Fersht, A.R. (1992). Effect of active site residues in barnase on activity and stability. J. Mol. Biol. 225, 585-589.
    • (1992) J. Mol. Biol. , vol.225 , pp. 585-589
    • Meiering, E.M.1    Serrano, L.2    Fersht, A.R.3
  • 30
    • 0026553768 scopus 로고
    • The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability
    • Serrano, L., Kellis, J.T., Cann, P., Matouschek, A. & Fersht, A.R. (1992). The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. J. Mol. Biol. 224, 783-804.
    • (1992) J. Mol. Biol. , vol.224 , pp. 783-804
    • Serrano, L.1    Kellis, J.T.2    Cann, P.3    Matouschek, A.4    Fersht, A.R.5
  • 31
    • 0031058410 scopus 로고    scopus 로고
    • NMR structure of the 35-residue villin headpiece subdomain
    • McKnight, C.J., Matsudaira, P.T. & Kim, P.S. (1997). NMR structure of the 35-residue villin headpiece subdomain. Nat. Struct. Biol. 4, 180-184.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 180-184
    • McKnight, C.J.1    Matsudaira, P.T.2    Kim, P.S.3
  • 32
    • 0008501653 scopus 로고    scopus 로고
    • A thermostable 35-residue subdomain within villin headpiece
    • McKnight, C.J., Doering, D.S., Matsudaira, P.T. & Kim, P.S. (1996). A thermostable 35-residue subdomain within villin headpiece. J. Mol. Biol. 260, 126-134.
    • (1996) J. Mol. Biol. , vol.260 , pp. 126-134
    • McKnight, C.J.1    Doering, D.S.2    Matsudaira, P.T.3    Kim, P.S.4
  • 33
    • 0031932170 scopus 로고    scopus 로고
    • Favorable domain size in proteins
    • Xu, D. & Nussinov, R. (1997). Favorable domain size in proteins. Fold. Des. 3, 11-17.
    • (1997) Fold. Des. , vol.3 , pp. 11-17
    • Xu, D.1    Nussinov, R.2
  • 34
    • 0028965951 scopus 로고
    • Analysis of the mechanism of assembly of cleaved barnase from two peptide fragments and its relevance to the folding pathway of uncleaved barnase
    • Kippen, A.D. & Fersht, A.R. (1995). Analysis of the mechanism of assembly of cleaved barnase from two peptide fragments and its relevance to the folding pathway of uncleaved barnase. Biochemistry 34, 1464-1468.
    • (1995) Biochemistry , vol.34 , pp. 1464-1468
    • Kippen, A.D.1    Fersht, A.R.2
  • 35
    • 0028335799 scopus 로고
    • Generation of a family of protein fragments for structure-folding studies. 1. folding complementation of two fragments of chymotrypsin inhibitor-2 formed by cleavage at its unique methionine residue
    • Gay, G.d.P. & Fersht, A.R. (1994). Generation of a family of protein fragments for structure-folding studies. 1. folding complementation of two fragments of chymotrypsin inhibitor-2 formed by cleavage at its unique methionine residue. Biochemistry 33, 7957-7963.
    • (1994) Biochemistry , vol.33 , pp. 7957-7963
    • Gay, G.D.P.1    Fersht, A.R.2
  • 36
    • 0028212643 scopus 로고
    • Autonomous subdomains in protein folding
    • Wu, L.C., Grandori, R. & Carey, J. (1994). Autonomous subdomains in protein folding. Protein Sci. 3, 369-371.
    • (1994) Protein Sci. , vol.3 , pp. 369-371
    • Wu, L.C.1    Grandori, R.2    Carey, J.3
  • 37
    • 0030472210 scopus 로고    scopus 로고
    • Relationships between thermal stability, degradation rate and expression yield of barnase variants in the periplasm of Escherichia coli
    • Kwon, W.S., Silva, N.A.D. & Kellis, J.T. (1996). Relationships between thermal stability, degradation rate and expression yield of barnase variants in the periplasm of Escherichia coli. Protein Eng. 9, 1197-1202.
    • (1996) Protein Eng. , vol.9 , pp. 1197-1202
    • Kwon, W.S.1    Silva, N.A.D.2    Kellis, J.T.3
  • 38
    • 0029980972 scopus 로고    scopus 로고
    • Active barnase variants with completely random hydrophobic cores
    • Axe, D.D., Foster, N.W. & Fersht, A.R. (1996). Active barnase variants with completely random hydrophobic cores. Proc. Natl Acad. Sci. USA 93, 5590-5594.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5590-5594
    • Axe, D.D.1    Foster, N.W.2    Fersht, A.R.3
  • 39
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • Waldburger, C.D., Schildbach, J.F. & Sauer, R.T. (1995). Are buried salt bridges important for protein stability and conformational specificity? Nat. Struct. Biol. 2, 122-128.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 40
    • 0030722164 scopus 로고    scopus 로고
    • Applications of DNA shuffling to pharmaceuticals and vaccines
    • Patten, P.A., Howard, R.J. & Stemmer, W.P.C. (1997). Applications of DNA shuffling to pharmaceuticals and vaccines. Curr. Opin. Biotechnol. 8, 724-733.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 724-733
    • Patten, P.A.1    Howard, R.J.2    Stemmer, W.P.C.3
  • 41
    • 0030878180 scopus 로고    scopus 로고
    • A protein designed by binary patterning of polar and nonpolar amino acids displays native-like properties
    • Roy, S., et al., & Hecht, M.H. (1997). A protein designed by binary patterning of polar and nonpolar amino acids displays native-like properties. J. Am. Chem. Soc. 119, 5302-5306.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 5302-5306
    • Roy, S.1    Hecht, M.H.2
  • 42
    • 0028670306 scopus 로고
    • Direct interaction rescue, a novel filamentous phage technique to study protein-protein interactions
    • Gramatikoff, K., Georgiev, O. & Schaffner, W. (1994). Direct interaction rescue, a novel filamentous phage technique to study protein-protein interactions. Nucleic Acids Res. 22, 5761-5762.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5761-5762
    • Gramatikoff, K.1    Georgiev, O.2    Schaffner, W.3
  • 43
    • 0027933750 scopus 로고
    • Clonal selection and amplification of phage displayed antibodies by linking antigen recognition and phage replication
    • Duenas, M. & Borrebaeck, C.A.K. (1994). Clonal selection and amplification of phage displayed antibodies by linking antigen recognition and phage replication. Bio/Technology 12, 999-1002.
    • (1994) Bio/Technology , vol.12 , pp. 999-1002
    • Duenas, M.1    Borrebaeck, C.A.K.2
  • 44
    • 0029585566 scopus 로고
    • Co-selection of cognate antibody-antigen pairs by selectively-infective phages
    • Krebber, C., Spada, S., Desplancq, D. & Plückthun, A. (1995). Co-selection of cognate antibody-antigen pairs by selectively-infective phages. FEBS Lett. 377, 227-231.
    • (1995) FEBS Lett. , vol.377 , pp. 227-231
    • Krebber, C.1    Spada, S.2    Desplancq, D.3    Plückthun, A.4
  • 46
    • 0025835310 scopus 로고
    • Making antibody fragments using phage display libraries
    • Clackson, T., Hoogenboom, H.R., Griffiths, A.D. & Winter, G. (1991). Making antibody fragments using phage display libraries. Nature 352, 624-628.
    • (1991) Nature , vol.352 , pp. 624-628
    • Clackson, T.1    Hoogenboom, H.R.2    Griffiths, A.D.3    Winter, G.4
  • 47
    • 0025226085 scopus 로고
    • Phage antibodies: Filamentous phage displaying antibody variable domains
    • McCafferty, J., Griffiths, A.D., Winter, G. & Chiswell, D.J. (1990). Phage antibodies: filamentous phage displaying antibody variable domains. Nature 348, 552-554.
    • (1990) Nature , vol.348 , pp. 552-554
    • McCafferty, J.1    Griffiths, A.D.2    Winter, G.3    Chiswell, D.J.4
  • 48
    • 0029821726 scopus 로고    scopus 로고
    • A strategy of exon shuffling for making large peptide repertoires displayed on filamentous bacteriophage
    • Fisch, I., et al., & Winter, G. (1996). A strategy of exon shuffling for making large peptide repertoires displayed on filamentous bacteriophage. Proc. Natl Acad. Sci. USA 93, 7761-7766.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7761-7766
    • Fisch, I.1    Winter, G.2
  • 49
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • Matouschek, A., Kellis, J.T., Serrano, L. & Fersht, A.R. (1989). Mapping the transition state and pathway of protein folding by protein engineering. Nature 340, 122-126.
    • (1989) Nature , vol.340 , pp. 122-126
    • Matouschek, A.1    Kellis, J.T.2    Serrano, L.3    Fersht, A.R.4
  • 50
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.