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Volumn 65, Issue 1, 2005, Pages 4-14

Azobenzene as photoresponsive conformational switch in cyclic peptides

Author keywords

amino azobenzenecarboxylic acids; Azobenzene; Biophysical properties; Conformational switches; Cyclic peptides; Photoisomerization; Synthesis

Indexed keywords

ALPHA AMINO ACID; AZOBENZENE; CYCLOPEPTIDE;

EID: 14044276271     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1399-3011.2004.00203.x     Document Type: Article
Times cited : (64)

References (73)
  • 1
  • 2
    • 33748241762 scopus 로고    scopus 로고
    • Control of the structure and functions of biomaterials by light
    • Willner, I. & Rubin, S. (1996) Control of the structure and functions of biomaterials by light. Angew. Chem. Int. Ed. Engl. 35, 367-385.
    • (1996) Angew. Chem. Int. Ed. Engl. , vol.35 , pp. 367-385
    • Willner, I.1    Rubin, S.2
  • 3
    • 0642375842 scopus 로고    scopus 로고
    • Photoswitchable biomaterials: En route to optobioelectronic systems
    • Willner, I. (1997) Photoswitchable biomaterials: en route to optobioelectronic systems. Acc. Chem. Res. 30, 347-356.
    • Acc. Chem. Res. , vol.30 , pp. 347-356
    • Willner, I.1
  • 4
    • 33845182895 scopus 로고
    • Photochemistry of azobenzene-containing polymers
    • Kumar, G.S. & Neckers, D.C. (1989) Photochemistry of azobenzene-containing polymers. Chem. Rev. 89, 1915-1925.
    • (1989) Chem. Rev. , vol.89 , pp. 1915-1925
    • Kumar, G.S.1    Neckers, D.C.2
  • 5
    • 0036856343 scopus 로고    scopus 로고
    • Photo-induced motions in azo-containing polymers
    • Natansohn, A. & Rochon, P. (2002) Photo-induced motions in azo-containing polymers. Chem. Rev. 102, 4139-4175.
    • (2002) Chem. Rev. , vol.102 , pp. 4139-4175
    • Natansohn, A.1    Rochon, P.2
  • 7
    • 0037403363 scopus 로고    scopus 로고
    • Photoactive liquid crystalline polymer systems with light-controllable structure and optical properties
    • Shibaev, V., Bobrovsky, A. & Boiko, N. (2003) Photoactive liquid crystalline polymer systems with light-controllable structure and optical properties. Prog. Polym. Sci. 28, 729-836.
    • (2003) Prog. Polym. Sci. , vol.28 , pp. 729-836
    • Shibaev, V.1    Bobrovsky, A.2    Boiko, N.3
  • 8
    • 0034840405 scopus 로고    scopus 로고
    • Cyclodextrin-based molecular machines
    • Harada, A. (2001) Cyclodextrin-based molecular machines. Acc. Chem. Res. 34, 456-464.
    • (2001) Acc. Chem. Res. , vol.34 , pp. 456-464
    • Harada, A.1
  • 9
    • 33751154443 scopus 로고    scopus 로고
    • Femtosecond time-resolved UV-visible absorption spectroscopy of trans-azobenzene in solution
    • Lednev, I.K., Ye, T.-Q., Hester, R.E. & Moore, J.N. (1996) Femtosecond time-resolved UV-visible absorption spectroscopy of trans-azobenzene in solution. J. Phys. Chem. 100, 13338-13341.
    • (1996) J. Phys. Chem. , vol.100 , pp. 13338-13341
    • Lednev, I.K.1    Ye, T.-Q.2    Hester, R.E.3    Moore, J.N.4
  • 12
    • 0035818132 scopus 로고    scopus 로고
    • Femtosecond time-resolved fluorescence study of photoisomerization of transazobenzene
    • Fujino, T., Arzhantsev, Y.S. & Tahara, T. (2001) Femtosecond time-resolved fluorescence study of photoisomerization of transazobenzene. J. Phys. Chem. A 105, 8123-8129.
    • (2001) J. Phys. Chem. A , vol.105 , pp. 8123-8129
    • Fujino, T.1    Arzhantsev, Y.S.2    Tahara, T.3
  • 13
    • 0037461222 scopus 로고    scopus 로고
    • Fluorescence spectra of trans- and cis-azobenzene - Emission from the Franck-Condon state
    • Satzger, H., Spörlein, S., Root, C., Wachtveitl, J., Zinth, W. & Gilch, P. (2003) Fluorescence spectra of trans- and cis-azobenzene - emission from the Franck-Condon state. Chem. Phys. Lett. 372, 216-223.
    • (2003) Chem. Phys. Lett. , vol.372 , pp. 216-223
    • Satzger, H.1    Spörlein, S.2    Root, C.3    Wachtveitl, J.4    Zinth, W.5    Gilch, P.6
  • 15
    • 37049155920 scopus 로고
    • Bond lengths and resonance in the cis-azobenzene molecule
    • Hampson, G.G. & Robertson, J.M. (1941) Bond lengths and resonance in the cis-azobenzene molecule. J. Chem. Soc., 409-413.
    • (1941) J. Chem. Soc. , pp. 409-413
    • Hampson, G.G.1    Robertson, J.M.2
  • 16
    • 0000367531 scopus 로고
    • Conformational aspects of polypeptide structure. XIX. Azoaromatic side chain effects
    • Goodman, M. & Kossoy, A. (1966) Conformational aspects of polypeptide structure. XIX. Azoaromatic side chain effects. J. Am. Chem. Soc. 88, 5010-5015.
    • (1966) J. Am. Chem. Soc. , vol.88 , pp. 5010-5015
    • Goodman, M.1    Kossoy, A.2
  • 17
    • 0014210941 scopus 로고
    • Conformational aspects of polypeptide structure. XXIII. Photoisomerization of azoaromatic polypeptides
    • Goodman, M. & Falxa, M.L. (1967) Conformational aspects of polypeptide structure. XXIII. Photoisomerization of azoaromatic polypeptides. J. Am. Chem. Soc. 89, 3863-3867.
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 3863-3867
    • Goodman, M.1    Falxa, M.L.2
  • 18
    • 0014382281 scopus 로고
    • Conformational aspects of polypeptide structure. XXVI. Azoaromatic side-chain effect from poly-L-p(p′-hydroxyphenylazo)-phenylalanine
    • Goodman, M. & Benedetti, E. (1968) Conformational aspects of polypeptide structure. XXVI. Azoaromatic side-chain effect from poly-L-p(p′-hydroxyphenylazo)-phenylalanine. Biochemistry 7, 4226-4234.
    • (1968) Biochemistry , vol.7 , pp. 4226-4234
    • Goodman, M.1    Benedetti, E.2
  • 19
    • 0014373463 scopus 로고
    • Conformational aspects of polypeptide structure. XXVII. Solvent effects on azoaromatic polypeptides
    • Benedetti, E., Kossoy, A., Falxa, M.L. & Goodman, M. (1968) Conformational aspects of polypeptide structure. XXVII. Solvent effects on azoaromatic polypeptides. Biochemistry 7, 4234-4242,
    • (1968) Biochemistry , vol.7 , pp. 4234-4242
    • Benedetti, E.1    Kossoy, A.2    Falxa, M.L.3    Goodman, M.4
  • 20
    • 0014365819 scopus 로고
    • Conformational aspects of polypeptide structure. XXVIII. Side-chain cotton effect from poly-L-p-(2′-hydroxy-5′-methylphenylazo)-phenyl- alanine
    • Benedetti, E. & Goodman, M. (1968) Conformational aspects of polypeptide structure. XXVIII. Side-chain cotton effect from poly-L-p-(2′-hydroxy-5′-methylphenylazo)-phenyl-alanine. Biochemistry 7, 4242-4247.
    • (1968) Biochemistry , vol.7 , pp. 4242-4247
    • Benedetti, E.1    Goodman, M.2
  • 22
    • 0029122069 scopus 로고
    • Photoregulation of cyclic peptide conformation
    • Ulysse, L., Cubillos, J. & Chmielewski, J. (1995) Photoregulation of cyclic peptide conformation. J. Am. Chem. Soc. 117, 8466-8467.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8466-8467
    • Ulysse, L.1    Cubillos, J.2    Chmielewski, J.3
  • 24
    • 0036009333 scopus 로고    scopus 로고
    • Using an azobenzene cross-linker to either increase or decrease peptide helix content upon trans-to-cis photoisomerization
    • Flint, D.G., Kumita, J.R., Smart, O.S. & Woolley, G.A. (2002) Using an azobenzene cross-linker to either increase or decrease peptide helix content upon trans-to-cis photoisomerization. Chem. Biol. 9,391-397.
    • (2002) Chem. Biol. , vol.9 , pp. 391-397
    • Flint, D.G.1    Kumita, J.R.2    Smart, O.S.3    Woolley, G.A.4
  • 25
    • 0036655377 scopus 로고    scopus 로고
    • Photo-control of peptide helix content by an azobenzene cross-linker: Steric interactions with underlying residues are not critical
    • Kumita, J.R., Flint, D.G., Smart, O.S. & Woolley, G.A. (2002) Photo-control of peptide helix content by an azobenzene cross-linker: steric interactions with underlying residues are not critical. Protein Eng. 15, 561-569.
    • (2002) Protein Eng. , vol.15 , pp. 561-569
    • Kumita, J.R.1    Flint, D.G.2    Smart, O.S.3    Woolley, G.A.4
  • 26
    • 37049175598 scopus 로고
    • The reduction of p-nitrobenzoic acid to hydrazo- and azobenzene-4: 4′-dicarboxylic acids by means of glucose
    • Tomlinson, M.L. (1946) The reduction of p-nitrobenzoic acid to hydrazo- and azobenzene-4:4′-dicarboxylic acids by means of glucose. J. Chem. Soc. 756.
    • (1946) J. Chem. Soc. , pp. 756
    • Tomlinson, M.L.1
  • 27
    • 37049072624 scopus 로고
    • Characterization of simple photoresponsive systems and their applications to metal ion transport
    • Ameerunisha, S. & Zacharias, P.S. (1995) Characterization of simple photoresponsive systems and their applications to metal ion transport. J. Chem. Soc. Perkin Trans. 2, 1679-1682.
    • (1995) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 1679-1682
    • Ameerunisha, S.1    Zacharias, P.S.2
  • 29
    • 0011210885 scopus 로고
    • Methoden zur herstellung und umwandlung von diazoarylverbindungen
    • (Müller, E., ed.). Georg Thieme, Stuttgart, 4. Aufl., Band
    • Schündehütte, K.H. (1965) Methoden zur Herstellung und Umwandlung von Diazoarylverbindungen. In: Houben-Weyl, Methoden der organischen Chemie (Müller, E., ed.), Vol. 10/3, pp. 214-465. Georg Thieme, Stuttgart, 4. Aufl., Band.
    • (1965) Houben-Weyl, Methoden der Organischen Chemie , vol.10 , Issue.3 , pp. 214-465
    • Schündehütte, K.H.1
  • 30
    • 0032730716 scopus 로고    scopus 로고
    • Photomodulation of conformational states. Synthesis of cyclic peptides with backbone-azobenzene moieties
    • Behrendt, R., Schenk, M., Musiol, H.-J. & Moroder, L. (1999) Photomodulation of conformational states. Synthesis of cyclic peptides with backbone-azobenzene moieties. J. Pept. Sci. 5, 519-529.
    • (1999) J. Pept. Sci. , vol.5 , pp. 519-529
    • Behrendt, R.1    Schenk, M.2    Musiol, H.-J.3    Moroder, L.4
  • 31
    • 0027963642 scopus 로고
    • The synthesis of a light-switchable amino acid for inclusion into conformationally mobile peptides
    • Ulysse, L. & Chmielewski, J. (1994) The synthesis of a light-switchable amino acid for inclusion into conformationally mobile peptides. Bioorg. Med. Chem. Lett. 4, 2145-2146.
    • (1994) Bioorg. Med. Chem. Lett. , vol.4 , pp. 2145-2146
    • Ulysse, L.1    Chmielewski, J.2
  • 32
    • 0005215827 scopus 로고
    • The 9-fluorenylmethyloxycarbonyl family of base-sensitive amino-protecting groups
    • Carpino, L.A. (1987) The 9-fluorenylmethyloxycarbonyl family of base-sensitive amino-protecting groups. Acc. Chem. Res. 20, 401-407.
    • (1987) Acc. Chem. Res. , vol.20 , pp. 401-407
    • Carpino, L.A.1
  • 33
    • 0028081131 scopus 로고
    • A simple method for the protection of aryl amines as their t-butylcarbamoyl (Boc) derivatives
    • Kelly, T.A. & McNeil, D.W. (1994) A simple method for the protection of aryl amines as their t-butylcarbamoyl (Boc) derivatives. Tetrahedron Lett. 35, 9003-9006.
    • (1994) Tetrahedron Lett. , vol.35 , pp. 9003-9006
    • Kelly, T.A.1    McNeil, D.W.2
  • 34
    • 0023655801 scopus 로고
    • Improved synthesis and iodination of a cleavable photoactivated probe
    • Murphy, H.R. & Harris, H.W. Jr (1987) Improved synthesis and iodination of a cleavable photoactivated probe. Anal. Biochem. 65, 88-95.
    • (1987) Anal. Biochem. , vol.65 , pp. 88-95
    • Murphy, H.R.1    Harris Jr., H.W.2
  • 35
    • 3843062398 scopus 로고    scopus 로고
    • Synthesis of photoswitchable amino acids based on azobenzene chromophores: Building blocks with potential for photoresponsive biomaterials
    • Juodaityte, J. & Sewald, N. (2004) Synthesis of photoswitchable amino acids based on azobenzene chromophores: building blocks with potential for photoresponsive biomaterials. J. Biotechnol. 112, 127-138.
    • (2004) J. Biotechnol. , vol.112 , pp. 127-138
    • Juodaityte, J.1    Sewald, N.2
  • 36
    • 0031055496 scopus 로고    scopus 로고
    • Novel cyclic biphenyl ether peptide β-strand mimetics and HIV-protease inhibitors
    • Janetka, J.W., Raman, P., Satyshur, K., Flentke, G.R. & Rich, D.H. (1997) Novel cyclic biphenyl ether peptide β-strand mimetics and HIV-protease inhibitors. J. Am. Chem. Soc. 119, 441-442.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 441-442
    • Janetka, J.W.1    Raman, P.2    Satyshur, K.3    Flentke, G.R.4    Rich, D.H.5
  • 37
    • 0030409162 scopus 로고    scopus 로고
    • A cyclic side-chain-linked biphenyl ether tripeptide: H3N+-cyclo-[Phe((4-0))-Phe-Phe((3-0))]-OMe.Cl
    • Janetka, J.W., Satyshur, K., Rich, D.H. (1996) A cyclic side-chain-linked biphenyl ether tripeptide: H3N+-cyclo-[Phe((4-0))-Phe-Phe((3-0))]-OMe.Cl-. Acta Crystallogr. Sect. C 52, 3112-3114.
    • (1996) Acta Crystallogr. Sect. C , vol.52 , pp. 3112-3114
    • Janetka, J.W.1    Satyshur, K.2    Rich, D.H.3
  • 39
    • 0036290843 scopus 로고    scopus 로고
    • Photomodulation of conformational states. III. Water-soluble bis-cysteinyl-peptides with (4-aminomethyl)-phenylazobenzoic acid as backbone constituent
    • Renner, C., Behrendt, R., Heim, N. & Moroder, L. (2002) Photomodulation of conformational states. III. Water-soluble bis-cysteinyl-peptides with (4-aminomethyl)-phenylazobenzoic acid as backbone constituent. Biopolymers 63, 382-393.
    • (2002) Biopolymers , vol.63 , pp. 382-393
    • Renner, C.1    Behrendt, R.2    Heim, N.3    Moroder, L.4
  • 40
    • 0025319619 scopus 로고
    • Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution
    • Katti, S.K., LeMaster, D.M. & Eklund, H. (1990) Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution. J. Mol. Biol. 212, 167-184.
    • (1990) J. Mol. Biol. , vol.212 , pp. 167-184
    • Katti, S.K.1    LeMaster, D.M.2    Eklund, H.3
  • 41
    • 0025925111 scopus 로고
    • Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin
    • Sodano, P., Xia, T.H., Bushweller, J.H., Bjornberg, O., Holmgren, A., Billeter, M. & Wüthrich, K. (1991) Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin. J. Mol. Biol. 221, 1311-1324.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1311-1324
    • Sodano, P.1    Xia, T.H.2    Bushweller, J.H.3    Bjornberg, O.4    Holmgren, A.5    Billeter, M.6    Wüthrich, K.7
  • 42
    • 0028220312 scopus 로고
    • Crystal structure of Escherichia coli thioredoxin reductase refined at 2 Å resolution. Implications for a large conformational change during catalysis
    • Waksman, G., Krishna, T.S., Williams, C.H. Jr & Kuriyan, J. (1994) Crystal structure of Escherichia coli thioredoxin reductase refined at 2 Å resolution. Implications for a large conformational change during catalysis. J. Mol. Biol. 136, 800-816.
    • (1994) J. Mol. Biol. , vol.236 , pp. 800-816
    • Waksman, G.1    Krishna, T.S.2    Williams Jr., C.H.3    Kuriyan, J.4
  • 43
    • 0028971683 scopus 로고
    • Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase
    • Kemmink, J., Darby, N.J., Dijkstra, K., Scheck, R.M. & Creighton, T.E. (1995) Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase. Protein Sci. 4, 2587-2593.
    • (1995) Protein Sci. , vol.4 , pp. 2587-2593
    • Kemmink, J.1    Darby, N.J.2    Dijkstra, K.3    Scheck, R.M.4    Creighton, T.E.5
  • 44
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin, J.L., Bardwell, J.C. & Kuriyan, J. (1993) Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 365, 464-468.
    • (1993) Nature , vol.365 , pp. 464-468
    • Martin, J.L.1    Bardwell, J.C.2    Kuriyan, J.3
  • 45
    • 0024324626 scopus 로고
    • Urea dependence of thiol-disulfide equilibria in thioredoxin: Confirmation of the linkage relationship and a sensitive assay for structure
    • Lin, T.Y. & Kim, P.S. (1989) Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structure. Biochemistry 28, 5282-5287.
    • (1989) Biochemistry , vol.28 , pp. 5282-5287
    • Lin, T.Y.1    Kim, P.S.2
  • 46
    • 0030868675 scopus 로고    scopus 로고
    • Elimination of all charged residues in the vicinity of the active-site helix of the disulfide oxidoreductase DsbA. Influence of electrostatic interactions on stability and redox properties
    • Jacobi, A., Huber-Wunderlich, M., Hennecke, J. & Glockshuber, R. (1997) Elimination of all charged residues in the vicinity of the active-site helix of the disulfide oxidoreductase DsbA. Influence of electrostatic interactions on stability and redox properties. J. Biol. Chem. 272, 21692-21699.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21692-21699
    • Jacobi, A.1    Huber-Wunderlich, M.2    Hennecke, J.3    Glockshuber, R.4
  • 47
    • 0031776171 scopus 로고    scopus 로고
    • A single dipeptide sequence modulates the redox properties of a whole enzyme family
    • Huber-Wunderlich, M. & Glockshuber, R. (1998) A single dipeptide sequence modulates the redox properties of a whole enzyme family. Folding Design 3, 161-171.
    • (1998) Folding Design , vol.3 , pp. 161-171
    • Huber-Wunderlich, M.1    Glockshuber, R.2
  • 48
    • 0027308079 scopus 로고
    • Redox potentials of active site bis-cysteinyl fragments of thiol-protein oxidoreductases
    • Siedler, F., Rudolph-Böhner, S., Doi, M., Musiol, H.-J. & Moroder, L. (1993) Redox potentials of active site bis-cysteinyl fragments of thiol-protein oxidoreductases. Biochemistry 32, 7488-7495.
    • (1993) Biochemistry , vol.32 , pp. 7488-7495
    • Siedler, F.1    Rudolph-Böhner, S.2    Doi, M.3    Musiol, H.-J.4    Moroder, L.5
  • 49
    • 0029893791 scopus 로고    scopus 로고
    • Oxidative folding of cystine-rich peptides vs. regioselective cysteine pairing strategies
    • Moroder, L., Besse, D., Musiol, H.-J., Rudolph-Böhner, S. & Siedler, F. (1996) Oxidative folding of cystine-rich peptides vs. regioselective cysteine pairing strategies. Pept. Sci. 40, 207-234.
    • (1996) Pept. Sci. , vol.40 , pp. 207-234
    • Moroder, L.1    Besse, D.2    Musiol, H.-J.3    Rudolph-Böhner, S.4    Siedler, F.5
  • 51
    • 0035986705 scopus 로고    scopus 로고
    • Redox-active cyclic bis(cysteinyl)peptides as catalysts for in vivo oxidative protein folding
    • Cabrele, C., Fiori, S., Pegoraro, S. & Moroder, L. (2002) Redox-active cyclic bis(cysteinyl)peptides as catalysts for in vivo oxidative protein folding. Chem. Biol. 9, 731-740.
    • (2002) Chem. Biol. , vol.9 , pp. 731-740
    • Cabrele, C.1    Fiori, S.2    Pegoraro, S.3    Moroder, L.4
  • 52
    • 2442756314 scopus 로고
    • Comparative analysis of the active site 3D-structures of thiol-protein oxidoreductases and related synthetic fragments
    • (Maia, H.L.S., ed.). ESCOM, Leiden
    • Rudolph-Böhner, S., Siedler, F. & Moroder, L. (1995) Comparative analysis of the active site 3D-structures of thiol-protein oxidoreductases and related synthetic fragments. In: Peptides (Maia, H.L.S., ed.), pp. 578-579. ESCOM, Leiden.
    • (1995) Peptides , pp. 578-579
    • Rudolph-Böhner, S.1    Siedler, F.2    Moroder, L.3
  • 54
    • 0034578592 scopus 로고    scopus 로고
    • Photomodulation of conformational states. I. Mono- and bicyclic peptides with (4-amino)phenylazobenzoic acid as backbone constituent
    • Renner, C., Behrendt, B., Spörlein, S., Wachtveitl, J. & Moroder, L. (2000) Photomodulation of conformational states. I. Mono- and bicyclic peptides with (4-amino)phenylazobenzoic acid as backbone constituent. Biopolymers 54, 489-500.
    • (2000) Biopolymers , vol.54 , pp. 489-500
    • Renner, C.1    Behrendt, B.2    Spörlein, S.3    Wachtveitl, J.4    Moroder, L.5
  • 55
    • 0034578637 scopus 로고    scopus 로고
    • Photomodulation of conformational states. II. Mono- and bicyclic peptides with (4-aminomethyl)phenylazobenzoic acid as backbone constituent
    • Renner, C., Cramer, J., Behrendt, R. & Moroder, L. (2000) Photomodulation of conformational states. II. Mono- and bicyclic peptides with (4-aminomethyl)phenylazobenzoic acid as backbone constituent. Biopolymers 54, 501-514.
    • (2000) Biopolymers , vol.54 , pp. 501-514
    • Renner, C.1    Cramer, J.2    Behrendt, R.3    Moroder, L.4
  • 62
    • 0000519682 scopus 로고
    • Reduction-potential of glutathione
    • Rost, J. & Rapoport, S. (1964) Reduction-potential of glutathione. Nature 201, 185.
    • (1964) Nature , vol.201 , pp. 185
    • Rost, J.1    Rapoport, S.2
  • 63
    • 0027481123 scopus 로고
    • Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
    • Wunderlich, M. & Glockshuber, R. (1993) Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli. Protein Sci. 2, 717-726.
    • (1993) Protein Sci. , vol.2 , pp. 717-726
    • Wunderlich, M.1    Glockshuber, R.2
  • 64
    • 73649177752 scopus 로고
    • Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver
    • Goldberger, R.F., Epstein, CJ. & Anfinsen, C.B. (1963) Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. J. Biol. Chem. 238, 628-635.
    • (1963) J. Biol. Chem. , vol.238 , pp. 628-635
    • Goldberger, R.F.1    Epstein, C.J.2    Anfinsen, C.B.3
  • 65
    • 0024337857 scopus 로고
    • Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteins
    • Freedman, R.B. (1989) Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins. Cell 57, 1069-1072.
    • (1989) Cell , vol.57 , pp. 1069-1072
    • Freedman, R.B.1
  • 66
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J.C., McGovern, K. & Beckwith, J. (1991) Identification of a protein required for disulfide bond formation in vivo. Cell 67, 581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 68
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: Building bridges in protein folding
    • Freedman, R.B., Hirst, T.R. & Tuite, M.F. (1994) Protein disulphide isomerase: building bridges in protein folding. Trends Biochem. Sci. 19, 331-336.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 69
    • 0030668155 scopus 로고    scopus 로고
    • Site-specific incorporation of photoisomerizable azobenzene groups into ribonuclease S
    • Liu, D., Karanicolas, J., Yu, C., Zhang, Z. & Woolley, G.A. (1997) Site-specific incorporation of photoisomerizable azobenzene groups into ribonuclease S. Bioorg. Med. Chem. Lett. 7, 2677-2680.
    • (1997) Bioorg. Med. Chem. Lett. , vol.7 , pp. 2677-2680
    • Liu, D.1    Karanicolas, J.2    Yu, C.3    Zhang, Z.4    Woolley, G.A.5
  • 70
  • 71
    • 0032361774 scopus 로고    scopus 로고
    • Photoswitching of the enzymatic activity of semisynthetic ribonuclease S' bearing phenylazophenylalanine at a specific site
    • Hamachi, I., Hiraoka, T., Yamada, Y. & Shinkai, S. (1998) Photoswitching of the enzymatic activity of semisynthetic ribonuclease S' bearing phenylazophenylalanine at a specific site. Chem. Lett. 17, 537-538.
    • (1998) Chem. Lett. , vol.27 , pp. 537-538
    • Hamachi, I.1    Hiraoka, T.2    Yamada, Y.3    Shinkai, S.4
  • 72
    • 0035709687 scopus 로고    scopus 로고
    • Kinetic characterization of ribonuclease S mutants containing photoisomerizable phenylazophenylalanine residues
    • James, D.A., Burns, D.C. & Woolley, G.A. (2001) Kinetic characterization of ribonuclease S mutants containing photoisomerizable phenylazophenylalanine residues. Protein Eng. 14, 983-991.
    • (2001) Protein Eng. , vol.14 , pp. 983-991
    • James, D.A.1    Burns, D.C.2    Woolley, G.A.3
  • 73
    • 0141885404 scopus 로고    scopus 로고
    • The kinetics of helix unfolding of an azobenzene cross-linked peptide probed by nanosecond time-resolved optical rotatory dispersion
    • Chen, E., Kumita, J.R., Woolley, G.A. & Kliger, D.S. (2003) The kinetics of helix unfolding of an azobenzene cross-linked peptide probed by nanosecond time-resolved optical rotatory dispersion. J. Am. Chem. Soc. 125, 12443-12449.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12443-12449
    • Chen, E.1    Kumita, J.R.2    Woolley, G.A.3    Kliger, D.S.4


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