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Volumn 9, Issue 9, 2003, Pages 574-593

Total chemical synthesis of enzymes

Author keywords

Backbone engineering; Chemical ligation; Chemical protein synthesis; Enzymes; HIV I protease; Native chemical ligation; Peptide synthesis; Peptide thioester; Solid phase chemical ligation; Solid phase peptide synthesis

Indexed keywords

ADAPTOR PROTEIN; AMIDE; AMINO ACID; ASPARTIC ACID; BARNASE; CARBOXYL GROUP; CHEMOKINE; CYSTEINE; CYTOKINE; DIMER; DISULFIDE; EPIDERMAL GROWTH FACTOR; ERYTHROPOIETIN; GLYCOPROTEIN; MVT 101; PEPSTATIN; PEPTIDE DERIVATIVE; PHOSPHOLIPASE A2; POLYPEPTIDE; PROTEINASE; PROTEINASE INHIBITOR; RAS PROTEIN; RUBREDOXIN; SERINE PROTEINASE INHIBITOR; THIOESTER; TRANSCRIPTION FACTOR; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG; UNINDEXED DRUG; ZINC FINGER PROTEIN;

EID: 0141504028     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/psc.475     Document Type: Article
Times cited : (62)

References (61)
  • 1
    • 84945084007 scopus 로고
    • Über einige Derivate des Glykokolls
    • Fischer E, Fourneau E. Über einige Derivate des Glykokolls. Ber. dtsch. chem. Ges. 1901; 34: 2868-2879.
    • (1901) Ber. Dtsch. Chem. Ges. , vol.34 , pp. 2868-2879
    • Fischer, E.1    Fourneau, E.2
  • 2
    • 0141747593 scopus 로고    scopus 로고
    • Fischer Nobel Prize
    • Fischer Nobel Prize: http://www.nobel.se/chemistry/laureates/1902/
  • 3
    • 84892166712 scopus 로고
    • Einfluss der Configuration auf die Wirkung den Enzyme
    • Fischer E. Einfluss der Configuration auf die Wirkung den Enzyme. Ber. Dtsch. Chem. Ges. 1894: 27: 2985-2993.
    • (1894) Ber. Dtsch. Chem. Ges. , vol.27 , pp. 2985-2993
    • Fischer, E.1
  • 4
    • 85047678643 scopus 로고
    • Ueber Bau und Gruppierung der Eiweisskörper
    • Hofmeister F. Ueber Bau und Gruppierung der Eiweisskörper. Ergeb. Physiol. 1902; 1: 759-802.
    • (1902) Ergeb. Physiol. , vol.1 , pp. 759-802
    • Hofmeister, F.1
  • 5
    • 0009344903 scopus 로고
    • Ueber die Hydrolyse der Proteinstoffe
    • (Hofmeister had presented his famous plenary lecture on protein structure in the morning of the 74th meeting of the Society of German Scientists and Physicians (1902, Karlsbad). That same afternoon, Fischer read his paper on the isolation of amino acids and peptides from protein hydrosylates, and suggested the coupling of amino acids in proteins). Adapted from
    • Fischer E. Ueber die Hydrolyse der Proteinstoffe. Chemiker Zeitung 1902; 26: 939-940. (Hofmeister had presented his famous plenary lecture on protein structure in the morning of the 74th meeting of the Society of German Scientists and Physicians (1902, Karlsbad). That same afternoon, Fischer read his paper on the isolation of amino acids and peptides from protein hydrosylates, and suggested the coupling of amino acids in proteins). Adapted from: http://www.pepnet.com/fischerbio.html
    • (1902) Chemiker Zeitung , vol.26 , pp. 939-940
    • Fischer, E.1
  • 6
    • 0141859162 scopus 로고
    • Synthese von Polypeptiden, IV. Derivate des Phenylalanins
    • Fischer E. Synthese von Polypeptiden, IV. Derivate des Phenylalanins. Ber. dtsch. chem. Ges. 1904; 37: 3062-3071.
    • (1904) Ber. Dtsch. Chem. Ges. , vol.37 , pp. 3062-3071
    • Fischer, E.1
  • 7
    • 84946388015 scopus 로고
    • Synthese von Polypeptiden, XVII
    • Fischer E. Synthese von Polypeptiden, XVII. Ber. dtsch. chem. Ges. 1907; 40: 1754-1767.
    • (1907) Ber. Dtsch. Chem. Ges. , vol.40 , pp. 1754-1767
    • Fischer, E.1
  • 8
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • Dawson PE, Kent SBH. Synthesis of native proteins by chemical ligation. Ann. Rev. Biochem. 2000; 69: 925-962.
    • (2000) Ann. Rev. Biochem. , vol.69 , pp. 925-962
    • Dawson, P.E.1    Kent, S.B.H.2
  • 11
    • 0025225682 scopus 로고
    • X-ray crystallographic structure of a complex between synthetic HIV-1 protease and a substrate-based hydroxyethylamine inhibitor
    • Swain AL, Miller M, Green J, Rich DH, Schneider J, Kent SBH, Wlodawer A. X-ray crystallographic structure of a complex between synthetic HIV-1 protease and a substrate-based hydroxyethylamine inhibitor. Proc. Natl Acad. Sci. USA 1990; 87: 8805-8809.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8805-8809
    • Swain, A.L.1    Miller, M.2    Green, J.3    Rich, D.H.4    Schneider, J.5    Kent, S.B.H.6    Wlodawer, A.7
  • 16
    • 0015522891 scopus 로고
    • The carboxylate ion in the active center of pepsin
    • Hartsuck JA, Tang J. The carboxylate ion in the active center of pepsin. J. Biol. Chem. 1972; 247: 2575-2580.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2575-2580
    • Hartsuck, J.A.1    Tang, J.2
  • 17
    • 0027137058 scopus 로고
    • Catalytic contribution of flap-substrate hydrogen bonds in HIV-1 protease explored by chemical synthesis
    • Baca M, Kent SBH. Catalytic contribution of flap-substrate hydrogen bonds in HIV-1 protease explored by chemical synthesis. Proc. Natl Acad. Sci. US 1993; 90: 11 638-11 642.
    • (1993) Proc. Natl. Acad. Sci. US , vol.90 , pp. 11638-11642
    • Baca, M.1    Kent, S.B.H.2
  • 18
  • 19
    • 0025641617 scopus 로고
    • Stability and activity of human immunodeficiency virus protease: Comparison of the natural dimer with a homologous, single-chain tethered dimer
    • Cheng YE, Yin FH, Foundling SF, Blomstrom S, Kettner CA. Stability and Activity of Human Immunodeficiency Virus Protease: Comparison of the Natural Dimer with a Homologous, Single-Chain Tethered Dimer. Proc. National Academy Sciences USA 1990; 87: 9660-9664.
    • (1990) Proc. National Academy Sciences USA , vol.87 , pp. 9660-9664
    • Cheng, Y.E.1    Yin, F.H.2    Foundling, S.F.3    Blomstrom, S.4    Kettner, C.A.5
  • 20
    • 0031042369 scopus 로고    scopus 로고
    • Activity of tethered human immunodeficiency virus 1 protease containing mutations in the flap region of one subunit
    • Tozer J, Yin FH, Cheng YS, Bagossi P, Weber IT, Harrison RW, Oroszlan S. Activity of tethered human immunodeficiency virus 1 protease containing mutations in the flap region of one subunit. Eur. J. Biochem. 1997; 244: 235-241.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 235-241
    • Tozer, J.1    Yin, F.H.2    Cheng, Y.S.3    Bagossi, P.4    Weber, I.T.5    Harrison, R.W.6    Oroszlan, S.7
  • 21
    • 0028810342 scopus 로고
    • Chemical ligation of cysteine-containing peptides: Synthesis of a 22 kDa tethered dimer of HIV-1 protease
    • Baca M, Muir TW, Schnölzer M, Kent SBH. Chemical ligation of cysteine-containing peptides: synthesis of a 22 kDa tethered dimer of HIV-1 protease. J. Am. Chem. Soc. 1995: 117: 1881-1887.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 1881-1887
    • Baca, M.1    Muir, T.W.2    Schnölzer, M.3    Kent, S.B.H.4
  • 22
    • 0034711433 scopus 로고    scopus 로고
    • Protein backbone engineering through total chemical synthesis: New insight into the mechanism of HIV-1 protease catalysis
    • Baca M, Kent SBH. Protein backbone engineering through total chemical synthesis: new insight into the mechanism of HIV-1 protease catalysis. Tetrahedron 2000; 56: 9503-9513.
    • (2000) Tetrahedron , vol.56 , pp. 9503-9513
    • Baca, M.1    Kent, S.B.H.2
  • 23
    • 0018133234 scopus 로고
    • Synthesis and biological activity of two disulphide bond isomers of human insulin: [A7-A11,A6-B7-cystine]- and [A6-A7,A11-B7-cystine]insulin (human)
    • Sieber P, Eisler K, Kamber B, Riniker B, Rittel W, et al. Synthesis and biological activity of two disulphide bond isomers of human insulin: [A7-A11,A6-B7-cystine]- and [A6-A7,A11-B7-cystine]insulin (human). Hoppe Selyler's Z. Physiol. Chem. 1978; 359: 113-123.
    • (1978) Hoppe Selyler's Z. Physiol. Chem. , vol.359 , pp. 113-123
    • Sieber, P.1    Eisler, K.2    Kamber, B.3    Riniker, B.4    Rittel, W.5
  • 24
    • 0022000347 scopus 로고
    • Studies on peptides. CXXVII. Synthesis of a tripentacontapeptide with epidermal growth factor activity
    • Akaji K, Fujii N, Yajima H, Hayashi K, Mizuta K, et al. Studies on peptides. CXXVII. Synthesis of a tripentacontapeptide with epidermal growth factor activity. Chem. Pharm. Bull. 1985; 33: 184-201.
    • (1985) Chem. Pharm. Bull. , vol.33 , pp. 184-201
    • Akaji, K.1    Fujii, N.2    Yajima, H.3    Hayashi, K.4    Mizuta, K.5
  • 25
    • 0027238026 scopus 로고
    • The structure of a centrosymmetric protein crystal
    • Zawadzke LE, Berg JM. The structure of a centrosymmetric protein crystal. Proteins 1993; 16: 301-305.
    • (1993) Proteins , vol.16 , pp. 301-305
    • Zawadzke, L.E.1    Berg, J.M.2
  • 26
    • 0029677674 scopus 로고    scopus 로고
    • Solution synthesis of human midkine, a novel heparin-binding neurotrophic factor consisting of 121 amino acid residues with five disulphide bonds
    • Inui T, Bodi J, Kubo S, Hishio H, Kimura T, Kojima S, Maruta H, Muramatsu T, Sakakibara S. Solution synthesis of human midkine, a novel heparin-binding neurotrophic factor consisting of 121 amino acid residues with five disulphide bonds. J. Peptide Sci. 1996; 2: 28-39.
    • (1996) J. Peptide Sci. , vol.2 , pp. 28-39
    • Inui, T.1    Bodi, J.2    Kubo, S.3    Hishio, H.4    Kimura, T.5    Kojima, S.6    Maruta, H.7    Muramatsu, T.8    Sakakibara, S.9
  • 27
    • 0001462324 scopus 로고
    • Development of a linker with an enhanced stability for the preparation of peptide thioesters and its application to the synthesis of a stable-isotope-labeled hu-type DNA-binding protein
    • Hojo H, Kwon Y, Kakuta Y, Tsuda S, Tanaka I, Hikichi K, Aimoto S. Development of a linker with an enhanced stability for the preparation of peptide thioesters and its application to the synthesis of a stable-isotope-labeled hu-type DNA-binding protein. Bull. Chem. Soc. Jpn. 1993; 66: 2700-2706.
    • (1993) Bull. Chem. Soc. Jpn. , vol.66 , pp. 2700-2706
    • Hojo, H.1    Kwon, Y.2    Kakuta, Y.3    Tsuda, S.4    Tanaka, I.5    Hikichi, K.6    Aimoto, S.7
  • 28
    • 0024421799 scopus 로고
    • Chemical synthesis in protein engineering: Total synthesis, purification, and covalent structural characterization of a mitogenic protein, human transforming growth factor-α
    • Woo DD-L, Clarke-Lewis I, Chait BT, Kent SBH. Chemical synthesis in protein engineering: total synthesis, purification, and covalent structural characterization of a mitogenic protein, human transforming growth factor-α. Protein Eng 1989; 3: 29-37.
    • (1989) Protein Eng. , vol.3 , pp. 29-37
    • Woo, D.D.-L.1    Clarke-Lewis, I.2    Chait, B.T.3    Kent, S.B.H.4
  • 29
    • 0026525457 scopus 로고
    • Constructing proteins by dovetailing unprotected synthetic peptides: Backbone engineered HIV protease
    • Schnölzer M, Kent S. Constructing proteins by dovetailing unprotected synthetic peptides: backbone engineered HIV protease. Science 1992; 256: 221-225.
    • (1992) Science , vol.256 , pp. 221-225
    • Schnölzer, M.1    Kent, S.2
  • 30
    • 0040555246 scopus 로고
    • Synthesis of proteins by chemical ligation of unprotected peptide segments: Mirror-image enzyme molecules, D- and L-HIV protease analogues
    • Angeletti R (ed.). Academic Press: New York
    • Milton R. deL, Milton S, Schnölzer M, Kent SBH. Synthesis of proteins by chemical ligation of unprotected peptide segments: mirror-image enzyme molecules, D- & L-HIV protease analogues. In Techniques in Protein Chemistry IV, Angeletti R (ed.). Academic Press: New York, 1993; 257-267.
    • (1993) Techniques in Protein Chemistry IV , pp. 257-267
    • Milton, R.deL.1    Milton, S.2    Schnölzer, M.3    Kent, S.B.H.4
  • 31
    • 0001702244 scopus 로고    scopus 로고
    • Probing the structural basis of the catalytic activity of HIV-1 protease through total chemical protein synthesis
    • Miller M, Baca M, Rao JKM, Kent S. Probing the structural basis of the catalytic activity of HIV-1 protease through total chemical protein synthesis. J. Molec. Structure (THEOCHEM) 1998; 423: 137-152.
    • (1998) J. Molec. Structure (THEOCHEM) , vol.423 , pp. 137-152
    • Miller, M.1    Baca, M.2    Rao, J.K.M.3    Kent, S.4
  • 32
    • 0001087039 scopus 로고    scopus 로고
    • Computational studies of the aminolysis of oxoesters and thioesters in aqueous solution
    • Yang W, Drueckhammer DG. Computational studies of the aminolysis of oxoesters and thioesters in aqueous solution. Organic Lett. 2000; 2: 4133-4136.
    • (2000) Organic Lett. , vol.2 , pp. 4133-4136
    • Yang, W.1    Drueckhammer, D.G.2
  • 33
    • 84939246733 scopus 로고
    • Uber peptidsynthesen. 8. Bildung von s-haltigen peptiden durch intramolekulare wanderung von aminoacylresten
    • Wieland Th, et al. Uber peptidsynthesen. 8. Bildung von s-haltigen peptiden durch intramolekulare wanderung von aminoacylresten. Liebig's Annalen der Chemie 1953; 583: 129-149.
    • (1953) Liebig's Annalen Der Chemie , vol.583 , pp. 129-149
    • Wieland, Th.1
  • 36
    • 0026706930 scopus 로고
    • Weighing naked proteins: Practical, high-accuracy mass measurement of peptides and proteins
    • Chait BT, Kent SBH. Weighing naked proteins: practical, high-accuracy mass measurement of peptides and proteins. Science 1992; 257: 1885-1894.
    • (1992) Science , vol.257 , pp. 1885-1894
    • Chait, B.T.1    Kent, S.B.H.2
  • 37
    • 0030973396 scopus 로고    scopus 로고
    • Modulation of reactivity in native chemical ligation through the use of thiol additives
    • Dawson PE, Churchill M, Ghadiri MR, Kent SBH. Modulation of reactivity in native chemical ligation through the use of thiol additives. J. Am. Chem. Soc. 1997; 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
  • 38
    • 0033621158 scopus 로고    scopus 로고
    • Protein synthesis by native chemical ligation: Expanded scope by using straightforward methodology
    • Hackeng TM, Griffin JH, Dawson PE. Protein synthesis by native chemical ligation: expanded scope by using straightforward methodology. Proc. Natl Acad. Sci. USA 1999; 96: 10 068-10 073.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10068-10073
    • Hackeng, T.M.1    Griffin, J.H.2    Dawson, P.E.3
  • 39
    • 0033168207 scopus 로고    scopus 로고
    • Probing intermolecular backbone H-bonding in serine-proteinase protein-inhibitor complexes
    • Lu W, Randal M, Kossiakoff A, Kent SBH. Probing intermolecular backbone H-bonding in serine-proteinase protein-inhibitor complexes. Chem. Biol. 1999; 6: 419-427.
    • (1999) Chem. Biol. , vol.6 , pp. 419-427
    • Lu, W.1    Randal, M.2    Kossiakoff, A.3    Kent, S.B.H.4
  • 41
    • 0030037155 scopus 로고    scopus 로고
    • Extending the applicability of native chemical ligation
    • Canne LE Bark SJ, Kent SBH. Extending the applicability of native chemical ligation. J. Am. Chem. Soc. 1996; 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
  • 42
    • 0033657692 scopus 로고    scopus 로고
    • Nalpha-2-mercaptobenzylamine-assisted chemical ligation
    • Offer J, Dawson PE. Nalpha-2-mercaptobenzylamine-assisted chemical ligation. Org Lett. 2000; 2: 23-26.
    • (2000) Org. Lett. , vol.2 , pp. 23-26
    • Offer, J.1    Dawson, P.E.2
  • 44
    • 0035811061 scopus 로고    scopus 로고
    • Total synthesis of cytochrome b562 by native chemical ligation using a removable auxiliary
    • Low DW, Hill MG, Carrasco MR, Botti P, Kent SBH. Total synthesis of cytochrome b562 by native chemical ligation using a removable auxiliary. Proc. Natl Acad. Sci. USA 2001; 98: 6554-6559.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6554-6559
    • Low, D.W.1    Hill, M.G.2    Carrasco, M.R.3    Botti, P.4    Kent, S.B.H.5
  • 45
    • 0034643993 scopus 로고    scopus 로고
    • A "traceless" Staudinger ligation for the chemoselective synthesis of amide bonds
    • Saxon E, Armstrong JI, Bertozzi CR. A "traceless" Staudinger ligation for the chemoselective synthesis of amide bonds. Org. Lett. 2000; 2: 2141-2143.
    • (2000) Org. Lett. , vol.2 , pp. 2141-2143
    • Saxon, E.1    Armstrong, J.I.2    Bertozzi, C.R.3
  • 46
    • 0035843279 scopus 로고    scopus 로고
    • High-yielding Staudinger ligation of a phosphinothioester and azide to form a peptide
    • Nilsson BL, Kiessling LL, Raines RT. High-yielding Staudinger ligation of a phosphinothioester and azide to form a peptide. Org. Lett. 2001; 3: 9-12.
    • (2001) Org. Lett. , vol.3 , pp. 9-12
    • Nilsson, B.L.1    Kiessling, L.L.2    Raines, R.T.3
  • 47
    • 0001414449 scopus 로고    scopus 로고
    • Probing intermolecular main chain H-bonding in serine proteinase-protein inhibitor complexes: Chemical synthesis of a backbone-engineered turkey ovomucoid third domain
    • Lu W, Qasim MA, Laskowski M Jr., Kent SBH. Probing intermolecular main chain H-bonding in serine proteinase-protein inhibitor complexes: chemical synthesis of a backbone-engineered turkey ovomucoid third domain. Biochemistry 1997; 36: 673-679.
    • (1997) Biochemistry , vol.36 , pp. 673-679
    • Lu, W.1    Qasim, M.A.2    Laskowski M., Jr.3    Kent, S.B.H.4
  • 48
    • 0029140496 scopus 로고
    • Total chemical synthesis of a unique transcription factor-related protein: cMyc-Max
    • Canne LE, Ferré-D'Amaré AR, Burley SK, Kent SBH. Total chemical synthesis of a unique transcription factor-related protein: cMyc-Max. J. Am. Chem. Soc. 1995; 117: 2998-3007.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2998-3007
    • Canne, L.E.1    Ferré-D'Amaré, A.R.2    Burley, S.K.3    Kent, S.B.H.4
  • 49
    • 0026486811 scopus 로고
    • "In situ" Neutralization protocols in Boc-chemistry solid phase peptide synthesis: Rapid, high yield assembly of difficult sequences
    • Schnolzer M, Alewood P, Alewood D, Kent SBH. "In situ" neutralization protocols in Boc-chemistry solid phase peptide synthesis: rapid, high yield assembly of difficult sequences. Int. J. Pept. Prot. Res. 1992: 40: 180-193.
    • (1992) Int. J. Pept. Prot. Res. , vol.40 , pp. 180-193
    • Schnolzer, M.1    Alewood, P.2    Alewood, D.3    Kent, S.B.H.4
  • 51
    • 0034674698 scopus 로고    scopus 로고
    • Protein synthesis by solid-phase chemical ligation using a safety catch linker
    • Brik A, Keinan E, Dawson PE. Protein synthesis by solid-phase chemical ligation using a safety catch linker. J. Org. Chem. 2000; 65: 3829-3835.
    • (2000) J. Org. Chem. , vol.65 , pp. 3829-3835
    • Brik, A.1    Keinan, E.2    Dawson, P.E.3
  • 52
    • 0037548053 scopus 로고    scopus 로고
    • Semisynthesis of proteins by expressed protein ligation
    • Tom W. Muir
    • Muir TW. Semisynthesis of proteins by expressed protein ligation. Tom W. Muir, Annu. Rev. Biochem. (2003) 72: 249-289.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 249-289
    • Muir, T.W.1
  • 53
    • 20744456789 scopus 로고
    • Solid phase peptide synthesis. 1. Synthesis of a tetrapeptide
    • Merrifield RB. Solid phase peptide synthesis. 1. Synthesis of a tetrapeptide. J. Am. Chem. Soc. 1963; 85: 2149.
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 2149
    • Merrifield, R.B.1
  • 54
    • 0027213390 scopus 로고
    • Structural engineering of HIV-1 protease with a β-turn mimic of fixed geometry
    • Baca M, Alewood P, Kent SBH. Structural engineering of HIV-1 protease with a β-turn mimic of fixed geometry. Protein Sci. 1993; 2: 1085-1091.
    • (1993) Protein Sci. , vol.2 , pp. 1085-1091
    • Baca, M.1    Alewood, P.2    Kent, S.B.H.3
  • 56
    • 0034924188 scopus 로고    scopus 로고
    • Segmental isotopic labeling using expressed protein ligation
    • Cowburn D, Muir TW. Segmental isotopic labeling using expressed protein ligation. Methods Enzymol 2001; 339: 41-54.
    • (2001) Methods Enzymol. , vol.339 , pp. 41-54
    • Cowburn, D.1    Muir, T.W.2
  • 57
    • 0030267666 scopus 로고    scopus 로고
    • Probing the chemical basis of binding activity in an SH3 domain by protein signature analysis
    • Muir TW, Dawson PE, Fitzgerald MC, Kent SBH. Probing the chemical basis of binding activity in an SH3 domain by protein signature analysis. Chem. Biol. 1996; 3: 817-825.
    • (1996) Chem. Biol. , vol.3 , pp. 817-825
    • Muir, T.W.1    Dawson, P.E.2    Fitzgerald, M.C.3    Kent, S.B.H.4
  • 58
    • 0036489968 scopus 로고    scopus 로고
    • The cyclotides: Novel macrocyclic peptides as scaffolds in drug design
    • Craik DJ, Simonsen S, Daly NL. The cyclotides: Novel macrocyclic peptides as scaffolds in drug design. Curr. Opin. Drug Discov. Devel. 2003; 5: 251-260.
    • (2003) Curr. Opin. Drug Discov. Devel. , vol.5 , pp. 251-260
    • Craik, D.J.1    Simonsen, S.2    Daly, N.L.3
  • 59
    • 0037459237 scopus 로고    scopus 로고
    • Thermodynamics of a designed protein catenane
    • Blankenship JW, Dawson PE. Thermodynamics of a designed protein catenane. J. Mol. Biol. 2003; 327: 537-548.
    • (2003) J. Mol. Biol. , vol.327 , pp. 537-548
    • Blankenship, J.W.1    Dawson, P.E.2
  • 60
    • 0038771224 scopus 로고    scopus 로고
    • Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain
    • Urban S, Freeman M. Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain. Molecular Cell 2003; 11: 1425-1434.
    • (2003) Molecular Cell , vol.11 , pp. 1425-1434
    • Urban, S.1    Freeman, M.2
  • 61
    • 0033554426 scopus 로고    scopus 로고
    • Total chemical synthesis of the integral membrane protein influenza A virus M2 proton channel: Role of its cytoplasmic domain for pore assembly
    • Salom D, Lear JD, Kent SBH. DeGrado WF. Total chemical synthesis of the integral membrane protein influenza A virus M2 proton channel: role of its cytoplasmic domain for pore assembly. Biochemistry 1999; 38: 11 905-11 913.
    • (1999) Biochemistry , vol.38 , pp. 11905-11913
    • Salom, D.1    Lear, J.D.2    Kent, S.B.H.3    DeGrado, W.F.4


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