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Volumn 9, Issue 4, 1998, Pages 370-376

The development of new biotechnologies using metalloprotein design

Author keywords

[No Author keywords available]

Indexed keywords

METALLOPROTEIN;

EID: 0032145656     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(98)80010-4     Document Type: Article
Times cited : (43)

References (79)
  • 4
    • 0027218815 scopus 로고
    • Metal compounds in therapy and diagnosis
    • Abrams MJ, Murrer BA. Metal compounds in therapy and diagnosis. Science. 261:1993;725-730.
    • (1993) Science , vol.261 , pp. 725-730
    • Abrams, M.J.1    Murrer, B.A.2
  • 5
    • 0011509370 scopus 로고    scopus 로고
    • Structural and functional aspects of metal sites in biology
    • Holm RH, Kennepohl P, Solomon EI. Structural and functional aspects of metal sites in biology. Chem Rev. 96:1996;2239-2314.
    • (1996) Chem Rev , vol.96 , pp. 2239-2314
    • Holm, R.H.1    Kennepohl, P.2    Solomon, E.I.3
  • 6
    • 0004281797 scopus 로고
    • S.J. Lippard, Berg J.M. Mil Valley: University Science Books
    • Lippard SJ, Berg JM. Principles of Bioinorganic Chemistry. 1994;University Science Books, Mil Valley.
    • (1994) Principles of Bioinorganic Chemistry
  • 7
    • 0004134954 scopus 로고
    • I. Bertini, H.B. Gray, S.J. Lippard, Valentine J.S. Sausalito: University Science Books
    • Bertini I, Gray HB, Lippard SJ, Valentine JS. Bioinorganic Chemistry. 1994;University Science Books, Sausalito.
    • (1994) Bioinorganic Chemistry
  • 9
    • 0004236008 scopus 로고
    • J.J.R.F.D. Silva, Williams R.J.P. Oxford: Clarendon Press
    • Silva JJRFD, Williams RJP. The Biological Chemistry of the Elements. 1991;Clarendon Press, Oxford.
    • (1991) The Biological Chemistry of the Elements
  • 10
    • 0025730892 scopus 로고
    • Engineered metal-binding proteins: Purification to protein folding
    • Arnold FH, Haymore BL. Engineered metal-binding proteins: purification to protein folding. Science. 252:1991;1796-1797.
    • (1991) Science , vol.252 , pp. 1796-1797
    • Arnold, F.H.1    Haymore, B.L.2
  • 14
    • 0027214480 scopus 로고
    • Metalloprotein design
    • Berg JM. Metalloprotein design. Curr Opin Struct Biol. 3:1993;585-588.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 585-588
    • Berg, J.M.1
  • 15
    • 0000428451 scopus 로고    scopus 로고
    • Design of metalloproteins
    • J.L. Cleland, Craik C.S. New York: Wiley-Liss
    • Hellinga HW. Design of metalloproteins. Cleland JL, Craik CS. Protein Engineering: Principles and Practice. 1996;369-398 Wiley-Liss, New York.
    • (1996) Protein Engineering: Principles and Practice , pp. 369-398
    • Hellinga, H.W.1
  • 16
    • 0031885768 scopus 로고    scopus 로고
    • The construction of metal centers in proteins by rational design
    • Hellinga HW. The construction of metal centers in proteins by rational design. Fold Des. 3:1998;R1-R8.
    • (1998) Fold Des , vol.3
    • Hellinga, H.W.1
  • 17
    • 0030801175 scopus 로고    scopus 로고
    • Engineering metal-binding sites in proteins
    • Lu Y, Valentine JS. Engineering metal-binding sites in proteins. Curr Opin Struct Biol. 7:1997;495-500.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 495-500
    • Lu, Y.1    Valentine, J.S.2
  • 18
    • 0027289198 scopus 로고
    • The design of metal binding sites in proteins
    • Regan L. The design of metal binding sites in proteins. Annu Rev Biophys Biomolec Struct. 22:1993;257-281.
    • (1993) Annu Rev Biophys Biomolec Struct , vol.22 , pp. 257-281
    • Regan, L.1
  • 19
    • 0029016430 scopus 로고
    • Protein design: Novel metal-binding sites
    • Regan L. Protein design: novel metal-binding sites. Trends Biotechnol. 20:1995;280-285.
    • (1995) Trends Biotechnol , vol.20 , pp. 280-285
    • Regan, L.1
  • 20
    • 0027199771 scopus 로고
    • Direct selection of antibodies that coordinate metals from semisynthetic combinatorial libraries
    • Barbas CF, Rosenblum JS, Lerner RA. Direct selection of antibodies that coordinate metals from semisynthetic combinatorial libraries. Proc Natl Acad Sci USA. 90:1993;6385-6389.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6385-6389
    • Barbas, C.F.1    Rosenblum, J.S.2    Lerner, R.A.3
  • 22
    • 0029850556 scopus 로고    scopus 로고
    • Grafting of discontinuous sites: A protein modeling strategy
    • Hornischer K, Blocker H. Grafting of discontinuous sites: a protein modeling strategy. Protein Eng. 9:1996;931-939.
    • (1996) Protein Eng , vol.9 , pp. 931-939
    • Hornischer, K.1    Blocker, H.2
  • 24
    • 0026335211 scopus 로고
    • Construction of new ligand binding sites in proteins of known structure. I. Computer-aided modeling of sites with pre-defined geometry
    • Hellinga HW, Richards FM. Construction of new ligand binding sites in proteins of known structure. I. Computer-aided modeling of sites with pre-defined geometry. J Mol Biol. 222:1991;763-785.
    • (1991) J Mol Biol , vol.222 , pp. 763-785
    • Hellinga, H.W.1    Richards, F.M.2
  • 25
    • 0028818241 scopus 로고
    • Metal Search - A computer program that helps design tetrahedral metal-binding sites
    • Clarke ND, Yuan SM. Metal Search - a computer program that helps design tetrahedral metal-binding sites. Nat Struct Biol. 2:1995;256-263.
    • (1995) Nat Struct Biol , vol.2 , pp. 256-263
    • Clarke, N.D.1    Yuan, S.M.2
  • 26
    • 0023812695 scopus 로고
    • Characterization of a helical protein designed from first principles
    • Regan L, DeGrado WF. Characterization of a helical protein designed from first principles. Science. 241:1988;976-978.
    • (1988) Science , vol.241 , pp. 976-978
    • Regan, L.1    DeGrado, W.F.2
  • 27
    • 0025644594 scopus 로고
    • A tetrahedral zinc(II)-binding site introduced into a designed protein
    • Regan L, Clarke ND. A tetrahedral zinc(II)-binding site introduced into a designed protein. Biochemistry. 29:1990;10878-10883.
    • (1990) Biochemistry , vol.29 , pp. 10878-10883
    • Regan, L.1    Clarke, N.D.2
  • 28
    • 0030978103 scopus 로고    scopus 로고
    • Construction of a catalytically active iron superoxide dismutase by rational protein design
    • Pinto AL, Hellinga HW, Caradonna JP. Construction of a catalytically active iron superoxide dismutase by rational protein design. Proc Natl Acad Sci USA. 94:1997;5562-5567.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5562-5567
    • Pinto, A.L.1    Hellinga, H.W.2    Caradonna, J.P.3
  • 29
    • 0030917147 scopus 로고    scopus 로고
    • The rational design and construction of a cuboidal iron-sulfur protein
    • Coldren CD, Hellinga HW, Caradonna JP. The rational design and construction of a cuboidal iron-sulfur protein. Proc Natl Acad Sci USA. 94:1997;6635-6640.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6635-6640
    • Coldren, C.D.1    Hellinga, H.W.2    Caradonna, J.P.3
  • 30
    • 0032546610 scopus 로고    scopus 로고
    • Construction of a novel redox protein by rational design: Conversion of a disulfide bridge into a mononuclear iron-sulfur center
    • Benson DE, Wisz MS, Liu W, Hellinga HW. Construction of a novel redox protein by rational design: conversion of a disulfide bridge into a mononuclear iron-sulfur center. Biochemistry. 1998;7070-7076.
    • (1998) Biochemistry , pp. 7070-7076
    • Benson, D.E.1    Wisz, M.S.2    Liu, W.3    Hellinga, H.W.4
  • 31
    • 0032499535 scopus 로고    scopus 로고
    • Construction of a family of Cys2His2 zinc binding sites in the hydrophobic core of thioredoxin by structure-based design
    • Wisz MS, Garrett CZ, Hellinga HW. Construction of a family of Cys2His2 zinc binding sites in the hydrophobic core of thioredoxin by structure-based design. Biochemistry. 37:1998;8269-8277.
    • (1998) Biochemistry , vol.37 , pp. 8269-8277
    • Wisz, M.S.1    Garrett, C.Z.2    Hellinga, H.W.3
  • 32
    • 0030220473 scopus 로고    scopus 로고
    • A Zn(II)-binding site engineered into retinol-binding protein exhibits metal-ion specificity and allows highly efficient affinity purification with a newly designed metal ligand
    • Schmidt AM, Muller HN, Skerra A. A Zn(II)-binding site engineered into retinol-binding protein exhibits metal-ion specificity and allows highly efficient affinity purification with a newly designed metal ligand. Chem Biol. 3:1996;645-653.
    • (1996) Chem Biol , vol.3 , pp. 645-653
    • Schmidt, A.M.1    Muller, H.N.2    Skerra, A.3
  • 33
    • 0026071781 scopus 로고
    • Metal-affinity separations: A new dimension in protein processing
    • Arnold FH. Metal-affinity separations: a new dimension in protein processing. Biotechnology. 9:1991;151-156.
    • (1991) Biotechnology , vol.9 , pp. 151-156
    • Arnold, F.H.1
  • 34
    • 0030069360 scopus 로고    scopus 로고
    • A nickel chelate microtiter plate assay for six histidine-containing proteins
    • Paborsky LR, Dunn KE, Gibbs CS, Dougherty JP. A nickel chelate microtiter plate assay for six histidine-containing proteins. Anal Biochem. 234:1996;60-65.
    • (1996) Anal Biochem , vol.234 , pp. 60-65
    • Paborsky, L.R.1    Dunn, K.E.2    Gibbs, C.S.3    Dougherty, J.P.4
  • 35
    • 0029008438 scopus 로고
    • Stable chelating linkage for reversible immobilization of oligohistidine tagged proteins in the BIAcore surface plasmon resonance detector
    • Gershon PD, Khilko S. Stable chelating linkage for reversible immobilization of oligohistidine tagged proteins in the BIAcore surface plasmon resonance detector. J Immun Methods. 183:1995;65-76.
    • (1995) J Immun Methods , vol.183 , pp. 65-76
    • Gershon, P.D.1    Khilko, S.2
  • 37
    • 0030077272 scopus 로고    scopus 로고
    • A self-assembled monolayer for the binding and study of histidine-tagged proteins by surface plasmon resonance
    • Sigal GB, Bamdad C, Barberis A, Strominger J, Whitesides GM. A self-assembled monolayer for the binding and study of histidine-tagged proteins by surface plasmon resonance. Anal Chem. 68:1996;490-497.
    • (1996) Anal Chem , vol.68 , pp. 490-497
    • Sigal, G.B.1    Bamdad, C.2    Barberis, A.3    Strominger, J.4    Whitesides, G.M.5
  • 38
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F1-ATPase
    • Noji H, Yasuda R, Yoshida M, Kinosita K. Direct observation of the rotation of F1-ATPase. Nature. 386:1997;299-302.
    • (1997) Nature , vol.386 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita, K.4
  • 39
    • 0030904290 scopus 로고    scopus 로고
    • Langmuir monolayer characterization of metal chelating lipids for protein targeting to membranes
    • Pack DW, Arnold FH. Langmuir monolayer characterization of metal chelating lipids for protein targeting to membranes. Chem Phys Lipids. 86:1997;135-152.
    • (1997) Chem Phys Lipids , vol.86 , pp. 135-152
    • Pack, D.W.1    Arnold, F.H.2
  • 40
    • 0030901962 scopus 로고    scopus 로고
    • A metal-chelating lipid for 2D protein crystallization via coordination of surface histidines
    • Pack DW, Chen G, Maloney KM, Chen CT, Arnold FH. A metal-chelating lipid for 2D protein crystallization via coordination of surface histidines. J Am Chem Soc. 119:1997;2479-2487.
    • (1997) J Am Chem Soc , vol.119 , pp. 2479-2487
    • Pack, D.W.1    Chen, G.2    Maloney, K.M.3    Chen, C.T.4    Arnold, F.H.5
  • 41
    • 0342722461 scopus 로고    scopus 로고
    • Structural study of the response regulator HupR from Rhodobacter capsulatus. Electron microscopy of two-dimensional crystals on a nickel-chelating lipid
    • Venien-Bryan C, Balavoine F, Toussaint B, Mioskowski C, Hewat EA, Helme B, Vignais PM. Structural study of the response regulator HupR from Rhodobacter capsulatus. Electron microscopy of two-dimensional crystals on a nickel-chelating lipid. J Mol Biol. 274:1997;687-692.
    • (1997) J Mol Biol , vol.274 , pp. 687-692
    • Venien-Bryan, C.1    Balavoine, F.2    Toussaint, B.3    Mioskowski, C.4    Hewat, E.A.5    Helme, B.6    Vignais, P.M.7
  • 43
    • 0026409452 scopus 로고
    • Structural biology of zinc
    • Christianson DW. Structural biology of zinc. Adv Protein Chem. 42:1991;281-355.
    • (1991) Adv Protein Chem , vol.42 , pp. 281-355
    • Christianson, D.W.1
  • 45
    • 0025040232 scopus 로고
    • De novo design expression and characterization of Felix: A four-helix bundle protein of native-like sequence
    • Hecht MH, Richardson JS, Richardson DC, Ogden RC. De novo design expression and characterization of Felix: a four-helix bundle protein of native-like sequence. Science. 249:1990;884-891.
    • (1990) Science , vol.249 , pp. 884-891
    • Hecht, M.H.1    Richardson, J.S.2    Richardson, D.C.3    Ogden, R.C.4
  • 47
    • 0030886443 scopus 로고    scopus 로고
    • Rational protein design: Combining theory and experiment
    • Hellinga HW. Rational protein design: combining theory and experiment. Proc Natl Acad Sci USA. 94:1997;10015-10017.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10015-10017
    • Hellinga, H.W.1
  • 49
    • 0027318293 scopus 로고
    • Engineering proteins for nonnatural environments
    • Arnold FH. Engineering proteins for nonnatural environments. FASEB J. 7:1993;744-749.
    • (1993) FASEB J , vol.7 , pp. 744-749
    • Arnold, F.H.1
  • 51
    • 0028500289 scopus 로고
    • Engineering an interfacial zinc site to increase hormone-receptor affinity
    • Matthews DJ, Wells JA. Engineering an interfacial zinc site to increase hormone-receptor affinity. Chem Biol. 1:1994;25-30.
    • (1994) Chem Biol , vol.1 , pp. 25-30
    • Matthews, D.J.1    Wells, J.A.2
  • 53
    • 0032054156 scopus 로고    scopus 로고
    • Protein engineering and the development of generic biosensors
    • Hellinga HW, Marvin JS. Protein engineering and the development of generic biosensors. Trends Biotechnol. 16:1998;183-189.
    • (1998) Trends Biotechnol , vol.16 , pp. 183-189
    • Hellinga, H.W.1    Marvin, J.S.2
  • 54
    • 0001013690 scopus 로고    scopus 로고
    • Design and evaluation of a peptidyl fluorescent chemosensor for divalent zinc
    • Walkup GK, Imperiali B. Design and evaluation of a peptidyl fluorescent chemosensor for divalent zinc. J Am Chem Soc. 118:1996;3053-3054.
    • (1996) J Am Chem Soc , vol.118 , pp. 3053-3054
    • Walkup, G.K.1    Imperiali, B.2
  • 55
    • 0030469797 scopus 로고    scopus 로고
    • New synthetic amino acids for the design and synthesis of peptide-based metal ion sensors
    • Torrado A, Imperiali B. New synthetic amino acids for the design and synthesis of peptide-based metal ion sensors. J Org Chem. 61:1996;8940-8948.
    • (1996) J Org Chem , vol.61 , pp. 8940-8948
    • Torrado, A.1    Imperiali, B.2
  • 56
    • 0030919897 scopus 로고    scopus 로고
    • Fluorescent chemosensors for divalent zinc based on zinc finger domains - Enhanced oxidative stability metal binding affinity and structural and functional characterization
    • Walkup GK, Imperiali B. Fluorescent chemosensors for divalent zinc based on zinc finger domains - enhanced oxidative stability metal binding affinity and structural and functional characterization. J Am Chem Soc. 119:1997;3443-3450.
    • (1997) J Am Chem Soc , vol.119 , pp. 3443-3450
    • Walkup, G.K.1    Imperiali, B.2
  • 57
    • 0030726112 scopus 로고    scopus 로고
    • Rational design of a calcium sensing system based on induced conformational changes of calmodulin
    • Schauer-Vukasinovic V, Cullen L, Daunert S. Rational design of a calcium sensing system based on induced conformational changes of calmodulin. J Am Chem Soc. 119:1997;11102-11103.
    • (1997) J Am Chem Soc , vol.119 , pp. 11102-11103
    • Schauer-Vukasinovic, V.1    Cullen, L.2    Daunert, S.3
  • 58
    • 0031011418 scopus 로고    scopus 로고
    • 2+-dependent changes in the fluorescence emission of an indicator composed of two green flourescent protein variants linked by a calmodulin-binding sequence
    • 2+-dependent changes in the fluorescence emission of an indicator composed of two green flourescent protein variants linked by a calmodulin-binding sequence. J Biol Chem. 272:1997;13270-13274.
    • (1997) J Biol Chem , vol.272 , pp. 13270-13274
    • Romoser, V.A.1    Hinkle, P.M.2    Persechini, A.3
  • 60
    • 0000726701 scopus 로고    scopus 로고
    • Carbonic anhydrase: Evolution of the zinc binding site by nature and design
    • Christianson DW, Fierke CA. Carbonic anhydrase: evolution of the zinc binding site by nature and design. Acc Chem Res. 29:1996;331-339.
    • (1996) Acc Chem Res , vol.29 , pp. 331-339
    • Christianson, D.W.1    Fierke, C.A.2
  • 61
    • 0001356438 scopus 로고
    • Enzyme-based fiber optic zinc biosensor
    • Thompson RB, Jones ER. Enzyme-based fiber optic zinc biosensor. Anal Chem. 65:1993;730-734.
    • (1993) Anal Chem , vol.65 , pp. 730-734
    • Thompson, R.B.1    Jones, E.R.2
  • 62
    • 0029930443 scopus 로고    scopus 로고
    • Fiber optic biosensor for Co(II) and Cu(II) based on fluorescence energy transfer with an enzyme transducer
    • Thompson RB, Ge Z, Patchan M, Huang CC, Fierke CA. Fiber optic biosensor for Co(II) and Cu(II) based on fluorescence energy transfer with an enzyme transducer. Biosens Bioelectron. 11:1996;557-564.
    • (1996) Biosens Bioelectron , vol.11 , pp. 557-564
    • Thompson, R.B.1    Ge, Z.2    Patchan, M.3    Huang, C.C.4    Fierke, C.A.5
  • 63
    • 0029790057 scopus 로고    scopus 로고
    • Structure-based design of a sulfonamide probe for fluorescence anisotropy detection of zinc with a carbonic anhydride-based biosensor
    • Elbaum D, Nair SK, Patchan MW, Thompson RB, Christianson DW. Structure-based design of a sulfonamide probe for fluorescence anisotropy detection of zinc with a carbonic anhydride-based biosensor. J Am Chem Soc. 118:1996;8381-8387.
    • (1996) J Am Chem Soc , vol.118 , pp. 8381-8387
    • Elbaum, D.1    Nair, S.K.2    Patchan, M.W.3    Thompson, R.B.4    Christianson, D.W.5
  • 65
    • 0029989461 scopus 로고    scopus 로고
    • Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II
    • Huang C-C, Lesburg CA, Kiefer LL, Fierke CA, Christianson DW. Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II. Biochemistry. 35:1996;3439-3446.
    • (1996) Biochemistry , vol.35 , pp. 3439-3446
    • Huang, C.-C.1    Lesburg, C.A.2    Kiefer, L.L.3    Fierke, C.A.4    Christianson, D.W.5
  • 66
    • 0030843294 scopus 로고    scopus 로고
    • Selection of carbonic anhydrase variants displayed on phage
    • Hunt JS, Fierke CA. Selection of carbonic anhydrase variants displayed on phage. J Biol Chem. 272:1997;20364-20372.
    • (1997) J Biol Chem , vol.272 , pp. 20364-20372
    • Hunt, J.S.1    Fierke, C.A.2
  • 68
    • 0027755990 scopus 로고
    • Search for new and improved radiolabeling methods for monoclonal antibodies: A review of different methods
    • Hiltunen JV. Search for new and improved radiolabeling methods for monoclonal antibodies: a review of different methods. Acta Oncol. 32:1993;831-839.
    • (1993) Acta Oncol , vol.32 , pp. 831-839
    • Hiltunen, J.V.1
  • 72
    • 0030839466 scopus 로고    scopus 로고
    • Conversion of myoglobin into a peroxygenase - A catalytic intermediate of sulfoxidation and epoxidation by the F43H/H64L mutant
    • Ozaki S, Matsui T, Watanabe Y. Conversion of myoglobin into a peroxygenase - a catalytic intermediate of sulfoxidation and epoxidation by the F43H/H64L mutant. J Am Chem Soc. 119:1997;6666-6667.
    • (1997) J Am Chem Soc , vol.119 , pp. 6666-6667
    • Ozaki, S.1    Matsui, T.2    Watanabe, Y.3
  • 73
    • 0031439169 scopus 로고    scopus 로고
    • A semisynthetic metalloenzyme based on a protein cavity that catalyzes the enantioselective hydrolysis of ester and amide substrates
    • Davies RR, Distefano MD. A semisynthetic metalloenzyme based on a protein cavity that catalyzes the enantioselective hydrolysis of ester and amide substrates. J Am Chem Soc. 119:1997;11643-11652.
    • (1997) J Am Chem Soc , vol.119 , pp. 11643-11652
    • Davies, R.R.1    Distefano, M.D.2
  • 74
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • Dahiyat BI, Mayo SL. De novo protein design: fully automated sequence selection. Science. 278:1997;82-87.
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 75
    • 0026905022 scopus 로고
    • Protein engineering for molecular electronics
    • Sligar SG, Salemme R. Protein engineering for molecular electronics. Curr Opin Biotechnol. 3:1992;388-393.
    • (1992) Curr Opin Biotechnol , vol.3 , pp. 388-393
    • Sligar, S.G.1    Salemme, R.2
  • 76
    • 0025319619 scopus 로고
    • Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution
    • Katti SK, LeMaster DM, Eklund H. Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution. J Mol Biol. 212:1990;167-184.
    • (1990) J Mol Biol , vol.212 , pp. 167-184
    • Katti, S.K.1    LeMaster, D.M.2    Eklund, H.3
  • 77
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. Molscript: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr. 24:1991;946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 78
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-hemolysin a heptameric transmembrane pore
    • Song L, Hobaugh MR, Shustak C, Cheley S, Bayley H, Gouaux JE. Structure of staphylococcal alpha-hemolysin a heptameric transmembrane pore. Science. 274:1996;1859-1866.
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 79
    • 0028090521 scopus 로고
    • Adipocyte lipid-binding protein complexed with arachidonic acid. Titration calorimetry and X-ray crystallographic studies
    • LaLonde JM, Levenson MA, Roe JJ, Bernlohr DA, Banaszak LJ. Adipocyte lipid-binding protein complexed with arachidonic acid. Titration calorimetry and X-ray crystallographic studies. J Biol Chem. 269:1994;25339-25347.
    • (1994) J Biol Chem , vol.269 , pp. 25339-25347
    • LaLonde, J.M.1    Levenson, M.A.2    Roe, J.J.3    Bernlohr, D.A.4    Banaszak, L.J.5


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