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Volumn 7, Issue 9, 2012, Pages

An Economical Method for Production of 2H,13CH3-Threonine for Solution NMR Studies of Large Protein Complexes: Application to the 670 kDa Proteasome

Author keywords

[No Author keywords available]

Indexed keywords

CARBON 13; DEUTERIUM; PROTEASOME; THREONINE; TRITIUM;

EID: 84866272306     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0043725     Document Type: Article
Times cited : (83)

References (65)
  • 1
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax A, Grzesiek S, (1993) Methodological advances in protein NMR. Acc Chem Res 26: 131-138.
    • (1993) Acc Chem Res , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 2
    • 0025871254 scopus 로고
    • Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy
    • Clore GM, Gronenborn AM, (1991) Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy. Science 252: 1390-1399.
    • (1991) Science , vol.252 , pp. 1390-1399
    • Clore, G.M.1    Gronenborn, A.M.2
  • 3
    • 0000061511 scopus 로고
    • Carbon-13 line narrowing by deuterium decoupling in deuterium/carbon-13/nitrogen-15 enriched proteins. Application to triple resonance 4D J connectivity of sequential amides
    • Grzesiek S, Anglister J, Ren H, Bax A, (1993) Carbon-13 line narrowing by deuterium decoupling in deuterium/carbon-13/nitrogen-15 enriched proteins. Application to triple resonance 4D J connectivity of sequential amides. J Am Chem Soc 115: 4369-4370.
    • (1993) J Am Chem Soc , vol.115 , pp. 4369-4370
    • Grzesiek, S.1    Anglister, J.2    Ren, H.3    Bax, A.4
  • 4
    • 33644774471 scopus 로고    scopus 로고
    • Optimal isotope labelling for NMR protein structure determinations
    • Kainosho M, Torizawa T, Iwashita Y, Terauchi T, Mei Ono A, et al. (2006) Optimal isotope labelling for NMR protein structure determinations. Nature 440: 52-57.
    • (2006) Nature , vol.440 , pp. 52-57
    • Kainosho, M.1    Torizawa, T.2    Iwashita, Y.3    Terauchi, T.4    Mei Ono, A.5
  • 5
    • 0033794450 scopus 로고    scopus 로고
    • New developments in isotope labeling strategies for protein solution NMR spectroscopy
    • Goto NK, Kay LE, (2000) New developments in isotope labeling strategies for protein solution NMR spectroscopy. Curr Opin Struct Biol 10: 585-592.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 585-592
    • Goto, N.K.1    Kay, L.E.2
  • 6
    • 0029905210 scopus 로고    scopus 로고
    • Dynamical Mapping of E. coli Thioredoxin via 13C NMR Relaxation Analysis
    • LeMaster DM, Kushlan DM, (1996) Dynamical Mapping of E. coli Thioredoxin via 13C NMR Relaxation Analysis. J Am Chem Soc 118: 9255-9264.
    • (1996) J Am Chem Soc , vol.118 , pp. 9255-9264
    • LeMaster, D.M.1    Kushlan, D.M.2
  • 8
    • 3943074512 scopus 로고    scopus 로고
    • Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins
    • Tugarinov V, Hwang PM, Kay LE, (2004) Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins. Annu Rev Biochem 73: 107-146.
    • (2004) Annu Rev Biochem , vol.73 , pp. 107-146
    • Tugarinov, V.1    Hwang, P.M.2    Kay, L.E.3
  • 9
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin K, Riek R, Wider G, Wüthrich K, (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc Natl Acad Sci U S A 94: 12366-12371.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 10
    • 0041930989 scopus 로고    scopus 로고
    • Cross-correlated relaxation enhanced 1H-13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes
    • Tugarinov V, Hwang PM, Ollerenshaw JE, Kay LE, (2003) Cross-correlated relaxation enhanced 1H-13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. J Am Chem Soc 125: 10420-10428.
    • (2003) J Am Chem Soc , vol.125 , pp. 10420-10428
    • Tugarinov, V.1    Hwang, P.M.2    Ollerenshaw, J.E.3    Kay, L.E.4
  • 11
    • 0030824756 scopus 로고    scopus 로고
    • Production and Incorporation of 15N, 13C, 2H (1H-δ1 Methyl) Isoleucine into Proteins for Multidimensional NMR Studies
    • Gardner KH, Kay LE, (1997) Production and Incorporation of 15N, 13C, 2H (1H-δ1 Methyl) Isoleucine into Proteins for Multidimensional NMR Studies. J Am Chem Soc 119: 7599-7600.
    • (1997) J Am Chem Soc , vol.119 , pp. 7599-7600
    • Gardner, K.H.1    Kay, L.E.2
  • 12
    • 0032898682 scopus 로고    scopus 로고
    • A robust and cost-effective method for the production of Val, Leu, Ile (δ1) methyl-protonated 15N-, 13C-, 2H-labeled proteins
    • Goto NK, Gardner KH, Mueller GA, Willis RC, Kay LE, (1999) A robust and cost-effective method for the production of Val, Leu, Ile (δ1) methyl-protonated 15N-, 13C-, 2H-labeled proteins. J Biomol NMR 13: 369-374.
    • (1999) J Biomol NMR , vol.13 , pp. 369-374
    • Goto, N.K.1    Gardner, K.H.2    Mueller, G.A.3    Willis, R.C.4    Kay, L.E.5
  • 13
    • 1242308875 scopus 로고    scopus 로고
    • An isotope labeling strategy for methyl TROSY spectroscopy
    • Tugarinov V, Kay LE, (2004) An isotope labeling strategy for methyl TROSY spectroscopy. J Biomol NMR 28: 165-172.
    • (2004) J Biomol NMR , vol.28 , pp. 165-172
    • Tugarinov, V.1    Kay, L.E.2
  • 14
    • 0242267427 scopus 로고    scopus 로고
    • Methyl TROSY: explanation and experimental verification
    • Ollerenshaw JE, Tugarinov V, Kay LE, (2003) Methyl TROSY: explanation and experimental verification. Magn Reson Chem 41: 843-852.
    • (2003) Magn Reson Chem , vol.41 , pp. 843-852
    • Ollerenshaw, J.E.1    Tugarinov, V.2    Kay, L.E.3
  • 15
    • 22144435546 scopus 로고    scopus 로고
    • The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy
    • Hamel DJ, Dahlquist FW, (2005) The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy. J Am Chem Soc 127: 9676-9677.
    • (2005) J Am Chem Soc , vol.127 , pp. 9676-9677
    • Hamel, D.J.1    Dahlquist, F.W.2
  • 16
    • 36049046667 scopus 로고    scopus 로고
    • Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR
    • Gelis I, Bonvin AMJJ, Keramisanou D, Koukaki M, Gouridis G, et al. (2007) Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR. Cell 131: 756-769.
    • (2007) Cell , vol.131 , pp. 756-769
    • Gelis, I.1    Bonvin, A.M.J.J.2    Keramisanou, D.3    Koukaki, M.4    Gouridis, G.5
  • 17
    • 27944482589 scopus 로고    scopus 로고
    • NMR analyses of the activation of the Arp2/3 complex by neuronal Wiskott-Aldrich syndrome protein
    • Kreishman-Deitrick M, Goley ED, Burdine L, Denison C, Egile C, et al. (2005) NMR analyses of the activation of the Arp2/3 complex by neuronal Wiskott-Aldrich syndrome protein. Biochemistry 44: 15247-15256.
    • (2005) Biochemistry , vol.44 , pp. 15247-15256
    • Kreishman-Deitrick, M.1    Goley, E.D.2    Burdine, L.3    Denison, C.4    Egile, C.5
  • 18
    • 79961085477 scopus 로고    scopus 로고
    • Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR
    • Kato H, van Ingen H, Zhou B-R, Feng H, Bustin M, et al. (2011) Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR. Proc Natl Acad Sci U S A 108: 12283-12288.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 12283-12288
    • Kato, H.1    van Ingen, H.2    Zhou, B.-R.3    Feng, H.4    Bustin, M.5
  • 19
    • 80054722790 scopus 로고    scopus 로고
    • Quaternary dynamics of αB-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus
    • Baldwin AJ, Hilton GR, Lioe H, Bagnéris C, Benesch JLP, et al. (2011) Quaternary dynamics of αB-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus. J Mol Biol 413: 310-320.
    • (2011) J Mol Biol , vol.413 , pp. 310-320
    • Baldwin, A.J.1    Hilton, G.R.2    Lioe, H.3    Bagnéris, C.4    Benesch, J.L.P.5
  • 20
    • 34547399613 scopus 로고    scopus 로고
    • A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase
    • Velyvis A, Yang YR, Schachman HK, Kay LE, (2007) A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase. Proc Natl Acad Sci U S A 104: 8815-8820.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 8815-8820
    • Velyvis, A.1    Yang, Y.R.2    Schachman, H.K.3    Kay, L.E.4
  • 21
    • 37849041010 scopus 로고    scopus 로고
    • A new labeling method for methyl transverse relaxation-optimized spectroscopy NMR spectra of alanine residues
    • Isaacson RL, Simpson PJ, Liu M, Cota E, Zhang X, et al. (2007) A new labeling method for methyl transverse relaxation-optimized spectroscopy NMR spectra of alanine residues. J Am Chem Soc 129: 15428-15429.
    • (2007) J Am Chem Soc , vol.129 , pp. 15428-15429
    • Isaacson, R.L.1    Simpson, P.J.2    Liu, M.3    Cota, E.4    Zhang, X.5
  • 22
    • 28044440088 scopus 로고    scopus 로고
    • Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release
    • Sprangers R, Gribun A, Hwang PM, Houry WA, Kay LE, (2005) Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release. Proc Natl Acad Sci U S A 102: 16678-16683.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 16678-16683
    • Sprangers, R.1    Gribun, A.2    Hwang, P.M.3    Houry, W.A.4    Kay, L.E.5
  • 23
    • 68049142495 scopus 로고    scopus 로고
    • Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies
    • Amero C, Schanda P, Durá MA, Ayala I, Marion D, et al. (2009) Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies. J Am Chem Soc 131: 3448-3449.
    • (2009) J Am Chem Soc , vol.131 , pp. 3448-3449
    • Amero, C.1    Schanda, P.2    Durá, M.A.3    Ayala, I.4    Marion, D.5
  • 24
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • Sprangers R, Kay LE, (2007) Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature 445: 618-622.
    • (2007) Nature , vol.445 , pp. 618-622
    • Sprangers, R.1    Kay, L.E.2
  • 25
    • 77957970501 scopus 로고    scopus 로고
    • The proteasome antechamber maintains substrates in an unfolded state
    • Ruschak AM, Religa TL, Breuer S, Witt S, Kay LE, (2010) The proteasome antechamber maintains substrates in an unfolded state. Nature 467: 868-871.
    • (2010) Nature , vol.467 , pp. 868-871
    • Ruschak, A.M.1    Religa, T.L.2    Breuer, S.3    Witt, S.4    Kay, L.E.5
  • 26
    • 77950497745 scopus 로고    scopus 로고
    • Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR
    • Religa TL, Sprangers R, Kay LE, (2010) Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR. Science 328: 98-102.
    • (2010) Science , vol.328 , pp. 98-102
    • Religa, T.L.1    Sprangers, R.2    Kay, L.E.3
  • 28
    • 58149463865 scopus 로고    scopus 로고
    • An efficient protocol for the complete incorporation of methyl-protonated alanine in perdeuterated protein
    • Ayala I, Sounier R, Usé N, Gans P, Boisbouvier J, (2009) An efficient protocol for the complete incorporation of methyl-protonated alanine in perdeuterated protein. J Biomol NMR 43: 111-119.
    • (2009) J Biomol NMR , vol.43 , pp. 111-119
    • Ayala, I.1    Sounier, R.2    Usé, N.3    Gans, P.4    Boisbouvier, J.5
  • 29
    • 84859406875 scopus 로고    scopus 로고
    • Methionine Scanning as an NMR Tool for Detecting and Analyzing Biomolecular Interaction Surfaces
    • Stoffregen MC, Schwer MM, Renschler FA, Wiesner S, (2012) Methionine Scanning as an NMR Tool for Detecting and Analyzing Biomolecular Interaction Surfaces. Structure 20: 573-581.
    • (2012) Structure , vol.20 , pp. 573-581
    • Stoffregen, M.C.1    Schwer, M.M.2    Renschler, F.A.3    Wiesner, S.4
  • 30
    • 34249023900 scopus 로고    scopus 로고
    • Synthesis of a 13C-methyl-group-labeled methionine precursor as a useful tool for simplifying protein structural analysis by NMR spectroscopy
    • Fischer M, Kloiber K, Häusler J, Ledolter K, Konrat R, et al. (2007) Synthesis of a 13C-methyl-group-labeled methionine precursor as a useful tool for simplifying protein structural analysis by NMR spectroscopy. Chembiochem 8: 610-612.
    • (2007) Chembiochem , vol.8 , pp. 610-612
    • Fischer, M.1    Kloiber, K.2    Häusler, J.3    Ledolter, K.4    Konrat, R.5
  • 31
    • 77949363063 scopus 로고    scopus 로고
    • Stereospecific isotopic labeling of methyl groups for NMR spectroscopic studies of high-molecular-weight proteins
    • Gans P, Hamelin O, Sounier R, Ayala I, Durá MA, et al. (2010) Stereospecific isotopic labeling of methyl groups for NMR spectroscopic studies of high-molecular-weight proteins. Angew Chem Int Ed Engl 49: 1958-1962.
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 1958-1962
    • Gans, P.1    Hamelin, O.2    Sounier, R.3    Ayala, I.4    Durá, M.A.5
  • 32
    • 79958789586 scopus 로고    scopus 로고
    • Site-directed methyl group labeling as an NMR probe of structure and dynamics in supramolecular protein systems: applications to the proteasome and to the ClpP protease
    • Religa TL, Ruschak AM, Rosenzweig R, Kay LE, (2011) Site-directed methyl group labeling as an NMR probe of structure and dynamics in supramolecular protein systems: applications to the proteasome and to the ClpP protease. J Am Chem Soc 133: 9063-9068.
    • (2011) J Am Chem Soc , vol.133 , pp. 9063-9068
    • Religa, T.L.1    Ruschak, A.M.2    Rosenzweig, R.3    Kay, L.E.4
  • 33
    • 0031565915 scopus 로고    scopus 로고
    • A structural census of genomes: comparing bacterial, eukaryotic, and archaeal genomes in terms of protein structure
    • Gerstein M, (1997) A structural census of genomes: comparing bacterial, eukaryotic, and archaeal genomes in terms of protein structure. J Mol Biol 274: 562-576.
    • (1997) J Mol Biol , vol.274 , pp. 562-576
    • Gerstein, M.1
  • 34
    • 81855190757 scopus 로고    scopus 로고
    • Specific labeling of threonine methyl groups for NMR studies of protein-nucleic acid complexes
    • Sinha K, Jen-Jacobson L, Rule GS, (2011) Specific labeling of threonine methyl groups for NMR studies of protein-nucleic acid complexes. Biochemistry 50: 10189-10191.
    • (2011) Biochemistry , vol.50 , pp. 10189-10191
    • Sinha, K.1    Jen-Jacobson, L.2    Rule, G.S.3
  • 35
    • 0023645203 scopus 로고
    • Interior and surface of monomeric proteins
    • Miller S, Janin J, Lesk AM, Chothia C, (1987) Interior and surface of monomeric proteins. J Mol Biol 196: 641-656.
    • (1987) J Mol Biol , vol.196 , pp. 641-656
    • Miller, S.1    Janin, J.2    Lesk, A.M.3    Chothia, C.4
  • 36
    • 0029060166 scopus 로고
    • Proteasome from Thermoplasma acidophilum: a threonine protease
    • Seemüller E, Lupas A, Stock D, Löwe J, Huber R, et al. (1995) Proteasome from Thermoplasma acidophilum: a threonine protease. Science 268: 579-582.
    • (1995) Science , vol.268 , pp. 579-582
    • Seemüller, E.1    Lupas, A.2    Stock, D.3    Löwe, J.4    Huber, R.5
  • 37
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg AL, (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 426: 895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 38
    • 80054984345 scopus 로고    scopus 로고
    • Hydrogen exchange study on the hydroxyl groups of serine and threonine residues in proteins and structure refinement using NOE restraints with polar side-chain groups
    • Takeda M, Jee J, Ono AM, Terauchi T, Kainosho M, (2011) Hydrogen exchange study on the hydroxyl groups of serine and threonine residues in proteins and structure refinement using NOE restraints with polar side-chain groups. J Am Chem Soc 133: 17420-17427.
    • (2011) J Am Chem Soc , vol.133 , pp. 17420-17427
    • Takeda, M.1    Jee, J.2    Ono, A.M.3    Terauchi, T.4    Kainosho, M.5
  • 39
    • 78149412689 scopus 로고    scopus 로고
    • A simple strategy for 13C, 1H labeling at the Ile-γ2 methyl position in highly deuterated proteins
    • Ruschak AM, Velyvis A, Kay LE, (2010) A simple strategy for 13C, 1H labeling at the Ile-γ2 methyl position in highly deuterated proteins. J Biomol NMR 48: 129-135.
    • (2010) J Biomol NMR , vol.48 , pp. 129-135
    • Ruschak, A.M.1    Velyvis, A.2    Kay, L.E.3
  • 40
    • 27644455713 scopus 로고    scopus 로고
    • Comparison of 13CH3, 13CH2D, and 13CHD2 methyl labeling strategies in proteins
    • Ollerenshaw JE, Tugarinov V, Skrynnikov NR, Kay LE, (2005) Comparison of 13CH3, 13CH2D, and 13CHD2 methyl labeling strategies in proteins. J Biomol NMR 33: 25-41.
    • (2005) J Biomol NMR , vol.33 , pp. 25-41
    • Ollerenshaw, J.E.1    Tugarinov, V.2    Skrynnikov, N.R.3    Kay, L.E.4
  • 41
    • 77954717665 scopus 로고    scopus 로고
    • Optimal methyl labeling for studies of supra-molecular systems
    • Religa TL, Kay LE, (2010) Optimal methyl labeling for studies of supra-molecular systems. J Biomol NMR 47: 163-169.
    • (2010) J Biomol NMR , vol.47 , pp. 163-169
    • Religa, T.L.1    Kay, L.E.2
  • 43
    • 41549124663 scopus 로고    scopus 로고
    • Four types of threonine aldolases: Similarities and differences in kinetics/thermodynamics
    • Fesko K, Reisinger C, Steinreiber J, Weber H, Schürmann M, et al. (2008) Four types of threonine aldolases: Similarities and differences in kinetics/thermodynamics. J Mol Catal B Enzym 52-53: 19-26.
    • (2008) J Mol Catal B Enzym , vol.52-53 , pp. 19-26
    • Fesko, K.1    Reisinger, C.2    Steinreiber, J.3    Weber, H.4    Schürmann, M.5
  • 44
    • 0027363658 scopus 로고
    • Threonine formation via the coupled activity of 2-amino-3-ketobutyrate coenzyme A lyase and threonine dehydrogenase
    • Marcus JP, Dekker EE, (1993) Threonine formation via the coupled activity of 2-amino-3-ketobutyrate coenzyme A lyase and threonine dehydrogenase. J Bacteriol 175: 6505-6511.
    • (1993) J Bacteriol , vol.175 , pp. 6505-6511
    • Marcus, J.P.1    Dekker, E.E.2
  • 45
    • 37049053900 scopus 로고
    • 287. alpha-Amino-beta-keto-acids. Part II. Rates of decarboxylation of the free acids and the behaviour of derivatives on titration
    • Laver WG, Neuberger A, Scott JJ, (1959) 287. alpha-Amino-beta-keto-acids. Part II. Rates of decarboxylation of the free acids and the behaviour of derivatives on titration. J Chem Soc 1483.
    • (1959) J Chem Soc , vol.1483
    • Laver, W.G.1    Neuberger, A.2    Scott, J.J.3
  • 46
    • 0027284369 scopus 로고
    • pH-dependent decarboxylation of 2-amino-3-ketobutyrate, the unstable intermediate in the threonine dehydrogenase-initiated pathway for threonine utilization
    • Marcus JP, Dekker EE, (1993) pH-dependent decarboxylation of 2-amino-3-ketobutyrate, the unstable intermediate in the threonine dehydrogenase-initiated pathway for threonine utilization. Biochem Biophys Res Commun 190: 1066-1072.
    • (1993) Biochem Biophys Res Commun , vol.190 , pp. 1066-1072
    • Marcus, J.P.1    Dekker, E.E.2
  • 47
    • 0027247937 scopus 로고
    • Identity and some properties of the L-threonine aldolase activity manifested by pure 2-amino-3-ketobutyrate ligase of Escherichia coli
    • Marcus JP, Dekker EE, (1993) Identity and some properties of the L-threonine aldolase activity manifested by pure 2-amino-3-ketobutyrate ligase of Escherichia coli. Biochim Biophys Acta 1164: 299-304.
    • (1993) Biochim Biophys Acta , vol.1164 , pp. 299-304
    • Marcus, J.P.1    Dekker, E.E.2
  • 48
    • 77950899704 scopus 로고    scopus 로고
    • Expanding metabolism for total biosynthesis of the nonnatural amino acid L-homoalanine
    • Zhang K, Li H, Cho KM, Liao JC, (2010) Expanding metabolism for total biosynthesis of the nonnatural amino acid L-homoalanine. Proc Natl Acad Sci U S A 107: 6234-6239.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 6234-6239
    • Zhang, K.1    Li, H.2    Cho, K.M.3    Liao, J.C.4
  • 49
    • 70349578970 scopus 로고    scopus 로고
    • Tricistronic overexpression of cytochrome P450cam, putidaredoxin, and putidaredoxin reductase provides a useful cell-based catalytic system
    • Kim D, Ortiz de Montellano PR, (2009) Tricistronic overexpression of cytochrome P450cam, putidaredoxin, and putidaredoxin reductase provides a useful cell-based catalytic system. Biotechnol Lett 31: 1427-1431.
    • (2009) Biotechnol Lett , vol.31 , pp. 1427-1431
    • Kim, D.1    Ortiz de Montellano, P.R.2
  • 51
    • 0034624234 scopus 로고    scopus 로고
    • Rational re-design of the substrate binding site of flavocytochrome P450 BM3
    • Ost TW, Miles CS, Murdoch J, Cheung Y, Reid G, et al. (2000) Rational re-design of the substrate binding site of flavocytochrome P450 BM3. FEBS Lett 486: 173-177.
    • (2000) FEBS Lett , vol.486 , pp. 173-177
    • Ost, T.W.1    Miles, C.S.2    Murdoch, J.3    Cheung, Y.4    Reid, G.5
  • 52
    • 0015221782 scopus 로고
    • 2-keto-4-hydroxybutyrate aldolase. Identification as 2-keto-4-hydroxyglutarate aldolase, catalytic properties, and role in the mammalian metabolism of L-homoserine
    • Lane RS, Shapley A, Dekker EE, (1971) 2-keto-4-hydroxybutyrate aldolase. Identification as 2-keto-4-hydroxyglutarate aldolase, catalytic properties, and role in the mammalian metabolism of L-homoserine. Biochemistry 10: 1353-1364.
    • (1971) Biochemistry , vol.10 , pp. 1353-1364
    • Lane, R.S.1    Shapley, A.2    Dekker, E.E.3
  • 53
    • 0026561521 scopus 로고
    • Cloning, nucleotide sequence, overexpression, and inactivation of the Escherichia coli 2-keto-4-hydroxyglutarate aldolase gene
    • Patil RV, Dekker EE, (1992) Cloning, nucleotide sequence, overexpression, and inactivation of the Escherichia coli 2-keto-4-hydroxyglutarate aldolase gene. J Bacteriol 174: 102-107.
    • (1992) J Bacteriol , vol.174 , pp. 102-107
    • Patil, R.V.1    Dekker, E.E.2
  • 55
    • 0030456053 scopus 로고    scopus 로고
    • Substrate specificity and identification of functional groups of homoserine kinase from Escherichia coli
    • Huo X, Viola RE, (1996) Substrate specificity and identification of functional groups of homoserine kinase from Escherichia coli. Biochemistry 35: 16180-16185.
    • (1996) Biochemistry , vol.35 , pp. 16180-16185
    • Huo, X.1    Viola, R.E.2
  • 56
    • 0028218431 scopus 로고
    • Mechanisms of interaction of Escherichia coli threonine synthase with substrates and inhibitors
    • Laber B, Gerbling KP, Harde C, Neff KH, Nordhoff E, et al. (1994) Mechanisms of interaction of Escherichia coli threonine synthase with substrates and inhibitors. Biochemistry 33: 3413-3423.
    • (1994) Biochemistry , vol.33 , pp. 3413-3423
    • Laber, B.1    Gerbling, K.P.2    Harde, C.3    Neff, K.H.4    Nordhoff, E.5
  • 57
    • 33747135959 scopus 로고    scopus 로고
    • Acetohydroxyacid synthase and its role in the biosynthetic pathway for branched-chain amino acids
    • McCourt JA, Duggleby RG, (2006) Acetohydroxyacid synthase and its role in the biosynthetic pathway for branched-chain amino acids. Amino Acids 31: 173-210.
    • (2006) Amino Acids , vol.31 , pp. 173-210
    • McCourt, J.A.1    Duggleby, R.G.2
  • 58
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution
    • Löwe J, Stock D, Jap B, Zwickl P, Baumeister W, et al. (1995) Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. Science 268: 533-539.
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5
  • 59
    • 19444387760 scopus 로고    scopus 로고
    • The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions
    • Förster A, Masters EI, Whitby FG, Robinson H, Hill CP, (2005) The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions. Mol Cell 18: 589-599.
    • (2005) Mol Cell , vol.18 , pp. 589-599
    • Förster, A.1    Masters, E.I.2    Whitby, F.G.3    Robinson, H.4    Hill, C.P.5
  • 60
    • 84555189440 scopus 로고    scopus 로고
    • Regulation and function of the RSK family of protein kinases
    • Romeo Y, Zhang X, Roux PP, (2012) Regulation and function of the RSK family of protein kinases. Biochem J 441: 553-569.
    • (2012) Biochem J , vol.441 , pp. 553-569
    • Romeo, Y.1    Zhang, X.2    Roux, P.P.3
  • 61
    • 80455173859 scopus 로고    scopus 로고
    • 14-3-3 Proteins: diverse functions in cell proliferation and cancer progression
    • Freeman AK, Morrison DK, (2011) 14-3-3 Proteins: diverse functions in cell proliferation and cancer progression. Semin Cell Dev Biol 22: 681-687.
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 681-687
    • Freeman, A.K.1    Morrison, D.K.2
  • 62
    • 80455160346 scopus 로고    scopus 로고
    • 14-3-3 proteins as signaling integration points for cell cycle control and apoptosis
    • Gardino AK, Yaffe MB, (2011) 14-3-3 proteins as signaling integration points for cell cycle control and apoptosis. Semin Cell Dev Biol 22: 688-695.
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 688-695
    • Gardino, A.K.1    Yaffe, M.B.2
  • 63
    • 44049118414 scopus 로고
    • A constant-time 2D overbodenhausen experiment for inverse correlation of isotopically enriched species
    • Santoro J, King GC, (1992) A constant-time 2D overbodenhausen experiment for inverse correlation of isotopically enriched species. J Magn Reson 97: 202-207.
    • (1992) J Magn Reson , vol.97 , pp. 202-207
    • Santoro, J.1    King, G.C.2
  • 64
    • 0001748180 scopus 로고
    • Resolution enhancement and spectral editing of uniformly 13C-enriched proteins by homonuclear broadband 13C decoupling
    • Vuister GW, Bax A, (1992) Resolution enhancement and spectral editing of uniformly 13C-enriched proteins by homonuclear broadband 13C decoupling. J Magn Reson 98: 428-435.
    • (1992) J Magn Reson , vol.98 , pp. 428-435
    • Vuister, G.W.1    Bax, A.2
  • 65
    • 0030093563 scopus 로고    scopus 로고
    • Multisite Band-Selective Decoupling in Proteins
    • Kupce E, Wagner G, (1996) Multisite Band-Selective Decoupling in Proteins. J Magn Reson B 110: 309-312.
    • (1996) J Magn Reson B , vol.110 , pp. 309-312
    • Kupce, E.1    Wagner, G.2


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