메뉴 건너뛰기




Volumn 8, Issue 12, 2013, Pages

Dynamics and flexibility of human aromatase probed by FTIR and time resolved fluorescence spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ANASTROZOLE; ANDROSTENEDIONE; AROMATASE; HISTIDINE;

EID: 84892398454     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0082118     Document Type: Article
Times cited : (29)

References (57)
  • 2
    • 33748802003 scopus 로고    scopus 로고
    • Structural basis for ligand promiscuity in cytochrome P450 3A4
    • Ekroos M, Sjögren T (2006) Structural basis for ligand promiscuity in cytochrome P450 3A4. Proc Natl Acad Sci U S A 103: 13682-13687.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 13682-13687
    • Ekroos, M.1    Sjögren, T.2
  • 3
    • 0345687195 scopus 로고    scopus 로고
    • An open conformation of mammalian cytochrome P450 2B4 at 1.6-A resolution
    • Scott E, He Y, Wester M, White M, Chin C, et al. (2003) An open conformation of mammalian cytochrome P450 2B4 at 1.6-A resolution. Proc Natl Acad Sci U S A 100: 13196-13201.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 13196-13201
    • Scott, E.1    He, Y.2    Wester, M.3    White, M.4    Chin, C.5
  • 4
    • 3042553224 scopus 로고    scopus 로고
    • Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9 Å resolution: Insight into the range of P450 conformations and the coordination of redox partner binding
    • Scott E, White M, He Y, Johnson E, Stout C, et al. (2004) Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9 Å resolution: insight into the range of P450 conformations and the coordination of redox partner binding. J Biol Chem 279: 27294-27301.
    • (2004) J Biol Chem , vol.279 , pp. 27294-27301
    • Scott, E.1    White, M.2    He, Y.3    Johnson, E.4    Stout, C.5
  • 6
    • 0031013972 scopus 로고    scopus 로고
    • The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
    • Li HY, Poulos TL (1997) The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid. Nat Struct Biol 4: 140-146.
    • (1997) Nat Struct Biol , vol.4 , pp. 140-146
    • Li, H.Y.1    Poulos, T.L.2
  • 9
    • 33846958772 scopus 로고    scopus 로고
    • Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3
    • Girvan HM, Seward HE, Toogood HS, Cheesman MR, Leys D, et al. (2007) Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3. J Biol Chem 282: 564-572.
    • (2007) J Biol Chem , vol.282 , pp. 564-572
    • Girvan, H.M.1    Seward, H.E.2    Toogood, H.S.3    Cheesman, M.R.4    Leys, D.5
  • 10
    • 84878747590 scopus 로고    scopus 로고
    • Structural basis for effector control and redox partner recognition in cytochrome P450
    • Tripathi S, Li H, Poulos TL (2013) Structural basis for effector control and redox partner recognition in cytochrome P450. Science 340: 1227-1230.
    • (2013) Science , vol.340 , pp. 1227-1230
    • Tripathi, S.1    Li, H.2    Poulos, T.L.3
  • 11
    • 0016272566 scopus 로고
    • The involvement of human placental microsomal cytochrome P-450 in aromatization
    • Thompson EA Jr, Siiteri PK (1974) The involvement of human placental microsomal cytochrome P-450 in aromatization. J Biol Chem 249: 5373-5378.
    • (1974) J Biol Chem , vol.249 , pp. 5373-5378
    • Thompson Jr., E.A.1    Siiteri, P.K.2
  • 12
    • 0016293443 scopus 로고
    • Utilization of oxygen and reduced nicotinamide adenine dinucleotide phosphate by human placental microsomes during aromatization of androstenedione
    • Thompson EA Jr, Siiteri PK (1974) Utilization of oxygen and reduced nicotinamide adenine dinucleotide phosphate by human placental microsomes during aromatization of androstenedione. J Biol Chem 249: 5364-5372.
    • (1974) J Biol Chem , vol.249 , pp. 5364-5372
    • Thompson Jr., E.A.1    Siiteri, P.K.2
  • 13
    • 0028332035 scopus 로고
    • Aromatase cytochrome P450, the enzyme responsible for estrogen biosynthesis
    • Simpson E, Mahendroo M, Means G, Kilgore M, Hinshelwood M, et al. (1994) Aromatase cytochrome P450, the enzyme responsible for estrogen biosynthesis. Endocr Rev 15: 342-55.
    • (1994) Endocr Rev , vol.15 , pp. 342-355
    • Simpson, E.1    Mahendroo, M.2    Means, G.3    Kilgore, M.4    Hinshelwood, M.5
  • 14
    • 58149339806 scopus 로고    scopus 로고
    • Structural basis for androgen specificity and oestrogen synthesis in human aromatase
    • Ghosh D, Griswold J, Erman M, Pangborn W (2009) Structural basis for androgen specificity and oestrogen synthesis in human aromatase. Nature 457: 219-223.
    • (2009) Nature , vol.457 , pp. 219-223
    • Ghosh, D.1    Griswold, J.2    Erman, M.3    Pangborn, W.4
  • 15
    • 3442896773 scopus 로고    scopus 로고
    • Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone
    • Williams P, Cosme J, Vinkovic D, Ward A, Angove H, et al. (2004) Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone. Science 305: 683-686.
    • (2004) Science , vol.305 , pp. 683-686
    • Williams, P.1    Cosme, J.2    Vinkovic, D.3    Ward, A.4    Angove, H.5
  • 17
    • 84867351811 scopus 로고    scopus 로고
    • Novel aromatase inhibitors by structure-guided design
    • Ghosh D, Lo J, Morton D, Valette D, Xi J, et al. (2012) Novel aromatase inhibitors by structure-guided design. J Med Chem 55: 8464-76.
    • (2012) J Med Chem , vol.55 , pp. 8464-8476
    • Ghosh, D.1    Lo, J.2    Morton, D.3    Valette, D.4    Xi, J.5
  • 18
    • 84857615120 scopus 로고    scopus 로고
    • Motion and flexibility in human cytochrome p450 aromatase
    • Jiang W, Ghosh D (2012) Motion and flexibility in human cytochrome p450 aromatase. Plos One 7: e32565.
    • (2012) Plos One , vol.7
    • Jiang, W.1    Ghosh, D.2
  • 19
    • 77951240144 scopus 로고    scopus 로고
    • Two-dimensional NMR and all-atom molecular dynamics of cytochrome P450 CYP119 reveal hidden conformational substates
    • Lampe JN, Brandman R, Sivaramakrishnan S, Ortiz de Montellano PR (2010) Two-dimensional NMR and all-atom molecular dynamics of cytochrome P450 CYP119 reveal hidden conformational substates. J Biol Chem 285: 9594-9603.
    • (2010) J Biol Chem , vol.285 , pp. 9594-9603
    • Lampe, J.N.1    Brandman, R.2    Sivaramakrishnan, S.3    Ortiz De Montellano, P.R.4
  • 20
    • 57149092138 scopus 로고    scopus 로고
    • Ligand-induced conformational heterogeneity of cytochrome P450 CYP119 identified by 2D NMR spectroscopy with the unnatural amino acid (13)C-p-methoxyphenylalanine
    • Lampe JN, Floor SN, Gross JD, Nishida CR, Jiang Y, et al. (2008) Ligand-induced conformational heterogeneity of cytochrome P450 CYP119 identified by 2D NMR spectroscopy with the unnatural amino acid (13)C-p- methoxyphenylalanine. J Am Chem Soc 130: 16168-16169.
    • (2008) J Am Chem Soc , vol.130 , pp. 16168-16169
    • Lampe, J.N.1    Floor, S.N.2    Gross, J.D.3    Nishida, C.R.4    Jiang, Y.5
  • 21
    • 32344450546 scopus 로고    scopus 로고
    • NMR studies of ligand binding to P450(eryF) provides insight into the mechanism of cooperativity
    • Roberts AG, Diaz MD, Lampe JN, Shireman LM, Grinstead JS, et al. (2006) NMR studies of ligand binding to P450(eryF) provides insight into the mechanism of cooperativity. Biochemistry 45: 1673-1684.
    • (2006) Biochemistry , vol.45 , pp. 1673-1684
    • Roberts, A.G.1    Diaz, M.D.2    Lampe, J.N.3    Shireman, L.M.4    Grinstead, J.S.5
  • 22
    • 7444264562 scopus 로고    scopus 로고
    • Conformational states of cytochrome P450cam revealed by trapping of synthetic molecular wires
    • Hays AM, Dunn AR, Chiu R, Gray HB, Stout CD, et al. (2004) Conformational states of cytochrome P450cam revealed by trapping of synthetic molecular wires. J Mol Biol 344: 455-469.
    • (2004) J Mol Biol , vol.344 , pp. 455-469
    • Hays, A.M.1    Dunn, A.R.2    Chiu, R.3    Gray, H.B.4    Stout, C.D.5
  • 23
    • 33646942269 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of ligand binding by cytochrome P450 3A4
    • Isin EM, Guengerich FP (2006) Kinetics and thermodynamics of ligand binding by cytochrome P450 3A4. J Biol Chem 281: 9127-9136.
    • (2006) J Biol Chem , vol.281 , pp. 9127-9136
    • Isin, E.M.1    Guengerich, F.P.2
  • 24
    • 33646357912 scopus 로고    scopus 로고
    • Conformational flexibility of mammalian cytochrome P450 2B4 in binding imidazole inhibitors with different ring chemistry and side chains. Solution thermodynamics and molecular modeling
    • Muralidhara BK, Negi S, Chin CC, Braun W, Halpert JR (2006) Conformational flexibility of mammalian cytochrome P450 2B4 in binding imidazole inhibitors with different ring chemistry and side chains. Solution thermodynamics and molecular modeling. J Biol Chem 281: 8051-8061.
    • (2006) J Biol Chem , vol.281 , pp. 8051-8061
    • Muralidhara, B.K.1    Negi, S.2    Chin, C.C.3    Braun, W.4    Halpert, J.R.5
  • 25
    • 0034077708 scopus 로고    scopus 로고
    • Flexibility and stability of the structure of cytochromes P450 3A4 and BM-3
    • Anzenbacherová E, Bec N, Anzenbacher P, Hudecek J, Soucek P, et al. (2000) Flexibility and stability of the structure of cytochromes P450 3A4 and BM-3. Eur J Biochem 267: 2916-2920.
    • (2000) Eur J Biochem , vol.267 , pp. 2916-2920
    • Anzenbacherová, E.1    Bec, N.2    Anzenbacher, P.3    Hudecek, J.4    Soucek, P.5
  • 26
    • 0035893819 scopus 로고    scopus 로고
    • Differences in flexibility of active sites of cytochromes P450 probed by resonance Raman and UV-Vis absorption spectroscopy
    • Anzenbacher P, Hudecek J (2001) Differences in flexibility of active sites of cytochromes P450 probed by resonance Raman and UV-Vis absorption spectroscopy. J Inorg Biochem 87: 209-213.
    • (2001) J Inorg Biochem , vol.87 , pp. 209-213
    • Anzenbacher, P.1    Hudecek, J.2
  • 27
    • 78649672754 scopus 로고    scopus 로고
    • Plasticity of cytochrome P450 2B4 as investigated by hydrogen-deuterium exchange mass spectrometry and X-ray crystallography
    • Wilderman PR, Shah MB, Liu T, Li S, Hsu S, et al. (2010) Plasticity of cytochrome P450 2B4 as investigated by hydrogen-deuterium exchange mass spectrometry and X-ray crystallography. J Biol Chem 285: 38602-38611.
    • (2010) J Biol Chem , vol.285 , pp. 38602-38611
    • Wilderman, P.R.1    Shah, M.B.2    Liu, T.3    Li, S.4    Hsu, S.5
  • 28
    • 66049156166 scopus 로고    scopus 로고
    • Steroid and protein ligand binding to cytochrome P450 46A1 as assessed by hydrogen-deuterium exchange and mass spectrometry
    • Liao WL, Dodder NG, Mast N, Pikuleva IA, Turko IV (2009) Steroid and protein ligand binding to cytochrome P450 46A1 as assessed by hydrogen-deuterium exchange and mass spectrometry. Biochemistry 48: 4150-4158.
    • (2009) Biochemistry , vol.48 , pp. 4150-4158
    • Liao, W.L.1    Dodder, N.G.2    Mast, N.3    Pikuleva, I.A.4    Turko, I.V.5
  • 29
    • 38149066135 scopus 로고    scopus 로고
    • Hydrogen-deuterium exchange mass spectrometry for investigation of backbone dynamics of oxidized and reduced cytochrome P450cam
    • Hamuro Y, Molnar KS, Coales SJ, OuYang B, Simorellis AK, et al. (2007) Hydrogen-deuterium exchange mass spectrometry for investigation of backbone dynamics of oxidized and reduced cytochrome P450cam. J Inorg Biochem 102: 364-370.
    • (2007) J Inorg Biochem , vol.102 , pp. 364-370
    • Hamuro, Y.1    Molnar, K.S.2    Coales, S.J.3    OuYang, B.4    Simorellis, A.K.5
  • 31
    • 0028986596 scopus 로고
    • CO binding kinetics of human cytochrome P450 3A4. Specific interaction of substrates with kinetically distinguishable conformers
    • 1995
    • Koley AP, Buters JT, Robinson RC, Markowitz A, Friedman FK (1995) CO binding kinetics of human cytochrome P450 3A4. Specific interaction of substrates with kinetically distinguishable conformers. J Biol Chem 1995 270: 5014-5018.
    • (1995) J Biol Chem , vol.270 , pp. 5014-5018
    • Koley, A.P.1    Buters, J.T.2    Robinson, R.C.3    Markowitz, A.4    Friedman, F.K.5
  • 32
    • 33646588326 scopus 로고    scopus 로고
    • Conformational equilibrium of cytochrome P450 BM-3 complexed with N-palmitoylglycine: A replica exchange molecular dynamics study
    • Ravindranathan KP, Gallicchio E, Friesner RA, McDermott AE, Levy RM (2006) Conformational equilibrium of cytochrome P450 BM-3 complexed with N-palmitoylglycine: a replica exchange molecular dynamics study. J Am Chem Soc 128: 5786-5791.
    • (2006) J Am Chem Soc , vol.128 , pp. 5786-5791
    • Ravindranathan, K.P.1    Gallicchio, E.2    Friesner, R.A.3    McDermott, A.E.4    Levy, R.M.5
  • 33
    • 84858987423 scopus 로고    scopus 로고
    • Binding of quinidine radically increases the stability and decreases the flexibility of the cytochrome P450 2D6 active site
    • Berka K, Anzenbacherová E, Hendrychová T, Lange R, Mašek V, et al. (2012) Binding of quinidine radically increases the stability and decreases the flexibility of the cytochrome P450 2D6 active site. J Inorg Biochem 110: 46-50.
    • (2012) J Inorg Biochem , vol.110 , pp. 46-50
    • Berka, K.1    Anzenbacherová, E.2    Hendrychová, T.3    Lange, R.4    Mašek, V.5
  • 34
    • 80052944899 scopus 로고    scopus 로고
    • Direct spectroscopic evidence for binding of anastrozole to the iron heme of human aromatase. Peering into the mechanism of aromatase inhibition
    • Maurelli S, Chiesa M, Giamello E, Di Nardo G, Ferrero VEV, et al. (2011) Direct spectroscopic evidence for binding of anastrozole to the iron heme of human aromatase. Peering into the mechanism of aromatase inhibition. Chem Comm 47: 10737-10739.
    • (2011) Chem Comm , vol.47 , pp. 10737-10739
    • Maurelli, S.1    Chiesa, M.2    Giamello, E.3    Di Nardo, G.4    Ferrero, V.E.V.5
  • 35
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth A, Zscherp C (2002) What vibrations tell us about proteins. Q Rev Biophys 35: 369-430.
    • (2002) Q Rev Biophys , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 36
    • 33846619697 scopus 로고    scopus 로고
    • Molecular basis for the aromatization reaction and exemestane-mediated irreversible inhibition of human aromatase
    • Hong Y, Yu B, Sherman M, Yuan Y, Zhou D, et al. (2007) Molecular basis for the aromatization reaction and exemestane-mediated irreversible inhibition of human aromatase. Mol Endocrinol 21: 401-414.
    • (2007) Mol Endocrinol , vol.21 , pp. 401-414
    • Hong, Y.1    Yu, B.2    Sherman, M.3    Yuan, Y.4    Zhou, D.5
  • 37
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I: Evidence for its hemoprotein nature
    • Omura T, Sato R (1964) The carbon monoxide-binding pigment of liver microsomes. I: evidence for its hemoprotein nature. J Biol Chem 239: 2370-2378.
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 38
    • 0026341320 scopus 로고
    • Assay of aromatase activity
    • Lephart E, Simpson E (1991) Assay of aromatase activity. Methods Enzymol 206: 477-483.
    • (1991) Methods Enzymol , vol.206 , pp. 477-483
    • Lephart, E.1    Simpson, E.2
  • 39
    • 0036829928 scopus 로고    scopus 로고
    • Expression and purification of a recombinant form of human aromatase from Escherichia coli
    • Zhang F, Zhou D, Kao YC, Ye J, Chen S (2002) Expression and purification of a recombinant form of human aromatase from Escherichia coli . Biochem Pharmacol 64: 1317-24.
    • (2002) Biochem Pharmacol , vol.64 , pp. 1317-1324
    • Zhang, F.1    Zhou, D.2    Kao, Y.C.3    Ye, J.4    Chen, S.5
  • 40
    • 2942595904 scopus 로고    scopus 로고
    • Characterization of stable human aromatase expressed in E. coli
    • Kagawa N, Hori H, Waterman MR, Yoshioka S (2004) Characterization of stable human aromatase expressed in E. coli. Steroids 69: 235-243.
    • (2004) Steroids , vol.69 , pp. 235-243
    • Kagawa, N.1    Hori, H.2    Waterman, M.R.3    Yoshioka, S.4
  • 41
    • 77952941507 scopus 로고    scopus 로고
    • Kinetic analysis of the three-step steroid aromatase reaction of human cytochrome P450 19A1
    • Sohl CD, Guengerich FP (2010) Kinetic analysis of the three-step steroid aromatase reaction of human cytochrome P450 19A1. J Biol Chem 285: 17734-17743.
    • (2010) J Biol Chem , vol.285 , pp. 17734-17743
    • Sohl, C.D.1    Guengerich, F.P.2
  • 42
    • 79952471723 scopus 로고    scopus 로고
    • Efficient expression of human aromatase (CYP19) in E. coli
    • Kagawa N (2011) Efficient expression of human aromatase (CYP19) in E. coli. Methods Mol Biol 705: 109-122.
    • (2011) Methods Mol Biol , vol.705 , pp. 109-122
    • Kagawa, N.1
  • 43
    • 84883210549 scopus 로고    scopus 로고
    • Structural basis for the functional roles of critical residues in human cytochrome P450 aromatase
    • Lo J, Di Nardo G, Griswold J, Egbuta C, Jiang W, et al. (2013) Structural basis for the functional roles of critical residues in human cytochrome P450 aromatase. Biochemistry 52: 5821-9.
    • (2013) Biochemistry , vol.52 , pp. 5821-5829
    • Lo, J.1    Di Nardo, G.2    Griswold, J.3    Egbuta, C.4    Jiang, W.5
  • 44
    • 35548933849 scopus 로고    scopus 로고
    • Rational engineering of human cytochrome P450 2B6 for enhanced expression and stability: Importance of a Leu264-. Phe substitution
    • Kumar S, Zhao Y, Sun L, Negi SS, Halpert JR, et al. (2007) Rational engineering of human cytochrome P450 2B6 for enhanced expression and stability: importance of a Leu264-. Phe substitution. Mol Pharmacol 72: 1191-1199.
    • (2007) Mol Pharmacol , vol.72 , pp. 1191-1199
    • Kumar, S.1    Zhao, Y.2    Sun, L.3    Negi, S.S.4    Halpert, J.R.5
  • 45
    • 33845644211 scopus 로고    scopus 로고
    • Engineering mammalian cytochrome P4502B1 by directed evolution for enhanced catalytic tolerance to temperature and dimethyl sulfoxide
    • Kumar S, Sun L, Liu H, Muralidhara BK, Halpert JR (2006) Engineering mammalian cytochrome P4502B1 by directed evolution for enhanced catalytic tolerance to temperature and dimethyl sulfoxide. Prot Eng Des Sel 19: 547-554.
    • (2006) Prot Eng des Sel , vol.19 , pp. 547-554
    • Kumar, S.1    Sun, L.2    Liu, H.3    Muralidhara, B.K.4    Halpert, J.R.5
  • 46
    • 0014059179 scopus 로고
    • Spectral studies of drug interaction with hepatic microsomal cytochrome
    • Schenkman JB, Remmer H, Estabrook RW (1967) Spectral studies of drug interaction with hepatic microsomal cytochrome. Mol Pharmacol 3: 113-23.
    • (1967) Mol Pharmacol , vol.3 , pp. 113-123
    • Schenkman, J.B.1    Remmer, H.2    Estabrook, R.W.3
  • 47
    • 0032584259 scopus 로고    scopus 로고
    • Step-scan time-resolved FTIR spectroscopy of cytochrome P-450(cam) carbon monoxide complex: A salt link involved in the ligand-rebinding process
    • Contzen J, Jung C (1998) Step-scan time-resolved FTIR spectroscopy of cytochrome P-450(cam) carbon monoxide complex: A salt link involved in the ligand-rebinding process. Biochemistry 37: 4317-4324.
    • (1998) Biochemistry , vol.37 , pp. 4317-4324
    • Contzen, J.1    Jung, C.2
  • 48
    • 0033667559 scopus 로고    scopus 로고
    • Insight into protein structure and protein-ligand recognition by Fourier transform infrared spectroscopy
    • Jung C (2000) Insight into protein structure and protein-ligand recognition by Fourier transform infrared spectroscopy. J Mol Recognit 13: 325-351.
    • (2000) J Mol Recognit , vol.13 , pp. 325-351
    • Jung, C.1
  • 49
    • 54949084248 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy as a tool to study structural properties of cytochromes P450 (CYPs)
    • Jung C (2008) Fourier transform infrared spectroscopy as a tool to study structural properties of cytochromes P450 (CYPs). Anal Bioanal Chem 392: 1031-1058.
    • (2008) Anal Bioanal Chem , vol.392 , pp. 1031-1058
    • Jung, C.1
  • 50
    • 0037188392 scopus 로고    scopus 로고
    • Ligand-induced conformational and structural dynamics changes in Escherichia coli cyclic AMP receptor protein
    • Dong A, Malecki JM, Lee L, Carpenter JF, Lee JC (2002) Ligand-induced conformational and structural dynamics changes in Escherichia coli cyclic AMP receptor protein. Biochemistry 41: 6660-6667.
    • (2002) Biochemistry , vol.41 , pp. 6660-6667
    • Dong, A.1    Malecki, J.M.2    Lee, L.3    Carpenter, J.F.4    Lee, J.C.5
  • 51
    • 33845999953 scopus 로고    scopus 로고
    • Dissecting the mechanism of Epac activation via hydrogen-deuterium exchange FT-IR and structural modeling
    • Yu S, Fan F, Flores FC, Mei F, Cheng X (2006) Dissecting the mechanism of Epac activation via hydrogen-deuterium exchange FT-IR and structural modeling. Biochemistry 45: 15318-15326.
    • (2006) Biochemistry , vol.45 , pp. 15318-15326
    • Yu, S.1    Fan, F.2    Flores, F.C.3    Mei, F.4    Cheng, X.5
  • 52
    • 0027504749 scopus 로고
    • Hydrogen exchange identifies native-state motional domains important in protein folding
    • Kim KS, Fuchs JA, Woodward CK (1993) Hydrogen exchange identifies native-state motional domains important in protein folding. Biochemistry 32: 9600-9608.
    • (1993) Biochemistry , vol.32 , pp. 9600-9608
    • Kim, K.S.1    Fuchs, J.A.2    Woodward, C.K.3
  • 53
    • 0028949949 scopus 로고
    • Tertiary stability of native and methionine-80 modified cytochrome c detected by proton-deuterium exchange using on-line Fourier transform infrared spectroscopy
    • de Jongh HH, Goormaghtigh E, Ruysschaert JM (1995) Tertiary stability of native and methionine-80 modified cytochrome c detected by proton-deuterium exchange using on-line Fourier transform infrared spectroscopy. Biochemistry 34: 172-179.
    • (1995) Biochemistry , vol.34 , pp. 172-179
    • De Jongh, H.H.1    Goormaghtigh, E.2    Ruysschaert, J.M.3
  • 54
    • 0037126711 scopus 로고    scopus 로고
    • Structure and dynamics of the modular halves of Escherichia coli cyclic AMP receptor protein
    • Li J, Cheng X, Lee JC (2002) Structure and dynamics of the modular halves of Escherichia coli cyclic AMP receptor protein. Biochemistry 41: 14771-14778.
    • (2002) Biochemistry , vol.41 , pp. 14771-14778
    • Li, J.1    Cheng, X.2    Lee, J.C.3
  • 55
    • 0028345259 scopus 로고
    • A unique environment of Trp48 in Pseudomonas aeruginosa azurin as probed by site-directed mutagenesis and dynamic fluorescence spectroscopy
    • Gilardi G, Mei G, Rosato N, Canters GW, Finazzi-Agrò (1994) A unique environment of Trp48 in Pseudomonas aeruginosa azurin as probed by site-directed mutagenesis and dynamic fluorescence spectroscopy. Biochemistry 33: 1425-1432.
    • (1994) Biochemistry , vol.33 , pp. 1425-1432
    • Gilardi, G.1    Mei, G.2    Rosato, N.3    Canters, G.W.4    Finazzi-Agrò5
  • 56
    • 0344824425 scopus 로고    scopus 로고
    • Cytochrome P450 flexibility
    • Poulos TL (2003) Cytochrome P450 flexibility. Proc Natl Acad Sci USA 100: 13121-13122.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13121-13122
    • Poulos, T.L.1
  • 57
    • 84874042214 scopus 로고    scopus 로고
    • Human aromatase: Perspectives in biochemistry and biotechnology
    • Di Nardo G, Gilardi G (2013) Human aromatase: perspectives in biochemistry and biotechnology Biotechnol Appl Biochem 60: 92-101.
    • (2013) Biotechnol Appl Biochem , vol.60 , pp. 92-101
    • Di Nardo, G.1    Gilardi, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.