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Volumn 312, Issue 1, 2003, Pages 65-74

Early years of cytochrome P450 research in Berlin-Buch: Its present state and origin of the biochemical and biophysical conferences

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450; HEMOPROTEIN; METHEMOGLOBIN; NITRO DERIVATIVE;

EID: 0345257928     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.09.238     Document Type: Article
Times cited : (7)

References (77)
  • 1
    • 34250951164 scopus 로고
    • Die beschleunigung der evipanoxydation und der demethylierung von methylaminoantipyrin durch barbiturate
    • Remmer H. Die beschleunigung der evipanoxydation und der demethylierung von methylaminoantipyrin durch barbiturate. Naunyn-Schmiedeberg's Arch. Exp. Pathol. Pharmakol. 237:1959;296-307.
    • (1959) Naunyn-Schmiedeberg's Arch. Exp. Pathol. Pharmakol. , vol.237 , pp. 296-307
    • Remmer, H.1
  • 2
    • 0344411629 scopus 로고
    • Reduced sensitivity to some drugs 48 h after chlorpromazine treatment
    • Kato R. Reduced sensitivity to some drugs 48. h after chlorpromazine treatment Experientia. 16:1960;427.
    • (1960) Experientia , vol.16 , pp. 427
    • Kato, R.1
  • 3
    • 0002753650 scopus 로고
    • Adaptive increases in drug-metabolizing enzymes induced by phenobarbital and other drugs
    • Conney A.H., Davidson C., Gastel R., Burns J.J. Adaptive increases in drug-metabolizing enzymes induced by phenobarbital and other drugs. J. Pharmacol. Exp. Ther. 130:1960;1-8.
    • (1960) J. Pharmacol. Exp. Ther. , vol.130 , pp. 1-8
    • Conney, A.H.1    Davidson, C.2    Gastel, R.3    Burns, J.J.4
  • 4
    • 0013799479 scopus 로고
    • Substrate-induced synthesis of the hydroxylating enzyme system of liver microsomes
    • Ernster L., Orrenius S. Substrate-induced synthesis of the hydroxylating enzyme system of liver microsomes. Fed. Proc. 24:1965;1190-1199.
    • (1965) Fed. Proc. , vol.24 , pp. 1190-1199
    • Ernster, L.1    Orrenius, S.2
  • 5
    • 0025226098 scopus 로고
    • Pharmacogenetics: Past and future
    • Kalow W. Pharmacogenetics: past and future. Life Sci. 47:1990;1385-1397.
    • (1990) Life Sci. , vol.47 , pp. 1385-1397
    • Kalow, W.1
  • 6
    • 0001600913 scopus 로고
    • Lichtabsorption und paramagnetische Suszeptibilität bei Derivaten des Pferde- und Chironomus-Methämoglobins sowie des Pferde-Metmyoglobins
    • Scheler W., Schoffa G., Jung F. Lichtabsorption und paramagnetische Suszeptibilität bei Derivaten des Pferde- und Chironomus- Methämoglobins sowie des Pferde-Metmyoglobins. Biochem. Z. 329:1957;232-246.
    • (1957) Biochem. Z. , vol.329 , pp. 232-246
    • Scheler, W.1    Schoffa, G.2    Jung, F.3
  • 7
    • 85012357549 scopus 로고
    • Über die Beziehungen zwischen magnetischen, optischen und chemischen Eigenschaften von Hämoglobinderivaten
    • Havemann R., Haberditzl W. Über die Beziehungen zwischen magnetischen, optischen und chemischen Eigenschaften von Hä moglobinderivaten. Z. Physiol. Chem. 209:1958;135-161.
    • (1958) Z. Physiol. Chem. , vol.209 , pp. 135-161
    • Havemann, R.1    Haberditzl, W.2
  • 8
    • 0344843239 scopus 로고
    • Über den Nachweis von zwei magnetischen Formen bei einigen Methämoglobinkomplexen
    • Rein H., Ristau O. Über den Nachweis von zwei magnetischen Formen bei einigen Methämoglobinkomplexen. Naturwissenschaften. 51:1964;480.
    • (1964) Naturwissenschaften , vol.51 , pp. 480
    • Rein, H.1    Ristau, O.2
  • 9
    • 0015242034 scopus 로고
    • Interaction of hemoglobin with ions; Allosteric effects of the binding of anions
    • Ruckpaul K., Rein H., Ristau O., Jänig G.-R., Jung F. Interaction of hemoglobin with ions; allosteric effects of the binding of anions. Biochim. Biophys. Acta. 236:1971;211-221.
    • (1971) Biochim. Biophys. Acta , vol.236 , pp. 211-221
    • Ruckpaul, K.1    Rein, H.2    Ristau, O.3    Jänig, G.-R.4    Jung, F.5
  • 10
    • 0015298959 scopus 로고
    • Kinetik der Dissoziation von Alkylisocyanidkomplexen monomerer und oligomerer Hämoglobine
    • Blanck J., Ruckpaul K., Scheler W., Jung F. Kinetik der Dissoziation von Alkylisocyanidkomplexen monomerer und oligomerer Hämoglobine. Eur. J. Biochem. 25:1972;476-482.
    • (1972) Eur. J. Biochem. , vol.25 , pp. 476-482
    • Blanck, J.1    Ruckpaul, K.2    Scheler, W.3    Jung, F.4
  • 12
    • 0014670327 scopus 로고
    • Resolution of the cytochrome P-450 containing ω-hydroxylation system of liver microsomes into three components
    • Lu A.Y.H., Junk K.W., Coon M.J. Resolution of the cytochrome P-450 containing ω-hydroxylation system of liver microsomes into three components. J. Biol. Chem. 244:1969;3714-3721.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3714-3721
    • Lu, A.Y.H.1    Junk, K.W.2    Coon, M.J.3
  • 13
    • 0014678449 scopus 로고
    • Hydroxylation of benzphetamine and other drugs by a solubilized form of cytochrome P-450 from liver microsomes: Lipid requirement for drug demethylation
    • Lu A.Y.H., Strobel H.W., Coon M.J. Hydroxylation of benzphetamine and other drugs by a solubilized form of cytochrome P-450 from liver microsomes: lipid requirement for drug demethylation. Biochem. Biophys. Res. Commun. 36:1969;545-551.
    • (1969) Biochem. Biophys. Res. Commun. , vol.36 , pp. 545-551
    • Lu, A.Y.H.1    Strobel, H.W.2    Coon, M.J.3
  • 14
    • 0012538590 scopus 로고
    • Complete amino acid sequence and predicted membrane topology of phenobarbital-induced cytochrome P-450 (isozyme 2) from rabbit liver microsomes
    • Tarr G.E., Black S.D., Fujita V.S., Coon M.J. Complete amino acid sequence and predicted membrane topology of phenobarbital-induced cytochrome P-450 (isozyme 2) from rabbit liver microsomes. Proc. Natl. Acad. Sci. USA. 80:1983;6552-6556.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6552-6556
    • Tarr, G.E.1    Black, S.D.2    Fujita, V.S.3    Coon, M.J.4
  • 15
    • 0014601945 scopus 로고
    • Elektronenspinresonanz Untersuchungen an Hämin-Mecaptan-Komplexen (Electron spin resonance investigation of hemin-mercaptan-complexes)
    • Röder A., Bayer E. Elektronenspinresonanz Untersuchungen an Hämin-Mecaptan-Komplexen (Electron spin resonance investigation of hemin-mercaptan-complexes). Eur. J. Biochem. 11:1969;89-92.
    • (1969) Eur. J. Biochem. , vol.11 , pp. 89-92
    • Röder, A.1    Bayer, E.2
  • 18
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P450cam
    • Poulos T.L., Barry C.F., Howard A.J. High-resolution crystal structure of cytochrome P450cam. J. Mol. Biol. 195:1987;687-700.
    • (1987) J. Mol. Biol. , vol.195 , pp. 687-700
    • Poulos, T.L.1    Barry, C.F.2    Howard, A.J.3
  • 20
    • 0018687198 scopus 로고
    • Infrared spectral studies of carbon monoxide complexes of microsomal cytochromes P450 and P448
    • Böhm S., Rein H., Butschak G., Scheunig G., Billwitz H., Ruckpaul K. Infrared spectral studies of carbon monoxide complexes of microsomal cytochromes P450 and P448. Acta Biol. Med. Germ. 38:1979;249-255.
    • (1979) Acta Biol. Med. Germ. , vol.38 , pp. 249-255
    • Böhm, S.1    Rein, H.2    Butschak, G.3    Scheunig, G.4    Billwitz, H.5    Ruckpaul, K.6
  • 22
    • 85030945671 scopus 로고    scopus 로고
    • C. Jung, Quantenchemische Berechnungen der Kohlenmonoxid- und Sauerstoffkomplexe des Zytochrome P450: Ein Beitrag zum Verständnis der spektralen Eigenschaften und der Sauerstoffaktivierung durch Zytochrom P450, PhD thesis, Academy of Sciences of the GDR, Berlin, 1980
    • C. Jung, Quantenchemische Berechnungen der Kohlenmonoxid- und Sauerstoffkomplexe des Zytochrome P450: Ein Beitrag zum Verständnis der spektralen Eigenschaften und der Sauerstoffaktivierung durch Zytochrom P450, PhD thesis, Academy of Sciences of the GDR, Berlin, 1980.
  • 23
    • 0342446136 scopus 로고
    • Biophysical properties of cytochrome P450, analysis of the reactions mechanism - Thermodynamic aspects
    • K. Ruckpaul, & H. Rein. Berlin: Akademie-Verlag
    • Rein H., Jung C., Ristau O., Friedrich J. Biophysical properties of cytochrome P450, analysis of the reactions mechanism - thermodynamic aspects. Ruckpaul K., Rein H. Cytochrome P450, Structural and Functional Relationships. 1984;163-249 Akademie-Verlag, Berlin.
    • (1984) Cytochrome P450, Structural and Functional Relationships , pp. 163-249
    • Rein, H.1    Jung, C.2    Ristau, O.3    Friedrich, J.4
  • 25
    • 0345706242 scopus 로고
    • Evidence of the existence of a high spin low spin equilibrium in liver microsomal cytochrome P450 and its role in the enzymatic mechanism
    • Rein H., Ristau O., Friedrich J., Jänig G.R., Ruckpaul K. Evidence of the existence of a high spin low spin equilibrium in liver microsomal cytochrome P450 and its role in the enzymatic mechanism. Croatica Chem. Acta. 49:1977;251-261.
    • (1977) Croatica Chem. Acta , vol.49 , pp. 251-261
    • Rein, H.1    Ristau, O.2    Friedrich, J.3    Jänig, G.R.4    Ruckpaul, K.5
  • 26
    • 0017170343 scopus 로고
    • Coupling of spin, substrate and redox equlibria in cytochrome P450
    • Sligar S.G. Coupling of spin, substrate and redox equlibria in cytochrome P450. Biochemistry. 15:1976;5399-5406.
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 27
    • 0018073645 scopus 로고
    • Quantitative analysis of the spin equilibrium of cytochrome P450 LM2 fraction from rabbit liver microsomes
    • Ristau O., Rein H., Jänig G.R., Ruckpaul K. Quantitative analysis of the spin equilibrium of cytochrome P450 LM2 fraction from rabbit liver microsomes. Biochim. Biophys. Acta. 536:1978;226-234.
    • (1978) Biochim. Biophys. Acta , vol.536 , pp. 226-234
    • Ristau, O.1    Rein, H.2    Jänig, G.R.3    Ruckpaul, K.4
  • 28
    • 0018629087 scopus 로고
    • The importance of the spin equilibrium in cytochrome P450 for the reduction rate of the heme iron
    • Rein H., Ristau O., Misselwitz R., Buder E., Ruckpaul K. The importance of the spin equilibrium in cytochrome P450 for the reduction rate of the heme iron. Acta Biol. Med. Germ. 38:1979;187-200.
    • (1979) Acta Biol. Med. Germ. , vol.38 , pp. 187-200
    • Rein, H.1    Ristau, O.2    Misselwitz, R.3    Buder, E.4    Ruckpaul, K.5
  • 29
    • 0020529118 scopus 로고
    • Correlations between spin equilibrium shift, reduction rate and N-demethylation activity in liver microsomal P450 and a series of benzphetamine analogues as substrates
    • Blanck J., Rein H., Sommer M., Ristau O., Smettan G., Ruckpaul K. Correlations between spin equilibrium shift, reduction rate and N-demethylation activity in liver microsomal P450 and a series of benzphetamine analogues as substrates. Biochem. Pharmacol. 32:1983;1683-1688.
    • (1983) Biochem. Pharmacol. , vol.32 , pp. 1683-1688
    • Blanck, J.1    Rein, H.2    Sommer, M.3    Ristau, O.4    Smettan, G.5    Ruckpaul, K.6
  • 30
  • 31
    • 0021189625 scopus 로고
    • Motional dynamics of a spin-labeled substrate bound to cytochrome P450 - Saturation transfer EPR studies
    • Schwarz D., Pirrwitz J., Rein H., Ruckpaul K. Motional dynamics of a spin-labeled substrate bound to cytochrome P450 - saturation transfer EPR studies. Biomed. Biochim. Acta. 43:1984;295-307.
    • (1984) Biomed. Biochim. Acta , vol.43 , pp. 295-307
    • Schwarz, D.1    Pirrwitz, J.2    Rein, H.3    Ruckpaul, K.4
  • 32
    • 0024213503 scopus 로고
    • A simple determination of the sideness of the NH2-terminus in the membrane-bound cytochrome P450 LM2
    • Bernhardt R., Kraft R., Ruckpaul K. A simple determination of the sideness of the NH2-terminus in the membrane-bound cytochrome P450 LM2. Biochem. Int. 17:1988;1143-1150.
    • (1988) Biochem. Int. , vol.17 , pp. 1143-1150
    • Bernhardt, R.1    Kraft, R.2    Ruckpaul, K.3
  • 33
    • 0023695280 scopus 로고
    • Electrostatic interactions between cytochrome P-450 LM2 and NADPH-cytochrome P450 reductase
    • Bernhardt R., Kraft R., Otto A., Ruckpaul K. Electrostatic interactions between cytochrome P-450 LM2 and NADPH-cytochrome P450 reductase. Biomed. Biochim. Acta. 47:1988;581-592.
    • (1988) Biomed. Biochim. Acta , vol.47 , pp. 581-592
    • Bernhardt, R.1    Kraft, R.2    Otto, A.3    Ruckpaul, K.4
  • 34
    • 0023659222 scopus 로고
    • Chemical modification of cytochrome P-450 LM4. Identification of functionally linked tyrosine residues
    • Jänig G.-R., Kraft R., Blanck J., Ristau O., Rabe H., Ruckpaul K. Chemical modification of cytochrome P-450 LM4. Identification of functionally linked tyrosine residues. Biochim. Biophys. Acta. 916:1987;512-5123.
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 512-5123
    • Jänig, G.-R.1    Kraft, R.2    Blanck, J.3    Ristau, O.4    Rabe, H.5    Ruckpaul, K.6
  • 36
    • 0028794689 scopus 로고
    • Cytochrome P450: Structure, function and generation of reactive oxygen species
    • Bernhardt R. Cytochrome P450: structure, function and generation of reactive oxygen species. Rev. Physiol. Biochem. Pharmacol. 127:1995;137-221.
    • (1995) Rev. Physiol. Biochem. Pharmacol. , vol.127 , pp. 137-221
    • Bernhardt, R.1
  • 37
    • 0026569583 scopus 로고
    • Membrane topology of the mammalian P450 cytochromes
    • Black S.D. Membrane topology of the mammalian P450 cytochromes. FASEB J. 6:1992;680-685.
    • (1992) FASEB J. , vol.6 , pp. 680-685
    • Black, S.D.1
  • 38
    • 0021271239 scopus 로고
    • Incorporation of the cytochrome P-450 monooxygenase system into large unilamellar liposomes using octylglucoside, especially for measurements of protein diffusion in membranes
    • Schwarz D., Gast K., Meyer H.W., Lachmann U., Coon M.J., Ruckpaul K. Incorporation of the cytochrome P-450 monooxygenase system into large unilamellar liposomes using octylglucoside, especially for measurements of protein diffusion in membranes. Biochem. Biophys. Res. Commun. 121:1984;118-125.
    • (1984) Biochem. Biophys. Res. Commun. , vol.121 , pp. 118-125
    • Schwarz, D.1    Gast, K.2    Meyer, H.W.3    Lachmann, U.4    Coon, M.J.5    Ruckpaul, K.6
  • 39
    • 0023740940 scopus 로고
    • Preparation and properties of large octylglucoside dialysis/adsorption liposomes
    • Schwarz D., Zirwer D., Gast K., Meyer H.W., Lachmann U. Preparation and properties of large octylglucoside dialysis/adsorption liposomes. Biomed. Biochim. Acta. 47:1988;609-621.
    • (1988) Biomed. Biochim. Acta , vol.47 , pp. 609-621
    • Schwarz, D.1    Zirwer, D.2    Gast, K.3    Meyer, H.W.4    Lachmann, U.5
  • 40
    • 0020147516 scopus 로고
    • Rotational diffusion of cytochrome P-450 in the microsomal membrane - Evidence for a clusterlike organization from saturation transfer EPR spectroscopy
    • Schwarz D., Pirrwitz J., Ruckpaul K. Rotational diffusion of cytochrome P-450 in the microsomal membrane - evidence for a clusterlike organization from saturation transfer EPR spectroscopy. Arch. Biochem. Biophys. 216:1982.
    • (1982) Arch. Biochem. Biophys. , vol.216
    • Schwarz, D.1    Pirrwitz, J.2    Ruckpaul, K.3
  • 41
    • 0025005497 scopus 로고
    • Membrane topology of microsomal cytochrome P-450: Saturation transfer EPR and freeze-fracture electron microscopy studies
    • Schwarz D., Pirrwitz J., Meyer H.W., Coon M.J., Ruckpaul K. Membrane topology of microsomal cytochrome P-450: saturation transfer EPR and freeze-fracture electron microscopy studies. Biochem. Biophys. Res. Commun. 171:1990;175-181.
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 175-181
    • Schwarz, D.1    Pirrwitz, J.2    Meyer, H.W.3    Coon, M.J.4    Ruckpaul, K.5
  • 43
    • 0021104520 scopus 로고
    • Reduction of cytochrome P-450 LM2 by NADPH in reconstituted phospholipid vesicles is dependent on membrane charge
    • Ingelman-Sundberg M., Blanck J., Smettan G., Ruckpaul K. Reduction of cytochrome P-450 LM2 by NADPH in reconstituted phospholipid vesicles is dependent on membrane charge. Eur. J. Biochem. 134:1983;157-162.
    • (1983) Eur. J. Biochem. , vol.134 , pp. 157-162
    • Ingelman-Sundberg, M.1    Blanck, J.2    Smettan, G.3    Ruckpaul, K.4
  • 44
    • 0021753879 scopus 로고
    • Mechanism of rate control of the NADPH-dependent reduction of cytochrome P-450 LM2 by lipids in reconstituted phospholipid vesicles
    • Blanck J., Smettan G., Ristau O., Ingelman-Sundberg M., Ruckpaul K. Mechanism of rate control of the NADPH-dependent reduction of cytochrome P-450 LM2 by lipids in reconstituted phospholipid vesicles. Eur. J. Biochem. 144:1984;509-513.
    • (1984) Eur. J. Biochem. , vol.144 , pp. 509-513
    • Blanck, J.1    Smettan, G.2    Ristau, O.3    Ingelman-Sundberg, M.4    Ruckpaul, K.5
  • 45
    • 0024317570 scopus 로고
    • Role of lipid in the electron transfer between NADPH-cytochrome P-450 reductase and cytochrome P-450 from mammalian liver cells
    • Blanck J., Jänig G.-R., Schwarz D., Ruckpaul K. Role of lipid in the electron transfer between NADPH-cytochrome P-450 reductase and cytochrome P-450 from mammalian liver cells. Xenobiotica. 19:1989;1231-1246.
    • (1989) Xenobiotica , vol.19 , pp. 1231-1246
    • Blanck, J.1    Jänig, G.-R.2    Schwarz, D.3    Ruckpaul, K.4
  • 46
    • 0027337942 scopus 로고
    • Rotation of cytochrome 450scc (CYP11A1) in proteoliposomes studied by delayed fluorescence depolarization
    • Schwarz D., Krüger V., Chernogolov A.A., Usanov S.A., Stier A. Rotation of cytochrome 450scc (CYP11A1) in proteoliposomes studied by delayed fluorescence depolarization. Biochem. Biophys. Res. Commun. 195:1993;889-896.
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , pp. 889-896
    • Schwarz, D.1    Krüger, V.2    Chernogolov, A.A.3    Usanov, S.A.4    Stier, A.5
  • 47
    • 0030665271 scopus 로고    scopus 로고
    • Evidence that nonbilayer phase propensity of the membrane is important for the side chain cleavage activity of cytochrome P450scc (CYP11A1)
    • Schwarz D., Kisselev P., Pfeil W., Pisch S., Bornscheuer U., Schmid R.D. Evidence that nonbilayer phase propensity of the membrane is important for the side chain cleavage activity of cytochrome P450scc (CYP11A1). Biochemistry. 36:1997;14262-14270.
    • (1997) Biochemistry , vol.36 , pp. 14262-14270
    • Schwarz, D.1    Kisselev, P.2    Pfeil, W.3    Pisch, S.4    Bornscheuer, U.5    Schmid, R.D.6
  • 48
    • 0031891483 scopus 로고    scopus 로고
    • Branched phosphatidylcholines stimulate activity of cytochrome P450scc (CYP11A1) in phospholipid vesicles by enhancing cholesterol binding, membrane incorporation and protein exchange
    • Kisselev P., Wessel R., Pisch S., Bornscheuer U., Schmid R.D., Schwarz D. Branched phosphatidylcholines stimulate activity of cytochrome P450scc (CYP11A1) in phospholipid vesicles by enhancing cholesterol binding, membrane incorporation and protein exchange. J. Biol. Chem. 273:1998;1380-1386.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1380-1386
    • Kisselev, P.1    Wessel, R.2    Pisch, S.3    Bornscheuer, U.4    Schmid, R.D.5    Schwarz, D.6
  • 49
    • 0035951779 scopus 로고    scopus 로고
    • Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis
    • Mueller J.J., Lapko A., Bourenkov B., Ruckpaul K., Heinemann U. Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis. J. Biol. Chem. 276:2001;2786-2789.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2786-2789
    • Mueller, J.J.1    Lapko, A.2    Bourenkov, B.3    Ruckpaul, K.4    Heinemann, U.5
  • 50
    • 0344953213 scopus 로고
    • Cytochromes P-450 of alkane-utilizing yeasts
    • K. Ruckpaul, & H. Rein. Berlin: Akademie-Verlag
    • Müller H.-G., Schunck W.-H., Kärgel E. Cytochromes P-450 of alkane-utilizing yeasts. Ruckpaul K., Rein H. Frontiers in Biotransformation. vol. 4:1991;87-126 Akademie-Verlag, Berlin.
    • (1991) Frontiers in Biotransformation , vol.4 , pp. 87-126
    • Müller, H.-G.1    Schunck, W.-H.2    Kärgel, E.3
  • 52
    • 0023188072 scopus 로고
    • Isolation of the alkane inducible cytochrome P450 (P450alk) gene from the yeast Candida tropicalis
    • Sanglard D., Chen C., Loper J.C. Isolation of the alkane inducible cytochrome P450 (P450alk) gene from the yeast Candida tropicalis. Biochem. Biophys. Res. Commun. 144:1987;251-257.
    • (1987) Biochem. Biophys. Res. Commun. , vol.144 , pp. 251-257
    • Sanglard, D.1    Chen, C.2    Loper, J.C.3
  • 54
    • 0025883783 scopus 로고
    • Comparison of two cytochromes P-450 from Candida maltosa: Primary structures, substrate specificities, and effects of their expression in Saccharomyces cerevisiae on the proliferation of the endoplasmic reticulum
    • Schunck W.-H., Vogel F., Gross B., Kärgel E., Mauersberger S., Köpke K., Gengnagel C., Müller H.-G. Comparison of two cytochromes P-450 from Candida maltosa: primary structures, substrate specificities, and effects of their expression in Saccharomyces cerevisiae on the proliferation of the endoplasmic reticulum. Eur. J. Cell Biol. 55:1991;336-345.
    • (1991) Eur. J. Cell Biol. , vol.55 , pp. 336-345
    • Schunck, W.-H.1    Vogel, F.2    Gross, B.3    Kärgel, E.4    Mauersberger, S.5    Köpke, K.6    Gengnagel, C.7    Müller, H.-G.8
  • 55
    • 0026161236 scopus 로고
    • CYP52 (cytochrome P450alk) multigene family in Candida maltosa: Molecular cloning and nucleotide sequence of the two tandemly arranged genes
    • Ohkuma M., Tanimoto T., Yano K., Takagi M. CYP52 (cytochrome P450alk) multigene family in Candida maltosa: molecular cloning and nucleotide sequence of the two tandemly arranged genes. DNA Cell Biol. 10:1991;271-282.
    • (1991) DNA Cell Biol. , vol.10 , pp. 271-282
    • Ohkuma, M.1    Tanimoto, T.2    Yano, K.3    Takagi, M.4
  • 56
    • 0026676224 scopus 로고
    • Identification and characterization of additional members of the cytochrome P450 multigene family CYP52 of Candida tropicalis
    • Seghezzi W., Meili C., Ruffiner R., Kuenzi R., Sanglard D., Fiechter A. Identification and characterization of additional members of the cytochrome P450 multigene family CYP52 of Candida tropicalis. DNA Cell Biol. 11:1992;767-780.
    • (1992) DNA Cell Biol. , vol.11 , pp. 767-780
    • Seghezzi, W.1    Meili, C.2    Ruffiner, R.3    Kuenzi, R.4    Sanglard, D.5    Fiechter, A.6
  • 57
    • 0028987581 scopus 로고
    • CYP52 (cytochrome P450alk) multigene family in Candida maltosa: Identification and characterization of eight members
    • Ohkuma M., Muraoka S., Tanimoto T., Fujii M., Ohta A., Takagi M. CYP52 (cytochrome P450alk) multigene family in Candida maltosa: identification and characterization of eight members. DNA Cell Biol. 14:1995;163-173.
    • (1995) DNA Cell Biol. , vol.14 , pp. 163-173
    • Ohkuma, M.1    Muraoka, S.2    Tanimoto, T.3    Fujii, M.4    Ohta, A.5    Takagi, M.6
  • 58
    • 0030000018 scopus 로고    scopus 로고
    • Characterization of the n -alkane and fatty acid hydroxylating cytochrome P450 forms 52A3 and 52A4
    • Scheller U., Zimmer T., Kärgel E., Schunck W.-H. Characterization of the. n -alkane and fatty acid hydroxylating cytochrome P450 forms 52A3 and 52A4 Arch. Biochem. Biophys. 328:1996;245-254.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 245-254
    • Scheller, U.1    Zimmer, T.2    Kärgel, E.3    Schunck, W.-H.4
  • 59
    • 0030601229 scopus 로고    scopus 로고
    • The CYP52 multigene family of Candida maltosa encodes functionally diverse n-alkane-inducible cytochromes P450
    • Zimmer T., Ohkuma M., Ohta A., Takagi M., Schunck W.-H. The CYP52 multigene family of Candida maltosa encodes functionally diverse n-alkane-inducible cytochromes P450. Biochem. Biophys. Res. Commun. 224:1996;784-789.
    • (1996) Biochem. Biophys. Res. Commun. , vol.224 , pp. 784-789
    • Zimmer, T.1    Ohkuma, M.2    Ohta, A.3    Takagi, M.4    Schunck, W.-H.5
  • 60
    • 0031718198 scopus 로고    scopus 로고
    • Mutual conversion of fatty acid substrate specificity by a single amino acid exchange at position 527 in P450Cm2 and P450ALK3A
    • Zimmer T., Scheller U., Takagi M., Schunck W.-H. Mutual conversion of fatty acid substrate specificity by a single amino acid exchange at position 527 in P450Cm2 and P450ALK3A. Eur. J. Biochem. 256:1998;398-403.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 398-403
    • Zimmer, T.1    Scheller, U.2    Takagi, M.3    Schunck, W.-H.4
  • 61
    • 0032512656 scopus 로고    scopus 로고
    • Isozyme function of n-alkane-inducible cytochromes P450 in Candida maltosa revealed by sequential gene disruption
    • Ohkuma M., Zimmer T., Iida T., Schunck W.-H., Ohta A., Takagi M. Isozyme function of n-alkane-inducible cytochromes P450 in Candida maltosa revealed by sequential gene disruption. J. Biol. Chem. 273:1998;3948-3953.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3948-3953
    • Ohkuma, M.1    Zimmer, T.2    Iida, T.3    Schunck, W.-H.4    Ohta, A.5    Takagi, M.6
  • 62
    • 15644376395 scopus 로고    scopus 로고
    • Oxygenation cascade in conversion of n-alkanes to -dioic acids catalyzed by cytochrome P450 52A3
    • Scheller U., Zimmer T., Becher D., Schauer F., Schunck W.-H. Oxygenation cascade in conversion of n-alkanes to -dioic acids catalyzed by cytochrome P450 52A3. J. Biol. Chem. 273:1998;32528-32534.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32528-32534
    • Scheller, U.1    Zimmer, T.2    Becher, D.3    Schauer, F.4    Schunck, W.-H.5
  • 63
    • 0032500817 scopus 로고    scopus 로고
    • Relation between evolutionary distance and enzymatic properties among members of the CYP52A subfamily of Candida maltosa
    • Zimmer T., Iida T., Schunck W.-H., Yoshida Y., Ohta A., Takagi M. Relation between evolutionary distance and enzymatic properties among members of the CYP52A subfamily of Candida maltosa. Biochem. Biophys. Res. Commun. 251:1998;244-247.
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 244-247
    • Zimmer, T.1    Iida, T.2    Schunck, W.-H.3    Yoshida, Y.4    Ohta, A.5    Takagi, M.6
  • 64
    • 0021233394 scopus 로고
    • The induction of cytochrome P-450 in the alkane-utilizing yeast Lodderomyces elongisporus: Alterations in the microsomal membrane fraction
    • Mauersberger S., Schunck W.-H., Müller H.-G. The induction of cytochrome P-450 in the alkane-utilizing yeast Lodderomyces elongisporus: alterations in the microsomal membrane fraction. Appl. Microbiol. Biotechnol. 19:1984;29-35.
    • (1984) Appl. Microbiol. Biotechnol. , vol.19 , pp. 29-35
    • Mauersberger, S.1    Schunck, W.-H.2    Müller, H.-G.3
  • 65
    • 0026583004 scopus 로고
    • Immunocytochemical localization of alkane-inducible cytochrome P-450 and its NADPH-dependent reductase in the yeast Candida maltosa
    • Vogel F., Gengnagel C., Kärgel E., Müller H.-G., Schunck W.-H. Immunocytochemical localization of alkane-inducible cytochrome P-450 and its NADPH-dependent reductase in the yeast Candida maltosa. Eur. J. Cell Biol. 57:1992;285-291.
    • (1992) Eur. J. Cell Biol. , vol.57 , pp. 285-291
    • Vogel, F.1    Gengnagel, C.2    Kärgel, E.3    Müller, H.-G.4    Schunck, W.-H.5
  • 66
    • 0342398228 scopus 로고    scopus 로고
    • Topogenesis of cytochromes P450 and induction of ER-proliferation in yeast
    • Menzel R., Kärgel E., Böttcher C., Schunck W.-H. Topogenesis of cytochromes P450 and induction of ER-proliferation in yeast. Arch. Biochem. Biophys. 330:1996;97-109.
    • (1996) Arch. Biochem. Biophys. , vol.330 , pp. 97-109
    • Menzel, R.1    Kärgel, E.2    Böttcher, C.3    Schunck, W.-H.4
  • 67
    • 0029867362 scopus 로고    scopus 로고
    • Candida maltosa NADPH-cytochrome P450 reductase: Cloning of a full-length cDNA, heterologous expression in Saccharomyces cerevisiae and function of the N-terminal region for membrane anchoring and proliferation of the endoplasmic reticulum
    • Kärgel E., Menzel R., Honeck H., Vogel F., Böhmer A., Schunck W.-H. Candida maltosa NADPH-cytochrome P450 reductase: cloning of a full-length cDNA, heterologous expression in Saccharomyces cerevisiae and function of the N-terminal region for membrane anchoring and proliferation of the endoplasmic reticulum. Yeast. 12:1996;333-348.
    • (1996) Yeast , vol.12 , pp. 333-348
    • Kärgel, E.1    Menzel, R.2    Honeck, H.3    Vogel, F.4    Böhmer, A.5    Schunck, W.-H.6
  • 68
    • 0028298478 scopus 로고
    • Generation of the soluble and functional cytosolic domain of microsomal cytochrome P450 52A3
    • Scheller U., Kraft R., Schröder K.-L., Schunck W.-H. Generation of the soluble and functional cytosolic domain of microsomal cytochrome P450 52A3. J. Biol. Chem. 269:1994;12779-12783.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12779-12783
    • Scheller, U.1    Kraft, R.2    Schröder, K.-L.3    Schunck, W.-H.4
  • 69
    • 0344416996 scopus 로고    scopus 로고
    • Regulation of endoplasmic reticulum biogenesis in response to cytochrome P450 overproduction
    • Sandig G., Kärgel E., Menzel R., Vogel F., Zimmer T., Schunck W.-H. Regulation of endoplasmic reticulum biogenesis in response to cytochrome P450 overproduction. Drug Metabol. Rev. 31:1999;393-410.
    • (1999) Drug Metabol. Rev. , vol.31 , pp. 393-410
    • Sandig, G.1    Kärgel, E.2    Menzel, R.3    Vogel, F.4    Zimmer, T.5    Schunck, W.-H.6
  • 70
    • 0027732208 scopus 로고
    • Overexpression of the ER-membrane protein P-450 CYP52A3 mimics sec mutant characteristics in Saccharomyces cerevisiae
    • Wiedmann B., Silver P., Schunck W.-H., Wiedmann M. Overexpression of the ER-membrane protein P-450 CYP52A3 mimics sec mutant characteristics in Saccharomyces cerevisiae. Biochim. Biophys. Acta. 1153:1993;267-276.
    • (1993) Biochim. Biophys. Acta , vol.1153 , pp. 267-276
    • Wiedmann, B.1    Silver, P.2    Schunck, W.-H.3    Wiedmann, M.4
  • 71
    • 0030828058 scopus 로고    scopus 로고
    • Inducible membranes in yeast: Relations to the unfolded protein response pathway
    • Menzel R., Vogel F., Kärgel E., Schunck W.-H. Inducible membranes in yeast: relations to the unfolded protein response pathway. Yeast. 13:1997;1211-1229.
    • (1997) Yeast , vol.13 , pp. 1211-1229
    • Menzel, R.1    Vogel, F.2    Kärgel, E.3    Schunck, W.-H.4


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