Citovanost publikací - doc. RNDr. Jiří Hudeček, CSc.

Transkript

1 Citovanost publikací - doc. RNDr. Jiří Hudeček, CSc. Přehled je zpracován ve struktuře předloženého seznamu publikací, podle stavu k , bez autocitací vlastních i autocitací všech spoluautorů (tj. s úplným vyloučením průniků mezi seznamy autorů citované a citující práce). Data jsou převzata z WoS s výjimkou dat označených hvězdičkou, která byla doplněna z databází Google Scholar a SciFinder (tj. Chemical Abstracts). Údaje byly v zásadě ponechány podle stavu ve WoS (pouze s určitým sjednocením formátu), byly doplněny ručně dohledané citace, které systém automaticky nenabízí v důsledku typografických problémů s diakritikou (Hudeček-Hudeeek-Hudeek), resp. v důsledku chyb v citaci. Celkový počet citací v tomto seznamu je 135. (Tento počet se odlišuje od dat získaných přímo z WoS pomocí funkce "citation report", která je přílohou žádosti, vzhledem k odlišné metodice výpočtu - počet citujících článků vs. počet jednotlivých citací, a také vzhledem k tomu, že WoS vylučuje pouze přímé autocitace.) 1.1 Hudeček, J., Kalous, V.: Fyzikálně chemická podmíněnost struktury bílkovin. Metody popisu a predikce struktury. Academia, Praha ISBN , Tato práce byla citována 4x 1. Mrázek J, Kypr J: Prediction of protein secondary structure. Chem. Listy, 85, (1991 ) 2. Karpenko V, Šinkorová L, Kodíček M: Effect of methanol on the structure of human blood-serum orosomucoid (acid alpha-1-glycoprotein). Coll. Czech. Chem. Commun. 57, ( Hof M, Vajda S, Fidler V, et al.: Picosecond tryptophan fluorescence of human blood serum orosomucoid. Coll. Czech. Chem. Commun. 61, (1996) 4. Švec M, Vondrášek J: Protein folding: State of the problem at the end of millenium. Chem Listy 94, (2000) 2.1 Hudeček, J., Anzenbacher, P.: Secondary structure prediction for cytochromes P-450. In: Cytochrome P-450, Biochemistry, Biophysics and Induction, (Vereczkey, L., Magyar, K., Eds.), pp , Akadémiai Kiadó, Budapest 1985 Tato práce byla citována 1x Usanov SA, Chernogolov AA, Chashchin VL: Immunochemical investigation of cholesterol-hydroxylating cytochrome-p topology of the polypeptide-chain of the hemoprotein in the phospholipid membrane. Biochemistry-Moscow 54, (1989) 2.7 Anzenbacher, P., Hudeček, J., Stiborová, M., Larroque, C., Lange, R., Heibel, G., Hildebrandt, P.: Comparison of the structures of different cytochromes P-450 as revealed by experimental and theoretical methods. In: Cytochrome P-450. Biochemistry and Biophysics (Archakov A.I., Bachmannova G.I., Eds.) pp. 1-8, INCO-TNC, Moscow Tato práce byla citována 1x *Lepesheva GI, Usanov SA: Comparative structural and immunochemical characterizaion of recombinant and natural cytochrome P450scc. Biochemistry-Moscow 63, (1998)

2 3.3 Hudeček, J., Anzenbacher, P., Kalous, V.: Interaction of insulin with metal (II) ions. FEBS Lett. 100, (1979). Tato práce byla citována 2x 1. Alameda GK, Evelhoch JL, Sudmeier JL, et al.: Characterization of the internal calcium(ii) binding-sites in dissolved insulin hexamer using europium(iii) fluorescence. Biochemistry 24, (1985). 2. Hoftiezer V, Berggren PO, Hellman BO: Effects of zinc during culture of an insulin-producing rat-cell line (RINM5F). Cancer Lett. 29, (1985). 3.4 Anzenbacher, P., Hudeček, J., Stružinský, P.: Study of thermal stability of cytochrome P-450 by differential scanning calorimetry. FEBS Lett. 149, (1982) Tato práce byla citována 9x 1. Maves SA, Sligar SG: Understanding thermostability in cytochrome P450 by combinatorial mutagenesis. Protein Sci. 10, (2001). 2. Kuhnvelten WN: Effects of compatible solutes on mammalian cytochrome P450 stability. Z. Naturforsch C 52, (1997). *3. Paolini M, Canteli-Forti G: On the metabolizing systems for short-term toxicity assays: a review. Mutat. Res. 387, (1997). 4. Kuhnvelten WN: Rapid down-regulation of testicular androgen biosynthesis at increased environmental temperature is due to cytochrome P450C17 (CYP17) thermolability in Leydig cells, but not in endoplasmic reticulum membranes Exp. Clin. Endocr. Diab. 104, (1996). 5. Pfeil W, Nolting BO, Jung C: Apocytochrome-P450CAM is a native protein with some intermediate-like properties. Biochemistry-US 32 (34), (1993). 6. Kuhnvelten WN: Thermodynamics and modulation of progesterone microcompartmentation and hydrophobic interaction with cytochrome-p450xvii based on quantification of local ligand concentrations in a complex multicomponent system Eur. J. Biochem. 197, (1991). 7. Kuhnvelten N, Rediger J, Staib W: Down-regulation of steroidogenic cytochrome- P450XVII in cryptorchid rat testes. Horm. Metab. Res. 22, (1990). 8. Engeseth HR, Mcmillin DR: Studies of thermally induced denaturation of azurin and azurin derivatives by differential scanning calorimetry - evidence for copper selectivity. Biochemistry-US 25, (1986). 9. Gondova T, Kralik P: Possibilities of the application of the thermal-analysis methods in the study of low-molecular organic-substances. Chem. Listy 80, (1986). 3.5 Hudeček, J., Anzenbacher, P.: Secondary structure prediction of liver microsomal cytochrome P-450: proposed model of spatial arrangement in a membrane. Biochim. Biophys. Acta 955, (1988) Tato práce byla citována 14x 1. Kanamura S, Watanabe J: Cell biology of cytochrome P-450 in the liver Int. Rev. Cytol. 198, (2000). *2. Lee AG: Structure of the SR/ER Ca2+ ATPase. In: Biomembranes. Volume 5 (Lee AG,

3 ed.), JAI Press/Elsevier 1996 (ISBN ), str Uvarov VY, Sotnichenko AI, Vodovozova EL, et al.: Determination of membranebound fragments of cytochrome-p-450 2B4. Eur. J. Biochem 222, (1994). 4. Edelman J: Quadratic minimization of predictors for protein secondary structure - application to transmembrane alpha-helices. J. Mol. Biol. 232, (1993). 5. Pernecky SJ, Larson JR, Philpot RM, et al.: Expression of truncated forms of liver microsomal P450 cytochromes 2B4 AND 2E1 in Escherichia-coli - influence of NH2-terminal region on localization in cytosol and membranes. Proc. Natl. Acad. Sci. USA 90, (1993). 6. Vermeir M, Boens N, Heirwegh KPM: Interaction of 7-N-alkoxycoumarins with cytochrome-p-450(2) and their partitioning into liposomal membranes - assessment of methods for determination of membrane partition-coefficients. Biochem. J. 284, (1992). 7. Black SD: Membrane topology of the mammalian P450-cytochromes. FASEB J. 6, (1992). 8. Li YC, Chiang JYL: The expression of a catalytically active cholesterol 7-alphahydroxylase cytochrome-p450 in Escherichia-coli. J. Biol. Chem. 266, (1991). 9. Shcherbakov VM, Dubrov YN, Korneva EN, et al.: NADPH-dependent reduction of amaranch in liver-microsomes characterized the quantity of low-spin forms of cytochrome-p-450. Biochem. Bioph. Res. Commun. 179, (1991). 10. Ouzounis CA, Melvin WT: Primary and secondary structural patterns in eukaryotic cytochrome-p-450 families correspond to structures of the helix-rich domain of pseudomonas-putida cytochrome-p-450cam - indications for a similar overall topology. Eur. J. Biochem. 198, (1991). 11. Larson JR, Coon MJ, Porter TD: Alcohol-inducible cytochrome-p-450iie1 lacking the hydrophobic NH2-terminal segment retains catalytic activity and is membranebound when expressed in Escherichia-coli. J. Biol. Chem. 266, (1991). 12. Edwards RJ, Murray BP, Singleton AM, et al.: Orientation of cytochromes-p450 in the endoplasmic-reticulum. Biochemistry-US 30, (1991). 13. Hildebrandt P, Garda H, Stier A, et al.: Protein protein interactions in microsomal cytochrome-p-450 isozyme LM2 and their effect on substrate binding. Eur. J. Biochem. 186, (1989) 14. Tretiakov VE, Degtyarenko KN, Uvarov VY, et al.: Secondary structure and membrane topology of cytochrome-p450s. Arch. Biochem. Biophys. 275, (1989) 3.6 Anzenbacher, P., Hudeček, J., Mojzeš, P., Baumruk, V., Štěpánek, J.: Resonance Raman study of the reduction of catalase - Evidence for a strong electron donation to the heme. Stud. Biophys. 123, (1988) Tato práce byla citována 2x 1. Gaspard S, Chottard G, Mahy JP, et al.: Study of the coordination chemistry of prostaglandin G/H synthase by resonance Raman spectroscopy. Eur. J. Biochem. 238, (1996) 2. Hu SH, Kincaid JR: Resonance Raman studies of the carbonmonoxy form of catalase

4 - evidence for and effects of phenolate ligation. FEBS Lett. 314, (1992) 3.7 Anzenbacher, P., Hudeček, J., Vajda, Š., Fidler, V.: Nanosecond fluorometry of the single tryptophan in cytochrome P-450e (P450IIB2). Biochem. Biophys. Res. Commun. 162, (1989) Tato práce byla citována 3x 1. Khan KK, Mazumdar S, Modi S, Sutcliffe M, Roberts GCK, Mitra S: Steady-state and picosecond-time-resolved fluorenscence studies on the recombinant heme domain of Bacillus megaterium cytochrome P-450. Eur. J. Biochem. 244, (1997) 2. Stevens JM, Uchida T, Daltrop O, Kitagawa T, Ferguson SJ: Dynamic Ligation properties of the Escherichia coli heme chaperone CcmE to non-covalently bound heme. J. Biol. Chem. 281, (1997) 3. Koymans L, Denkelder GMDO, Te JMK. et al.: Cytochromes P450 - their active site structure and mechanism of oxidation. Drug Metabol. Rev. 25, (1993) 3.8 Chmelík, J., Hudeček, J., Putyera, K., Kalous, V., Chmelíková, J.: Characterization of the hydrophobic properties of amino acids on the basis oh their partition and distribution coefficients in the 1-octanol/water system. Coll. Czech. Chem. Commun. 56, (1991) Tato práce byla citována 8x 1. Palecz B: Enthalpic pair interaction coefficient between zwitterions of L-alphaamino acids and urea molecule as a hydrophobicity parameter of amino acid side chains. J. Am. Chem. Soc. 127, (2005) 2. Bretti C, Crea F, Foti C, et al.: Solubility and activity coefficients of acidic and basic nonelectrolytes in aqueous salt solutions. 1. Solubility and activity coefficients of o-phthalic acid and L-cystine in NaCl(aq), (CH3)(4)NCl(aq), and (C2H5)(4)NI(aq) at different ionic strengths and at t=25 degrees C. J. Chem. Eng. Data 50, (2005). *3. Avdeef A: Physicochemical Profiling (Solubility, Permeability and Charge State) Frontiers Med. Chem. - Online 1, (2004) 4. Palecz B: Enthalpic homogeneous pair interaction coefficients of L-alpha-amino acids as a hydrophobicity parameter of amino acid side chains. J. Am. Chem. Soc. 124, (2002). 5. Priolo N, Arribere CM, Caffini N, et al.: Isolation and purification of cysteine peptidases from the latex of Araujia hortorum fruits - Study of their esterase activities using partial least-squares (PLS) modeling. J. Mol. Catal. B 15, (2001). 6. Silva MF, Chipre LF, Raba J, et al.: Amino acids characterization by reversedphase liquid chromatography. Partial least-squares modeling of their transport properties. Chromatographia 53, (2001) 7. Roberts JD, Daugulis AJ: Evaluation of UNIFAC for the prediction of partitioning in 2-phase aqueous-organic systems containing amino-acids and oligomers. Biotechnol. Progr. 11, (1995) 8. Vandewaterbeemd H, Karajiannis H, Eltayar N: Lipophilicity of amino-acids. Amino Acids 7, (1994) 3.9 Anzenbacher, P., Hudeček, J., Vajda, Š., Fidler, V., Larroque, C., Lange, R.: Nanosecond fluorescence of tryptophans in cytochrome P-450scc (CYP11A1). Effect of substrate binding.

5 Biochem. Biophys. Res. Commun. 181, (1991) Tato práce byla citována 8x 1. Soni V, Yasui T, Cahir-McFarland E, Kieff, E: LMP1 transmembrane domain 1 and 2 (TM1-2) FWLY mediates intermolecular interactions with TM3-6 to activate NF-kappa B J. Virol. 80, (2006). 2. Yasui T, Luftig M, Soni V, Kieff, E.: Latent infection membrane protein transmembrane FWLY is critical for intermolecular interaction, raft localization, and signaling. Proc. Natl. Acad. Sci. USA 101, (2004). 3. Headlam MJ, Wilce MCJ, Tuckey RC: The F-G loop region of cytochrome P450scc (CYP11A1) interacts with the phospholipid membrane. Biochim. Biophys. Acta 1617, (2003) *4. Maity H., Jarori GK: Fluorescence quenching f dimeric and monomeric forms of yeast hexokinase. Physiol. Chem. Phys. NMR 34, (2002) *5. Kuchroo K, Maity H, Kasturi SR: Effects of urea denaturation on tryptophan fluorescence and nucleotide binding on tubulin. Physiol. Chem. Phys. NMR 33, (2001) 6. Maity H, Maiti NC, Jarori GK: Time-resolved fluorescence of tryptophans in yeast hexokinase-pi: effect of subunit dimerization and ligand binding. J. Photochem. Photobiol. B 55, (2000) 7. Khan KK, Mazumdar S, Modi S, Sutcliffe M, Roberts GCK, Mitra S: Steady-state and picosecond-time-resolved fluorenscence studies on the recombinant heme domain of Bacillus megaterium cytochrome P-450. Eur. J. Biochem. 244, (1997) 8. Das TK, Mazumdar S: Time-resolved study of tryptophan fluorescence in vesicle reconstituted cytochrome-oxidase-effect of redox transition. FEBS Lett. 336, (1993) 3.10 Hudeček, J., Baumruk, V., Anzenbacher, P., Munro, A.W.: Catalytically self-sufficient P450 CYP102 (cytochrome P-450 BM-3): resonance Raman spectral characterization of the heme domain and of the holoenzyme. Biochem.Biophys. Res. Commun. 243, (1998) Tato práce byla citována 5x 1. Jovanovic T, Harris M, McDermott AE: Cytochrome P450BM-3 in complex with its substrate: Temperature-dependent spin state equilibria in the oxidized and reduced states Appl. Magn. Resonance 31, (2007) 2. Chen ZC, Ost TWB, Schelvis JPM: Phe393 mutants of cytochrome P450BM3 with modified heme redox potentials have altered heme vinyl and propionate conformations Biochemistry-US 43, (2004) 3. Smith SJ, Munro AW, Smith WE: Resonance Raman scattering of cytochrome P450BM3 and effect of imidazole inhibitors. Biopolymers 70, (2003) 4. Chroma L, Mackova M, Macek T, Martínek V., Stiborová M.: Plant cytochromes P450 and peroxidases and their role in degradation of environmental contaminants. Chem. Listy 95, (2001) 5. Larive CK, Lunte SM, Zhong M, et al. : Separation and analysis of peptides and proteins Anal. Chem. 71, 389R-423R (1999) 3.11 Anzenbacher, P., Bec, N., Hudeček, J., Lange, R., Anzenbacherová, E.: High conformational

6 stability of cytochrome P-450 1A2. Evidence from UV absorption spectra. Coll. Czech. Chem. Commun. 63, (1998) Tato práce byla citována 4x 1. Davydov DR, Baas BJ, Sligar SG, et al.: Allosteric mechanisms in cytochrome P450 3A4 studied by high-pressure spectroscopy: Pivotal role of substrate-induced changes in the accessibility and degree of hydration of the heme pocket. Biochemistry 46, (2007). 2. Davydov DR, Halpert JR, Renaud JP, et al.: Conformational heterogeneity of cytochrome P450 3A4 revealed by high pressure spectroscopy Biochem. Biophys. Res. Commun.. 312, (2003) 3. Davydov DR, Petushkova NA, Archakov AI, et al.: Stabilization of P4502B4 by its association with P450 1A2 revealed by high-pressure spectroscopy. Biochem. Biophys. Res. Commun. 276, (2000) 4. Larive CK, Lunte SM, Zhong M, et al.: Separation and analysis of peptides and proteins Anal. Chem. 71, 389R-423R (1999) 3.13 Anzenbacherová, E., Bec, N., Anzenbacher, P., Hudeček, J., Souček, P., Jung, C., Munro, A.W., Lange, R.: Flexibility and stability of cytochromes P450 3A4 and BM-3. Eur. J. Biochem. 267, (2000) Tato práce byla citována 14x *1. Tatzel S: Modelierung von Cytochrom P450-Monooxygenasen. Univ. Stuttgart, dokt. disertace (2008) 2. Hlavica P: Control by substrate of the cytochrome p450-dependent redox machinery: Mechanistic insights. Curr. Drug. Metabol. 8, (2007) 3. Davydov DR, Baas BJ, Sligar SG, Halpert JR: Allosteric mechanisms in cytochrome P450 3A4 studied by high-pressure spectroscopy: Pivotal role of substrate-induced changes in the accessibility and degree of hydration of the heme pocket. Biochemistry 46, (2007) 4. Eiben S, Bartelmas H, Urlacher VB: Construction of a thermostable cytochrome P450 chimera derived from self-sufficient mesophilic parents. Appl. Microbiol. Biotech. 75, Marechal JD, Yu JL, Brown S, Kapelioukh I, Rankin EM, Wolf CR, Roberts GCK, Paine MJI, Sutcliffe MJ: In silico and in vitro screening for inhibition of cytochrome P450CYP3A4 by comedications commonly used by patients with cancer. Drug Metabol. Disp. 34, (2006) 6. Sawada Y, Ayabe SI: Multiple mutagenesis of P450 isoflavonoid synthase reveals a key active-site residue Biochem Biophys Res Commun 330, (2005) 7. Chen ZC, Ost TWB, Schelvis JPM : Phe393 mutants of cytochrome P450BM3 with modified heme redox potentials have altered heme vinyl and propionate conformations. Biochemistry-US 43, (2004) *8. Hendler I, Baum M, Kreiser D, Schiff E, et al.: End-tidal breath carbon monoxide measurements are lower in pregnant women with uterine contractions. J. Perinatol. 24, (2004) 9. Davydov DR, Halpert JR, Renaud JP, et al.: Conformational heterogeneity of cytochrome P450 3A4 revealed by high pressure spectroscopy Biochem. Biophys. Res.

7 Commun. 312, (2003) 10. Cryle MJ, Stok JE, de Voss JJ: Reactions catalyzed by bacterial cytochromes P450. Aust. J. Chem. 56, (2003) *11. Cruciani G, Carosati E, Clement S: Three dimensional quantitative structureproperty relationships. In: Practice of Medicinal Chemistry (Wermuth GG, ed.), Elsevier London 2003, str Jung C: Cytochrome P-450-CO and substrates: lessons from ligand binding under high pressure Biochim. Biophys. Acta 1595, (2002) 13. Tschirret-Guth RA, Koo LS, Hui Bon Hoa G, et al.: Reversible pressure deformation of a thermophilic cytochrome P450 enzyme (CYP119) and its active-site mutants. J. Am. Chem. Soc. 123, (2001) 14. Ekins S, Waller CL, Swaan PW, et al.: Progress in predicting human ADME parameters in silico. J. Pharmacol. Toxicol. 44, (2000) Döpner, S., Hudeček, J., Ludwig, B., Witt, H., Hildebrandt, P.: Structural changes in cytochrome c oxidase induced by cytochrome c binding. A resonance Raman study. Biochim. Biophys. Acta 1480, (2000) Tato práce byla citována 5x 1. Friedrich MG, Robertson JWF, Walz D, Knoll W, Naumann RLC: Electronic wiring of a multi-redox site membrane protein in a biomimetic surface architecture. Biophys. J. 94, (2008) 2. Zhong TS, Qu YX, Huang SS, Li FH: Electrochemical studies of cytochrome c on gold electrodes with promotor of humic acid and 4-aminothiophenol. Microchim. Acta 158, (2007) *3. Siddiqui MQ: Association of membrane respiratory complexes. J. W. Goethe Univ.Frankfurt/M, dokt. disertace (2006) 4. Hoang, L., Maity, H., Krishna, M.M.G., Lin Y, Englander SW.: Folding units govern the cytochrome c alkaline transition. J. Mol. Biol. 331, (2003) 5.Hunte, C., Solmaz, S, Lange, C.: Electron transfer between yeast cytochrome bc(1) complex and cytochrome c: a structural analysis. Biochim. Biophys. Acta. 1555, (2002) 3.15 Hudeček, J., Anzenbacherová, E., Anzenbacher, P., Munro, A.W., Hildebrandt, P.: Structural similarities and differences of the heme pockets of various P450 isoforms as revealed by resonance Raman spectroscopy. Arch. Biochem. Biophys., 383, (2000) Tato práce byla citována 7x 1. Bonifacio A, Millo D, Keizers PHJ, et al.: Active-site structure, binding and redox activity of the heme-thiolate enzyme CYP2D6 immobilized on coated Ag electrodes: a surface-enhanced resonance Raman scattering study. J. Biol. Inorg. Chem. 13, (2008) *2. Bonifacio A: Resonance Raman spectroscopy of human cytochrome P450 2D6 in solution and on nanostructured metal surfaces. Vrije Univ. Amsterdam, dokt. disertace (2007) 3. Bonifacio A, Groenhof AR, Keizers PHJ, et al.: Altered spin state equilibrium in

8 the T309V mutant of cytochrome P450 2D6: a spectroscopic and computational study. J. Biol. Inorg. Chem. 12, (2007) 4. Jovanovic T, Harris M, McDermott AE: Cytochrome P450BM-3 in complex with its substrate: Temperature-dependent spin state equilibria in the oxidized and reduced states. Appl Magnet Resonance 31, (2007) 5. Herrmann C, Reiher M: First-principles approach to vibrational spectroscopy of biomolecules. In: Atomistic approaches in modern biology: from quantum chemistry to molecular simulations (Top. Curr. Chem. Vol. 268), (2007) 6. Bonifacio A, Keizers PHJ, Vermeulen NPE, et al.: Surface-enhanced resonance Raman scattering of cytochrome P450-2D6 on coated silver hydrosols. Langmuir 23, (2007) 7. Chen ZC, Ost TWB, Schelvis JPM: Phe393 mutants of cytochrome P450BM3 with modified heme redox potentials have altered heme vinyl and propionate conformations Biochemistry-US 43, (2004) 3.16 Mikšanová, M., Hudeček, J., Páca, J., Stiborová, M.: To the mechanism of horseradish peroxidase-mediated degradation of a recaciltrant dye Remazol Brilliant Blue R. Coll. Czech. Chem. Commun.66, (2001) Tato práce byla citována 5x 1. Tortella GR, Diez MC, Duran N: Fungal diversity and use in decomposition of environmental pollutants Crit. Rev. Microbiol. 31, (2005) 2. Gujarathi NP, Haney BJ, Linden JC: Phytoremediation potential of Myriophyllum aquaticum and Pistia stratiotes to modify antibiotic growth promoters, tetracycline, and oxytetracycline, in aqueous wastewater systems. Int. J. Phytoremediation 7, (2005) 3. Gujarathi NP, Haney BJ, Park HJ, Wickramasinghe SR, Linden JC: Hairy roots of Helianthus annuus: A model system to study phytoremediation of tetracycline and oxytetracycline. Biotechnology Prog. 21, (2005) 4. Chroma L, Macek T, Demnerova K, Mackova M: Decolorization of RBBR by plant cells and correlation with the transformation of PCBs. Chemosphere 49, (2002) 5. Shaffiqu TS, Roy JJ, Nair RA, et al.: Degradation of textile dyes mediated by plant peroxidases. Appl. Biochem. Biotech. 102, (2002) 3.17 Beneš, M., Hudeček, J., Anzenbacher, P., Hof M.: Coumarine 6, Resorufin, Hypericine, and Flavins: Suitable Chromophores for Fluorescence Correlation Spectroscopy of Biological Molecules. Coll. Czech. Chem.Commum., 66, (2001) Tato práce byla citována 4x *1. Chen K, Vo-Dinh T: Simple molecule detection techniques for monitoring celular activity at nanoscale level. In: Nonotechnologz in Biology and Medicine (Vo-Dinh T, ed.), 16/1-16/24, CRC Press, Boca Raton, *2. Strehle MA, Gerunda M, Deckert V, et al.: Fibrinogen adsorption on implant materials. Asian Chem. Lett. 7, (2007) *3. Auberson Y: Preparation of coumarins as biomarkers for the staining of brain tissue. PCT Appl WO2003-EP

9 4. Scholler M, Hauck A, Thull R, et al.: Laser scanning microscopy study on adsorption of biologically relevant proteins on implant materials. Biopolymers 67, (2002) 3.18 Anzenbacher, P., Hudeček, J.: Differences in flexibility of active sites of cytochromes P-450 probed by resonance Raman and UV-Vis absorption spectroscopy. J Inorg. Biochem 87, (2001) Tato práce byla citována 8x *1. Tatzel S: Modelierung von Cytochrom P450-Monooxygenasen. Univ. Stuttgart, dokt. disertace (2008) *2. Munro AW, McLean KJ, Girvan HM: Interactions of cytochrome P450 with nitric oxide and related ligands. Metal Ions Life Sci. 3, (2007) *3. Ohmae E, Murakami C, Gekko K, Kato C: Pressure effects on enzyme function. J. Biol. Macromol. 7, (2007) 4. Clodfelter KH, Waxman DJ, Vajda S: Computational solvent mapping reveals the importance of local conformational changes for broad substrate specificity in mammalian cytochromes P450. Biochemistry 45, (2006) 5. Marechal JD, Yu JL, Brown S, Kapelioukh I, Rankin EM, Wolf CR, Roberts GCK, Paine MJI, Sutcliffe MJ: In silico and in vitro screening for inhibition of cytochrome P450CYP3A4 by comedications commonly used by patients with cancer. Drug Metabolism Disp. 34, (2006) 6. Faber MS, Jetter A, Fuhr U: Assessment of CYP1A2 activity in clinical practice: Why, how, and when? Basic Clin. Pharmacol. Toxicol. 97, (2005) *7. Hombrecher A: Molecular Modelling Studien am humanem Cytochrom P450 1A2. Cuvillier Verlag, Göttingen 2005 (ISBN: ), str Chen ZC, Ost TWB, Schelvis JPM: Phe393 mutants of cytochrome P450BM3 with modified heme redox potentials have altered heme vinyl and propionate conformations. Biochemistry-US 43, (2004) 3.19 Moré, S.D., Hudeček, J., Urisu, T.: Hydrophobic/hydrophilic interactions of cytochrome c with functionalized self-assembled monolayers on silicon. Surf Sci, 532, (2003) Tato práce byla citována 8x 1. Mendes RK, Carvalhal RF, Kubota LTE: ffects of different self-assembled monolayers on enzyme immobilization procedures in peroxidase-based biosensor development. J. Electroanal. Chem. 612, (2008) 2. Doneux T, Steichen M, Bouchta T, Buess-Herman C: Mixed self-assembled monolayers of 2-mercaptobenzimidazole and 2-mercaptobenzimidazole-5-sulfonate: Determination and control of the surface composition. J. Electroanal. Chem. 599, (2007) 3. Mengistu TZ, DeSouza L, Morin S: Proteins on functionalized silicon surfaces using matrix-assisted laser desorption/ionization mass spectrometry. J. Chromatogr. A 1135, (2006) 4. Mengistu TZ, Goel V, Horton JH, Morin S: Chemical force titrations of functionalized Si(111) surfaces. Langmuir (2006) *5. de Smet LCDM: Covalently bound organic monolayers on silicon surfaces. Univ. Wageningen 2006 (ISBN )

10 6. Mengistu TZ, DeSouza L, Morin S: Functionalized porous silicon surfaces as MALDI-MS substrates for protein identification studies. Chem. Commun (2005) 7. de Smet LCPM, Pukin AV, Sun QY, Eves BJ, Lopinski GP, Visser GM, Zuilhof H, Sudholter EJR: Visible-light attachment of Si-C linked functionalized organic monolayers on silicon surfaces. Appl. Surf. Sci. 252, (2005) 8. Silva LP: Imaging proteins with atomic force microscopy: An overview. Curr. Protein Peptide Sci. 6, (2005) 3.20 Stiborová, M., Sejbal, J., Bořek-Dohalská, L., Aimová, D., Poljaková, J., Forsterová, K., Rupertová, M., Wiesner, J., Hudeček, J., Wiessler, M., Frei, E.: The anticancer drug ellipticine forms covalent DNA adducts, mediated by human cytochromes P450, through metabolism to 13- hydroxyellipticine and ellipticine N-2-oxide. Cancer Res. 64, (2004) Tato práce byla citována 6x *1 Fung S-Y: Self-assembling peptides as potential carriers for the delivery of hydrophobic anticancer agent ellipticine. Univ. Waterloo, Canada, dokt. disertace (2008) 2. Tian E, Landowski TH, Stephens OW, et al.: Ellipticine derivative NSC represents a potential new antineoplastic agent for the treatment of multiple myeloma. Mol. Canc. Therap. 7, (2008) 3. Wheate NJ, Brodie CR, Collins JG, et al.: DNA intercalators in cancer therapy: Organic and inorganic drugs and their spectroscopic tools of analysis. Mini-Rev. Med. Chem. 6, (2007) *4. Darwiche N, El-Banna S, Gali-Muhtasib H: Cell cycle modulatory and apoptotic effects of plant-derived anticancer drugs. Expert Opin. Drug. Discov. 2, (2007) *5. Asche C, Demeneunynck M: Antitumor carbazoles. Anti-Canc. Agents Med. Chem. 7, (2007) *6. Brielman HL, Setzer WN, Kaufman PB, et. al.: Phytochemicals. In: Natural Products in Plants 2nd Ed.(Cseke LJ, Kirakosyan A, Kaufman PB, et al., Eds.) CRC Press, Boca Raton 2006 (ISBN ), str Hodek, P., Bořek-Dohalská, L., Sopko, B., Šulc, M., Smrček, S., Hudeček J., Janků, J., Stiborová, M.: Structural requirements for inhibitors of cytochromes P450 2B: assessment of the enzyme interaction with diamondoids. J. Enzyme Inhib. Med. Chem. 20, (2005) Tato práce byla citována 2x 1. Schwertfeger H, Fokin AA, Schreiner PR: Diamonds are a chemist's best friend: Diamondoid chemistry beyond adamantane. Angew. Chem.-Int. Ed. Engl. 47, (2008) 2. Grichko VP, Shenderova OA: Nanodiamond: designing the bio-platform. Ultrananocryst. Diamond 2006, Stiborová, M, Sopko, B., Hodek, P., Frei, E., Schmeisser, H.H., Hudeček, J.: The binding of aristolochic acid I to the active site of human cytochromes P450 1A1 and 1A2 explains their potential toreductively activate this human carcinogen. Cancer Lett. 229, (2005)

11 Tato práce byla citována 8x 1. Xiao Y, Ge M, Xue X, et al.: Hepatic cytochrome P450s metabolize aristolochic acid and reduce its kidney toxicity. Kidney Int. 73, (2008) 2. Chen T: Genotoxicity of aristolochic acid: A review. J. Food Drug Anal. 15, (2007) 3. Wu KY, Jiang LP, Cao J, et al.: Genotoxic effect and nitrative DNA damage in HepG2 cells exposed to aristolochic acid. Mutation Res. 630, (2007) *4. Wahlstrom JL, Rock DA, Slatter JG, Wienkers LC: Advances in predicting CYPmediated drug interactions in the drug discovery setting. Expert. Opin. Drug. Discov. 1, (2006) 5. Mandlekar S, Hong JL, Kong ANT: Modulation of metabolic enzymes by dietary phytochemicals. Curr. Drug. Metabol. 7, (2006) *6. V Kairys, MK Gilson, MX Fernandes: Using Protein Homology Models for Structure- Based Studies: Approaches to Model Refinement. TheScientificWorldJournal 6, (2006) 7. Mei N, Arlt VM, Phillips DH, et al: DNA adduct formation and mutation induction by aristolochic acid in rat kidney and liver. Mutation Res (2006) *8. Qiao H-X, Li L-D, Wu L-M: Molecular cellular toxicology of aristolochic acid and its advances Chin J Pharmacol Toxicol (Zhongguo Yaolixue Yu Dulixue Zazhi) 27, (2006) 3.24 Anzenbacherová, E., Hudeček, J., Murgida, D., Hildebrandt, P., Marchal, S., Lange, R., Anzenbacher, P.. Active sites of two orthologous cytochromes P4502E1: Differences revealed by spectroscopic methods. Biochem. Biophys. Res. Commun. 338, (2005) Tato práce byla citována 1x Smith SV, Robinson RC, Smith TG, et al.: Rapid conformational dynamics of cytochrome p450 2E1 in a natural biological membrane environment. Biochemistry 45, (2006) 3.26 Stiborová, M., Bořek-Dohalská, L., Aimová, D., Kotrbová, V., Kukačková, K., Janouchová, K., Rupertová, M., Ryšlavá, H., Hudeček, J., Frei, E.: Oxidation pattern of the anticancer drug ellipticine by hepatic microsomes - Similarity between human and rat systems. Gen. Physiol. Biophys. 25, (2006) Tato práce byla citována 1x Kang HJ, Song IS, Lee SS, et al.: Effects of dietary salt on the expression of drug transporters, cytochrome P4503a, and nuclear receptors in rats. Xenobiotica 38, (2008) 3.27 Hudeček, J., Hodek, P., Anzenbacherová, E., Anzenbacher, P.: Structural analysis of cytochromes P450 shows differences in flexibility of heme 2- and 4-vinyls. Biochim. Biophys. Acta 1770, (2007) Tato práce byla citována 4x 1. Mendieta-Wejebe JE, Rosales-Hernandez MC, Rios H, et al.: Comparing the electronic properties and docking calculations of heme derivatives on CYP2B4. J.

12 Mol. Modeling 14, (2008) 2.Bonifacio A, Millo D, Keizers PHJ, et al.: Active-site structure, binding and redox activity of the heme-thiolate enzyme CYP2D6 immobilized on coated Ag electrodes: a surface-enhanced resonance Raman scattering study. J. Biol. Inorg. Chem. 13, (2008) *3. Bonifacio A: Resonance Raman spectroscopy of human cytochrome P450 2D6 in solution and on nanostructured metal surfaces. Vrije Univ. Amsterdam, dokt. disertace (2007) 4. Lepesheva GI, Seliskar M, Knutson CG, et al.: Conformational dynamics in the F/G segment of CYP51 from Mycobacterium tuberculosis monitored by FRET. Arch. Biochem. Biophys. 464, (2007) 4.1 Anzenbacher, P., Hudeček, J.: Diferenční a derivační spektrofotometrie, použití ke studiu proteinů. Chem. Listy 75, (1981) Tato práce byla citována 2x 1. Kalous V: Structure of orosomucoid - An example of the study of a glycoprotein investigated by physicochemical methods. Chem. Listy 94, (2000) 2. Kalal P, Kalous V: The tyrosyl and tryptophyl residues of orosomucoid studied by difference and derivative spectrophotometry. Coll. Czech. Chem. Commun. 49, (1984) 7.1 Stiborová, M., Hudeček, J., Hodek, P., Frei, E.: Cytochromy P-450 a lidské zdraví. Chem. Listy 93, (1999) Tato práce byla citována 1x *Široká Z, Drastichová J: Biochemical markers of aquatic environment contamination - cytochrome P450 in fish. Acta Veter. Brno 73, (2004) 7.2. Stiborová, M., Hudeček, J., Páca, J.: Enzymové systémy biotransformující cizorodé látky. Bull. Čes. Spol. Biochem. Mol. Biol. 28, (2000) Tato práce byla citována 1x *Borovanský J, Elleder M: Melanosome degradation: Fact or fiction. Pigment Cell Res. 16, (2003)