메뉴 건너뛰기




Volumn 8, Issue 1, 2013, Pages 71-81

Transition states, analogues, and drug development

Author keywords

[No Author keywords available]

Indexed keywords

5' METHYLTHIOADENOSINE PHOSPHORYLASE; FORODESINE; INDINAVIR; MENAQUINONE; NUCLEOSIDASE; PURINE NUCLEOSIDE PHOSPHORYLASE; RIBOSOME INACTIVATING PROTEIN;

EID: 84872556816     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb300631k     Document Type: Review
Times cited : (115)

References (94)
  • 1
    • 0033136041 scopus 로고    scopus 로고
    • Conformational aspects of inhibitor design: Enzyme-substrate interactions in the transition state
    • DOI 10.1016/S0968-0896(98)00247-8, PII S0968089698002478
    • Wolfenden, R. (1999) Conformational aspects of inhibitor design: enzyme-substrate interactions in the transition state Bioorg. Med. Chem. 7, 647-652 (Pubitemid 29238061)
    • (1999) Bioorganic and Medicinal Chemistry , vol.7 , Issue.5 , pp. 647-652
    • Wolfenden, R.1
  • 2
    • 79959420922 scopus 로고    scopus 로고
    • Enzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes
    • Schramm, V. L. (2011) Enzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes Annu. Rev. Biochem. 80, 703-732
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 703-732
    • Schramm, V.L.1
  • 4
    • 68049093016 scopus 로고    scopus 로고
    • Enzymatic transition states and dynamic motion in barrier crossing
    • Schwartz, S. D. and Schramm, V. L. (2009) Enzymatic transition states and dynamic motion in barrier crossing Nat. Chem. Biol. 5, 551-558
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 551-558
    • Schwartz, S.D.1    Schramm, V.L.2
  • 5
    • 78650157687 scopus 로고    scopus 로고
    • Conformational dynamics in human purine nucleoside phosphorylase with reactants and transition-state analogues
    • Hirschi, J. S., Arora, K., Brooks, C. L., 3rd, and Schramm, V. L. (2010) Conformational dynamics in human purine nucleoside phosphorylase with reactants and transition-state analogues J. Phys. Chem. B 114, 16263-16272
    • (2010) J. Phys. Chem. B , vol.114 , pp. 16263-16272
    • Hirschi, J.S.1    Arora, K.2    Brooks III, C.L.3    Schramm, V.L.4
  • 6
    • 0034604660 scopus 로고    scopus 로고
    • Femtochemistry: Atomic-scale dynamics of the chemical bond using ultrafast lasers (Nobel lecture)
    • DOI 10.1002/1521-3773(20000804)39:15<2586::AID-ANIE2586>3.0.CO;2-O
    • Zewail, A. H. (2000) Femtochemistry: Atomic-scale dynamics of the chemical bond using ultrafast lasers (Nobel Lecture) Angew. Chem., Int. Ed. 39, 2586-2631 (Pubitemid 30629182)
    • (2000) Angewandte Chemie - International Edition , vol.39 , Issue.15 , pp. 2586-2631
    • Zewail, A.H.1
  • 8
    • 0000925575 scopus 로고
    • Femtosecond vibrational transition-state dynamics in a chemical reaction
    • Pedersen, S., Bañares, L., and Zewail, A. H. (1992) Femtosecond vibrational transition-state dynamics in a chemical reaction J. Chem. Phys. 97, 8801-8804
    • (1992) J. Chem. Phys. , vol.97 , pp. 8801-8804
    • Pedersen, S.1    Bañares, L.2    Zewail, A.H.3
  • 9
    • 0345082644 scopus 로고
    • Direct observation of the transition state
    • Polanyi, J. C. and Zewail, A. H. (1995) Direct observation of the transition state Acc. Chem. Res. 28, 119-132
    • (1995) Acc. Chem. Res. , vol.28 , pp. 119-132
    • Polanyi, J.C.1    Zewail, A.H.2
  • 10
    • 0036424048 scopus 로고    scopus 로고
    • Transition path sampling: Throwing ropes over rough mountain passes in the dark
    • Bolhuis, P. G., Chandler, D., Dellago, C., and Geissler, P. L. (2002) Transition path sampling: throwing ropes over rough mountain passes in the dark Annu. Rev. Phys. Chem. 53, 291-318
    • (2002) Annu. Rev. Phys. Chem. , vol.53 , pp. 291-318
    • Bolhuis, P.G.1    Chandler, D.2    Dellago, C.3    Geissler, P.L.4
  • 11
    • 0000801009 scopus 로고    scopus 로고
    • Efficient transition path sampling: Application to Lennard-Jones cluster rearrangements
    • Dellago, C., Bolhuis, P. G., and Chandler, D. (1998) Efficient transition path sampling: application to Lennard-Jones cluster rearrangements J. Chem. Phys. 108, 9236-9245 (Pubitemid 128571335)
    • (1998) Journal of Chemical Physics , vol.108 , Issue.22 , pp. 9236-9245
    • Dellago, C.1    Bolhuis, P.G.2    Chandler, D.3
  • 12
    • 26444486352 scopus 로고    scopus 로고
    • How enzyme dynamics helps catalyze a reaction in atomic detail: A transition path sampling study
    • DOI 10.1021/ja043320h
    • Basner, J. E. and Schwartz, S. D. (2005) How enzyme dynamics helps catalyze a chemical reaction in atomic detail: a transition path sampling study J. Am. Chem. Soc. 127, 13822-13831 (Pubitemid 41437032)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.40 , pp. 13822-13831
    • Basner, J.E.1    Schwartz, S.D.2
  • 13
    • 84255214322 scopus 로고    scopus 로고
    • Protein dynamics and enzymatic chemical barrier passage
    • Antoniou, D. and Schwartz, S. D. (2011) Protein dynamics and enzymatic chemical barrier passage J. Phys. Chem. B 115, 15147-15158
    • (2011) J. Phys. Chem. B , vol.115 , pp. 15147-15158
    • Antoniou, D.1    Schwartz, S.D.2
  • 14
    • 68049085675 scopus 로고    scopus 로고
    • A 21st century revisionist's view at a turning point in enzymology
    • Nagel, Z. D. and Klinman, J. P. (2009) A 21st century revisionist's view at a turning point in enzymology Nat. Chem. Biol. 5, 543-550
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 543-550
    • Nagel, Z.D.1    Klinman, J.P.2
  • 15
    • 0042355696 scopus 로고    scopus 로고
    • Just a near attack conformer for catalysis (chorismate to prephenate rearrangements in water, antibody, enzymes, and their mutants)
    • DOI 10.1021/ja0357846
    • Hur, S. and Bruice, T. C. (2003) Just a near attack conformer for catalysis (chorismate to prephenate rearrangements in water, antibody, enzymes, and their mutants) J. Am. Chem. Soc. 125, 10540-10542 (Pubitemid 37055905)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.35 , pp. 10540-10542
    • Hur, S.1    Bruice, T.C.2
  • 16
    • 79959431109 scopus 로고    scopus 로고
    • Benchmark reaction rates, the stability of biological molecules in water, and the evolution of catalytic power in enzymes
    • Wolfenden, R. (2011) Benchmark reaction rates, the stability of biological molecules in water, and the evolution of catalytic power in enzymes Annu. Rev. Biochem. 80, 645-667
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 645-667
    • Wolfenden, R.1
  • 17
    • 81755172909 scopus 로고    scopus 로고
    • Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme
    • Silva, R. G., Murkin, A. S., and Schramm, V. L. (2011) Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme Proc. Natl. Acad. Sci. U.S.A. 108, 18661-18665
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 18661-18665
    • Silva, R.G.1    Murkin, A.S.2    Schramm, V.L.3
  • 18
    • 82555185640 scopus 로고    scopus 로고
    • Mass-dependent bond vibrational dynamics influence catalysis by HIV-1 protease
    • Kipp, D. R., Silva, R. G., and Schramm, V. L. (2011) Mass-dependent bond vibrational dynamics influence catalysis by HIV-1 protease J. Am. Chem. Soc. 133, 19358-19361
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 19358-19361
    • Kipp, D.R.1    Silva, R.G.2    Schramm, V.L.3
  • 19
    • 84867065402 scopus 로고    scopus 로고
    • Capturing the reaction pathway in near-atomic-resolution crystal structures of HIV-1 protease
    • Shen, C. H., Tie, Y., Yu, X., Wang, Y. F., Kovalevsky, A. Y., Harrison, R. W., and Weber, I. T. (2012) Capturing the reaction pathway in near-atomic-resolution crystal structures of HIV-1 protease Biochemistry 51, 7726-7732
    • (2012) Biochemistry , vol.51 , pp. 7726-7732
    • Shen, C.H.1    Tie, Y.2    Yu, X.3    Wang, Y.F.4    Kovalevsky, A.Y.5    Harrison, R.W.6    Weber, I.T.7
  • 21
    • 0028920872 scopus 로고
    • Isotope effects: Determination of enzyme transition state structure
    • Cleland, W. W. (1995) Isotope effects: determination of enzyme transition state structure Methods Enzymol. 249, 341-373
    • (1995) Methods Enzymol. , vol.249 , pp. 341-373
    • Cleland, W.W.1
  • 22
    • 0016904563 scopus 로고
    • Transition state analog inhibitors and enzyme catalysis
    • Wolfenden, R. (1976) Transition state analog inhibitors and enzyme catalysis Annu. Rev. Biophys. Bioeng. 5, 271-306
    • (1976) Annu. Rev. Biophys. Bioeng. , vol.5 , pp. 271-306
    • Wolfenden, R.1
  • 23
    • 0014681301 scopus 로고
    • Transition state analogues for enzyme catalysis
    • Wolfenden, R. (1969) Transition state analogues for enzyme catalysis Nature 223, 704-705
    • (1969) Nature , vol.223 , pp. 704-705
    • Wolfenden, R.1
  • 26
    • 0032860328 scopus 로고    scopus 로고
    • Enzymatic transition-state analysis and transition-state analogs
    • DOI 10.1016/S0076-6879(99)08015-5
    • Schramm, V. L. (1999) Enzymatic transition-sate analysis and transition-state analogs Methods Enzymol. 308, 301-355 (Pubitemid 29418909)
    • (1999) Methods in Enzymology , vol.308 , pp. 301-355
    • Schramm, V.L.1
  • 28
    • 84912208190 scopus 로고
    • Chemical achievement and hope for the future
    • Pauling, L. (1948) Chemical achievement and hope for the future Am. Sci. 36, 51-58
    • (1948) Am. Sci. , vol.36 , pp. 51-58
    • Pauling, L.1
  • 30
    • 0035695812 scopus 로고    scopus 로고
    • Atomic motion in enzymatic reaction coordinates
    • DOI 10.1016/S0959-440X(01)00269-X
    • Schramm, V. L. and Shi, W. (2001) Atomic motion in enzymatic reaction coordinates Curr. Opin. Struct. Biol. 11, 657-665 (Pubitemid 34076625)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.6 , pp. 657-665
    • Schramm, V.L.1    Shi, W.2
  • 32
    • 78650152378 scopus 로고    scopus 로고
    • Slow conformational motions that favor sub-picosecond motions important for catalysis
    • Exequiel, J. R., Pineda, T., Antoniou, D., and Schwartz, S. D. (2010) Slow conformational motions that favor sub-picosecond motions important for catalysis J. Phys. Chem. B 114, 15985-15990
    • (2010) J. Phys. Chem. B , vol.114 , pp. 15985-15990
    • Exequiel, J.R.1    Pineda, T.2    Antoniou, D.3    Schwartz, S.D.4
  • 33
    • 0346726109 scopus 로고    scopus 로고
    • How Enzymes Work: Analysis by Modern Rate Theory and Computer Simulations
    • DOI 10.1126/science.1088172
    • Garcia-Viloca, M., Gao, J., Karplus, M., and Truhlar, D. G. (2004) How enzymes work: analysis by modern rate theory and computer simulations Science 303, 186-195 (Pubitemid 38057561)
    • (2004) Science , vol.303 , Issue.5655 , pp. 186-195
    • Garcia-Viloca, M.1    Gao, J.2    Karplus, M.3    Truhlar, D.G.4
  • 35
    • 0016765942 scopus 로고
    • Tight-binding inhibitors-II. Non-steady state nature of inhibition of milk xanthine oxidase by allopurinol and alloxanthine and of human erythrocytic adenosine deaminase by coformycin
    • Cha, S., Agarwal, R. P., and Parks, R. E., Jr. (1975) Tight-binding inhibitors-II. Non-steady state nature of inhibition of milk xanthine oxidase by allopurinol and alloxanthine and of human erythrocytic adenosine deaminase by coformycin Biochem. Pharmacol. 24, 2187-2197
    • (1975) Biochem. Pharmacol. , vol.24 , pp. 2187-2197
    • Cha, S.1    Agarwal, R.P.2    Parks, Jr.R.E.3
  • 36
    • 84869067961 scopus 로고    scopus 로고
    • Methylthioadenosine deaminase in an alternative quorum sensing pathway in Pseudomonas aeruginosa
    • Guan, R., Ho, M. C., Fröhlich, R. F., Tyler, P. C., Almo, S. C., and Schramm, V. L. (2012) Methylthioadenosine deaminase in an alternative quorum sensing pathway in Pseudomonas aeruginosa Biochemistry 51, 9094-9103
    • (2012) Biochemistry , vol.51 , pp. 9094-9103
    • Guan, R.1    Ho, M.C.2    Fröhlich, R.F.3    Tyler, P.C.4    Almo, S.C.5    Schramm, V.L.6
  • 37
    • 84866695338 scopus 로고    scopus 로고
    • Femtomolar inhibitors bind to 5′-methylthioadenosine nucleosidases with favorable enthalpy and entropy
    • Thomas, K., Haapalainen, A. M., Burgos, E. S., Evans, G. B., Tyler, P. C., Gulab, S., Guan, R., and Schramm, V. L. (2012) Femtomolar inhibitors bind to 5′-methylthioadenosine nucleosidases with favorable enthalpy and entropy Biochemistry 51, 7541-7550
    • (2012) Biochemistry , vol.51 , pp. 7541-7550
    • Thomas, K.1    Haapalainen, A.M.2    Burgos, E.S.3    Evans, G.B.4    Tyler, P.C.5    Gulab, S.6    Guan, R.7    Schramm, V.L.8
  • 39
    • 84864964706 scopus 로고    scopus 로고
    • Transition state analogue inhibitors of human methylthioadenosine phosphorylase and bacterial methylthioadenosine/S-adenosylhomocysteine nucleosidase incorporating acyclic ribooxacarbenium ion mimics
    • Clinch, K., Evans, G. B., Fröhlich, R. F., Gulab, S. A., Gutierrez, J. A., Mason, J. M., Schramm, V. L., Tyler, P. C., and Woolhouse, A. D. (2012) Transition state analogue inhibitors of human methylthioadenosine phosphorylase and bacterial methylthioadenosine/S-adenosylhomocysteine nucleosidase incorporating acyclic ribooxacarbenium ion mimics Bioorg. Med. Chem. 20, 5181-5187
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 5181-5187
    • Clinch, K.1    Evans, G.B.2    Fröhlich, R.F.3    Gulab, S.A.4    Gutierrez, J.A.5    Mason, J.M.6    Schramm, V.L.7    Tyler, P.C.8    Woolhouse, A.D.9
  • 40
    • 0021152172 scopus 로고
    • Effects of allosteric activation on the primary and secondary kinetic isotope effects for three AMP nucleosidases
    • Parkin, D. W. and Schramm, V. L. (1984) Effects of allosteric activation on the primary and secondary kinetic isotope effects for three AMP nucleosidases J. Biol. Chem. 259, 9418-25 (Pubitemid 14060500)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.15 , pp. 9418-9425
    • Parkin, D.W.1    Schramm, V.L.2
  • 41
    • 0023129244 scopus 로고
    • Transition-state structures for N-glycoside hydrolysis of AMP by acid and by AMP nucleosidase in the presence and absence of allosteric activator
    • DOI 10.1021/bi00377a037
    • Mentch, F., Parkin, D. W., and Schramm, V. L. (1987) Transition-state structures for N-glycoside hydrolysis of AMP by acid and by AMP nucleosidase in the presence and absence of allosteric activator Biochemistry 26, 921-930 (Pubitemid 17021074)
    • (1987) Biochemistry , vol.26 , Issue.3 , pp. 921-930
    • Mentch, F.1    Parkin, D.W.2    Schramm, V.L.3
  • 42
    • 0023127914 scopus 로고
    • Catalytic and allosteric mechanism of AMP nucleosidase from primary, β-secondary, and multiple heavy atom kinetic isotope effects
    • DOI 10.1021/bi00377a036
    • Parkin, D. W. and Schramm, V. L. (1987) Catalytic and allosteric mechanism of AMP nucleosidase from primary, beta-secondary, and multiple heavy atom kinetic isotope effects Biochemistry 26, 913-920 (Pubitemid 17021073)
    • (1987) Biochemistry , vol.26 , Issue.3 , pp. 913-920
    • Parkin, D.W.1    Schramm, V.L.2
  • 44
    • 0028074975 scopus 로고
    • Electrostatic potential surface analysis of the transition state for AMP nucleosidase and for formycin 5'-phosphate, a transition-state inhibitor
    • DOI 10.1021/bi00196a005
    • Ehrlich, J. I. and Schramm, V. L. (1994) Electrostatic potential surface analysis of the transition state for AMP nucleosidase and for formycin 5′-phosphate, a transition-state inhibitor Biochemistry 33, 8890-8896 (Pubitemid 24257996)
    • (1994) Biochemistry , vol.33 , Issue.30 , pp. 8890-8896
    • Ehrlich, J.I.1    Schramm, V.L.2
  • 45
    • 0008501948 scopus 로고
    • The enzymatic cleavage of adenylic acid to adenine and ribose 5-phosphate
    • Hurwitz, J., Heppel, L. A., and Horecker, B. L. (1957) The enzymatic cleavage of adenylic acid to adenine and ribose 5-phosphate J. Biol. Chem. 226, 525-540
    • (1957) J. Biol. Chem. , vol.226 , pp. 525-540
    • Hurwitz, J.1    Heppel, L.A.2    Horecker, B.L.3
  • 46
    • 34250201455 scopus 로고    scopus 로고
    • Transition state analysis of acid-catalyzed dAMP hydrolysis
    • DOI 10.1021/ja067371l
    • McCann, J. A. and Berti, P. J. (2007) Transition state analysis of acid-catalyzed dAMP hydrolysis J. Am. Chem. Soc. 129, 7055-7064 (Pubitemid 46903270)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.22 , pp. 7055-7064
    • McCann, J.A.B.1    Berti, P.J.2
  • 47
    • 0017140479 scopus 로고
    • Comparison of initial velocity and binding data for allosteric adenosine monophosphate nucleosidase
    • Schramm, V. L. (1976) Comparison of initial velocity and binding data for allosteric adenosine monophosphate nucleosidase J. Biol. Chem. 251, 3417-3424
    • (1976) J. Biol. Chem. , vol.251 , pp. 3417-3424
    • Schramm, V.L.1
  • 49
    • 4143089174 scopus 로고    scopus 로고
    • Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases
    • DOI 10.1016/j.str.2004.05.015, PII S0969212604002175
    • Zhang, Y., Cottet, S. E., and Ealick, S. E. (2004) Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases Structure 12, 1383-1394 (Pubitemid 39092083)
    • (2004) Structure , vol.12 , Issue.8 , pp. 1383-1394
    • Zhang, Y.1    Cottet, S.E.2    Ealick, S.E.3
  • 50
    • 0019132908 scopus 로고
    • Adenylate degradation in Escherichia coli. The role of AMP nucleosidase and properties of the purified enzyme
    • Leung, H,B. and Schramm, V. L. (1980) Adenylate degradation in Escherichia coli. The role of AMP nucleosidase and properties of the purified enzyme J. Biol. Chem. 255, 10867-10874 (Pubitemid 11171742)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.22 , pp. 10867-10874
    • Leung, H.B.1    Schramm, V.L.2
  • 51
    • 40949094869 scopus 로고    scopus 로고
    • An AMP nucleosidase gene knockout in Escherichia coli elevates intracellular ATP levels and increases cold tolerance
    • DOI 10.1098/rsbl.2007.0432, PII 1125660826183P39
    • Morrison, B. A. and Shain, D. H. (2008) An AMP nucleosidase gene knockout in Escherichia coli elevates intracellular ATP levels and increases cold tolerance Biol. Lett. 4, 53-56 (Pubitemid 351598296)
    • (2008) Biology Letters , vol.4 , Issue.1 , pp. 53-56
    • Morrison, B.A.1    Shain, D.H.2
  • 52
    • 79959486576 scopus 로고    scopus 로고
    • Manipulations of AMP metabolic genes increase growth rate and cold tolerance in Escherichia coli: Implications for psychrophilic evolution
    • Parry, B. R. and Shain, D. H. (2011) Manipulations of AMP metabolic genes increase growth rate and cold tolerance in Escherichia coli: implications for psychrophilic evolution Mol. Biol. Evol. 28, 2139-2145
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2139-2145
    • Parry, B.R.1    Shain, D.H.2
  • 53
    • 84919573117 scopus 로고
    • Nucleoside-phosphorylase deficiency in a child with severely defective T-cell immunity and normal B-cell immunity
    • Giblett, E. R., Ammann, A. J., Wara, D. W., Sandman, R., and Diamond, L. K. (1975) Nucleoside-phosphorylase deficiency in a child with severely defective T-cell immunity and normal B-cell immunity Lancet 1, 1010-1013
    • (1975) Lancet , vol.1 , pp. 1010-1013
    • Giblett, E.R.1    Ammann, A.J.2    Wara, D.W.3    Sandman, R.4    Diamond, L.K.5
  • 54
    • 0017054309 scopus 로고
    • Abnormal purine metabolism and purine overproduction in a patient deficient in purine nucleoside phosphorylase
    • Cohen, A., Doyle, D., Martin, D. W., Jr., and Ammann, A. J. (1976) Abnormal purine metabolism and purine overproduction in a patient deficient in purine nucleoside phosphorylase New Engl. J. Med. 295, 1449-1454 (Pubitemid 8003705)
    • (1976) New England Journal of Medicine , vol.295 , Issue.26 , pp. 1449-1454
    • Cohen, A.1    Doyle, D.2    Martin Jr., D.W.3    Ammann, A.J.4
  • 55
    • 0017807276 scopus 로고
    • Deoxyguanosine triphosphate as a possible toxic metabolite in the immunodeficiency associated with purine nucleoside phosphorylase deficiency
    • Cohen, A., Gudas, L. J., Ammann, A. J., Staal, G. E., and Martin, D. W., Jr. (1978) Deoxyguanosine triphosphate as a possible toxic metabolite in the immunodeficiency associated with purine nucleoside phosphorylase deficiency J. Clin. Invest. 61, 1405-1409
    • (1978) J. Clin. Invest. , vol.61 , pp. 1405-1409
    • Cohen, A.1    Gudas, L.J.2    Ammann, A.J.3    Staal, G.E.4    Martin, Jr.D.W.5
  • 56
    • 0343517471 scopus 로고    scopus 로고
    • Inhibitors of the enzyme purine nucleoside phosphorylase as potential therapy for psoriasis
    • Morris, P. E., and Omura, G. A. (2000) Inhibitors of the enzyme purine nucleoside phosphorylase as potential therapy for psoriasis Curr. Pharm. Des. 6, 943-959 (Pubitemid 30409391)
    • (2000) Current Pharmaceutical Design , vol.6 , Issue.9 , pp. 943-959
    • Morris Jr., P.E.1    Omura, G.A.2
  • 57
    • 0027729453 scopus 로고
    • Purine nucleoside phosphorylase. Catalytic mechanism and transition-state analysis of the arsenolysis reaction
    • DOI 10.1021/bi00211a033
    • Kline, P. C. and Schramm, V. L. (1993) Purine nucleoside phosphorylase. Catalytic mechanism and transition-state analysis of the arsenolysis reaction Biochemistry 32, 13212-13219 (Pubitemid 24005930)
    • (1993) Biochemistry , vol.32 , Issue.48 , pp. 13212-13219
    • Kline, P.C.1    Schramm, V.L.2
  • 58
    • 0032537481 scopus 로고    scopus 로고
    • One-third-the-sites transition-state inhibitors for purine nucleoside phosphorylase
    • DOI 10.1021/bi980658d
    • Miles, R. W., Tyler, P. C., Furneaux, R. H., Bagdassarian, C. K., and Schramm, V. L. (1998) One-third-the-sites transition-state inhibitors for purine nucleoside phosphorylase Biochemistry 37, 8615-8621 (Pubitemid 28299598)
    • (1998) Biochemistry , vol.37 , Issue.24 , pp. 8615-8621
    • Miles, R.W.1    Tyler, P.C.2    Furneaux, R.H.3    Bagdassarian, C.K.4    Schramm, V.L.5
  • 61
    • 1042299983 scopus 로고    scopus 로고
    • Transition State Analysis for Human and Plasmodium falciparum Purine Nucleoside Phosphorylases
    • DOI 10.1021/bi0359123
    • Lewandowicz, A. and Schramm, V. L. (2004) Transition state analysis for human and Plasmodium falciparum purine nucleoside phosphorylases Biochemistry 43, 1458-1468 (Pubitemid 38200551)
    • (2004) Biochemistry , vol.43 , Issue.6 , pp. 1458-1468
    • Lewandowicz, A.1    Schramm, V.L.2
  • 62
    • 0242691662 scopus 로고    scopus 로고
    • Synthesis of Second-Generation Transition State Analogues of Human Purine Nucleoside Phosphorylase
    • DOI 10.1021/jm030305z
    • Evans, G. B., Furneaux, R. H., Lewandowicz, A., Schramm, V. L., and Tyler, P. C. (2003) Synthesis of second-generation transition state analogues of human purine nucleoside phosphorylase J. Med. Chem. 46, 5271-5276 (Pubitemid 37414195)
    • (2003) Journal of Medicinal Chemistry , vol.46 , Issue.24 , pp. 5271-5276
    • Evans, G.B.1    Furneaux, R.H.2    Lewandowicz, A.3    Schramm, V.L.4    Tyler, P.C.5
  • 64
    • 0036479245 scopus 로고    scopus 로고
    • Purine-less death in Plasmodium falciparum induced by immucillin-H, a transition state analogue of purine nucleoside phosphorylase
    • DOI 10.1074/jbc.M105906200
    • Kicska, G. A., Tyler, P. C., Evans, G. B., Furneaux, R. H., Schramm, V. L., and Kim, K. (2002) Purine-less death in Plasmodium falciparum induced by immucillin-H, a transition state analogue of purine nucleoside phosphorylase J. Biol. Chem. 277, 3226-3231 (Pubitemid 34953185)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3226-3231
    • Kicska, G.A.1    Tyler, P.C.2    Evans, G.B.3    Furneaux, R.H.4    Schramm, V.L.5    Kim, K.6
  • 65
    • 34347227434 scopus 로고    scopus 로고
    • Transition-state variation in human, bovine, and Plasmodium falciparum adenosine deaminases
    • DOI 10.1021/ja072122y
    • Luo, M., Singh, V., Taylor, E. A., and Schramm, V. L. (2007) Transition-state variation in human, bovine, and Plasmodium falciparum adenosine deaminases J. Am. Chem. Soc. 129, 8008-8017 (Pubitemid 46998200)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.25 , pp. 8008-8017
    • Luo, M.1    Singh, V.2    Taylor, E.A.3    Schramm, V.L.4
  • 67
    • 33750979005 scopus 로고    scopus 로고
    • Transition-state structure of human 5′-methylthioadenosine phosphorylase
    • DOI 10.1021/ja065419p
    • Singh, V. and Schramm, V. L. (2006) Transition-state structure of human 5′-methylthioadenosine phosphorylase J. Am. Chem. Soc. 128, 14691-14696 (Pubitemid 44749872)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.45 , pp. 14691-14696
    • Singh, V.1    Schramm, V.L.2
  • 68
    • 2542531592 scopus 로고    scopus 로고
    • Targeting the polyamine pathway with transition-state analogue inhibitors of 5′-methylthioadenosine phosphorylase
    • DOI 10.1021/jm0306475
    • Evans, G. B., Furneaux, R. H., Schramm, V. L., Singh, V., and Tyler, P. C. (2004) Targeting the polyamine pathway with transition-state analogue inhibitors of 5′-methylthioadenosine phosphorylase J. Med. Chem. 47, 3275-3281 (Pubitemid 38702720)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.12 , pp. 3275-3281
    • Evans, G.B.1    Furneaux, R.H.2    Schramm, V.L.3    Singh, V.4    Tyler, P.C.5
  • 69
    • 34547102012 scopus 로고    scopus 로고
    • A transition state analogue of 5′-methylthioadenosine phosphorylase induces apoptosis in head and neck cancers
    • DOI 10.1074/jbc.M702287200
    • Basu, I., Cordovano, G., Das, I., Belbin, T. J., Guha, C., and Schramm, V. L. (2007) A transition state analogue of 5′-methylthioadenosine phosphorylase induces apoptosis in head and neck cancers J. Biol. Chem. 282, 21477-21486 (Pubitemid 47099931)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.29 , pp. 21477-21486
    • Basu, I.1    Cordovano, G.2    Das, I.3    Belbin, T.J.4    Guha, C.5    Schramm, V.L.6
  • 70
    • 79953000186 scopus 로고    scopus 로고
    • Growth and metastases of human lung cancer are inhibited in mouse xenografts by a transition state analogue of 5′-methylthioadenosine phosphorylase
    • Basu, I., Locker, J., Cassera, M. B., Belbin, T. J., Merino, E. F., Dong, X., Hemeon, I., Evans, G. B., Guha, C., and Schramm, V. L. (2011) Growth and metastases of human lung cancer are inhibited in mouse xenografts by a transition state analogue of 5′-methylthioadenosine phosphorylase J. Biol. Chem. 286, 4902-4911
    • (2011) J. Biol. Chem. , vol.286 , pp. 4902-4911
    • Basu, I.1    Locker, J.2    Cassera, M.B.3    Belbin, T.J.4    Merino, E.F.5    Dong, X.6    Hemeon, I.7    Evans, G.B.8    Guha, C.9    Schramm, V.L.10
  • 72
    • 0034686760 scopus 로고    scopus 로고
    • Transition-state analysis for depurination of DNA by ricin A-chain
    • DOI 10.1021/ja992751a
    • Chen, X.-Y., Berti, P. J., and Schramm, V. L. (2000) Transition state analysis for depurination of DNA by Ricin A-chain J. Am. Chem. Soc. 122, 6527-6534 (Pubitemid 30489970)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.28 , pp. 6527-6534
    • Chen, X.-Y.1    Berti, P.J.2    Schramm, V.L.3
  • 73
    • 34247857453 scopus 로고    scopus 로고
    • Circular DNA and DNA/RNA hybrid molecules as scaffolds for Ricin inhibitor design
    • DOI 10.1021/ja068054h
    • Sturm, M. B., Roday, S., and Schramm, V. L. (2007) Circular DNA and DNA/RNA hybrid molecules as scaffolds for ricin inhibitor design J. Am. Chem. Soc. 129, 5544-5550 (Pubitemid 46697642)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.17 , pp. 5544-5550
    • Sturm, M.B.1    Roday, S.2    Schramm, V.L.3
  • 74
    • 70350072944 scopus 로고    scopus 로고
    • Transition state analogues rescue ribosomes from saporin-L1 ribosome inactivating protein
    • Sturm, M. B., Tyler, P. C., Evans, G. B., and Schramm, V. L. (2009) Transition state analogues rescue ribosomes from saporin-L1 ribosome inactivating protein Biochemistry 48, 9941-9948
    • (2009) Biochemistry , vol.48 , pp. 9941-9948
    • Sturm, M.B.1    Tyler, P.C.2    Evans, G.B.3    Schramm, V.L.4
  • 75
    • 73949090667 scopus 로고    scopus 로고
    • Transition state analogues in structures of ricin and saporin ribosome-inactivating proteins
    • Ho, M. C., Sturm, M. B., Almo, S. C., and Schramm, V. L. (2009) Transition state analogues in structures of ricin and saporin ribosome-inactivating proteins Proc. Natl. Acad. Sci. U.S.A. 106, 20276-20281
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 20276-20281
    • Ho, M.C.1    Sturm, M.B.2    Almo, S.C.3    Schramm, V.L.4
  • 76
    • 0014868746 scopus 로고
    • The cellular control of the synthesis and activity of the bacterial luminescent system
    • Nealson, K., Platt, T., and Hastings, J. W. (1970) The cellular control of the synthesis and activity of the bacterial luminescent system J. Bacteriol. 104, 313-322
    • (1970) J. Bacteriol. , vol.104 , pp. 313-322
    • Nealson, K.1    Platt, T.2    Hastings, J.W.3
  • 77
    • 84855865173 scopus 로고    scopus 로고
    • Modelling the onset of virulence in pathogenic bacteria
    • Kepseu, W. D., Van Gijsegem, F., and Sepulchre, J. A. (2012) Modelling the onset of virulence in pathogenic bacteria Methods Mol. Biol. 804, 501-517
    • (2012) Methods Mol. Biol. , vol.804 , pp. 501-517
    • Kepseu, W.D.1    Van Gijsegem, F.2    Sepulchre, J.A.3
  • 78
    • 84862091097 scopus 로고    scopus 로고
    • LsrR-mediated quorum sensing controls invasiveness of Salmonella typhimurium by regulating SPI-1 and flagella genes
    • Choi, J., Shin, D., Kim, M., Park, J., Lim, S., and Ryu, S. (2012) LsrR-mediated quorum sensing controls invasiveness of Salmonella typhimurium by regulating SPI-1 and flagella genes PLoS One 7, e37059
    • (2012) PLoS One , vol.7 , pp. 37059
    • Choi, J.1    Shin, D.2    Kim, M.3    Park, J.4    Lim, S.5    Ryu, S.6
  • 79
    • 84864006267 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa global regulator VqsR directly inhibits QscR to control quorum-sensing and virulence gene expression
    • Liang, H., Deng, X., Ji, Q., Sun, F., Shen, T., and He, C. (2012) The Pseudomonas aeruginosa global regulator VqsR directly inhibits QscR to control quorum-sensing and virulence gene expression J. Bacteriol. 194, 3098-3108
    • (2012) J. Bacteriol. , vol.194 , pp. 3098-3108
    • Liang, H.1    Deng, X.2    Ji, Q.3    Sun, F.4    Shen, T.5    He, C.6
  • 82
    • 23944446462 scopus 로고    scopus 로고
    • Transition state structure of 5′-methylthioadenosine/S- adenosylhomocysteine nucleosidase from Escherichia coli and its similarity to transition state analogues
    • DOI 10.1021/bi050863a
    • Singh, V., Lee, J. E., Núñez, S., Howell, P. L., and Schramm, V. L. (2005) Transition state structure of 5′- methylthioadenosine/S-adenosylhomocysteine nucleosidase from Escherichia coli and its similarity to transition state analogues Biochemistry 44, 11647-11659 (Pubitemid 41262698)
    • (2005) Biochemistry , vol.44 , Issue.35 , pp. 11647-11659
    • Singh, V.1    Lee, J.E.2    Nunez, S.3    Howell, P.L.4    Schramm, V.L.5
  • 83
    • 33947201538 scopus 로고    scopus 로고
    • Transition-state analysis of S. pneumoniae 5′-methylthioadenosine nucleosidase
    • DOI 10.1021/ja065082r
    • Singh, V. and Schramm, V. L. (2007) Transition-state analysis of S. pneumoniae 5′-methylthioadenosine nucleosidase J. Am. Chem. Soc. 129, 2783-2795 (Pubitemid 46417953)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.10 , pp. 2783-2795
    • Singh, V.1    Schramm, V.L.2
  • 84
    • 36148932926 scopus 로고    scopus 로고
    • Transition-state structure of Neisseria meningitides 5′- methylthioadenosine/S-adenosylhomocysteine nucleosidase
    • DOI 10.1021/ja0754204
    • Singh, V., Luo, M., Brown, R. L., Norris, G. E., and Schramm, V. L. (2007) Transition-state structure of Neisseria meningitides 5′- methylthioadenosine/S-adenosylhomocysteine nucleosidase J. Am. Chem. Soc. 129, 13831-13833 (Pubitemid 350106071)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.45 , pp. 13831-13833
    • Singh, V.1    Luo, M.2    Brown, R.L.3    Norris, G.E.4    Schramm, V.L.5
  • 87
    • 79957616242 scopus 로고    scopus 로고
    • 5′-methylthioadenosine nucleosidase is implicated in playing a key role in a modified futalosine pathway for menaquinone biosynthesis in Campylobacter jejuni
    • Li, X., Apel, D., Gaynor, E. C., and Tanner, M. E. (2011) 5′-methylthioadenosine nucleosidase is implicated in playing a key role in a modified futalosine pathway for menaquinone biosynthesis in Campylobacter jejuni J. Biol. Chem. 286, 19392-19398
    • (2011) J. Biol. Chem. , vol.286 , pp. 19392-19398
    • Li, X.1    Apel, D.2    Gaynor, E.C.3    Tanner, M.E.4
  • 88
  • 89
    • 84866483156 scopus 로고    scopus 로고
    • Menaquinone biosyntheses in microorganisms
    • Dairi, T. (2012) Menaquinone biosyntheses in microorganisms Methods Enzymol. 515, 107-22
    • (2012) Methods Enzymol. , vol.515 , pp. 107-122
    • Dairi, T.1
  • 91
    • 79951876264 scopus 로고    scopus 로고
    • Transition state analysis of the arsenolytic depyrimidination of thymidine by human thymidine phosphorylase
    • Schwartz, P. A., Vetticatt, M. J., and Schramm, V. L. (2011) Transition state analysis of the arsenolytic depyrimidination of thymidine by human thymidine phosphorylase Biochemistry 50, 1412-1420
    • (2011) Biochemistry , vol.50 , pp. 1412-1420
    • Schwartz, P.A.1    Vetticatt, M.J.2    Schramm, V.L.3
  • 92
    • 77957167437 scopus 로고    scopus 로고
    • Transition state analysis of thymidine hydrolysis by human thymidine phosphorylase
    • Schwartz, P. A., Vetticatt, M. J., and Schramm, V. L. (2010) Transition state analysis of thymidine hydrolysis by human thymidine phosphorylase J. Am. Chem. Soc. 132, 13425-13433
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 13425-13433
    • Schwartz, P.A.1    Vetticatt, M.J.2    Schramm, V.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.