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Volumn 9, Issue 12, 2014, Pages 2875-2882

Phosphatase-inert glucosamine 6-phosphate mimics serve as actuators of the glms riboswitch

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSAMINE DERIVATIVE; MALONIC ACID DERIVATIVE; PHOSPHONIC ACID DERIVATIVE; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; COMPONENT S, GLUTAMATE MUTASE PROTEIN, BACTERIA; GLUCOSAMINE; GLUCOSAMINE 6-PHOSPHATE; GLUCOSE 6 PHOSPHATE; PHOSPHATASE; PROTEIN BINDING; RIBOSWITCH; RIBOZYME;

EID: 84919615317     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb500458f     Document Type: Article
Times cited : (26)

References (58)
  • 2
    • 84872543206 scopus 로고    scopus 로고
    • A Decade of Riboswitches
    • Serganov, A. and Nudler, E. (2013) A Decade of Riboswitches Cell 152, 17-24
    • (2013) Cell , vol.152 , pp. 17-24
    • Serganov, A.1    Nudler, E.2
  • 3
    • 1642586299 scopus 로고    scopus 로고
    • Control of gene expression by a natural metabolite-responsive ribozyme
    • Winkler, W. C., Nahvi, A., Roth, A., Collins, J. A., and Breaker, R. R. (2004) Control of gene expression by a natural metabolite-responsive ribozyme Nature 428, 281-286
    • (2004) Nature , vol.428 , pp. 281-286
    • Winkler, W.C.1    Nahvi, A.2    Roth, A.3    Collins, J.A.4    Breaker, R.R.5
  • 4
    • 0037013983 scopus 로고    scopus 로고
    • Glucosamine-6-phosphate synthase: The multi-facets enzyme
    • Milewski, S. (2002) Glucosamine-6-phosphate synthase: the multi-facets enzyme Biochim. Biophys. Acta 1597, 173-192
    • (2002) Biochim. Biophys. Acta , vol.1597 , pp. 173-192
    • Milewski, S.1
  • 5
    • 0001083651 scopus 로고
    • Mechanistic investigations on glucosamine-6-phosphate synthase
    • Badet-Denisot, M. A., Rene, L., and Badet, B. (1993) Mechanistic investigations on glucosamine-6-phosphate synthase Bull. Soc. Chim. Fr. 130, 249-255
    • (1993) Bull. Soc. Chim. Fr. , vol.130 , pp. 249-255
    • Badet-Denisot, M.A.1    Rene, L.2    Badet, B.3
  • 6
    • 80053041142 scopus 로고    scopus 로고
    • Riboswitches: Discovery of drugs that target bacterial gene-regulatory RNAs
    • Deigan, K. E. and Ferre-DAmare, A. R. (2011) Riboswitches: discovery of drugs that target bacterial gene-regulatory RNAs Acc. Chem. Res. 44, 1329-1338
    • (2011) Acc. Chem. Res. , vol.44 , pp. 1329-1338
    • Deigan, K.E.1    Ferre-Damare, A.R.2
  • 7
    • 84892514964 scopus 로고    scopus 로고
    • The promise of riboswitches as potential antibacterial drug targets
    • Lunse, C. E., Schuller, A., and Mayer, G. (2014) The promise of riboswitches as potential antibacterial drug targets Int. J. Med. Microbiol. 304, 79-92
    • (2014) Int. J. Med. Microbiol. , vol.304 , pp. 79-92
    • Lunse, C.E.1    Schuller, A.2    Mayer, G.3
  • 8
    • 33845700514 scopus 로고    scopus 로고
    • Riboswitches as antibacterial drug targets
    • Blount, K. F. and Breaker, R. R. (2006) Riboswitches as antibacterial drug targets Nat. Biotechnol. 24, 1558-1564
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1558-1564
    • Blount, K.F.1    Breaker, R.R.2
  • 9
    • 33845745224 scopus 로고    scopus 로고
    • "Turning on" riboswitches to their antibacterial potential
    • Lea, C. R. and Piccirilli, J. A. (2006) "Turning on" riboswitches to their antibacterial potential Nat. Chem. Biol. 3, 16-17
    • (2006) Nat. Chem. Biol. , vol.3 , pp. 16-17
    • Lea, C.R.1    Piccirilli, J.A.2
  • 11
    • 84896697569 scopus 로고    scopus 로고
    • The structural and functional uniqueness of the glmS ribozyme
    • Soukup, J. K. (2013) The structural and functional uniqueness of the glmS ribozyme Prog. Mol. Biol. Transl. 120, 173-193
    • (2013) Prog. Mol. Biol. Transl. , vol.120 , pp. 173-193
    • Soukup, J.K.1
  • 13
    • 37249040135 scopus 로고    scopus 로고
    • Mechanism of mRNA destabilization by the glmS ribozyme
    • Collins, J. A., Irnov, I., Baker, S., and Winkler, W. C. (2007) Mechanism of mRNA destabilization by the glmS ribozyme Genes Dev. 21, 3356-3368
    • (2007) Genes Dev. , vol.21 , pp. 3356-3368
    • Collins, J.A.1    Irnov, I.2    Baker, S.3    Winkler, W.C.4
  • 14
    • 33744936038 scopus 로고    scopus 로고
    • Backbone and nucleobase contacts to glucosamine-6-phosphate in the glmS ribozyme
    • Jansen, J. A., McCarthy, T. J., Soukup, G. A., and Soukup, J. K. (2006) Backbone and nucleobase contacts to glucosamine-6-phosphate in the glmS ribozyme Nat. Struct. Mol. Biol. 13, 517-523
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 517-523
    • Jansen, J.A.1    McCarthy, T.J.2    Soukup, G.A.3    Soukup, J.K.4
  • 15
    • 33748325570 scopus 로고    scopus 로고
    • Structural basis of glmS ribozyme activation by glucosamine-6-phosphate
    • Klein, D. J. and Ferre-DAmare, A. R. (2006) Structural basis of glmS ribozyme activation by glucosamine-6-phosphate Science 313, 1752-1756
    • (2006) Science , vol.313 , pp. 1752-1756
    • Klein, D.J.1    Ferre-Damare, A.R.2
  • 16
    • 33846279049 scopus 로고    scopus 로고
    • Structural investigation of the glmS ribozyme bound to its catalytic cofactor
    • Cochrane, J. C., Lipchock, S. V., and Strobel, S. A. (2007) Structural investigation of the glmS ribozyme bound to its catalytic cofactor Chem. Biol. 14, 97-105
    • (2007) Chem. Biol. , vol.14 , pp. 97-105
    • Cochrane, J.C.1    Lipchock, S.V.2    Strobel, S.A.3
  • 17
    • 36849061230 scopus 로고    scopus 로고
    • Essential role of an active-site guanine in glmS ribozyme catalysis
    • Klein, D. J., Been, M. D., and Ferre-DAmare, A. R. (2007) Essential role of an active-site guanine in glmS ribozyme catalysis J. Am. Chem. Soc. 129, 14858-14859
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14858-14859
    • Klein, D.J.1    Been, M.D.2    Ferre-Damare, A.R.3
  • 18
    • 34548591567 scopus 로고    scopus 로고
    • Requirement of helix P2.2 and nucleotide G1 for positioning the cleavage site and cofactor of the glmS ribozyme
    • Klein, D. J., Wilkinson, S. R., Been, M. D., and Ferre-DAmare, A. R. (2007) Requirement of helix P2.2 and nucleotide G1 for positioning the cleavage site and cofactor of the glmS ribozyme J. Mol. Biol. 373, 178-189
    • (2007) J. Mol. Biol. , vol.373 , pp. 178-189
    • Klein, D.J.1    Wilkinson, S.R.2    Been, M.D.3    Ferre-Damare, A.R.4
  • 19
    • 33947728975 scopus 로고    scopus 로고
    • Trans-acting glmS catalytic riboswitch: Locked and loaded
    • Tinsley, R. A., Furchak, J. R. W., and Walter, N. G. (2007) Trans-acting glmS catalytic riboswitch: locked and loaded RNA 13, 468-477
    • (2007) RNA , vol.13 , pp. 468-477
    • Tinsley, R.A.1    Furchak, J.R.W.2    Walter, N.G.3
  • 20
    • 65249184394 scopus 로고    scopus 로고
    • Structural and chemical basis for glucosamine 6-phosphate binding and activation of the glmS ribozyme
    • Cochrane, J. C., Lipchock, S. V., Smith, K. D., and Strobel, S. A. (2009) Structural and chemical basis for glucosamine 6-phosphate binding and activation of the glmS ribozyme Biochemistry 48, 3239-3246
    • (2009) Biochemistry , vol.48 , pp. 3239-3246
    • Cochrane, J.C.1    Lipchock, S.V.2    Smith, K.D.3    Strobel, S.A.4
  • 21
    • 77954332068 scopus 로고    scopus 로고
    • Protonation States of the Key Active Site Residues and Structural Dynamics of the glmS Riboswitch As Revealed by Molecular Dynamics
    • Banas, P., Walter, N. G., Sponer, J., and Otyepka, M. (2010) Protonation States of the Key Active Site Residues and Structural Dynamics of the glmS Riboswitch As Revealed by Molecular Dynamics J. Phys. Chem. B 114, 8701-8712
    • (2010) J. Phys. Chem. B , vol.114 , pp. 8701-8712
    • Banas, P.1    Walter, N.G.2    Sponer, J.3    Otyepka, M.4
  • 22
    • 80755123378 scopus 로고    scopus 로고
    • An Active-Site Guanine Participates in glmS Ribozyme Catalysis in Its Protonated State
    • Viladoms, J., Scott, L. G., and Fedor, M. J. (2011) An Active-Site Guanine Participates in glmS Ribozyme Catalysis in Its Protonated State J. Am. Chem. Soc. 133, 18388-18396
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 18388-18396
    • Viladoms, J.1    Scott, L.G.2    Fedor, M.J.3
  • 23
    • 84869440996 scopus 로고    scopus 로고
    • The glmS ribozyme cofactor is a general acid-base catalyst
    • Viladoms, J. and Fedor, M. J. (2012) The glmS ribozyme cofactor is a general acid-base catalyst J. Am. Chem. Soc. 134, 19043-19049
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 19043-19049
    • Viladoms, J.1    Fedor, M.J.2
  • 24
    • 33750149294 scopus 로고    scopus 로고
    • Characteristics of ligand recognition by a glmS self-cleaving ribozyme
    • Lim, J., Grove, B. C., Roth, A., and Breaker, R. R. (2006) Characteristics of ligand recognition by a glmS self-cleaving ribozyme Angew. Chem., Int. Ed. 45, 6689-6693
    • (2006) Angew. Chem., Int. Ed. , vol.45 , pp. 6689-6693
    • Lim, J.1    Grove, B.C.2    Roth, A.3    Breaker, R.R.4
  • 25
    • 0027949817 scopus 로고
    • Value of General Acid-Base Catalysis to Ribonuclease A
    • Thompson, J. E. and Raines, R. T. (1994) Value of General Acid-Base Catalysis to Ribonuclease A J. Am. Chem. Soc. 116, 5467-5468
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 5467-5468
    • Thompson, J.E.1    Raines, R.T.2
  • 26
    • 0029788628 scopus 로고    scopus 로고
    • On the mechanism of action of ribonuclease A: Relevance of enzymic studies with a p-nitrophenylphosphate ester and a thiophosphate ester
    • Breslow, R. and Chapman, W. H., Jr. (1996) On the mechanism of action of ribonuclease A: relevance of enzymic studies with a p-nitrophenylphosphate ester and a thiophosphate ester Proc. Natl. Acad. Sci. U. S. A. 93, 10018-10021
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 10018-10021
    • Breslow, R.1    Chapman, W.H.2
  • 27
    • 0347763707 scopus 로고    scopus 로고
    • Catalytic roles for proton transfer and protonation in ribozymes
    • Bevilacqua, P. C., Brown, T. S., Nakano, S.-i., and Yajima, R. (2004) Catalytic roles for proton transfer and protonation in ribozymes Biopolymers 73, 90-109
    • (2004) Biopolymers , vol.73 , pp. 90-109
    • Bevilacqua, P.C.1    Brown, T.S.2    Nakano, S.-I.3    Yajima, R.4
  • 30
    • 78649640602 scopus 로고    scopus 로고
    • Deciphering the role of glucosamine-6-phosphate in the riboswitch action of glmS ribozyme
    • Xin, Y. and Hamelberg, D. (2010) Deciphering the role of glucosamine-6-phosphate in the riboswitch action of glmS ribozyme RNA 16, 2455-2463
    • (2010) RNA , vol.16 , pp. 2455-2463
    • Xin, Y.1    Hamelberg, D.2
  • 31
    • 79960487609 scopus 로고    scopus 로고
    • Carba-sugars activate the glmS -riboswitch of Staphylococcus aureus
    • Lünse, C. E., Schmidt, M. S., Wittmann, V., and Mayer, G. (2011) Carba-sugars activate the glmS -riboswitch of Staphylococcus aureus ACS Chem. Biol. 6, 675-678
    • (2011) ACS Chem. Biol. , vol.6 , pp. 675-678
    • Lü, E.1    Schmidt, M.S.2    Wittmann, V.3    Mayer, G.4
  • 32
    • 84867063026 scopus 로고    scopus 로고
    • Synthesis and evaluation of glucosamine-6-phosphate analogues as activators of glmS riboswitch
    • Wang, G. N., Lau, P. S., Li, Y. F., and Ye, X. S. (2012) Synthesis and evaluation of glucosamine-6-phosphate analogues as activators of glmS riboswitch Tetrahedron 68, 9405-9412
    • (2012) Tetrahedron , vol.68 , pp. 9405-9412
    • Wang, G.N.1    Lau, P.S.2    Li, Y.F.3    Ye, X.S.4
  • 34
    • 67650743221 scopus 로고    scopus 로고
    • Biosynthesis of phosphonic and phosphinic acid natural products
    • Metcalf, W. W. and van der Donk, W. A. (2009) Biosynthesis of phosphonic and phosphinic acid natural products Annu. Rev. Biochem. 78, 65-94
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 65-94
    • Metcalf, W.W.1    Van Der Donk, W.A.2
  • 37
    • 84901923883 scopus 로고    scopus 로고
    • Alteration of the Flexible Loop in 1-Deoxy-D-xylulose-5-phosphate Reductoisomerase Boosts Enthalpy-Driven Inhibition by Fosmidomycin
    • Kholodar, S. A., Tombline, G., Liu, J., Tan, Z., Allen, C. L., Gulick, A. M., and Murkin, A. S. (2014) Alteration of the Flexible Loop in 1-Deoxy-D-xylulose-5-phosphate Reductoisomerase Boosts Enthalpy-Driven Inhibition by Fosmidomycin Biochemistry 53, 3423-3431
    • (2014) Biochemistry , vol.53 , pp. 3423-3431
    • Kholodar, S.A.1    Tombline, G.2    Liu, J.3    Tan, Z.4    Allen, C.L.5    Gulick, A.M.6    Murkin, A.S.7
  • 39
    • 84862750033 scopus 로고    scopus 로고
    • Unleashing a "true" pSer-Mimic in the Cell
    • Panigrahi, K., Nelson, D. L., and Berkowitz, D. B. (2012) Unleashing a "True" pSer-Mimic in the Cell Chem. Biol. 19, 666-667
    • (2012) Chem. Biol. , vol.19 , pp. 666-667
    • Panigrahi, K.1    Nelson, D.L.2    Berkowitz, D.B.3
  • 40
    • 70349191367 scopus 로고    scopus 로고
    • The alpha,alpha-Difluorinated Phosphonate L-pSer-Analogue: An Accessible Chemical Tool for Studying Kinase-Dependent Signal Transduction
    • Panigrahi, K., Eggen, M., Maeng, J. H., Shen, Q. R., and Berkowitz, D. B. (2009) The alpha,alpha-Difluorinated Phosphonate L-pSer-Analogue: An Accessible Chemical Tool for Studying Kinase-Dependent Signal Transduction Chem. Biol. 16, 928-936
    • (2009) Chem. Biol. , vol.16 , pp. 928-936
    • Panigrahi, K.1    Eggen, M.2    Maeng, J.H.3    Shen, Q.R.4    Berkowitz, D.B.5
  • 41
    • 0001397262 scopus 로고    scopus 로고
    • A Convergent Triflate Displacement Approach to (alpha-Monofluoroalkyl)phosphonates
    • Berkowitz, D. B., Bose, M., and Asher, N. G. (2001) A Convergent Triflate Displacement Approach to (alpha-Monofluoroalkyl)phosphonates Org. Lett. 3, 2009-2012
    • (2001) Org. Lett. , vol.3 , pp. 2009-2012
    • Berkowitz, D.B.1    Bose, M.2    Asher, N.G.3
  • 42
    • 0035169222 scopus 로고    scopus 로고
    • (Alpha-monofluoroalkyl)phosphonates: A class of isoacidic and "tunable" mimics of biological phosphates
    • Berkowitz, D. B. and Bose, M. (2001) (Alpha-monofluoroalkyl)phosphonates: a class of isoacidic and "tunable" mimics of biological phosphates J. Fluor. Chem. 112, 13-33
    • (2001) J. Fluor. Chem. , vol.112 , pp. 13-33
    • Berkowitz, D.B.1    Bose, M.2
  • 43
    • 0033525461 scopus 로고    scopus 로고
    • Facile installation of the phosphonate and (alpha,alpha-difluoromethyl)phosphonate functionalities equipped with benzyl protection
    • Berkowitz, D. B., Bhuniya, D., and Peris, G. (1999) Facile installation of the phosphonate and (alpha,alpha-difluoromethyl)phosphonate functionalities equipped with benzyl protection Tetrahedron Lett. 40, 1869-1872
    • (1999) Tetrahedron Lett. , vol.40 , pp. 1869-1872
    • Berkowitz, D.B.1    Bhuniya, D.2    Peris, G.3
  • 44
    • 0029885050 scopus 로고    scopus 로고
    • Ready Access to Fluorinated Phosphonate Mimics of Secondary Phosphates. Synthesis of the (alpha,alpha-Difluoroalkyl)phosphonate Analogs of L-Phosphoserine, L-Phosphoallothreonine, and L-Phosphothreonine
    • Berkowitz, D. B., Eggen, M., Shen, Q., and Shoemaker, R. K. (1996) Ready Access to Fluorinated Phosphonate Mimics of Secondary Phosphates. Synthesis of the (alpha,alpha-Difluoroalkyl)phosphonate Analogs of L-Phosphoserine, L-Phosphoallothreonine, and L-Phosphothreonine J. Org. Chem. 61, 4666-4675
    • (1996) J. Org. Chem. , vol.61 , pp. 4666-4675
    • Berkowitz, D.B.1    Eggen, M.2    Shen, Q.3    Shoemaker, R.K.4
  • 45
    • 33751155275 scopus 로고
    • Diallyl (Lithiodifluoromethyl)phosphonate: A New Reagent for the Introduction of the (Difluoromethylene)phosphonate Functionality
    • Berkowitz, D. B. and Sloss, D. G. (1995) Diallyl (Lithiodifluoromethyl)phosphonate: A New Reagent for the Introduction of the (Difluoromethylene)phosphonate Functionality J. Org. Chem. 60, 7047-7050
    • (1995) J. Org. Chem. , vol.60 , pp. 7047-7050
    • Berkowitz, D.B.1    Sloss, D.G.2
  • 46
    • 0034725770 scopus 로고    scopus 로고
    • Alpha-Fluorinated Phosphonates as Substrate Mimics for Glucose 6-Phosphate Dehydrogenase: The CHF Stereochemistry Matters
    • Berkowitz, D. B., Bose, M., Pfannenstiel, T. J., and Doukov, T. (2000) alpha-Fluorinated Phosphonates as Substrate Mimics for Glucose 6-Phosphate Dehydrogenase: the CHF Stereochemistry Matters J. Org. Chem. 65, 4498-4508
    • (2000) J. Org. Chem. , vol.65 , pp. 4498-4508
    • Berkowitz, D.B.1    Bose, M.2    Pfannenstiel, T.J.3    Doukov, T.4
  • 47
    • 43549108315 scopus 로고    scopus 로고
    • A set of phosphatase-inert "molecular rulers" to probe for bivalent mannose 6-phosphate ligand-receptor interactions
    • Fei, X., Connelly, C. M., MacDonald, R. G., and Berkowitz, D. B. (2008) A set of phosphatase-inert "molecular rulers" to probe for bivalent mannose 6-phosphate ligand-receptor interactions Bioorg. Med. Chem. Lett. 18, 3085-3089
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 3085-3089
    • Fei, X.1    Connelly, C.M.2    Macdonald, R.G.3    Berkowitz, D.B.4
  • 48
    • 12344286971 scopus 로고    scopus 로고
    • Mono- and bivalent ligands bearing mannose 6-phosphate (M6P) surrogates: Targeting the M6P/insulin-like growth factor II receptor
    • Berkowitz, D. B., Maiti, G., Charette, B. D., Dreis, C. D., and MacDonald, R. G. (2004) Mono- and bivalent ligands bearing mannose 6-phosphate (M6P) surrogates: targeting the M6P/insulin-like growth factor II receptor Org. Lett. 6, 4921-4924
    • (2004) Org. Lett. , vol.6 , pp. 4921-4924
    • Berkowitz, D.B.1    Maiti, G.2    Charette, B.D.3    Dreis, C.D.4    Macdonald, R.G.5
  • 49
    • 0028223767 scopus 로고
    • Displacement of Sugar Triflates with C-Nucleophiles - D-Glucopyranose and D-Ribofuranose Chain Extension and Functionalization
    • Shen, Q. R., Sloss, D. G., and Berkowitz, D. B. (1994) Displacement of Sugar Triflates with C-Nucleophiles-D-Glucopyranose and D-Ribofuranose Chain Extension and Functionalization Synth. Commun. 24, 1519-1530
    • (1994) Synth. Commun. , vol.24 , pp. 1519-1530
    • Shen, Q.R.1    Sloss, D.G.2    Berkowitz, D.B.3
  • 50
    • 0001180846 scopus 로고
    • Synthesis of (alpha,alpha-Difluoroalkyl)Phosphonates by Displacement of Primary Triflates
    • Berkowitz, D. B., Eggen, M., Shen, Q., and Sloss, D. G. (1993) Synthesis of (alpha,alpha-Difluoroalkyl)Phosphonates by Displacement of Primary Triflates J. Org. Chem. 58, 6174-6176
    • (1993) J. Org. Chem. , vol.58 , pp. 6174-6176
    • Berkowitz, D.B.1    Eggen, M.2    Shen, Q.3    Sloss, D.G.4
  • 51
    • 0000360619 scopus 로고
    • Sulfonamidoglycosylation of glycals. A route to oligosaccharides with 2-aminohexose subunits
    • Griffith, D. A. and Danishefsky, S. J. (1990) Sulfonamidoglycosylation of glycals. A route to oligosaccharides with 2-aminohexose subunits J. Am. Chem. Soc. 112, 5811-5819
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 5811-5819
    • Griffith, D.A.1    Danishefsky, S.J.2
  • 52
    • 0000288777 scopus 로고
    • Total synthesis of allosamidin. An application of the sulfonamidoglycosylation of glycals
    • Griffith, D. A. and Danishefsky, S. J. (1991) Total synthesis of allosamidin. An application of the sulfonamidoglycosylation of glycals J. Am. Chem. Soc. 113, 5863-5864
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5863-5864
    • Griffith, D.A.1    Danishefsky, S.J.2
  • 53
    • 0028223767 scopus 로고
    • Displacement of sugar triflates with C-Nucleophiles: D-glucopyranose and D-ribofuranose chain extension and functionalization
    • Shen, Q. R., Sloss, D. G., and Berkowitz, D. B. (1994) Displacement of sugar triflates with C-Nucleophiles: D-glucopyranose and D-ribofuranose chain extension and functionalization Synth. Commun. 24, 1519-1530
    • (1994) Synth. Commun. , vol.24 , pp. 1519-1530
    • Shen, Q.R.1    Sloss, D.G.2    Berkowitz, D.B.3
  • 54
    • 79959561253 scopus 로고    scopus 로고
    • Polarizable Water Networks in Ligand-Metalloprotein Recognition. Impact on the Relative Complexation Energies of Zn-Dependent Phosphomannose Isomerase with D-Mannose 6-Phosphate Surrogates
    • Gresh, N., de Courcy, B., Piquemal, J.-P., Foret, J., Courtiol-Legourd, S., and Salmon, L. (2011) Polarizable Water Networks in Ligand-Metalloprotein Recognition. Impact on the Relative Complexation Energies of Zn-Dependent Phosphomannose Isomerase with D-Mannose 6-Phosphate Surrogates J. Phys. Chem. B 115, 8304-8316
    • (2011) J. Phys. Chem. B , vol.115 , pp. 8304-8316
    • Gresh, N.1    De Courcy, B.2    Piquemal, J.-P.3    Foret, J.4    Courtiol-Legourd, S.5    Salmon, L.6
  • 55
    • 0000370316 scopus 로고    scopus 로고
    • Inhibitor Ionization as a Determinant of Binding to 3-Dehydroquinate Synthase
    • Tian, F., Montchamp, J.-L., and Frost, J. W. (1996) Inhibitor Ionization as a Determinant of Binding to 3-Dehydroquinate Synthase J. Org. Chem. 61, 7373-7381
    • (1996) J. Org. Chem. , vol.61 , pp. 7373-7381
    • Tian, F.1    Montchamp, J.-L.2    Frost, J.W.3
  • 56
    • 0029563920 scopus 로고
    • New EPSP synthase inhibitors: Synthesis and evaluation of an aromatic tetrahedral intermediate mimic containing a 3-malonate ether as a 3-phosphate surrogate
    • Miller, M. J., Cleary, D. G., Ream, J. E., Snyder, K. R., and Sikorski, J. A. (1995) New EPSP synthase inhibitors: synthesis and evaluation of an aromatic tetrahedral intermediate mimic containing a 3-malonate ether as a 3-phosphate surrogate Bioorg. Med. Chem. 3, 1685-1692
    • (1995) Bioorg. Med. Chem. , vol.3 , pp. 1685-1692
    • Miller, M.J.1    Cleary, D.G.2    Ream, J.E.3    Snyder, K.R.4    Sikorski, J.A.5
  • 57
    • 0001180846 scopus 로고
    • Synthesis of (alpha,alpha-difluoroalkyl)phosphonates by displacement of primary triflates
    • Berkowitz, D. B., Eggen, M., Shen, Q., and Sloss, D. G. (1993) Synthesis of (alpha,alpha-difluoroalkyl)phosphonates by displacement of primary triflates J. Org. Chem. 58, 6174-6176
    • (1993) J. Org. Chem. , vol.58 , pp. 6174-6176
    • Berkowitz, D.B.1    Eggen, M.2    Shen, Q.3    Sloss, D.G.4
  • 58
    • 67649207845 scopus 로고    scopus 로고
    • A rate-limiting conformational step in the catalytic pathway of the glmS ribozyme
    • Brooks, K. M. and Hampel, K. J. (2009) A rate-limiting conformational step in the catalytic pathway of the glmS ribozyme Biochemistry 48, 5669-5678
    • (2009) Biochemistry , vol.48 , pp. 5669-5678
    • Brooks, K.M.1    Hampel, K.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.