메뉴 건너뛰기




Volumn 53, Issue 9, 2014, Pages 1511-1520

A conformational investigation of propeptide binding to the integral membrane protein γ-glutamyl carboxylase using nanodisc hydrogen exchange mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRAL MEMBRANE PROTEINS; MEMBRANE-BOUND ENZYMES; STRUCTURAL CHARACTERIZATION; STRUCTURAL CONFIGURATIONS; STRUCTURAL REARRANGEMENT; STRUCTURAL REORIENTATION; STRUCTURAL STABILITIES; THREE-DIMENSIONAL STRUCTURE;

EID: 84896076495     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401536m     Document Type: Article
Times cited : (45)

References (65)
  • 1
    • 33845382214 scopus 로고    scopus 로고
    • Identification of the N-linked glycosylation sites of vitamin K-dependent carboxylase and effect of glycosylation on carboxylase function
    • Tie, J. K., Zheng, M. Y., Pope, R. M., Straight, D. L., and Stafford, D. W. (2006) Identification of the N-linked glycosylation sites of vitamin K-dependent carboxylase and effect of glycosylation on carboxylase function Biochemistry 45, 14755-14763
    • (2006) Biochemistry , vol.45 , pp. 14755-14763
    • Tie, J.K.1    Zheng, M.Y.2    Pope, R.M.3    Straight, D.L.4    Stafford, D.W.5
  • 2
    • 0034254613 scopus 로고    scopus 로고
    • A topological study of the human gamma-glutamyl carboxylase
    • Tie, J. K., Wu, S. M., Jin, D. Y., Nicchitta, C. V., and Stafford, D. W. (2000) A topological study of the human gamma-glutamyl carboxylase Blood 96, 973-978
    • (2000) Blood , vol.96 , pp. 973-978
    • Tie, J.K.1    Wu, S.M.2    Jin, D.Y.3    Nicchitta, C.V.4    Stafford, D.W.5
  • 3
    • 0242580898 scopus 로고    scopus 로고
    • Determination of disulfide bond assignment of human vitamin K-dependent gamma-glutamyl carboxylase by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Tie, J. K., Mutucumarana, V. P., Straight, D. L., Carrick, K. L., Pope, R. M., and Stafford, D. W. (2003) Determination of disulfide bond assignment of human vitamin K-dependent gamma-glutamyl carboxylase by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry J. Biol. Chem. 278, 45468-45475
    • (2003) J. Biol. Chem. , vol.278 , pp. 45468-45475
    • Tie, J.K.1    Mutucumarana, V.P.2    Straight, D.L.3    Carrick, K.L.4    Pope, R.M.5    Stafford, D.W.6
  • 4
    • 0018136725 scopus 로고
    • Mechanism of coumarin action: Significance of vitamin K epoxide reductase inhibition
    • Whitlon, D. S., Sadowski, J. A., and Suttie, J. W. (1978) Mechanism of coumarin action: significance of vitamin K epoxide reductase inhibition Biochemistry 17, 1371-1377
    • (1978) Biochemistry , vol.17 , pp. 1371-1377
    • Whitlon, D.S.1    Sadowski, J.A.2    Suttie, J.W.3
  • 6
    • 0025008168 scopus 로고
    • Sequence logos - A new way to display consensus sequences
    • Schneider, T. D. and Stephens, R. M. (1990) Sequence logos-a new way to display consensus sequences Nucleic Acids Res. 18, 6097-6100
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 7
    • 0023667781 scopus 로고
    • Recognition site directing vitamin-K-dependent gamma-carboxylation resides on the propeptide of factor-IX
    • Jorgensen, M. J., Cantor, A. B., Furie, B. C., Brown, C. L., Shoemaker, C. B., and Furie, B. (1987) Recognition site directing vitamin-K-dependent gamma-carboxylation resides on the propeptide of factor-IX Cell 48, 185-191
    • (1987) Cell , vol.48 , pp. 185-191
    • Jorgensen, M.J.1    Cantor, A.B.2    Furie, B.C.3    Brown, C.L.4    Shoemaker, C.B.5    Furie, B.6
  • 8
    • 0003603482 scopus 로고
    • The propeptide of rat bone gamma-carboxyglutamic acid protein shares homology with other vitamin-K-dependent protein precursors
    • Pan, L. C. and Price, P. A. (1985) The propeptide of rat bone gamma-carboxyglutamic acid protein shares homology with other vitamin-K-dependent protein precursors Proc. Natl. Acad. Sci. U.S.A. 82, 6109-6113
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 6109-6113
    • Pan, L.C.1    Price, P.A.2
  • 9
    • 0033546393 scopus 로고    scopus 로고
    • The propeptides of the vitamin K-dependent proteins possess different affinities for the vitamin K-dependent carboxylase
    • Stanley, T. B., Jin, D. Y., Lin, P. J., and Stafford, D. W. (1999) The propeptides of the vitamin K-dependent proteins possess different affinities for the vitamin K-dependent carboxylase J. Biol. Chem. 274, 16940-16944
    • (1999) J. Biol. Chem. , vol.274 , pp. 16940-16944
    • Stanley, T.B.1    Jin, D.Y.2    Lin, P.J.3    Stafford, D.W.4
  • 10
    • 1342325432 scopus 로고    scopus 로고
    • Binding of the factor IX gamma-carboxyglutamic acid domain to the vitamin K-dependent gamma-glutamyl carboxylase active site induces an allosteric effect that may ensure processive carboxylation and regulate the release of carboxylated product
    • Lin, P. J., Straight, D. L., and Stafford, D. W. (2004) Binding of the factor IX gamma-carboxyglutamic acid domain to the vitamin K-dependent gamma-glutamyl carboxylase active site induces an allosteric effect that may ensure processive carboxylation and regulate the release of carboxylated product J. Biol. Chem. 279, 6560-6566
    • (2004) J. Biol. Chem. , vol.279 , pp. 6560-6566
    • Lin, P.J.1    Straight, D.L.2    Stafford, D.W.3
  • 11
    • 0037047297 scopus 로고    scopus 로고
    • The putative vitamin K-dependent gamma-glutamyl carboxylase internal propeptide appears to be the propeptide binding site
    • Lin, P. J., Jin, D. Y., Tie, J. K., Presnell, S. R., Straight, D. L., and Stafford, D. W. (2002) The putative vitamin K-dependent gamma-glutamyl carboxylase internal propeptide appears to be the propeptide binding site J. Biol. Chem. 277, 28584-28591
    • (2002) J. Biol. Chem. , vol.277 , pp. 28584-28591
    • Lin, P.J.1    Jin, D.Y.2    Tie, J.K.3    Presnell, S.R.4    Straight, D.L.5    Stafford, D.W.6
  • 12
    • 0030922587 scopus 로고    scopus 로고
    • The propeptide binding site of the bovine gamma-glutamyl carboxylase
    • Wu, S. M., Mutucumarana, V. P., Geromanos, S., and Stafford, D. W. (1997) The propeptide binding site of the bovine gamma-glutamyl carboxylase J. Biol. Chem. 272, 11718-11722
    • (1997) J. Biol. Chem. , vol.272 , pp. 11718-11722
    • Wu, S.M.1    Mutucumarana, V.P.2    Geromanos, S.3    Stafford, D.W.4
  • 13
    • 0343505604 scopus 로고
    • Comparison of amino-acid sequence of bovine coagulation Factor-IX (Christmas Factor) with that of other vitamin K-dependent plasma proteins
    • Katayama, K., Ericsson, L. H., Enfield, D. L., Walsh, K. A., Neurath, H., Davie, E. W., and Titani, K. (1979) Comparison of amino-acid sequence of bovine coagulation Factor-IX (Christmas Factor) with that of other vitamin K-dependent plasma proteins Proc. Natl. Acad. Sci. U.S.A. 76, 4990-4994
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4990-4994
    • Katayama, K.1    Ericsson, L.H.2    Enfield, D.L.3    Walsh, K.A.4    Neurath, H.5    Davie, E.W.6    Titani, K.7
  • 14
    • 0017620768 scopus 로고
    • Vitamin K-dependent formation of gamma-carboxyglutamic acid
    • Stenflo, J. and Suttie, J. W. (1977) Vitamin K-dependent formation of gamma-carboxyglutamic acid Annu. Rev. Biochem. 46, 157-172
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 157-172
    • Stenflo, J.1    Suttie, J.W.2
  • 15
    • 0018850473 scopus 로고
    • Mechanism of action of vitamin K: Synthesis of gamma-carboxyglutamic acid
    • Suttie, J. W. (1980) Mechanism of action of vitamin K: synthesis of gamma-carboxyglutamic acid CRC Crit. Rev. Biochem. 8, 191-223
    • (1980) CRC Crit. Rev. Biochem. , vol.8 , pp. 191-223
    • Suttie, J.W.1
  • 16
    • 0029586502 scopus 로고
    • Processive post-translational modification. Vitamin K-dependent carboxylation of a peptide substrate
    • Morris, D. P., Stevens, R. D., Wright, D. J., and Stafford, D. W. (1995) Processive post-translational modification. Vitamin K-dependent carboxylation of a peptide substrate J. Biol. Chem. 270, 30491-30498
    • (1995) J. Biol. Chem. , vol.270 , pp. 30491-30498
    • Morris, D.P.1    Stevens, R.D.2    Wright, D.J.3    Stafford, D.W.4
  • 17
    • 0035964295 scopus 로고    scopus 로고
    • Tethered processivity of the vitamin K-dependent carboxylase: Factor IX is efficiently modified in a mechanism which distinguishes Gla's from Glu's and which accounts for comprehensive carboxylation in vivo
    • Stenina, O., Pudota, B. N., McNally, B. A., Hommema, E. L., and Berkner, K. L. (2001) Tethered processivity of the vitamin K-dependent carboxylase: factor IX is efficiently modified in a mechanism which distinguishes Gla's from Glu's and which accounts for comprehensive carboxylation in vivo Biochemistry 40, 10301-10309
    • (2001) Biochemistry , vol.40 , pp. 10301-10309
    • Stenina, O.1    Pudota, B.N.2    McNally, B.A.3    Hommema, E.L.4    Berkner, K.L.5
  • 18
    • 0029822179 scopus 로고    scopus 로고
    • Biosynthesis of prothrombin: Intracellular localization of the vitamin K-dependent carboxylase and the sites of gamma-carboxylation
    • Bristol, J. A., Ratcliffe, J. V., Roth, D. A., Jacobs, M. A., Furie, B. C., and Furie, B. (1996) Biosynthesis of prothrombin: intracellular localization of the vitamin K-dependent carboxylase and the sites of gamma-carboxylation Blood 88, 2585-2593
    • (1996) Blood , vol.88 , pp. 2585-2593
    • Bristol, J.A.1    Ratcliffe, J.V.2    Roth, D.A.3    Jacobs, M.A.4    Furie, B.C.5    Furie, B.6
  • 19
    • 0029130392 scopus 로고
    • Vitamin-K and energy transduction: A base strength amplification mechanism
    • Dowd, P., Hershline, R., Ham, S. W., and Naganathan, S. (1995) Vitamin-K and energy transduction: a base strength amplification mechanism Science 269, 1684-1691
    • (1995) Science , vol.269 , pp. 1684-1691
    • Dowd, P.1    Hershline, R.2    Ham, S.W.3    Naganathan, S.4
  • 20
    • 0023653447 scopus 로고
    • Vitamin K-dependent oxygenase/carboxylase; Differential inactivation by sulfhydryl reagents
    • Canfield, L. M. (1987) Vitamin K-dependent oxygenase/carboxylase; differential inactivation by sulfhydryl reagents Biochem. Biophys. Res. Commun. 148, 184-191
    • (1987) Biochem. Biophys. Res. Commun. , vol.148 , pp. 184-191
    • Canfield, L.M.1
  • 22
    • 0034700163 scopus 로고    scopus 로고
    • Identification of the vitamin K-dependent carboxylase active site: Cys-99 and Cys-450 are required for both epoxidation and carboxylation
    • Pudota, B. N., Miyagi, M., Hallgren, K. W., West, K. A., Crabb, J. W., Misono, K. S., and Berkner, K. L. (2000) Identification of the vitamin K-dependent carboxylase active site: Cys-99 and Cys-450 are required for both epoxidation and carboxylation Proc. Natl. Acad. Sci. U.S.A. 97, 13033-13038
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13033-13038
    • Pudota, B.N.1    Miyagi, M.2    Hallgren, K.W.3    West, K.A.4    Crabb, J.W.5    Misono, K.S.6    Berkner, K.L.7
  • 23
    • 11144222572 scopus 로고    scopus 로고
    • Chemical modification of cysteine residues is a misleading indicator of their status as active site residues in the vitamin K-dependent gamma-glutamyl carboxylation reaction
    • Tie, J. K., Jin, D. Y., Loiselle, D. R., Pope, R. M., Straight, D. L., and Stafford, D. W. (2004) Chemical modification of cysteine residues is a misleading indicator of their status as active site residues in the vitamin K-dependent gamma-glutamyl carboxylation reaction J. Biol. Chem. 279, 54079-54087
    • (2004) J. Biol. Chem. , vol.279 , pp. 54079-54087
    • Tie, J.K.1    Jin, D.Y.2    Loiselle, D.R.3    Pope, R.M.4    Straight, D.L.5    Stafford, D.W.6
  • 24
    • 4644243445 scopus 로고    scopus 로고
    • A new model for vitamin K-dependent carboxylation: The catalytic base that deprotonates vitamin K hydroquinone is not Cys but an activated amine
    • Rishavy, M. A., Pudota, B. N., Hallgren, K. W., Qian, W., Yakubenko, A. V., Song, J. H., Runge, K. W., and Berkner, K. L. (2004) A new model for vitamin K-dependent carboxylation: the catalytic base that deprotonates vitamin K hydroquinone is not Cys but an activated amine Proc. Natl. Acad. Sci. U.S.A. 101, 13732-13737
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 13732-13737
    • Rishavy, M.A.1    Pudota, B.N.2    Hallgren, K.W.3    Qian, W.4    Yakubenko, A.V.5    Song, J.H.6    Runge, K.W.7    Berkner, K.L.8
  • 25
    • 33750709274 scopus 로고    scopus 로고
    • Brønsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation
    • Rishavy, M. A., Hallgren, K. W., Yakubenko, A. V., Shtofman, R. L., Runge, K. W., and Berkner, K. L. (2006) Brønsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation Biochemistry 45, 13239-13248
    • (2006) Biochemistry , vol.45 , pp. 13239-13248
    • Rishavy, M.A.1    Hallgren, K.W.2    Yakubenko, A.V.3    Shtofman, R.L.4    Runge, K.W.5    Berkner, K.L.6
  • 26
    • 0032500835 scopus 로고    scopus 로고
    • Identification of the five hydrophilic residues (Lys-217, Lys-218, Arg-359, His-360, and Arg-513) essential for the structure and activity of vitamin K-dependent carboxylase
    • Shimizu, A., Sugiura, I., Matsushita, T., Kojima, T., Hirai, M., and Saito, H. (1998) Identification of the five hydrophilic residues (Lys-217, Lys-218, Arg-359, His-360, and Arg-513) essential for the structure and activity of vitamin K-dependent carboxylase Biochem. Biophys. Res. Commun. 251, 22-26
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 22-26
    • Shimizu, A.1    Sugiura, I.2    Matsushita, T.3    Kojima, T.4    Hirai, M.5    Saito, H.6
  • 27
    • 0029954236 scopus 로고    scopus 로고
    • Profactor IX propeptide and glutamate substrate binding sites on the vitamin K-dependent carboxylase identified by site-directed mutagenesis
    • Sugiura, I., Furie, B., Walsh, C. T., and Furie, B. C. (1996) Profactor IX propeptide and glutamate substrate binding sites on the vitamin K-dependent carboxylase identified by site-directed mutagenesis J. Biol. Chem. 271, 17837-17844
    • (1996) J. Biol. Chem. , vol.271 , pp. 17837-17844
    • Sugiura, I.1    Furie, B.2    Walsh, C.T.3    Furie, B.C.4
  • 28
    • 34548026301 scopus 로고    scopus 로고
    • Quantum chemical study of the mechanism of action of vitamin K carboxylase (VKC). IV. Intermediates and transition states
    • Davis, C. H., Deerfield, D., Stafford, D. W., and Pedersen, L. G. (2007) Quantum chemical study of the mechanism of action of vitamin K carboxylase (VKC). IV. Intermediates and transition states J. Phys. Chem. A 111, 7257-7261
    • (2007) J. Phys. Chem. A , vol.111 , pp. 7257-7261
    • Davis, C.H.1    Deerfield, D.2    Stafford, D.W.3    Pedersen, L.G.4
  • 29
    • 34548232630 scopus 로고    scopus 로고
    • A quantum chemical study of the mechanism of action of vitamin K carboxylase (VKC) - III. Intermediates and transition states
    • Davis, C. H., Deerfield, D., Wymore, T., Stafford, D. W., and Pedersen, L. G. (2007) A quantum chemical study of the mechanism of action of vitamin K carboxylase (VKC)-III. Intermediates and transition states J. Mol. Graphics Modell. 26, 409-414
    • (2007) J. Mol. Graphics Modell. , vol.26 , pp. 409-414
    • Davis, C.H.1    Deerfield, D.2    Wymore, T.3    Stafford, D.W.4    Pedersen, L.G.5
  • 30
    • 33750899462 scopus 로고    scopus 로고
    • Quantum chemical study of the mechanism of action of vitamin K epoxide reductase (VKOR)
    • Deerfield, D., Davis, C. H., Wymore, T., Stafford, D. W., and Pedersen, L. G. (2006) Quantum chemical study of the mechanism of action of vitamin K epoxide reductase (VKOR) Int. J. Quantum Chem. 106, 2944-2952
    • (2006) Int. J. Quantum Chem. , vol.106 , pp. 2944-2952
    • Deerfield, D.1    Davis, C.H.2    Wymore, T.3    Stafford, D.W.4    Pedersen, L.G.5
  • 31
    • 0032535284 scopus 로고    scopus 로고
    • A missense mutation in gamma-glutamyl carboxylase gene causes combined deficiency of all vitamin K-dependent blood coagulation factors
    • Brenner, B., Sanchez-Vega, B., Wu, S. M., Lanir, N., Stafford, D. W., and Solera, J. (1998) A missense mutation in gamma-glutamyl carboxylase gene causes combined deficiency of all vitamin K-dependent blood coagulation factors Blood 92, 4554-4559
    • (1998) Blood , vol.92 , pp. 4554-4559
    • Brenner, B.1    Sanchez-Vega, B.2    Wu, S.M.3    Lanir, N.4    Stafford, D.W.5    Solera, J.6
  • 32
    • 0345306692 scopus 로고    scopus 로고
    • A conserved region of human vitamin K-dependent carboxylase between residues 393 and 404 is important for its interaction with the glutamate substrate
    • Mutucumarana, V. P., Acher, F., Straight, D. L., Jin, D. Y., and Stafford, D. W. (2003) A conserved region of human vitamin K-dependent carboxylase between residues 393 and 404 is important for its interaction with the glutamate substrate J. Biol. Chem. 278, 46488-46493
    • (2003) J. Biol. Chem. , vol.278 , pp. 46488-46493
    • Mutucumarana, V.P.1    Acher, F.2    Straight, D.L.3    Jin, D.Y.4    Stafford, D.W.5
  • 33
    • 77954193701 scopus 로고    scopus 로고
    • Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry
    • Hebling, C. M., Morgan, C. R., Stafford, D. W., Jorgenson, J. W., Rand, K. D., and Engen, J. R. (2010) Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry Anal. Chem. 82, 5415-5419
    • (2010) Anal. Chem. , vol.82 , pp. 5415-5419
    • Hebling, C.M.1    Morgan, C.R.2    Stafford, D.W.3    Jorgenson, J.W.4    Rand, K.D.5    Engen, J.R.6
  • 34
    • 0035567106 scopus 로고    scopus 로고
    • Structure of melittin bound to phospholipid micelles studied using hydrogen-deuterium exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
    • Akashi, S. and Takio, K. (2001) Structure of melittin bound to phospholipid micelles studied using hydrogen-deuterium exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry J. Am. Soc. Mass Spectrom. 12, 1247-1253
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 1247-1253
    • Akashi, S.1    Takio, K.2
  • 35
    • 33750282788 scopus 로고    scopus 로고
    • Mapping protein dynamics in catalytic intermediates of the redox-driven proton pump cytochrome c oxidase
    • Busenlehner, L. S., Salomonsson, L., Brzezinski, P., and Armstrong, R. N. (2006) Mapping protein dynamics in catalytic intermediates of the redox-driven proton pump cytochrome c oxidase Proc. Natl. Acad. Sci. U.S.A. 103, 15398-15403
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 15398-15403
    • Busenlehner, L.S.1    Salomonsson, L.2    Brzezinski, P.3    Armstrong, R.N.4
  • 36
    • 0034118193 scopus 로고    scopus 로고
    • Solvent effects on the conformation of the transmembrane peptide gramicidin A: Insights from electrospray ionization mass spectrometry
    • Bouchard, M., Benjamin, D. R., Tito, P., Robinson, C. V., and Dobson, C. M. (2000) Solvent effects on the conformation of the transmembrane peptide gramicidin A: insights from electrospray ionization mass spectrometry Biophys. J. 78, 1010-1017
    • (2000) Biophys. J. , vol.78 , pp. 1010-1017
    • Bouchard, M.1    Benjamin, D.R.2    Tito, P.3    Robinson, C.V.4    Dobson, C.M.5
  • 37
    • 0035860765 scopus 로고    scopus 로고
    • Interfacial positioning and stability of transmembrane peptides in lipid bilayers studied by combining hydrogen/deuterium exchange and mass spectrometry
    • Demmers, J. A., van Duijn, E., Haverkamp, J., Greathouse, D. V., Koeppe, R. E., II, Heck, A. J., and Killian, J. A. (2001) Interfacial positioning and stability of transmembrane peptides in lipid bilayers studied by combining hydrogen/deuterium exchange and mass spectrometry J. Biol. Chem. 276, 34501-34508
    • (2001) J. Biol. Chem. , vol.276 , pp. 34501-34508
    • Demmers, J.A.1    Van Duijn, E.2    Haverkamp, J.3    Greathouse, D.V.4    Koeppe II, R.E.5    Heck, A.J.6    Killian, J.A.7
  • 38
    • 0036884106 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange of hydrophobic peptides in model membranes by electrospray ionization mass spectrometry
    • Hansen, R. K., Broadhurst, R. W., Skelton, P. C., and Arkin, I. T. (2002) Hydrogen/deuterium exchange of hydrophobic peptides in model membranes by electrospray ionization mass spectrometry J. Am. Soc. Mass Spectrom. 13, 1376-1387
    • (2002) J. Am. Soc. Mass Spectrom. , vol.13 , pp. 1376-1387
    • Hansen, R.K.1    Broadhurst, R.W.2    Skelton, P.C.3    Arkin, I.T.4
  • 40
    • 33947599164 scopus 로고    scopus 로고
    • Defining the interacting regions between apomyoglobin and lipid membrane by hydrogen/deuterium exchange coupled to mass spectrometry
    • Man, P., Montagner, C., Vernier, G., Dublet, B., Chenal, A., Forest, E., and Forge, V. (2007) Defining the interacting regions between apomyoglobin and lipid membrane by hydrogen/deuterium exchange coupled to mass spectrometry J. Mol. Biol. 368, 464-472
    • (2007) J. Mol. Biol. , vol.368 , pp. 464-472
    • Man, P.1    Montagner, C.2    Vernier, G.3    Dublet, B.4    Chenal, A.5    Forest, E.6    Forge, V.7
  • 43
    • 1642382983 scopus 로고    scopus 로고
    • Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size
    • Denisov, I. G., Grinkova, Y. V., Lazarides, A. A., and Sligar, S. G. (2004) Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size J. Am. Chem. Soc. 126, 3477-3487
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 44
    • 4244120872 scopus 로고
    • Microdetermination of phosphorus
    • Chen, P. S., Toribara, T. Y., and Warner, H. (1956) Microdetermination of phosphorus Anal. Chem. 28, 1756-1758
    • (1956) Anal. Chem. , vol.28 , pp. 1756-1758
    • Chen, P.S.1    Toribara, T.Y.2    Warner, H.3
  • 45
    • 0242380854 scopus 로고    scopus 로고
    • Preparation and quantitation of small unilamellar liposomes and large unilamellar reverse-phase evaporation liposomes
    • Düzgünes, N. (2003) Preparation and quantitation of small unilamellar liposomes and large unilamellar reverse-phase evaporation liposomes Methods Enzymol. 367, 23-27
    • (2003) Methods Enzymol. , vol.367 , pp. 23-27
    • Düzgünes, N.1
  • 46
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein-structure elucidation
    • Zhang, Z. Q. and Smith, D. L. (1993) Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein-structure elucidation Protein Sci. 2, 522-531
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.Q.1    Smith, D.L.2
  • 47
    • 0036463721 scopus 로고    scopus 로고
    • Hydrogen exchange-mass spectrometry: Optimization of digestion conditions
    • Wang, L., Pan, H., and Smith, D. L. (2002) Hydrogen exchange-mass spectrometry: optimization of digestion conditions Mol Cell Proteomics 1, 132-138
    • (2002) Mol Cell Proteomics , vol.1 , pp. 132-138
    • Wang, L.1    Pan, H.2    Smith, D.L.3
  • 48
    • 51549121010 scopus 로고    scopus 로고
    • High-speed and high-resolution UPLC separation at zero degrees Celsius
    • Wales, T. E., Fadgen, K. E., Gerhardt, G. C., and Engen, J. R. (2008) High-speed and high-resolution UPLC separation at zero degrees Celsius Anal. Chem. 80, 6815-6820
    • (2008) Anal. Chem. , vol.80 , pp. 6815-6820
    • Wales, T.E.1    Fadgen, K.E.2    Gerhardt, G.C.3    Engen, J.R.4
  • 49
    • 33751337111 scopus 로고    scopus 로고
    • Semi-automated data processing of hydrogen exchange mass spectra using HX-Express
    • Weis, D. D., Engen, J. R., and Kass, I. J. (2006) Semi-automated data processing of hydrogen exchange mass spectra using HX-Express J. Am. Soc. Mass Spectrom. 17, 17700-11703
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 17700-11703
    • Weis, D.D.1    Engen, J.R.2    Kass, I.J.3
  • 51
    • 77957810981 scopus 로고    scopus 로고
    • Effect of vitamin K-dependent protein precursor propeptide, vitamin K hydroquinone, and glutamate substrate binding on the structure and function of γ-glutamyl carboxylase
    • Higgins-Gruber, S. L., Mutucumarana, V. P., Lin, P. J., Jorgenson, J. W., Stafford, D. W., and Straight, D. L. (2010) Effect of vitamin K-dependent protein precursor propeptide, vitamin K hydroquinone, and glutamate substrate binding on the structure and function of γ-glutamyl carboxylase J. Biol. Chem. 285, 31502-31508
    • (2010) J. Biol. Chem. , vol.285 , pp. 31502-31508
    • Higgins-Gruber, S.L.1    Mutucumarana, V.P.2    Lin, P.J.3    Jorgenson, J.W.4    Stafford, D.W.5    Straight, D.L.6
  • 52
    • 0035797889 scopus 로고    scopus 로고
    • A novel fluorescence assay to study propeptide interaction with gamma-glutamyl carboxylase
    • Presnell, S. R., Tripathy, A., Lentz, B. R., Jin, D. Y., and Stafford, D. W. (2001) A novel fluorescence assay to study propeptide interaction with gamma-glutamyl carboxylase Biochemistry 40, 11723-11733
    • (2001) Biochemistry , vol.40 , pp. 11723-11733
    • Presnell, S.R.1    Tripathy, A.2    Lentz, B.R.3    Jin, D.Y.4    Stafford, D.W.5
  • 54
    • 79959456892 scopus 로고    scopus 로고
    • Advances in the mass spectrometry of membrane proteins: From individual proteins to intact complexes
    • Barrera, N. P. and Robinson, C. V. (2011) Advances in the mass spectrometry of membrane proteins: from individual proteins to intact complexes Annu. Rev. Biochem. 80, 247-271
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 247-271
    • Barrera, N.P.1    Robinson, C.V.2
  • 55
    • 79951907062 scopus 로고    scopus 로고
    • Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactions
    • Chalmers, M. J., Busby, S. A., Pascal, B. D., West, G. M., and Griffin, P. R. (2011) Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactions Expert Rev. Proteomics 8, 43-59
    • (2011) Expert Rev. Proteomics , vol.8 , pp. 43-59
    • Chalmers, M.J.1    Busby, S.A.2    Pascal, B.D.3    West, G.M.4    Griffin, P.R.5
  • 56
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander, S. W. and Kallenbach, N. R. (1983) Hydrogen exchange and structural dynamics of proteins and nucleic acids Q. Rev. Biophys. 16, 521-655
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 57
    • 0023656864 scopus 로고
    • Vitamin K-dependent carboxylase. Control of enzyme activity by the propeptide region of factor X
    • Knobloch, J. E. and Suttie, J. W. (1987) Vitamin K-dependent carboxylase. Control of enzyme activity by the propeptide region of factor X J. Biol. Chem. 262, 15334-15337
    • (1987) J. Biol. Chem. , vol.262 , pp. 15334-15337
    • Knobloch, J.E.1    Suttie, J.W.2
  • 58
    • 84870503275 scopus 로고    scopus 로고
    • Methylation of γ-carboxylated Glu (Gla) allows detection by liquid chromatography-mass spectrometry and the identification of Gla residues in the γ-glutamyl carboxylase
    • Hallgren, K. W., Zhang, D., Kinter, M., Willard, B., and Berkner, K. L. (2013) Methylation of γ-carboxylated Glu (Gla) allows detection by liquid chromatography-mass spectrometry and the identification of Gla residues in the γ-glutamyl carboxylase J. Proteome Res. 12, 2365-2374
    • (2013) J. Proteome Res. , vol.12 , pp. 2365-2374
    • Hallgren, K.W.1    Zhang, D.2    Kinter, M.3    Willard, B.4    Berkner, K.L.5
  • 59
    • 0031906040 scopus 로고    scopus 로고
    • Vitamin K-dependent carboxylation of the carboxylase
    • Berkner, K. L. and Pudota, B. N. (1998) Vitamin K-dependent carboxylation of the carboxylase Proc. Natl. Acad. Sci. U.S.A. 95, 466-471
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 466-471
    • Berkner, K.L.1    Pudota, B.N.2
  • 60
    • 79953887250 scopus 로고    scopus 로고
    • A hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle
    • Wu, S., Liu, S. B., Davis, C. H., Stafford, D. W., Kulman, J. D., and Pedersen, L. G. (2011) A hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle J. Theor. Biol. 279, 143-149
    • (2011) J. Theor. Biol. , vol.279 , pp. 143-149
    • Wu, S.1    Liu, S.B.2    Davis, C.H.3    Stafford, D.W.4    Kulman, J.D.5    Pedersen, L.G.6
  • 63
    • 33748693300 scopus 로고    scopus 로고
    • Compound heterozygosity of novel missense mutations in the gamma-glutamyl-carboxylase gene causes hereditary combined vitamin K-dependent coagulation factor deficiency
    • Darghouth, D., Hallgren, K. W., Shtofman, R. L., Mrad, A., Gharbi, Y., Maherzi, A., Kastally, R., LeRicousse, S., Berkner, K. L., and Rosa, J. P. (2006) Compound heterozygosity of novel missense mutations in the gamma-glutamyl-carboxylase gene causes hereditary combined vitamin K-dependent coagulation factor deficiency Blood 108, 1925-1931
    • (2006) Blood , vol.108 , pp. 1925-1931
    • Darghouth, D.1    Hallgren, K.W.2    Shtofman, R.L.3    Mrad, A.4    Gharbi, Y.5    Maherzi, A.6    Kastally, R.7    Lericousse, S.8    Berkner, K.L.9    Rosa, J.P.10
  • 64
    • 51849094451 scopus 로고    scopus 로고
    • Insight into the coupling mechanism of the vitamin K-dependent carboxylase: Mutation of histidine 160 disrupts glutamic acid carbanion formation and efficient coupling of vitamin K epoxidation to glutamic acid carboxylation
    • Rishavy, M. A. and Berkner, K. L. (2008) Insight into the coupling mechanism of the vitamin K-dependent carboxylase: mutation of histidine 160 disrupts glutamic acid carbanion formation and efficient coupling of vitamin K epoxidation to glutamic acid carboxylation Biochemistry 47, 9836-9846
    • (2008) Biochemistry , vol.47 , pp. 9836-9846
    • Rishavy, M.A.1    Berkner, K.L.2
  • 65
    • 84455161786 scopus 로고    scopus 로고
    • 2 to facilitate glutamate deprotonation in a concerted mechanism that drives catalysis
    • 2 to facilitate glutamate deprotonation in a concerted mechanism that drives catalysis J. Biol. Chem. 286, 44821-44832
    • (2011) J. Biol. Chem. , vol.286 , pp. 44821-44832
    • Rishavy, M.A.1    Hallgren, K.W.2    Berkner, K.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.