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Volumn 24, Issue 9, 2013, Pages 1328-1337

Analysis of a soluble (UreD:UreF:UreG)2 accessory protein complex and its interactions with klebsiella aerogenes urease by mass spectrometry

Author keywords

Chemical cross linking; Enzyme activation; Ion mobility spectrometry; MALDI TOF MS; Protein complex

Indexed keywords

CHEMICAL CROSS-LINKING; ENZYME ACTIVATION; ION MOBILITY SPECTROMETRY; MALDI TOF MS; PROTEIN COMPLEXES;

EID: 84881583095     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-013-0677-y     Document Type: Article
Times cited : (12)

References (47)
  • 3
    • 0024514293 scopus 로고
    • Microbial ureases: Significance, regulation, and molecular characterization
    • 1:CAS:528:DyaL1MXhs1yktrk%3D
    • Mobley, H.L.T.; Hausinger, R.P.: Microbial ureases: Significance, regulation, and molecular characterization. Microbiol. Rev. 53, 85-108 (1989)
    • (1989) Microbiol. Rev. , vol.53 , pp. 85-108
    • Mobley, H.L.T.1    Hausinger, R.P.2
  • 4
    • 78651492262 scopus 로고    scopus 로고
    • Urea metabolism in plants
    • 10.1016/j.plantsci.2010.11.010 1:CAS:528:DC%2BC3MXpvFSitw%3D%3D
    • Witte, C.-P.: Urea metabolism in plants. Plant Sci 180, 431-438 (2011)
    • (2011) Plant Sci , vol.180 , pp. 431-438
    • Witte, C.-P.1
  • 5
    • 0029647957 scopus 로고
    • The crystal structure of urease from Klebsiella aerogenes
    • 10.1126/science.7754395 1:CAS:528:DyaK2MXlslegsb8%3D
    • Jabri, E.; Carr, M.B.; Hausinger, R.P.; Karplus, P.A.: The crystal structure of urease from Klebsiella aerogenes. Science 268, 998-1004 (1995)
    • (1995) Science , vol.268 , pp. 998-1004
    • Jabri, E.1    Carr, M.B.2    Hausinger, R.P.3    Karplus, P.A.4
  • 6
    • 84877690063 scopus 로고    scopus 로고
    • Biosynthesis of the urease metallocenter
    • 10.1074/jbc.R112.446526 1:CAS:528:DC%2BC3sXnsFSku7Y%3D
    • Farrugia, M.A.; Macomber, L.; Hausinger, R.P.: Biosynthesis of the urease metallocenter. J. Biol. Chem. 288, 13178-13185 (2013)
    • (2013) J. Biol. Chem. , vol.288 , pp. 13178-13185
    • Farrugia, M.A.1    Macomber, L.2    Hausinger, R.P.3
  • 7
    • 0025356783 scopus 로고
    • Purification, characterization, and in vivo reconstitution of Klebsiella aerogenes urease apoenzyme
    • 1:CAS:528:DyaK3cXltFWgtb0%3D
    • Lee, M.H.; Mulrooney, S.B.; Hausinger, R.P.: Purification, characterization, and in vivo reconstitution of Klebsiella aerogenes urease apoenzyme. J. Bacteriol. 172, 4427-4431 (1990)
    • (1990) J. Bacteriol. , vol.172 , pp. 4427-4431
    • Lee, M.H.1    Mulrooney, S.B.2    Hausinger, R.P.3
  • 8
    • 23444435977 scopus 로고
    • In vitro activation of urease apoprotein and role of UreD as a chaperone required for nickel metallocenter assembly
    • 10.1073/pnas.91.8.3233 1:CAS:528:DyaK2cXkslOhsr8%3D
    • Park, I.-S.; Carr, M.B.; Hausinger, R.P.: In vitro activation of urease apoprotein and role of UreD as a chaperone required for nickel metallocenter assembly. Proc. Natl. Acad. Sci. U. S. A. 91, 3233-3237 (1994)
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 3233-3237
    • Park, I.-S.1    Carr, M.B.2    Hausinger, R.P.3
  • 9
    • 0029809744 scopus 로고    scopus 로고
    • Purification and activation properties of UreD-UreF-urease apoprotein complexes
    • 1:CAS:528:DyaK28Xls1eku7Y%3D
    • Moncrief, M.B.C.; Hausinger, R.P.: Purification and activation properties of UreD-UreF-urease apoprotein complexes. J. Bacteriol. 178, 5417-5421 (1996)
    • (1996) J. Bacteriol. , vol.178 , pp. 5417-5421
    • Moncrief, M.B.C.1    Hausinger, R.P.2
  • 10
    • 0028963917 scopus 로고
    • Evidence for the presence of urease apoprotein complexes containing UreD, UreF, and UreG in cells that are competent for in vivo enzyme activation
    • 1:CAS:528:DyaK2MXkvFemu7Y%3D
    • Park, I.-S.; Hausinger, R.P.: Evidence for the presence of urease apoprotein complexes containing UreD, UreF, and UreG in cells that are competent for in vivo enzyme activation. J. Bacteriol. 177, 1947-1951 (1995)
    • (1995) J. Bacteriol. , vol.177 , pp. 1947-1951
    • Park, I.-S.1    Hausinger, R.P.2
  • 11
    • 0030873130 scopus 로고    scopus 로고
    • Characterization of UreG, identification of a UreD-UreF-UreG complex, and evidence suggesting that a nucleotide-binding site in UreG is required for in vivo metallocenter assembly of Klebsiella aerogenes urease
    • 1:CAS:528:DyaK2sXkt1GntLc%3D
    • Moncrief, M.B.C.; Hausinger, R.P.: Characterization of UreG, identification of a UreD-UreF-UreG complex, and evidence suggesting that a nucleotide-binding site in UreG is required for in vivo metallocenter assembly of Klebsiella aerogenes urease. J. Bacteriol. 179, 4081-4086 (1997)
    • (1997) J. Bacteriol. , vol.179 , pp. 4081-4086
    • Moncrief, M.B.C.1    Hausinger, R.P.2
  • 12
    • 0029651190 scopus 로고
    • Requirement of carbon dioxide for in vitro assembly of the urease nickel metallocenter
    • 10.1126/science.7855593 1:CAS:528:DyaK2MXktVKjsLY%3D
    • Park, I.-S.; Hausinger, R.P.: Requirement of carbon dioxide for in vitro assembly of the urease nickel metallocenter. Science 267, 1156-1158 (1995)
    • (1995) Science , vol.267 , pp. 1156-1158
    • Park, I.-S.1    Hausinger, R.P.2
  • 13
    • 0027164052 scopus 로고
    • Purification and characterization of Klebsiella aerogenes UreE protein: A nickel-binding protein that functions in urease metallocenter assembly
    • 10.1002/pro.5560020617 1:CAS:528:DyaK3sXlslKiu7s%3D
    • Lee, M.H.; Pankratz, H.S.; Wang, S.; Scott, R.A.; Finnegan, M.G.; Johnson, M.K.; Ippolito, J.A.; Christianson, D.W.; Hausinger, R.P.: Purification and characterization of Klebsiella aerogenes UreE protein: A nickel-binding protein that functions in urease metallocenter assembly. Protein Sci. 2, 1042-1052 (1993)
    • (1993) Protein Sci. , vol.2 , pp. 1042-1052
    • Lee, M.H.1    Pankratz, H.S.2    Wang, S.3    Scott, R.A.4    Finnegan, M.G.5    Johnson, M.K.6    Ippolito, J.A.7    Christianson, D.W.8    Hausinger, R.P.9
  • 14
    • 0033613130 scopus 로고    scopus 로고
    • GTP-dependent activation of urease apoprotein in complex with the UreD, UreF, and UreG accessory proteins
    • 10.1073/pnas.96.20.11140 1:CAS:528:DyaK1MXmvVCnu78%3D
    • Soriano, A.; Hausinger, R.P.: GTP-dependent activation of urease apoprotein in complex with the UreD, UreF, and UreG accessory proteins. Proc. Natl. Acad. Sci. U. S. A. 96, 11140-11144 (1999)
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 11140-11144
    • Soriano, A.1    Hausinger, R.P.2
  • 15
    • 2442572212 scopus 로고    scopus 로고
    • Chemical crosslinking and mass spectrometric identification of sites of interaction for UreD, UreF, and urease
    • 10.1074/jbc.M312979200 1:CAS:528:DC%2BD2cXivVKgsLc%3D
    • Chang, Z.; Kuchar, J.; Hausinger, R.P.: Chemical crosslinking and mass spectrometric identification of sites of interaction for UreD, UreF, and urease. J. Biol. Chem. 279, 15305-15313 (2004)
    • (2004) J. Biol. Chem. , vol.279 , pp. 15305-15313
    • Chang, Z.1    Kuchar, J.2    Hausinger, R.P.3
  • 16
    • 55549099562 scopus 로고    scopus 로고
    • The structure of urease activation complexes examined by flexibility analysis, mutagenesis, and small-angle X-ray scattering
    • 10.1016/j.abb.2008.09.004 1:CAS:528:DC%2BD1cXhtlGhu7zO
    • Quiroz-Valenzuela, S.; Sukuru, S.C.K.; Hausinger, R.P.; Kuhn, L.A.; Heller, W.T.: The structure of urease activation complexes examined by flexibility analysis, mutagenesis, and small-angle X-ray scattering. Arch. Biochem. Biophys. 480, 51-57 (2008)
    • (2008) Arch. Biochem. Biophys. , vol.480 , pp. 51-57
    • Quiroz-Valenzuela, S.1    Sukuru, S.C.K.2    Hausinger, R.P.3    Kuhn, L.A.4    Heller, W.T.5
  • 17
    • 9444234584 scopus 로고    scopus 로고
    • Structures of the Klebsiella aerogenes urease apoprotein and two active-site mutants
    • 10.1021/bi960424z 1:CAS:528:DyaK28XksFyjtbs%3D
    • Jabri, E.; Karplus, P.A.: Structures of the Klebsiella aerogenes urease apoprotein and two active-site mutants. Biochemistry 35, 10616-10626 (1996)
    • (1996) Biochemistry , vol.35 , pp. 10616-10626
    • Jabri, E.1    Karplus, P.A.2
  • 19
    • 83355169697 scopus 로고    scopus 로고
    • Assembly of the preactivation complex for urease maturation in Helicobacter pylori: Crystal structure of the UreF/UreH protein complex
    • 10.1074/jbc.M111.296830 1:CAS:528:DC%2BC3MXhs1ShurnL
    • Fong, Y.H.; Wong, H.C.; Chuck, C.P.; Chen, Y.W.; Sun, H.; Wong, K.-B.: Assembly of the preactivation complex for urease maturation in Helicobacter pylori: Crystal structure of the UreF/UreH protein complex. J. Biol. Chem. 286, 43241-43249 (2011)
    • (2011) J. Biol. Chem. , vol.286 , pp. 43241-43249
    • Fong, Y.H.1    Wong, H.C.2    Chuck, C.P.3    Chen, Y.W.4    Sun, H.5    Wong, K.-B.6
  • 20
    • 33748749374 scopus 로고    scopus 로고
    • Structural insights into HypB, a GTP-binding protein that regulates metal binding
    • 10.1074/jbc.M600809200 1:CAS:528:DC%2BD28XptlKmtLk%3D
    • Gasper, R.; Scrima, A.; Wittinghofer, A.: Structural insights into HypB, a GTP-binding protein that regulates metal binding. J. Biol. Chem. 281, 27492-27502 (2006)
    • (2006) J. Biol. Chem. , vol.281 , pp. 27492-27502
    • Gasper, R.1    Scrima, A.2    Wittinghofer, A.3
  • 22
    • 33947407216 scopus 로고    scopus 로고
    • Biochemical studies on Mycobacterium tuberculosis UreG and comparative modeling reveal structural and functional conservation among the bacterial UreG family
    • 10.1021/bi6024676 1:CAS:528:DC%2BD2sXhvVGqurs%3D
    • Zambelli, B.; Musiani, F.; Savini, M.; Tucker, P.; Ciurli, S.: Biochemical studies on Mycobacterium tuberculosis UreG and comparative modeling reveal structural and functional conservation among the bacterial UreG family. Biochemistry 46, 3171-3182 (2007)
    • (2007) Biochemistry , vol.46 , pp. 3171-3182
    • Zambelli, B.1    Musiani, F.2    Savini, M.3    Tucker, P.4    Ciurli, S.5
  • 23
    • 77954583264 scopus 로고    scopus 로고
    • Mutagenesis of Klebsiella aerogenes UreG to probe nickel binding and interactions with other urease-related proteins
    • 10.1021/bi1004987 1:CAS:528:DC%2BC3cXnvVehtrg%3D
    • Boer, J.L.; Quiroz-Valenzuela, S.; Anderson, K.L.; Hausinger, R.P.: Mutagenesis of Klebsiella aerogenes UreG to probe nickel binding and interactions with other urease-related proteins. Biochemistry 49, 5859-5869 (2010)
    • (2010) Biochemistry , vol.49 , pp. 5859-5869
    • Boer, J.L.1    Quiroz-Valenzuela, S.2    Anderson, K.L.3    Hausinger, R.P.4
  • 24
    • 77951048038 scopus 로고    scopus 로고
    • Characterization of Klebsiella aerogenes urease accessory protein UreD in fusion with the maltose binding protein
    • 10.1128/JB.01426-09 1:CAS:528:DC%2BC3cXlsFKnsb0%3D
    • Carter, E.L.; Hausinger, R.P.: Characterization of Klebsiella aerogenes urease accessory protein UreD in fusion with the maltose binding protein. J. Bacteriol. 192, 2294-2304 (2010)
    • (2010) J. Bacteriol. , vol.192 , pp. 2294-2304
    • Carter, E.L.1    Hausinger, R.P.2
  • 25
    • 84858669770 scopus 로고    scopus 로고
    • Klebsiella aerogenes UreF: Identification of the UreG binding site and role in enhancing the fidelity of urease activation
    • 10.1021/bi3000897 1:CAS:528:DC%2BC38XivVCmsLo%3D
    • Boer, J.L.; Hausinger, R.P.: Klebsiella aerogenes UreF: Identification of the UreG binding site and role in enhancing the fidelity of urease activation. Biochemistry 51, 2298-2308 (2012)
    • (2012) Biochemistry , vol.51 , pp. 2298-2308
    • Boer, J.L.1    Hausinger, R.P.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • Laemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 (1970)
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 80051609875 scopus 로고    scopus 로고
    • Characterizing the resolution and accuracy of a second-generation traveling-wave ion mobility separator for biomolecular ions
    • 10.1039/c0an00987c 1:CAS:528:DC%2BC3MXpvFCqtr0%3D
    • Zhong, Y.Y.; Hyung, S.J.; Ruotolo, B.T.: Characterizing the resolution and accuracy of a second-generation traveling-wave ion mobility separator for biomolecular ions. Analyst 136, 3534-3541 (2011)
    • (2011) Analyst , vol.136 , pp. 3534-3541
    • Zhong, Y.Y.1    Hyung, S.J.2    Ruotolo, B.T.3
  • 29
    • 50249108483 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry analysis of large protein complexes
    • 10.1038/nprot.2008.78 1:CAS:528:DC%2BD1cXotFakurc%3D
    • Ruotolo, B.T.; Benesch, J.L.P.; Sandercock, A.M.; Hyung, S.J.; Robinson, C.V.: Ion mobility-mass spectrometry analysis of large protein complexes. Nat. Prot. 3, 1139-1152 (2008)
    • (2008) Nat. Prot. , vol.3 , pp. 1139-1152
    • Ruotolo, B.T.1    Benesch, J.L.P.2    Sandercock, A.M.3    Hyung, S.J.4    Robinson, C.V.5
  • 30
    • 34347228701 scopus 로고    scopus 로고
    • Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry
    • 10.1038/nprot.2007.73 1:CAS:528:DC%2BD2sXhtFGntbfP
    • Hernandez, H.; Robinson, C.V.: Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry. Nat. Prot. 2, 715-726 (2007)
    • (2007) Nat. Prot. , vol.2 , pp. 715-726
    • Hernandez, H.1    Robinson, C.V.2
  • 31
    • 78449267576 scopus 로고    scopus 로고
    • Collision cross sections of proteins and their complexes: A calibration framework and database for gas-phase structural biology
    • 10.1021/ac1022953 1:CAS:528:DC%2BC3cXhtlCltbjO
    • Bush, M.F.; Hall, Z.; Giles, K.; Hoyes, J.; Robinson, C.V.; Ruotolo, B.T.: Collision cross sections of proteins and their complexes: A calibration framework and database for gas-phase structural biology. Anal. Chem. 82, 9557-9565 (2010)
    • (2010) Anal. Chem. , vol.82 , pp. 9557-9565
    • Bush, M.F.1    Hall, Z.2    Giles, K.3    Hoyes, J.4    Robinson, C.V.5    Ruotolo, B.T.6
  • 32
    • 84862663706 scopus 로고    scopus 로고
    • Integrating mass spectrometry of intact protein complexes into structural proteomics
    • 10.1002/pmic.201100520 1:CAS:528:DC%2BC38Xoslegtbc%3D
    • Hyung, S.J.; Ruotolo, B.T.: Integrating mass spectrometry of intact protein complexes into structural proteomics. Proteomics 12, 1547-1564 (2012)
    • (2012) Proteomics , vol.12 , pp. 1547-1564
    • Hyung, S.J.1    Ruotolo, B.T.2
  • 33
    • 80053577815 scopus 로고    scopus 로고
    • Mass spectrometry: Come of age for structural and dynamical biology
    • 10.1016/j.sbi.2011.08.002 1:CAS:528:DC%2BC3MXht12rtbnE
    • Benesch, J.L.P.; Ruotolo, B.T.: Mass spectrometry: Come of age for structural and dynamical biology. Curr. Opin. Struct. Biol. 21, 641-649 (2011)
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 641-649
    • Benesch, J.L.P.1    Ruotolo, B.T.2
  • 35
    • 56149087277 scopus 로고    scopus 로고
    • Native mass spectrometry: A bridge between interactomics and structural biology
    • 10.1038/nmeth.1265 1:CAS:528:DC%2BD1cXhtlSkt77N
    • Heck, A.J.R.: Native mass spectrometry: A bridge between interactomics and structural biology. Nat. Methods 5, 927-933 (2008)
    • (2008) Nat. Methods , vol.5 , pp. 927-933
    • Heck, A.J.R.1
  • 36
    • 34548426979 scopus 로고    scopus 로고
    • The role of mass spectrometry in structure elucidation of dynamic protein complexes
    • 10.1146/annurev.biochem.76.061005.090816 1:CAS:528:DC%2BD2sXhtVehtb7K
    • Sharon, M.; Robinson, C.V.: The role of mass spectrometry in structure elucidation of dynamic protein complexes. Annu. Rev. Biochem. 76, 167-193 (2007)
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 167-193
    • Sharon, M.1    Robinson, C.V.2
  • 37
    • 34548215681 scopus 로고    scopus 로고
    • Protein complexes in the gas phase: Technology for structural genomics and proteomics
    • 10.1021/cr068289b 1:CAS:528:DC%2BD2sXotVKhu7Y%3D
    • Benesch, J.L.P.; Ruotolo, B.T.; Simmons, D.A.; Robinson, C.V.: Protein complexes in the gas phase: Technology for structural genomics and proteomics. Chem. Rev. 107, 3544-3567 (2007)
    • (2007) Chem. Rev. , vol.107 , pp. 3544-3567
    • Benesch, J.L.P.1    Ruotolo, B.T.2    Simmons, D.A.3    Robinson, C.V.4
  • 38
    • 34547131554 scopus 로고    scopus 로고
    • Analysis of protein complexes using mass spectrometry
    • 10.1038/nrm2208 1:CAS:528:DC%2BD2sXotVahtro%3D
    • Gingras, A.C.; Gstaiger, M.; Raught, B.; Aebersold, R.: Analysis of protein complexes using mass spectrometry. Nat. Rev. Mol. Cell Biol. 8, 645-654 (2007)
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 645-654
    • Gingras, A.C.1    Gstaiger, M.2    Raught, B.3    Aebersold, R.4
  • 39
    • 33748368713 scopus 로고    scopus 로고
    • Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes
    • 10.1021/ja061468q 1:CAS:528:DC%2BD28Xot1Khurc%3D
    • McKay, A.R.; Ruotolo, B.T.; Ilag, L.L.; Robinson, C.V.: Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes. J. Am. Chem. Soc. 128, 11433-11442 (2006)
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11433-11442
    • McKay, A.R.1    Ruotolo, B.T.2    Ilag, L.L.3    Robinson, C.V.4
  • 40
    • 60649094510 scopus 로고    scopus 로고
    • Collisional activation of protein complexes: Picking up the pieces
    • 10.1016/j.jasms.2008.11.014 1:CAS:528:DC%2BD1MXisFait7c%3D
    • Benesch, J.L.P.: Collisional activation of protein complexes: Picking up the pieces. J. Am. Soc. Mass Spectrom. 20, 341-348 (2009)
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 341-348
    • Benesch, J.L.P.1
  • 41
    • 33745192792 scopus 로고    scopus 로고
    • Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies
    • 10.1016/j.chembiol.2006.04.006 1:CAS:528:DC%2BD28XlvFGqsL8%3D
    • Benesch, J.L.P.; Aquilina, J.A.; Ruotolo, B.T.; Sobott, F.; Robinson, C.V.: Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies. Chem. Biol. 13, 597-605 (2006)
    • (2006) Chem. Biol. , vol.13 , pp. 597-605
    • Benesch, J.L.P.1    Aquilina, J.A.2    Ruotolo, B.T.3    Sobott, F.4    Robinson, C.V.5
  • 42
    • 4344666177 scopus 로고    scopus 로고
    • Characterising electrosprayed biomolecules using tandem-MS - The noncovalent GroEL chaperonin assembly
    • 10.1016/j.ijms.2004.05.010 1:CAS:528:DC%2BD2cXmvVOrsLY%3D
    • Sobott, F.; Robinson, C.V.: Characterising electrosprayed biomolecules using tandem-MS - the noncovalent GroEL chaperonin assembly. Int. J. Mass Spectrom. 236, 25-32 (2004)
    • (2004) Int. J. Mass Spectrom. , vol.236 , pp. 25-32
    • Sobott, F.1    Robinson, C.V.2
  • 43
    • 78649712290 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry reveals the influence of subunit packing and charge on the dissociation of multiprotein complexes
    • 10.1021/ac101778e 1:CAS:528:DC%2BC3cXhtlyks7vI
    • Erba, E.B.; Ruotolo, B.T.; Barsky, D.; Robinson, C.V.: Ion mobility-mass spectrometry reveals the influence of subunit packing and charge on the dissociation of multiprotein complexes. Anal. Chem. 82, 9702-9710 (2010)
    • (2010) Anal. Chem. , vol.82 , pp. 9702-9710
    • Erba, E.B.1    Ruotolo, B.T.2    Barsky, D.3    Robinson, C.V.4
  • 44
    • 84856614421 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry for structural proteomics
    • 10.1586/epr.11.75 1:CAS:528:DC%2BC38XhslGmt7w%3D
    • Zhong, Y.Y.; Hyung, S.J.; Ruotolo, B.T.: Ion mobility-mass spectrometry for structural proteomics. Exp. Rev. Proteom. 9, 47-58 (2012)
    • (2012) Exp. Rev. Proteom. , vol.9 , pp. 47-58
    • Zhong, Y.Y.1    Hyung, S.J.2    Ruotolo, B.T.3
  • 45
    • 77951582169 scopus 로고    scopus 로고
    • Ion mobility mass spectrometry of proteins and protein assemblies
    • 10.1039/b914002f 1:CAS:528:DC%2BC3cXltFKgtrg%3D
    • Uetrecht, C.; Rose, R.J.; van Duijn, E.; Lorenzen, K.; Heck, A.J.R.: Ion mobility mass spectrometry of proteins and protein assemblies. Chem. Soc. Rev. 39, 1633-1655 (2010)
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 1633-1655
    • Uetrecht, C.1    Rose, R.J.2    Van Duijn, E.3    Lorenzen, K.4    Heck, A.J.R.5
  • 46
    • 77954383490 scopus 로고    scopus 로고
    • Crystal structure of the first plant urease from jack bean: 83 years of journey from its first crystal to molecular structure
    • 10.1016/j.jmb.2010.05.009 1:CAS:528:DC%2BC3cXos1yltrk%3D
    • Balasubramanian, A.; Ponnuraj, K.: Crystal structure of the first plant urease from jack bean: 83 years of journey from its first crystal to molecular structure. J. Mol. Biol. 400, 274-283 (2010)
    • (2010) J. Mol. Biol. , vol.400 , pp. 274-283
    • Balasubramanian, A.1    Ponnuraj, K.2


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