메뉴 건너뛰기




Volumn 1844, Issue 9, 2014, Pages 1662-1674

Molecular landscape of the interaction between the urease accessory proteins UreE and UreG

Author keywords

Calorimetry; Nuclear magnetic resonance; Protein protein docking; Urease; UreE; UreG

Indexed keywords

DIMER; MONOMER; NICKEL; OLIGOMER; UNCLASSIFIED DRUG; UREASE; UREASE ACCESSORY PROTEIN E; UREASE ACCESSORY PROTEIN G;

EID: 84904181185     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2014.06.016     Document Type: Article
Times cited : (33)

References (82)
  • 1
    • 84899519638 scopus 로고    scopus 로고
    • Nonredox nickel enzymes
    • M.J. Maroney, and S. Ciurli Nonredox nickel enzymes Chem. Rev. 114 2014 4206 4228
    • (2014) Chem. Rev. , vol.114 , pp. 4206-4228
    • Maroney, M.J.1    Ciurli, S.2
  • 2
    • 0024514293 scopus 로고
    • Microbial ureases: Significance, regulation, and molecular characterization
    • H.L.T. Mobley, and R.P. Hausinger Microbial urease: significance, regulation and molecular characterization Microbiol. Rev. 53 1989 85 108 (Pubitemid 19080948)
    • (1989) Microbiological Reviews , vol.53 , Issue.1 , pp. 85-108
    • Mobley, H.L.T.1    Hausinger, R.P.2
  • 4
    • 0033303297 scopus 로고    scopus 로고
    • Structural properties of the nickel ions in urease: Novel insights into the catalytic and inhibition mechanisms
    • S. Ciurli, S. Benini, W.R. Rypniewski, K.S. Wilson, S. Miletti, and S. Mangani Structural properties of the nickel ions in urease: novel insights into the catalytic and inhibition mechanisms Coord. Chem. Rev. 190-192 1999 331 355
    • (1999) Coord. Chem. Rev. , vol.190-192 , pp. 331-355
    • Ciurli, S.1    Benini, S.2    Rypniewski, W.R.3    Wilson, K.S.4    Miletti, S.5    Mangani, S.6
  • 5
    • 0034039960 scopus 로고    scopus 로고
    • Bacterial ureases in infectious diseases
    • DOI 10.1016/S1286-4579(00)00312-9
    • R.A. Burne, and Y.Y. Chen Bacterial ureases in infectious diseases Microbes Infect. 2 2000 533 542 (Pubitemid 30387207)
    • (2000) Microbes and Infection , vol.2 , Issue.5 , pp. 533-542
    • Burne, R.A.1    Chen, Y.-Y.M.2
  • 6
    • 84865429422 scopus 로고    scopus 로고
    • Urease. Recent insights in the role of nickel
    • John Wiley & Sons, Ltd Chichester, UK
    • S. Ciurli Urease. Recent insights in the role of nickel Nickel and its surprising impact in nature vol. 2 2007 John Wiley & Sons, Ltd Chichester, UK 241 278
    • (2007) Nickel and Its Surprising Impact in Nature , vol.2 VOL. , pp. 241-278
    • Ciurli, S.1
  • 7
    • 64649100132 scopus 로고    scopus 로고
    • Functional, catalytic and kinetic properties: A review
    • B. Krajewska, and I. Ureases Functional, catalytic and kinetic properties: a review J. Mol. Catal. B Enzym. 59 2009 9 21
    • (2009) J. Mol. Catal. B Enzym. , vol.59 , pp. 9-21
    • Krajewska, B.1    Ureases, I.2
  • 9
    • 84878839032 scopus 로고    scopus 로고
    • The crystal structure of Sporosarcina pasteurii urease in a complex with citrate provides new hints for inhibitor design
    • S. Benini, P. Kosikowska, M. Cianci, L. Mazzei, A.G. Vara, Ł. Berlicki, and S. Ciurli The crystal structure of Sporosarcina pasteurii urease in a complex with citrate provides new hints for inhibitor design J. Biol. Inorg. Chem. 18 2013 391 399
    • (2013) J. Biol. Inorg. Chem. , vol.18 , pp. 391-399
    • Benini, S.1    Kosikowska, P.2    Cianci, M.3    Mazzei, L.4    Vara, A.G.5    Berlicki, Ł.6    Ciurli, S.7
  • 12
    • 0029647957 scopus 로고
    • The crystal structure of urease from Klebsiella aerogenes
    • E. Jabri, M.B. Carr, R.P. Hausinger, and P.A. Karplus The crystal structure of urease from Klebsiella aerogenes Science 268 1995 998 1004
    • (1995) Science , vol.268 , pp. 998-1004
    • Jabri, E.1    Carr, M.B.2    Hausinger, R.P.3    Karplus, P.A.4
  • 13
    • 0033081891 scopus 로고    scopus 로고
    • A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: Why urea hydrolysis costs two nickels
    • DOI 10.1016/S0969-2126(99)80026-4
    • S. Benini, W.R. Rypniewski, K.S. Wilson, S. Miletti, S. Ciurli, and S. Mangani A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels Structure 7 1999 205 216 (Pubitemid 29159705)
    • (1999) Structure , vol.7 , Issue.2 , pp. 205-216
    • Benini, S.1    Rypniewski, W.R.2    Wilson, K.S.3    Miletti, S.4    Ciurli, S.5    Mangani, S.6
  • 14
    • 0034995248 scopus 로고    scopus 로고
    • Supramolecular assembly and acid resistance of Helicobacter pylori urease
    • DOI 10.1038/88563
    • N.-C. Ha, S.-T. Oh, J.Y. Sung, K.A. Cha, M.H. Lee, and B.-H. Oh Supramolecular assembly and acid resistance of Helicobacter pylori urease Nat. Struct. Biol. 8 2001 505 509 (Pubitemid 32525008)
    • (2001) Nature Structural Biology , vol.8 , Issue.6 , pp. 505-509
    • Ha, N.-C.1    Oh, S.-T.2    Sung, J.Y.3    Cha, K.A.4    Lee, M.H.5    Oh, B.-H.6
  • 15
    • 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
    • A. Balasubramanian, and K. Ponnuraj 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 2010 274 283
    • (2010) J. Mol. Biol. , vol.400 , pp. 274-283
    • Balasubramanian, A.1    Ponnuraj, K.2
  • 18
    • 0026704632 scopus 로고
    • Klebsiella aerogenes urease gene cluster: Sequence of ureD and demonstration that four accessory genes (ureD, ureE, ureF, ureG) are involved in nickel metallocenter biosynthesis
    • M.H. Lee, S.B. Mulrooney, M.J. Renner, Y. Markowicz, and R.P. Hausinger Klebsiella aerogenes urease gene cluster: sequence of ureD and demonstration that four accessory genes (ureD, ureE, ureF, ureG) are involved in nickel metallocenter biosynthesis J. Bacteriol. 174 1992 4324 4330
    • (1992) J. Bacteriol. , vol.174 , pp. 4324-4330
    • Lee, M.H.1    Mulrooney, S.B.2    Renner, M.J.3    Markowicz, Y.4    Hausinger, R.P.5
  • 19
    • 0029651190 scopus 로고
    • Requirement of carbon dioxide for in vitro assembly of the urease nickel metallocenter
    • I.S. Park, and R.P. Hausinger Requirement of carbon dioxide for in vitro assembly of the urease nickel metallocenter Science 267 1995 1156 1158
    • (1995) Science , vol.267 , pp. 1156-1158
    • Park, I.S.1    Hausinger, R.P.2
  • 20
    • 0030598563 scopus 로고    scopus 로고
    • Metal ion interactions with urease and ureD-urease apoproteins
    • DOI 10.1021/bi952894j
    • I.-S. Park, and R.P. Hausinger Metal ion interactions with urease and UreD-urease apoproteins Biochemistry 35 1996 5345 5352 (Pubitemid 26129477)
    • (1996) Biochemistry , vol.35 , Issue.16 , pp. 5345-5352
    • Park, I.-S.1    Hausinger, R.P.2
  • 21
    • 0034633882 scopus 로고    scopus 로고
    • UreE stimulation of GTP-dependent urease activation in the UreD-UreF-UreG-urease apoprotein complex
    • A. Soriano, G.J. Colpas, and R.P. Hausinger UreE stimulation of GTP-dependent urease activation in the UreD-UreF-UreG-urease apoprotein complex Biochemistry 39 2000 12435 12440
    • (2000) Biochemistry , vol.39 , pp. 12435-12440
    • Soriano, A.1    Colpas, G.J.2    Hausinger, R.P.3
  • 22
    • 84886602296 scopus 로고    scopus 로고
    • Structure of UreG/UreF/UreH complex reveals how urease accessory proteins facilitate maturation of Helicobacter pylori urease
    • Y.H. Fong, H.C. Wong, M.H. Yuen, P.H. Lau, Y.W. Chen, and K.-B. Wong Structure of UreG/UreF/UreH complex reveals how urease accessory proteins facilitate maturation of Helicobacter pylori urease PLoS Biol. 11 2013 e1001678
    • (2013) PLoS Biol. , vol.11 , pp. 1001678
    • Fong, Y.H.1    Wong, H.C.2    Yuen, M.H.3    Lau, P.H.4    Chen, Y.W.5    Wong, K.-B.6
  • 23
    • 0035966111 scopus 로고    scopus 로고
    • 2 + transport and assembly of the urease active site by the metallochaperone UreE from Bacillus pasteurii
    • 2 + transport and assembly of the urease active site by the metallochaperone UreE from Bacillus pasteurii J. Biol. Chem. 276 2001 49365 49370
    • (2001) J. Biol. Chem. , vol.276 , pp. 49365-49370
    • Remaut, H.1    Safarov, N.2    Ciurli, S.3    Van Beeumen, J.4
  • 24
    • 84892149797 scopus 로고    scopus 로고
    • Selectivity of Ni(II) and Zn(II) binding to Sporosarcina pasteurii UreE, a metallochaperone in the urease assembly: A calorimetric and crystallographic study
    • B. Zambelli, K. Banaszak, A. Merloni, A. Kiliszek, W. Rypniewski, and S. Ciurli Selectivity of Ni(II) and Zn(II) binding to Sporosarcina pasteurii UreE, a metallochaperone in the urease assembly: a calorimetric and crystallographic study J. Biol. Inorg. Chem. 18 2013 1005 1017
    • (2013) J. Biol. Inorg. Chem. , vol.18 , pp. 1005-1017
    • Zambelli, B.1    Banaszak, K.2    Merloni, A.3    Kiliszek, A.4    Rypniewski, W.5    Ciurli, S.6
  • 25
    • 0035966067 scopus 로고    scopus 로고
    • Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation
    • H.-K. Song, S.B. Mulrooney, R. Huber, and R.P. Hausinger Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation J. Biol. Chem. 276 2001 49359 49364
    • (2001) J. Biol. Chem. , vol.276 , pp. 49359-49364
    • Song, H.-K.1    Mulrooney, S.B.2    Huber, R.3    Hausinger, R.P.4
  • 26
    • 77955689110 scopus 로고    scopus 로고
    • Crystal structures of spo and metal-bound forms of the UreE protein from Helicobacter pylori: Role of multiple metal binding sites
    • R. Shi, C. Munger, A. Asinas, S.L. Benoit, E. Miller, A. Matte, R.J. Maier, and M. Cygler Crystal structures of spo and metal-bound forms of the UreE protein from Helicobacter pylori: role of multiple metal binding sites Biochemistry 49 2010 7080 7088
    • (2010) Biochemistry , vol.49 , pp. 7080-7088
    • Shi, R.1    Munger, C.2    Asinas, A.3    Benoit, S.L.4    Miller, E.5    Matte, A.6    Maier, R.J.7    Cygler, M.8
  • 28
    • 2342527079 scopus 로고    scopus 로고
    • Nickel trafficking: Insights into the fold and function of UreE, a urease metallochaperone
    • DOI 10.1016/j.jinorgbio.2003.12.012, PII S0162013403004720
    • F. Musiani, B. Zambelli, M. Stola, and S. Ciurli Nickel trafficking: insights into the fold and function of UreE, a urease metallochaperone J. Inorg. Biochem. 98 2004 803 813 (Pubitemid 38607377)
    • (2004) Journal of Inorganic Biochemistry , vol.98 , Issue.5 , pp. 803-813
    • Musiani, F.1    Zambelli, B.2    Stola, M.3    Ciurli, S.4
  • 29
    • 0041559754 scopus 로고    scopus 로고
    • Dependence of Helicobacter pylori urease activity on the nickel-sequestering ability of the UreE accessory protein
    • DOI 10.1128/JB.185.16.4787-4795.2003
    • S. Benoit, and R.J. Maier Dependence of Helicobacter pylori urease activity on the nickel-sequestering ability of the UreE accessory protein J. Bacteriol. 185 2003 4787 4795 (Pubitemid 36962286)
    • (2003) Journal of Bacteriology , vol.185 , Issue.16 , pp. 4787-4795
    • Benoit, S.1    Maier, R.J.2
  • 31
    • 33646913281 scopus 로고    scopus 로고
    • The nickel site of Bacillus pasteurii UreE, a urease metallo-chaperone, as revealed by metal-binding studies and X-ray absorption spectroscopy
    • DOI 10.1021/bi0601003
    • M. Stola, F. Musiani, S. Mangani, P. Turano, N. Safarov, B. Zambelli, and S. Ciurli The nickel site of Bacillus pasteurii UreE, a urease metallo-chaperone, as revealed by metal-binding studies and X-ray absorption spectroscopy Biochemistry 45 2006 6495 6509 (Pubitemid 43791966)
    • (2006) Biochemistry , vol.45 , Issue.20 , pp. 6495-6509
    • Stola, M.1    Musiani, F.2    Mangani, S.3    Turano, P.4    Safarov, N.5    Zambelli, B.6    Ciurli, S.7
  • 34
    • 2342478470 scopus 로고    scopus 로고
    • Structural Characterization of the Nickel-binding Properties of Bacillus pasteurii Urease Accessory Protein (Ure)E in Solution
    • DOI 10.1074/jbc.M308390200
    • H.S. Won, Y.H. Lee, J.H. Kim, I.S. Shin, M.H. Lee, and B.J. Lee Structural characterization of the nickel-binding properties of Bacillus pasteurii urease accessory protein (Ure)E in solution J. Biol. Chem. 279 2004 17466 17472 (Pubitemid 38568100)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 17466-17472
    • Won, H.-S.1    Lee, Y.-H.2    Kim, J.-H.3    Shin, I.S.4    Lee, M.H.5    Lee, B.-J.6
  • 36
    • 84878736311 scopus 로고    scopus 로고
    • Structure of the UreD-UreF-UreG-UreE complex in Helicobacter pylori: A model study
    • F. Biagi, F. Musiani, and S. Ciurli Structure of the UreD-UreF-UreG-UreE complex in Helicobacter pylori: a model study J. Biol. Inorg. Chem. 18 2013 571 577
    • (2013) J. Biol. Inorg. Chem. , vol.18 , pp. 571-577
    • Biagi, F.1    Musiani, F.2    Ciurli, S.3
  • 37
    • 65649135871 scopus 로고    scopus 로고
    • Practical protocols for production of very high yields of recombinant proteins using Escherichia coli
    • A. Sivashanmugam, V. Murray, C. Cui, Y. Zhang, J. Wang, and Q. Li Practical protocols for production of very high yields of recombinant proteins using Escherichia coli Protein Sci. 18 2009 936 948
    • (2009) Protein Sci. , vol.18 , pp. 936-948
    • Sivashanmugam, A.1    Murray, V.2    Cui, C.3    Zhang, Y.4    Wang, J.5    Li, Q.6
  • 41
    • 33746248741 scopus 로고    scopus 로고
    • Optimizing the process of nuclear magnetic resonance spectrum analysis and computer aided resonance assignment
    • Swiss Federal Institute of Technology of Zurich Zurich
    • R.L.J. Keller Optimizing the process of nuclear magnetic resonance spectrum analysis and computer aided resonance assignment Swiss Federal Institute of Technology 2004 Swiss Federal Institute of Technology of Zurich Zurich
    • (2004) Swiss Federal Institute of Technology
    • Keller, R.L.J.1
  • 42
    • 0030666085 scopus 로고    scopus 로고
    • Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation
    • DOI 10.1021/bi9712091
    • R.A. Williamson, M.D. Carr, T.A. Frenkiel, J. Feeney, and R.B. Freedman Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation Biochemistry 36 1997 13882 13889 (Pubitemid 27494895)
    • (1997) Biochemistry , vol.36 , Issue.45 , pp. 13882-13889
    • Williamson, R.A.1    Carr, M.D.2    Frenkiel, T.A.3    Feeney, J.4    Freedman, R.B.5
  • 43
    • 84880167453 scopus 로고    scopus 로고
    • Using chemical shift perturbation to characterise ligand binding
    • M.P. Williamson Using chemical shift perturbation to characterise ligand binding Prog. Nucl. Magn. Reson. Spectrosc. 73 2013 1 16
    • (2013) Prog. Nucl. Magn. Reson. Spectrosc. , vol.73 , pp. 1-16
    • Williamson, M.P.1
  • 44
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: A tool for multiple protein sequence and structure alignments
    • DOI 10.1093/nar/gkn072
    • J. Pei, B.H. Kim, and N.V. Grishin PROMALS3D: a tool for multiple protein sequence and structure alignments Nucleic Acids Res. 36 2008 2295 2300 (Pubitemid 351567002)
    • (2008) Nucleic Acids Research , vol.36 , Issue.7 , pp. 2295-2300
    • Pei, J.1    Kim, B.-H.2    Grishin, N.V.3
  • 46
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • DOI 10.1110/ps.062416606
    • M.Y. Shen, and A. Sali Statistical potential for assessment and prediction of protein structures Protein Sci. 15 2006 2507 2524 (Pubitemid 44771688)
    • (2006) Protein Science , vol.15 , Issue.11 , pp. 2507-2524
    • Shen, M.-Y.1    Sali, A.2
  • 48
    • 3242875210 scopus 로고    scopus 로고
    • ElNemo: A normal mode web server for protein movement analysis and the generation of templates for molecular replacement
    • K. Suhre, and Y.H. Sanejouand ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement Nucleic Acids Res. 32 2004 W610 W614
    • (2004) Nucleic Acids Res. , vol.32
    • Suhre, K.1    Sanejouand, Y.H.2
  • 49
    • 84898999318 scopus 로고    scopus 로고
    • FeON-FeOFF: The Helicobacter pylori fur regulator commutates iron-responsive transcription by discriminative readout of opposed DNA grooves
    • F. Agriesti, D. Roncarati, F. Musiani, C. Del Campo, M. Iurlaro, F. Sparla, S. Ciurli, A. Danielli, and V. Scarlato FeON-FeOFF: the Helicobacter pylori Fur regulator commutates iron-responsive transcription by discriminative readout of opposed DNA grooves Nucleic Acids Res. 42 2014 3138 3151
    • (2014) Nucleic Acids Res. , vol.42 , pp. 3138-3151
    • Agriesti, F.1    Roncarati, D.2    Musiani, F.3    Del Campo, C.4    Iurlaro, M.5    Sparla, F.6    Ciurli, S.7    Danielli, A.8    Scarlato, V.9
  • 50
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • DOI 10.1021/ja026939x
    • C. Dominguez, R. Boelens, and A.M. Bonvin HADDOCK: a protein-protein docking approach based on biochemical or biophysical information J. Am. Chem. Soc. 125 2003 1731 1737 (Pubitemid 36232568)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.7 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 52
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • H. Ashkenazy, E. Erez, E. Martz, T. Pupko, and N. Ben-Tal ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids Nucleic Acids Res. 38 2010 W529 W533
    • (2010) Nucleic Acids Res. , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 53
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information
    • DOI 10.1093/bioinformatics/19.1.163
    • F. Glaser, T. Pupko, I. Paz, R.E. Bell, D. Bechor-Shental, E. Martz, and N. Ben-Tal ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information Bioinformatics 19 2003 163 164 (Pubitemid 36150199)
    • (2003) Bioinformatics , vol.19 , Issue.1 , pp. 163-164
    • Glaser, F.1    Pupko, T.2    Paz, I.3    Bell, R.E.4    Bechor-Shental, D.5    Martz, E.6    Ben-Tal, N.7
  • 57
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • B. Honig, and A. Nicholls Classical electrostatics in biology and chemistry Science 268 1995 1144 1149
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 60
    • 33746268615 scopus 로고    scopus 로고
    • Intrinsically disordered structure of Bacillus pasteurii UreG as revealed by steady-state and time-resolved fluorescence spectroscopy
    • DOI 10.1021/bi060227s
    • P. Neyroz, B. Zambelli, and S. Ciurli Intrinsically disordered structure of Bacillus pasteurii UreG as revealed by steady-state and time-resolved fluorescence spectroscopy Biochemistry 45 2006 8918 8930 (Pubitemid 44100688)
    • (2006) Biochemistry , vol.45 , Issue.29 , pp. 8918-8930
    • Neyroz, P.1    Zambelli, B.2    Ciurli, S.3
  • 61
    • 84877012927 scopus 로고    scopus 로고
    • Conformational fluctuations of UreG, an intrinsically disordered enzyme
    • F. Musiani, E. Ippoliti, C. Micheletti, P. Carloni, and S. Ciurli Conformational fluctuations of UreG, an intrinsically disordered enzyme Biochemistry 52 2013 2949 2954
    • (2013) Biochemistry , vol.52 , pp. 2949-2954
    • Musiani, F.1    Ippoliti, E.2    Micheletti, C.3    Carloni, P.4    Ciurli, S.5
  • 62
    • 33947407216 scopus 로고    scopus 로고
    • Biochemical studies on Mycobacterium tuberculosis UreG and comparative modeling reveal structural and functional conservation among the bacterial UreG family
    • DOI 10.1021/bi6024676
    • B. Zambelli, F. Musiani, M. Savini, P. Tucker, and S. Ciurli Biochemical studies on Mycobacterium tuberculosis UreG and comparative modeling reveal structural and functional conservation among the bacterial UreG family Biochemistry 46 2007 3171 3182 (Pubitemid 46449139)
    • (2007) Biochemistry , vol.46 , Issue.11 , pp. 3171-3182
    • Zambelli, B.1    Musiani, F.2    Savini, M.3    Tucker, P.4    Ciurli, S.5
  • 63
    • 58949095956 scopus 로고    scopus 로고
    • 2 +-linked dimerization of UreG from Helicobacter pylori, a chaperone involved in nickel trafficking and urease activation
    • 2 +-linked dimerization of UreG from Helicobacter pylori, a chaperone involved in nickel trafficking and urease activation Proteins 74 2009 222 239
    • (2009) Proteins , vol.74 , pp. 222-239
    • Zambelli, B.1    Turano, P.2    Musiani, F.3    Neyroz, P.4    Ciurli, S.5
  • 64
    • 82655175484 scopus 로고    scopus 로고
    • Insights in the (un)structural organization of Bacillus pasteurii UreG, an intrinsically disordered GTPase enzyme
    • B. Zambelli, N. Cremades, P. Neyroz, P. Turano, V.N. Uversky, and S. Ciurli Insights in the (un)structural organization of Bacillus pasteurii UreG, an intrinsically disordered GTPase enzyme Mol. Biosyst. 8 2012 220 228
    • (2012) Mol. Biosyst. , vol.8 , pp. 220-228
    • Zambelli, B.1    Cremades, N.2    Neyroz, P.3    Turano, P.4    Uversky, V.N.5    Ciurli, S.6
  • 65
    • 84856908404 scopus 로고    scopus 로고
    • Biochemical and structural studies on native and recombinant Glycine max UreG: A detailed characterization of a plant urease accessory protein
    • R. Real-Guerra, F. Staniscuaski, B. Zambelli, F. Musiani, S. Ciurli, and C.R. Carlini Biochemical and structural studies on native and recombinant Glycine max UreG: a detailed characterization of a plant urease accessory protein Plant Mol. Biol. 78 2012 461 475
    • (2012) Plant Mol. Biol. , vol.78 , pp. 461-475
    • Real-Guerra, R.1    Staniscuaski, F.2    Zambelli, B.3    Musiani, F.4    Ciurli, S.5    Carlini, C.R.6
  • 66
    • 0037014597 scopus 로고    scopus 로고
    • Effects of salt and nickel ion on the conformational stability of Bacillus pasteurii UreE
    • DOI 10.1016/S0014-5793(02)02919-8, PII S0014579302029198
    • Y.-H. Lee, H.-S. Won, M.-H. Lee, and B.-J. Lee Effects of salt and nickel ion on the conformational stability of Bacillus pasteurii UreE FEBS Lett. 522 2002 135 140 (Pubitemid 34722512)
    • (2002) FEBS Letters , vol.522 , Issue.1-3 , pp. 135-140
    • Lee, Y.-H.1    Won, H.-S.2    Lee, M.-H.3    Lee, B.-J.4
  • 69
    • 0034669882 scopus 로고    scopus 로고
    • Why are natively unfolded proteins unstructured under physiologic conditions?
    • V.N. Uversky, J.R. Gillespie, and A.L. Fink Why are natively unfolded proteins unstructured under physiologic conditions? Proteins 41 2000 415 427
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 71
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • DOI 10.1016/j.tibs.2005.07.008, PII S0968000405002185
    • P. Tompa, C. Szasz, and L. Buday Structural disorder throws new light on moonlighting Trends Biochem. Sci. 30 2005 484 489 (Pubitemid 41206503)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.9 , pp. 484-489
    • Tompa, P.1    Szasz, C.2    Buday, L.3
  • 72
    • 33751552347 scopus 로고    scopus 로고
    • Sensitivity of secondary structure propensities to sequence differences between α- and γ-synuclein: Implications for fibrillation
    • DOI 10.1110/ps.062465306
    • J.A. Marsh, V.K. Singh, Z. Jia, and J.D. Forman-Kay Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation Protein Sci. 15 2006 2795 2804 (Pubitemid 44833760)
    • (2006) Protein Science , vol.15 , Issue.12 , pp. 2795-2804
    • Marsh, J.A.1    Singh, V.K.2    Jia, Z.3    Forman-Kay, J.D.4
  • 73
    • 68349093958 scopus 로고    scopus 로고
    • TALOS +: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Y. Shen, F. Delaglio, G. Cornilescu, and A. Bax TALOS +: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts J. Biomol. NMR 44 2009 213 223
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 74
    • 30044434744 scopus 로고    scopus 로고
    • Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state
    • DOI 10.1073/pnas.0507603102
    • D. Tobi, and I. Bahar Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state Proc. Natl. Acad. Sci. U. S. A. 102 2005 18908 18913 (Pubitemid 43049540)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.52 , pp. 18908-18913
    • Tobi, D.1    Bahar, I.2
  • 75
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • D.D. Boehr, R. Nussinov, and P.E. Wright The role of dynamic conformational ensembles in biomolecular recognition Nat. Chem. Biol. 5 2009 789 796
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 76
    • 2642605367 scopus 로고    scopus 로고
    • Demonstration of protein-protein interaction specificity by NMR chemical shift mapping
    • P. Rajagopal, E.B. Waygood, J. Reizer, M.H. Saier Jr., and R.E. Klevit Demonstration of protein-protein interaction specificity by NMR chemical shift mapping Protein Sci. 6 1997 2624 2627 (Pubitemid 28006699)
    • (1997) Protein Science , vol.6 , Issue.12 , pp. 2624-2627
    • Rajagopal, P.1    Bruce Waygood, E.2    Reizer, J.3    Saier Jr., M.H.4    Klevit, R.E.5
  • 77
    • 0038470801 scopus 로고    scopus 로고
    • Transient protein interactions studied by NMR spectroscopy: The case of cytochrome c and adrenodoxin
    • DOI 10.1021/bi0342968
    • J.A. Worrall, W. Reinle, R. Bernhardt, and M. Ubbink Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C and adrenodoxin Biochemistry 42 2003 7068 7076 (Pubitemid 36706490)
    • (2003) Biochemistry , vol.42 , Issue.23 , pp. 7068-7076
    • Worrall, J.A.R.1    Reinle, W.2    Bernhardt, R.3    Ubbink, M.4
  • 78
    • 0141750584 scopus 로고    scopus 로고
    • Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats
    • DOI 10.1016/j.jmb.2003.08.050
    • J. Morrison, J.C. Yang, M. Stewart, and D. Neuhaus Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats J. Mol. Biol. 333 2003 587 603 (Pubitemid 37222408)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.3 , pp. 587-603
    • Morrison, J.1    Yang, J.-C.2    Stewart, M.3    Neuhaus, D.4
  • 79
    • 84896717085 scopus 로고    scopus 로고
    • An ensemble of rapidly interconverting orientations in electrostatic protein-peptide complexes characterized by NMR spectroscopy
    • J.Y. Guan, J.M. Foerster, J.W. Drijfhout, M. Timmer, A. Blok, G.M. Ullmann, and M. Ubbink An ensemble of rapidly interconverting orientations in electrostatic protein-peptide complexes characterized by NMR spectroscopy Chembiochem 15 2014 556 566
    • (2014) Chembiochem , vol.15 , pp. 556-566
    • Guan, J.Y.1    Foerster, J.M.2    Drijfhout, J.W.3    Timmer, M.4    Blok, A.5    Ullmann, G.M.6    Ubbink, M.7
  • 81
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • DOI 10.1016/0022-2836(88)90606-7
    • J. Janin, S. Miller, and C. Chothia Surface, subunit interfaces and interior of oligomeric proteins J. Mol. Biol. 204 1988 155 164 (Pubitemid 19011740)
    • (1988) Journal of Molecular Biology , vol.204 , Issue.1 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.