메뉴 건너뛰기




Volumn 8, Issue 1, 2004, Pages 60-65

Structural change in response to ligand binding

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEIC ACID;

EID: 1042298844     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2003.11.005     Document Type: Review
Times cited : (33)

References (41)
  • 1
    • 0034716184 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry: A technology for studying noncovalent macromolecular complexes
    • Loo J.A. Electrospray ionization mass spectrometry: a technology for studying noncovalent macromolecular complexes. Int. J. Mass Spectrom. 200:2000;175-186.
    • (2000) Int. J. Mass Spectrom. , vol.200 , pp. 175-186
    • Loo, J.A.1
  • 3
    • 0035861570 scopus 로고    scopus 로고
    • Dynamic protein complexes: Insights from mass spectrometry
    • Hernandez H., Robinson C.V. Dynamic protein complexes: Insights from mass spectrometry. J. Biol. Chem. 276:2001;46685-46688.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46685-46688
    • Hernandez, H.1    Robinson, C.V.2
  • 4
    • 0036296745 scopus 로고    scopus 로고
    • Protein complexes take flight
    • Robinson C.V. Protein complexes take flight. Nat. Struct. Biol. 9:2002;505-506.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 505-506
    • Robinson, C.V.1
  • 5
    • 0035914473 scopus 로고    scopus 로고
    • Virtual interaction profiles of proteins
    • Wollacott A.M., Desjatlais J.R. Virtual interaction profiles of proteins. J. Mol. Biol. 313:2001;317-342.
    • (2001) J. Mol. Biol. , vol.313 , pp. 317-342
    • Wollacott, A.M.1    Desjatlais, J.R.2
  • 6
    • 0033496231 scopus 로고    scopus 로고
    • Combinatorial chemistry, automation and molecular diversity: New trends in the pharmaceutical industry
    • Van Hijfte L., Marciniak G., Froloff N. Combinatorial chemistry, automation and molecular diversity: new trends in the pharmaceutical industry. J. Chromatogr. B Biomed. Sci. Appl. 725:1999;3-15.
    • (1999) J. Chromatogr. B Biomed. Sci. Appl. , vol.725 , pp. 3-15
    • Van Hijfte, L.1    Marciniak, G.2    Froloff, N.3
  • 7
    • 0036006578 scopus 로고    scopus 로고
    • Drug screening of pharmaceutical discovery compounds by micro-size exclusion chromatography/mass spectrometry
    • Wabnitz P.A., Loo J.A. Drug screening of pharmaceutical discovery compounds by micro-size exclusion chromatography/mass spectrometry. Rapid Commun. Mass Spectrom. 16:2002;85-91.
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 85-91
    • Wabnitz, P.A.1    Loo, J.A.2
  • 8
    • 0036780842 scopus 로고    scopus 로고
    • Fourier transform-ion cyclotron resonance mass spectrometric resolution, identification and screening of non-covalent complexes of Hck scr homology 2 domain receptor and ligands from a 324 member peptide combinatorial library
    • Wigger M., Eyler J.R., Benner S.A., Li W., Marshall A.G. Fourier transform-ion cyclotron resonance mass spectrometric resolution, identification and screening of non-covalent complexes of Hck scr homology 2 domain receptor and ligands from a 324 member peptide combinatorial library. J. Am. Soc. Mass Spectrom. 13:2002;1162-1169.
    • (2002) J. Am. Soc. Mass Spectrom. , vol.13 , pp. 1162-1169
    • Wigger, M.1    Eyler, J.R.2    Benner, S.A.3    Li, W.4    Marshall, A.G.5
  • 9
    • 0038690168 scopus 로고    scopus 로고
    • Ligand screening by exoproteolysis and mass spectrometry in combination with computer modelling
    • Villanueva J., Fernandez-Ballaster G., Querol E., Aviles F.X., Serrano L. Ligand screening by exoproteolysis and mass spectrometry in combination with computer modelling. J. Mol. Biol. 330:2003;1039-1048.
    • (2003) J. Mol. Biol. , vol.330 , pp. 1039-1048
    • Villanueva, J.1    Fernandez-Ballaster, G.2    Querol, E.3    Aviles, F.X.4    Serrano, L.5
  • 10
    • 0034710882 scopus 로고    scopus 로고
    • Mass spectrometry and immobilized enzymes for the screening of inhibitor libraries
    • A novel twist to existing methods in which ligand depletion from a library is measured.
    • Cancilla M.T., Leavell M.D., Chow J., Leary J.A. Mass spectrometry and immobilized enzymes for the screening of inhibitor libraries. Proc. Natl. Acad. Sci. U.S.A. 97:2000;12008-12013 A novel twist to existing methods in which ligand depletion from a library is measured.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 12008-12013
    • Cancilla, M.T.1    Leavell, M.D.2    Chow, J.3    Leary, J.A.4
  • 14
    • 0036277955 scopus 로고    scopus 로고
    • Screening transthyretin amyloid fibril inhibitors - Characterisation of novel multi-protein, multi-ligand complexes by mass spectrometry
    • This paper reports the mass spectrum of a multiprotein target bound simultaneously to two hormone and two ligand molecules.
    • McCammon M.G., Scott D.J., Keetch C.A., Greene L.H., Purkey H.E., Petrassi H.M., Kelly J.W., Robinson C.V. Screening transthyretin amyloid fibril inhibitors - characterisation of novel multi-protein, multi-ligand complexes by mass spectrometry. Structure. 10:2002;851-863 This paper reports the mass spectrum of a multiprotein target bound simultaneously to two hormone and two ligand molecules.
    • (2002) Structure , vol.10 , pp. 851-863
    • McCammon, M.G.1    Scott, D.J.2    Keetch, C.A.3    Greene, L.H.4    Purkey, H.E.5    Petrassi, H.M.6    Kelly, J.W.7    Robinson, C.V.8
  • 15
    • 0141482197 scopus 로고    scopus 로고
    • Use of a microchip device coupled with mass spectrometry for ligand screening of a multi-protein target
    • Keetch C.A., Hernandez H., Sterling A., Baumert M., Allen M.H., Robinson C.V. Use of a microchip device coupled with mass spectrometry for ligand screening of a multi-protein target. Anal. Chem. 75:2003;4937-4941.
    • (2003) Anal. Chem. , vol.75 , pp. 4937-4941
    • Keetch, C.A.1    Hernandez, H.2    Sterling, A.3    Baumert, M.4    Allen, M.H.5    Robinson, C.V.6
  • 16
    • 0029638418 scopus 로고
    • Oligodeoxynucleotide fragmentation in MALDI/TOF mass spectrometry using 355-nm radiation
    • Zhu L., Parr G.R., Fitzeferald M.C., Nelson C.M., Smith L.M. Oligodeoxynucleotide fragmentation in MALDI/TOF mass spectrometry using 355-nm radiation. J. Am. Chem. Soc. 117:1995;6048-6056.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6048-6056
    • Zhu, L.1    Parr, G.R.2    Fitzeferald, M.C.3    Nelson, C.M.4    Smith, L.M.5
  • 17
    • 0037824632 scopus 로고    scopus 로고
    • Indirect assessment of small hydrophobic ligand binding to a model protein using a combination of ESI-MS and HDX/ESI MS
    • Xiao H., Kaltahov I.A., Eyles S.J. Indirect assessment of small hydrophobic ligand binding to a model protein using a combination of ESI-MS and HDX/ESI MS. J. Am. Soc. Mass Spectrom. 14:2003;506-515.
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 506-515
    • Xiao, H.1    Kaltahov, I.A.2    Eyles, S.J.3
  • 19
    • 0037172782 scopus 로고    scopus 로고
    • Determination of the stability of the noncovalent phospholipid transfer protein-lipid complex by electrospray time-of-flight mass spectrometry
    • deBrouwer A.P.M., Versluis C., Westerman J., Roelofsen B., Heck A.J.R., Wirtz K.W.A. Determination of the stability of the noncovalent phospholipid transfer protein-lipid complex by electrospray time-of-flight mass spectrometry. Biochemistry. 41:2002;8013-8018.
    • (2002) Biochemistry , vol.41 , pp. 8013-8018
    • Debrouwer, A.P.M.1    Versluis, C.2    Westerman, J.3    Roelofsen, B.4    Heck, A.J.R.5    Wirtz, K.W.A.6
  • 21
    • 0345413247 scopus 로고    scopus 로고
    • Phospholipid complexation and association with apolipoprotein C-II -insights from mass spectrometry
    • Hanson C.L., Ilag L.L., Malo J., Hatters D.M., Howlett G.J., Robinson C.V. Phospholipid complexation and association with apolipoprotein C-II -insights from mass spectrometry. Biophys. J. 85:2003;3802-3812.
    • (2003) Biophys. J. , vol.85 , pp. 3802-3812
    • Hanson, C.L.1    Ilag, L.L.2    Malo, J.3    Hatters, D.M.4    Howlett, G.J.5    Robinson, C.V.6
  • 22
    • 0037351309 scopus 로고    scopus 로고
    • Macromolecular assembly of Helicobacter pylori urease investigated by mass spectrometry
    • Pinkse M.W.H., Maier C.S., Kim J.I., Oh B.H., Heck A.J.R. Macromolecular assembly of Helicobacter pylori urease investigated by mass spectrometry. J. Mass Spectrom. 38:2003;315-320.
    • (2003) J. Mass Spectrom. , vol.38 , pp. 315-320
    • Pinkse, M.W.H.1    Maier, C.S.2    Kim, J.I.3    Oh, B.H.4    Heck, A.J.R.5
  • 23
    • 0034639980 scopus 로고    scopus 로고
    • Electrospray time-of-flight mass spectrometry of the intact MS2 virus capsid
    • Tito M.A., Tars K., Valegard K., Hajdu J., Robinson C.V. Electrospray time-of-flight mass spectrometry of the intact MS2 virus capsid. J. Am. Chem. Soc. 122:2000;3550-3551.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3550-3551
    • Tito, M.A.1    Tars, K.2    Valegard, K.3    Hajdu, J.4    Robinson, C.V.5
  • 24
    • 1042296536 scopus 로고    scopus 로고
    • Investigating viral proteins and intact viruses with mass spectrometry
    • Trauger S.A., Junker T., Siuzdak G. Investigating viral proteins and intact viruses with mass spectrometry. Top Curr. Chem. 225:2003;265-282.
    • (2003) Top Curr. Chem. , vol.225 , pp. 265-282
    • Trauger, S.A.1    Junker, T.2    Siuzdak, G.3
  • 25
    • 0042349690 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for protein structural modeling
    • Back J.W., deJong L., Muijsers A.O., deKoster C.G. Chemical cross-linking and mass spectrometry for protein structural modeling. J. Mol. Biol. 331:2003;303-313.
    • (2003) J. Mol. Biol. , vol.331 , pp. 303-313
    • Back, J.W.1    Dejong, L.2    Muijsers, A.O.3    Dekoster, C.G.4
  • 26
    • 2242437182 scopus 로고    scopus 로고
    • Characterization of an antagonist interleukin-6 dimer by stable isotope labeling, cross-linking, and mass spectrometry
    • Taverner T., Hall N.E., O'Hair R.A.J., Simpson R.J. Characterization of an antagonist interleukin-6 dimer by stable isotope labeling, cross-linking, and mass spectrometry. J. Biol. Chem. 277:2002;46487-46492.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46487-46492
    • Taverner, T.1    Hall, N.E.2    O'Hair, R.A.J.3    Simpson, R.J.4
  • 27
    • 0037058982 scopus 로고    scopus 로고
    • Identification of specific HIV-1 reverse transcriptase contacts to the viral RNA: TRNA complex by mass spectrometry and a primary amine selective reagent
    • Kvaratskhelia M., Miller J., Budihas S., Pannell L., Grice S.L. Identification of specific HIV-1 reverse transcriptase contacts to the viral RNA: tRNA complex by mass spectrometry and a primary amine selective reagent. Proc. Natl. Acad. Sci. U.S.A. 99:2002;15988-15993.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 15988-15993
    • Kvaratskhelia, M.1    Miller, J.2    Budihas, S.3    Pannell, L.4    Grice, S.L.5
  • 28
    • 0035942229 scopus 로고    scopus 로고
    • Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: Use of a chemically preactivated reagent
    • Itoh Y., Cai K., Khorana H.G. Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: use of a chemically preactivated reagent. Proc. Natl. Acad. Sci. U.S.A. 98:2001;4883-4887.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 4883-4887
    • Itoh, Y.1    Cai, K.2    Khorana, H.G.3
  • 30
    • 0036102156 scopus 로고    scopus 로고
    • Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein
    • Baerga-Ortiz A., Hughes C.A., Mandell J.G., Komives E.A. Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein. Protein Sci. 11:2002;1300-1308.
    • (2002) Protein Sci. , vol.11 , pp. 1300-1308
    • Baerga-Ortiz, A.1    Hughes, C.A.2    Mandell, J.G.3    Komives, E.A.4
  • 33
    • 0035263299 scopus 로고    scopus 로고
    • Electrospray ionisation mass spectrometry of oligonucleotide complexes with drugs, metals and proteins
    • Beck J.L., Colgrave M.L., Ralph S.F., Sheil M.M. Electrospray ionisation mass spectrometry of oligonucleotide complexes with drugs, metals and proteins. Mass. Spectrom. Rev. 20:2001;61-87.
    • (2001) Mass. Spectrom. Rev. , vol.20 , pp. 61-87
    • Beck, J.L.1    Colgrave, M.L.2    Ralph, S.F.3    Sheil, M.M.4
  • 34
    • 0034967293 scopus 로고    scopus 로고
    • Mass spectrometric study of the Escherichia coli repressor proteins, Iclr and GclR, and their complexes with DNA
    • Donald L.J., Hosfield D.J., Cuvelier S.L., Ens W., Standing K.G., Duckworth H.W. Mass spectrometric study of the Escherichia coli repressor proteins, Iclr and GclR, and their complexes with DNA. Protein Sci. 10:2001;1370-1380.
    • (2001) Protein Sci. , vol.10 , pp. 1370-1380
    • Donald, L.J.1    Hosfield, D.J.2    Cuvelier, S.L.3    Ens, W.4    Standing, K.G.5    Duckworth, H.W.6
  • 35
    • 0036882288 scopus 로고    scopus 로고
    • Analysis of protein-nucleic acid interactions by photochemical cross linking and mass spectrometry
    • Steen H., Jensen O.N. Analysis of protein-nucleic acid interactions by photochemical cross linking and mass spectrometry. Mass Spectrom. Rev. 21:2002;163-182.
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 163-182
    • Steen, H.1    Jensen, O.N.2
  • 38
  • 39
    • 0035826625 scopus 로고    scopus 로고
    • NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate
    • MacRaild C.A., Hatters D.M., Howlett G.J., Gooley P.R. NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate. Biochemistry. 40:2001;5414-5421.
    • (2001) Biochemistry , vol.40 , pp. 5414-5421
    • MacRaild, C.A.1    Hatters, D.M.2    Howlett, G.J.3    Gooley, P.R.4
  • 40
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-55.
    • (1996) J. Mol. Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 41
    • 0042820036 scopus 로고    scopus 로고
    • Direct mass spectrometric determination of the stoichiometry and binding affinity of the complexes between nucleocapsid protein and RNA stem-loop hairpins of the HIV-1 psi-recognition element
    • This reports a very recent investigation of protein-RNA binding, providing a rank order of binding affinity for three RNA hairpins that bind the HIV-1 nucleocapsid protein P7.
    • Hagan N., Fabris D. Direct mass spectrometric determination of the stoichiometry and binding affinity of the complexes between nucleocapsid protein and RNA stem-loop hairpins of the HIV-1 psi-recognition element. Biochemistry. 42:2003;10736-10745 This reports a very recent investigation of protein-RNA binding, providing a rank order of binding affinity for three RNA hairpins that bind the HIV-1 nucleocapsid protein P7.
    • (2003) Biochemistry , vol.42 , pp. 10736-10745
    • Hagan, N.1    Fabris, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.