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Volumn 48, Issue 21, 2009, Pages 4577-4586

Mapping protein-protein interactions by localized oxidation: Consequences of the reach of hydroxyl radical

Author keywords

[No Author keywords available]

Indexed keywords

[CARBONYL; AFFINITY PURIFICATION; CARBONYL FORMATION; CLEAVAGE EVENTS; CYSTEINE RESIDUES; FENTON REACTIONS; FOOTPRINTING; HYDROXYL RADICALS; IRON CHELATE; LOCALIZED OXIDATION; POLYPEPTIDE BACKBONES; PROTEIN CARBONYLS; PROTEIN FOOTPRINTING; PROTEIN-PROTEIN INTERACTIONS; RNA POLYMERASE; SIDE CHAIN MODIFICATIONS; SPECIFIC TAGS; TETRAACETIC ACID;

EID: 66349091586     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900273j     Document Type: Article
Times cited : (23)

References (27)
  • 1
    • 48149085922 scopus 로고    scopus 로고
    • Synchrotron protein footprinting supports substrate translocation by ClpA via ATP-induced movements of the D2 loop
    • Bohon, J., Jennings, L. D., Phillips, C. M., Licht, S., and Chance, M. R. (2008) Synchrotron protein footprinting supports substrate translocation by ClpA via ATP-induced movements of the D2 loop. Structure 16, 1157-1165.
    • (2008) Structure , vol.16 , pp. 1157-1165
    • Bohon, J.1    Jennings, L.D.2    Phillips, C.M.3    Licht, S.4    Chance, M.R.5
  • 2
    • 34548337296 scopus 로고    scopus 로고
    • Hydroxyl Radical-Mediated Modification of Proteins as Probes for Structural Proteomics
    • Xu, G., and Chance, M. R. (2007) Hydroxyl Radical-Mediated Modification of Proteins as Probes for Structural Proteomics. Chem. Rev. 107, 3514-3543.
    • (2007) Chem. Rev. , vol.107 , pp. 3514-3543
    • Xu, G.1    Chance, M.R.2
  • 3
    • 5444275331 scopus 로고    scopus 로고
    • Mapping the Location of TFIIB within the RNA Polymerase II Transcription Preinitiation Complex: A Model for the Structure of the PIC
    • Chen, H.-T., and Hahn, S. (2004) Mapping the Location of TFIIB within the RNA Polymerase II Transcription Preinitiation Complex: A Model for the Structure of the PIC. Cell 119, 169-180.
    • (2004) Cell , vol.119 , pp. 169-180
    • Chen, H.-T.1    Hahn, S.2
  • 4
    • 33745842952 scopus 로고    scopus 로고
    • A DNA-tethered cleavage probe reveals the path for promoter DNA in the yeast preinitiation complex
    • Miller, G., and Hahn, S. (2006) A DNA-tethered cleavage probe reveals the path for promoter DNA in the yeast preinitiation complex. Nat. Struct. Mol. Biol. 13, 603-610.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 603-610
    • Miller, G.1    Hahn, S.2
  • 5
    • 0025718819 scopus 로고
    • Transfer of Oxygen from an Artificial Protease to Peptide Carbon during Proteolysis
    • Rana, T. M., and Meares, C. F. (1991) Transfer of Oxygen from an Artificial Protease to Peptide Carbon During Proteolysis. Proc. Natl. Acad. Sci. U.S.A. 88, 10578-10582.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10578-10582
    • Rana, T.M.1    Meares, C.F.2
  • 7
    • 0034284365 scopus 로고    scopus 로고
    • Protein-protein interactions mapped by artificial proteases: Where σ factors bind to RNA polymerase
    • Datwyler, S. A., and Meares, C. F. (2000) Protein-protein interactions mapped by artificial proteases: Where σ factors bind to RNA polymerase. Trends Biochem. Sci. 25, 408-414.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 408-414
    • Datwyler, S.A.1    Meares, C.F.2
  • 8
    • 0027183423 scopus 로고
    • Oxidation of Free Amino Acids and Amino Acid Residues in Proteins by Radiolysis and by Metal-Catalyzed Reactions
    • Stadtman, E. R. (1993) Oxidation of Free Amino Acids and Amino Acid Residues in Proteins by Radiolysis and by Metal-Catalyzed Reactions. Annu. Rev. Biochem. 62, 797-821.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 10
    • 0025108594 scopus 로고
    • Use of Mono Q High-Resolution Ion-Exchange Chromatography to Obtain Highly Pure and Active Escherichia coli RNA Polymerase
    • Hager, D. A., Jin, D. J., and Burgess, R. R. (1990) Use of Mono Q High-Resolution Ion-Exchange Chromatography to Obtain Highly Pure and Active Escherichia coli RNA Polymerase. Biochemistry 29, 7890-7894.
    • (1990) Biochemistry , vol.29 , pp. 7890-7894
    • Hager, D.A.1    Jin, D.J.2    Burgess, R.R.3
  • 11
    • 0016748261 scopus 로고
    • Procedure for the rapid, large-scale purification of Escherichia coli DNA-dependent RNA polymerase involving polymin P precipitation and DNA-cellulose chromatography
    • Burgess, R. R., and Jendrisak, J. J. (1975) Procedure for the rapid, large-scale purification of Escherichia coli DNA-dependent RNA polymerase involving polymin P precipitation and DNA-cellulose chromatography. Biochemistry 14, 4634-4638.
    • (1975) Biochemistry , vol.14 , pp. 4634-4638
    • Burgess, R.R.1    Jendrisak, J.J.2
  • 12
    • 0037006985 scopus 로고    scopus 로고
    • Proteolytic DNA for mapping protein-DNA interactions
    • Schmidt, B. D., and Meares, C. F. (2002) Proteolytic DNA for mapping protein-DNA interactions. Biochemistry 41, 4186-4192.
    • (2002) Biochemistry , vol.41 , pp. 4186-4192
    • Schmidt, B.D.1    Meares, C.F.2
  • 14
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. K., McCormack, A. L., and Yates, J. R. III (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 16
    • 0030954272 scopus 로고    scopus 로고
    • Computational modelling of low-energy electron-induced DNA damage by early physical and chemical events
    • Nikjoo, H., O'Neill, P., Goodhead, D. T., and Terrissol, M. (1997) Computational modelling of low-energy electron-induced DNA damage by early physical and chemical events. Int. J. Radiat. Biol. 71, 467-483.
    • (1997) Int. J. Radiat. Biol. , vol.71 , pp. 467-483
    • Nikjoo, H.1    O'Neill, P.2    Goodhead, D.T.3    Terrissol, M.4
  • 17
    • 0026318881 scopus 로고
    • + Current in the Molluscan Neuron: A Diffusion- Reaction Model
    • + Current in the Molluscan Neuron: A Diffusion- Reaction Model. J. Gen. Physiol. 98, 835-848.
    • (1991) J. Gen. Physiol. , vol.98 , pp. 835-848
    • Huang, R.-C.1    Gillette, R.2
  • 20
    • 8144221240 scopus 로고    scopus 로고
    • Quantifying Aggregation and Association in Three-Dimensional Landscapes
    • Scheuerell, M. D. (2004) Quantifying Aggregation and Association in Three-Dimensional Landscapes. Ecology 85, 2332-2340.
    • (2004) Ecology , vol.85 , pp. 2332-2340
    • Scheuerell, M.D.1
  • 21
    • 33644846943 scopus 로고    scopus 로고
    • Method to site-specifically identify and quantitate carbonyl end products of protein oxidation using oxidation-dependent element coded affinity tags (O-ECAT) and nanoliquid chromatography Fourier transform mass spectrometry
    • Lee, S., Young, N. L., Whetstone, P. A., Cheal, S. M., Benner, W. H., Lebrilla, C. B., and Meares, C. F. (2006) Method to site-specifically identify and quantitate carbonyl end products of protein oxidation using oxidation-dependent element coded affinity tags (O-ECAT) and nanoliquid chromatography Fourier transform mass spectrometry. J. Proteome Res. 5, 539-547.
    • (2006) J. Proteome Res. , vol.5 , pp. 539-547
    • Lee, S.1    Young, N.L.2    Whetstone, P.A.3    Cheal, S.M.4    Benner, W.H.5    Lebrilla, C.B.6    Meares, C.F.7
  • 22
    • 17644362744 scopus 로고    scopus 로고
    • Affinity Chromatographic Selection of Carbonylated Proteins Followed by Identification of Oxidation Sites Using Tandem Mass Spectrometry
    • Mirzaei, H., and Regnier, F. E. (2005) Affinity Chromatographic Selection of Carbonylated Proteins Followed by Identification of Oxidation Sites Using Tandem Mass Spectrometry. Anal. Chem. 77, 2386-2392.
    • (2005) Anal. Chem. , vol.77 , pp. 2386-2392
    • Mirzaei, H.1    Regnier, F.E.2
  • 24
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., and Aebersold, R. (1999) Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17, 994-999.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 25
  • 27
    • 0037123659 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution
    • Murakami, K. S., Masuda, S., and Darst, S. A. (2002) Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution. Science 296, 1280-1284.
    • (2002) Science , vol.296 , pp. 1280-1284
    • Murakami, K.S.1    Masuda, S.2    Darst, S.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.