메뉴 건너뛰기




Volumn 446, Issue , 2008, Pages 109-130

Mass spectrometric determination of protein ubiquitination

Author keywords

Diagnostic ions; Mass spectrometry; MS MS; Ubiquitination

Indexed keywords


EID: 84934441154     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-60327-84-7_8     Document Type: Article
Times cited : (4)

References (34)
  • 1
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. (1996) Ubiquitin-dependent protein degradation. Ann. Rev. Genet. 30, 405-439.
    • (1996) Ann. Rev. Genet , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 2
    • 0020055316 scopus 로고
    • Selective arrangement of ubiquitinated and Dl protein-containing nucleosomes within the Drosophila genome
    • Levinger, L. and Varshavsky, A. (1982) Selective arrangement of ubiquitinated and Dl protein-containing nucleosomes within the Drosophila genome. Cell 28, 375-385.
    • (1982) Cell , vol.28 , pp. 375-385
    • Levinger, L.1    Varshavsky, A.2
  • 3
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzer, M., Murray, A. W., and Kirschner, M. W. (1991) Cyclin is degraded by the ubiquitin pathway. Nature 349, 132-138.
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 4
    • 0037462645 scopus 로고    scopus 로고
    • The N-terminal truncated isoform of SOCS3 translated from an alternative initiation AUG codon under stress conditions is stable due to the lack of a major ubiquitination site, Lys-6
    • Sasaki, A., Inagaki-Ohara, K., Yoshida, T., Yamanaka, A., Sasaki, M., Yasukawa, H., Koromilas, A., and Yoshimura, A. (2003) The N-terminal truncated isoform of SOCS3 translated from an alternative initiation AUG codon under stress conditions is stable due to the lack of a major ubiquitination site, Lys-6. Journal of Biological Chemistry 278, 2432-2436.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 2432-2436
    • Sasaki, A.1    Inagaki-Ohara, K.2    Yoshida, T.3    Yamanaka, A.4    Sasaki, M.5    Yasukawa, H.6    Koromilas, A.7    Yoshimura, A.8
  • 5
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A. and Ciechanover, A. (1992) The ubiquitin system for protein degradation. Ann. Rev. Biochem. 61.
    • (1992) Ann. Rev. Biochem , vol.61
    • Hershko, A.1    Ciechanover, A.2
  • 6
    • 0034791090 scopus 로고    scopus 로고
    • Ubiquitin enters the new millennium
    • Pickart, C. M. (2001) Ubiquitin enters the new millennium. Mol. Cell 8, 499-504.
    • (2001) Mol. Cell , vol.8 , pp. 499-504
    • Pickart, C.M.1
  • 7
    • 0035823032 scopus 로고    scopus 로고
    • A new ticket for entry into budding vesicles-ubiquitin
    • Hicke, L. (2001) A new ticket for entry into budding vesicles-ubiquitin. Cell 106, 527-530.
    • (2001) Cell , vol.106 , pp. 527-530
    • Hicke, L.1
  • 9
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun, Z. W., and Allis, C. D. (2002) Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 418, 104-108.
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 10
    • 0037123605 scopus 로고    scopus 로고
    • Emerging roles of ubiquitin in transcription regulation
    • Conaway, R. C., Brower, C. S., and Conaway, J. W. (2002) Emerging roles of ubiquitin in transcription regulation. Science 296, 1254-1258.
    • (2002) Science , vol.296 , pp. 1254-1258
    • Conaway, R.C.1    Brower, C.S.2    Conaway, J.W.3
  • 11
    • 0034253588 scopus 로고    scopus 로고
    • Evolution and function of ubiquitin-like protein-conjugation systems
    • Hochstrasser, M. (2002) Evolution and function of ubiquitin-like protein-conjugation systems. Nature Cell Biology 2, E153-E157.
    • (2002) Nature Cell Biology , vol.2
    • Hochstrasser, M.1
  • 12
    • 23144452492 scopus 로고    scopus 로고
    • Weighing in on ubiquitin: The expanding role of mass-spectrometry-based proteomics
    • Kirkpatrick, D. S., Denison, C., and Gygi, S. P. (2005) Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics. Nature Cell Biology 7, 750-757.
    • (2005) Nature Cell Biology , vol.7 , pp. 750-757
    • Kirkpatrick, D.S.1    Denison, C.2    Gygi, S.P.3
  • 14
    • 0042734593 scopus 로고    scopus 로고
    • Multiple functional categories of proteins identified in an in vitro cellular ubiquitin affinity extract using shotgun peptide sequencing
    • Gururaja, T., Li, W., Noble, W. S., Payan, D. G., and Anderson, D. C. (2003) Multiple functional categories of proteins identified in an in vitro cellular ubiquitin affinity extract using shotgun peptide sequencing. Journal of proteome research 2, 394-404.
    • (2003) Journal of proteome research , vol.2 , pp. 394-404
    • Gururaja, T.1    Li, W.2    Noble, W.S.3    Payan, D.G.4    Anderson, D.C.5
  • 15
    • 20044373693 scopus 로고    scopus 로고
    • Proteomic identification of ubiquitinated proteins from human cells expressing His-tagged ubiquitin
    • Kirkpatrick, D. S., Weldon, S. F., Tsaprailis, G., Liebler, D. C., and Gandolfi, A. J. (2005) Proteomic identification of ubiquitinated proteins from human cells expressing His-tagged ubiquitin. Proteomics 5, 2104-2111.
    • (2005) Proteomics , vol.5 , pp. 2104-2111
    • Kirkpatrick, D.S.1    Weldon, S.F.2    Tsaprailis, G.3    Liebler, D.C.4    Gandolfi, A.J.5
  • 16
    • 29144505073 scopus 로고    scopus 로고
    • Proteomic Analysis of Ubiquitinated Proteins from Human MCF-7 Breast Cancer Cells by Immunoaffinity Purification and Mass Spectrometry
    • Vasilescu, J., Smith, J. C., Ethier, M., and Figeys, D. (2005) Proteomic Analysis of Ubiquitinated Proteins from Human MCF-7 Breast Cancer Cells by Immunoaffinity Purification and Mass Spectrometry. Journal of Proteome Research 4, 2192-2200.
    • (2005) Journal of Proteome Research , vol.4 , pp. 2192-2200
    • Vasilescu, J.1    Smith, J.C.2    Ethier, M.3    Figeys, D.4
  • 19
    • 0032528012 scopus 로고    scopus 로고
    • Modulation of calmodulin function by ubiquitin-calmodulin ligase and identification of the responsible ubiquitylation site in vertebrate calmodulin
    • Laub, M., Steppuhn, J. A., Bluggel, M., Immler, D., Meyer, H. E., and Jennissen, H. P. (1998) Modulation of calmodulin function by ubiquitin-calmodulin ligase and identification of the responsible ubiquitylation site in vertebrate calmodulin. European Journal of Biochemistry 255, 422-431.
    • (1998) European Journal of Biochemistry , vol.255 , pp. 422-431
    • Laub, M.1    Steppuhn, J.A.2    Bluggel, M.3    Immler, D.4    Meyer, H.E.5    Jennissen, H.P.6
  • 20
    • 0037161303 scopus 로고    scopus 로고
    • Direct Identification of a G Protein Ubiquitination Site by Mass Spectrometry
    • Marotti, L. A., Jr., Newitt, R., Wang, Y., Aebersold, R., and Dohlman, H. G. (2002) Direct Identification of a G Protein Ubiquitination Site by Mass Spectrometry. Biochemistry 41, 5067-5074.
    • (2002) Biochemistry , vol.41 , pp. 5067-5074
    • Marotti Jr., L.A.1    Newitt, R.2    Wang, Y.3    Aebersold, R.4    Dohlman, H.G.5
  • 21
    • 13944257472 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry of model peptides reveals diagnostic fragment ions for protein ubiquitination
    • Warren, M. R. E., Parker, C. E., Mocanu, V., Klapper, D. G., and Borchers, C. H. (2005) Electrospray ionization tandem mass spectrometry of model peptides reveals diagnostic fragment ions for protein ubiquitination. Rapid Communie. Mass Spectrom. 19, 429-437.
    • (2005) Rapid Communie. Mass Spectrom , vol.19 , pp. 429-437
    • Warren, M.R.E.1    Parker, C.E.2    Mocanu, V.3    Klapper, D.G.4    Borchers, C.H.5
  • 22
  • 23
    • 0033655079 scopus 로고    scopus 로고
    • Parker, C. E. and Tomer, K. B. (2000) in Methods in Molecular Biology (Chapman, J. R., Ed.), 146 (Mass Spectrometry of Proteins and Peptides), pp. 185-201, Humana Press, Totowa, NJ.
    • Parker, C. E. and Tomer, K. B. (2000) in Methods in Molecular Biology (Chapman, J. R., Ed.), Vol. 146 (Mass Spectrometry of Proteins and Peptides), pp. 185-201, Humana Press, Totowa, NJ.
  • 25
    • 0032810855 scopus 로고    scopus 로고
    • A preliminary comparison of precursor scans and LC/MS/MS on a hybrid quadrupole time-of-flight mass spectrometer
    • Borchers, C., Parker, C. E., Deterding, L. J., and Tomer, K. B. (1999) A preliminary comparison of precursor scans and LC/MS/MS on a hybrid quadrupole time-of-flight mass spectrometer. J. Chromatogr. A 854, 119-130.
    • (1999) J. Chromatogr. A , vol.854 , pp. 119-130
    • Borchers, C.1    Parker, C.E.2    Deterding, L.J.3    Tomer, K.B.4
  • 26
    • 0035298820 scopus 로고    scopus 로고
    • Detection of tyrosine phosphorylated peptides by precursor ion scanning quadrupole TOF mass spectrometry in positive ion mode
    • Steen, H., Kuester, B., Fernandez, M., Pandey, A., and Mann, M. (2001) Detection of tyrosine phosphorylated peptides by precursor ion scanning quadrupole TOF mass spectrometry in positive ion mode. Anal. Chem. 73, 1440-1448.
    • (2001) Anal. Chem , vol.73 , pp. 1440-1448
    • Steen, H.1    Kuester, B.2    Fernandez, M.3    Pandey, A.4    Mann, M.5
  • 27
    • 0037059770 scopus 로고    scopus 로고
    • Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway
    • Steen, H., Kuster, B., Fernandez, M., Pandey, A., and Mann, M. (2002) Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway. J. of Biol. Chem. 277, 1031-1039.
    • (2002) J. of Biol. Chem , vol.277 , pp. 1031-1039
    • Steen, H.1    Kuster, B.2    Fernandez, M.3    Pandey, A.4    Mann, M.5
  • 28
    • 14744281219 scopus 로고    scopus 로고
    • Approach for determining protein ubiquitination sites by MALDI-TOF mass spectrometry
    • Wang, D. and Cotter, R. J. (2005) Approach for determining protein ubiquitination sites by MALDI-TOF mass spectrometry. Analytical Chemistry 77, 1458-1466.
    • (2005) Analytical Chemistry , vol.77 , pp. 1458-1466
    • Wang, D.1    Cotter, R.J.2
  • 29
    • 26844507482 scopus 로고    scopus 로고
    • Direct Identification of Ubiquitination Sites on Ubiquitin-Conjugated CHIP Using MALDI Mass Spectrometry
    • Wang, D., Xu, W., McGrath, S. C., Patterson, C., Neckers, L., and Cotter, R. J. (2005) Direct Identification of Ubiquitination Sites on Ubiquitin-Conjugated CHIP Using MALDI Mass Spectrometry. Journal of Proteome Research 4, 1554-1560.
    • (2005) Journal of Proteome Research , vol.4 , pp. 1554-1560
    • Wang, D.1    Xu, W.2    McGrath, S.C.3    Patterson, C.4    Neckers, L.5    Cotter, R.J.6
  • 30
    • 0001394390 scopus 로고
    • Preparation of phenyl thiohydantoins from some natural amino acids
    • Edman, P. (1950) Preparation of phenyl thiohydantoins from some natural amino acids. Acta Chem. Scand. 4, 277-282.
    • (1950) Acta Chem. Scand , vol.4 , pp. 277-282
    • Edman, P.1
  • 31
    • 0037397184 scopus 로고    scopus 로고
    • Sulfonic acid derivatives for peptide sequencing by MALDI MS
    • Keough, T., Youngquist, R. S., and Lacey, M. P. (2003) Sulfonic acid derivatives for peptide sequencing by MALDI MS. Analytical Chemistry 75, 156A-165A.
    • (2003) Analytical Chemistry , vol.75
    • Keough, T.1    Youngquist, R.S.2    Lacey, M.P.3
  • 32
    • 0346158179 scopus 로고    scopus 로고
    • Improved procedures for N-terminal sulfonation of peptides for matrix-assisted laser desorption/ionization post-source decay peptide sequencing
    • Wang, D., Kalb, S. R., and Cotter, R. J. (2004) Improved procedures for N-terminal sulfonation of peptides for matrix-assisted laser desorption/ionization post-source decay peptide sequencing. Rapid communications in mass spectrometry 18, 96-102.
    • (2004) Rapid communications in mass spectrometry , vol.18 , pp. 96-102
    • Wang, D.1    Kalb, S.R.2    Cotter, R.J.3
  • 33
    • 0035880528 scopus 로고    scopus 로고
    • A general strategy for epitope mapping by direct MALDI-TOF mass spectrometry using secondary antibodies and cross-linking
    • Peter, J. F. and Tomer, K. B. (2001) A general strategy for epitope mapping by direct MALDI-TOF mass spectrometry using secondary antibodies and cross-linking. Anal. Chem. 73, 4012-4019.
    • (2001) Anal. Chem , vol.73 , pp. 4012-4019
    • Peter, J.F.1    Tomer, K.B.2
  • 34
    • 0038607954 scopus 로고    scopus 로고
    • Mnd2 and Swml Are Core Subunits of the Saccharomyces cerevisiae Anaphase-promoting Complex
    • Hall, M. C., Torres, M. P., Schroeder, G. K., and Borchers, C. H. (2003) Mnd2 and Swml Are Core Subunits of the Saccharomyces cerevisiae Anaphase-promoting Complex. J. Biol. Chem. 278, 16698-16705.
    • (2003) J. Biol. Chem , vol.278 , pp. 16698-16705
    • Hall, M.C.1    Torres, M.P.2    Schroeder, G.K.3    Borchers, C.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.