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Volumn 5, Issue 4, 2006, Pages 671-685

Proteomic analysis of bovine brain G protein γ subunit processing heterogeneity

Author keywords

[No Author keywords available]

Indexed keywords

BRAIN PROTEIN; CYSTEINE; GUANINE NUCLEOTIDE BINDING PROTEIN GAMMA SUBUNIT; ISOPROTEIN; PROTEIN SUBUNIT;

EID: 33645719214     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M500223-MCP200     Document Type: Article
Times cited : (26)

References (86)
  • 1
    • 0037370373 scopus 로고    scopus 로고
    • Proteomics: The first decade and beyond
    • Patterson, S. D., and Aebersold, R. H. (2003) Proteomics: the first decade and beyond. Nat. Genet. 33, (suppl.) 311-323
    • (2003) Nat. Genet. , vol.33 , Issue.SUPPL. , pp. 311-323
    • Patterson, S.D.1    Aebersold, R.H.2
  • 3
    • 6344221680 scopus 로고    scopus 로고
    • Implications of new proteomics strategies for biology and medicine
    • Domon, B., and Broder, S. (2004) Implications of new proteomics strategies for biology and medicine. J. Proteome Res. 3, 253-260
    • (2004) J. Proteome Res. , vol.3 , pp. 253-260
    • Domon, B.1    Broder, S.2
  • 4
    • 4644335402 scopus 로고    scopus 로고
    • Systems biology, proteomics, and the future of health care: Toward predictive, preventative, and personalized medicine
    • Weston, A., and Hood, L. (2004) Systems biology, proteomics, and the future of health care: toward predictive, preventative, and personalized medicine. J. Proteome Res. 3, 179-196
    • (2004) J. Proteome Res. , vol.3 , pp. 179-196
    • Weston, A.1    Hood, L.2
  • 6
    • 0025254559 scopus 로고
    • Transduction of receptor signal into modulation of effector activity by G proteins: The first 20 years or so
    • Birnbaumer, L. (1990) Transduction of receptor signal into modulation of effector activity by G proteins: the first 20 years or so. FASEB J. 4, 3178-3188
    • (1990) FASEB J. , vol.4 , pp. 3178-3188
    • Birnbaumer, L.1
  • 8
    • 0028011112 scopus 로고
    • Proteins: Critical control points for transmembrane signals
    • Neer, E. J. (1994) G proteins: critical control points for transmembrane signals. Protein Sci. 3, 3-14
    • (1994) Protein Sci. , vol.3 , pp. 3-14
    • Neer, E.J.G.1
  • 9
    • 0030771361 scopus 로고    scopus 로고
    • Role of subunit diversity in signaling by heterotrimeric G proteins
    • Hildebrandt, J. D. (1997) Role of subunit diversity in signaling by heterotrimeric G proteins. Biochem. Pharmacol. 54, 325-339
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 325-339
    • Hildebrandt, J.D.1
  • 10
    • 0031984517 scopus 로고    scopus 로고
    • The many faces of G protein signaling
    • Hamm, H. E. (1998) The many faces of G protein signaling. J. Biol. Chem. 273, 669-672
    • (1998) J. Biol. Chem. , vol.273 , pp. 669-672
    • Hamm, H.E.1
  • 11
    • 0029282131 scopus 로고
    • Proteins and regulation of adenylyl cyclase
    • Gilman, A. G. (1995) G proteins and regulation of adenylyl cyclase. Biosci. Rep. 15, 65-97
    • (1995) Biosci. Rep. , vol.15 , pp. 65-97
    • Gilman, A.G.G.1
  • 12
    • 0027068060 scopus 로고
    • Receptor-to-effector signalling through G proteins: Roles for β /γ dimers as well as a subunits
    • Birnbaumer, L. (1992) Receptor-to-effector signalling through G proteins: Roles for β/γ dimers as well as a subunits. Cell 71, 1069-1072
    • (1992) Cell , vol.71 , pp. 1069-1072
    • Birnbaumer, L.1
  • 13
    • 0027495684 scopus 로고
    • New roles for G protein β/γ dimers in transmembrane signalling
    • Clapham, D. E., and Neer, E. J. (1993) New roles for G protein β /γ dimers in transmembrane signalling. Nature 365, 403-406
    • (1993) Nature , vol.365 , pp. 403-406
    • Clapham, D.E.1    Neer, E.J.2
  • 15
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the humane genome
    • International Human Genome Sequencing Consortium
    • International Human Genome Sequencing Consortium (2001) Initial sequencing and analysis of the humane genome. Nature 409, 860-921
    • (2001) Nature , vol.409 , pp. 860-921
  • 18
    • 0025834532 scopus 로고
    • Diversity of G proteins in signal transduction
    • Simon, M. I., Strathmann, M. P., and Gautam, N. (1991) Diversity of G proteins in signal transduction. Science 252, 802-808
    • (1991) Science , vol.252 , pp. 802-808
    • Simon, M.I.1    Strathmann, M.P.2    Gautam, N.3
  • 20
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang, F. L., and Casey, P. (1996) Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65, 241-269
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.2
  • 21
    • 0029966304 scopus 로고    scopus 로고
    • Protein prenyltransferases
    • Casey, P. J., and Seabra, M. (1996) Protein prenyltransferases. J. Biol. Chem. 271, 5289-5292
    • (1996) J. Biol. Chem. , vol.271 , pp. 5289-5292
    • Casey, P.J.1    Seabra, M.2
  • 22
    • 0034630098 scopus 로고    scopus 로고
    • Recent advances in the study of prenylated proteins
    • Sinensky, M. (2000) Recent advances in the study of prenylated proteins. Biochim. Biophys. Acta 1484, 93-106
    • (2000) Biochim. Biophys. Acta , vol.1484 , pp. 93-106
    • Sinensky, M.1
  • 23
    • 0033392946 scopus 로고    scopus 로고
    • Enzymology and biology of CaaX protein prenylation
    • Fu, H.-W., and Casey, P. (1999) Enzymology and biology of CaaX protein prenylation. Recent. Prog. Horm. Res. 54, 315-343
    • (1999) Recent. Prog. Horm. Res. , vol.54 , pp. 315-343
    • Fu, H.-W.1    Casey, P.2
  • 24
    • 0037470819 scopus 로고    scopus 로고
    • Protein prenylation: A pivotal posttranslational process
    • Roskoski, R. (2003) Protein prenylation: a pivotal posttranslational process. Biochem. Biophys. Res. Commun. 303, 1-7
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 1-7
    • Roskoski, R.1
  • 25
    • 0029036379 scopus 로고
    • Mutation and analysis of prenylation signal sequences
    • Cox, A. D. (1995) Mutation and analysis of prenylation signal sequences. Methods Enzymol. 250, 105-121
    • (1995) Methods Enzymol. , vol.250 , pp. 105-121
    • Cox, A.D.1
  • 26
    • 0041526704 scopus 로고    scopus 로고
    • Therapeutic efficacy of prenylation inhibitors in the treatment of myeloid leukemia
    • Morgan, H. E., Ganser, A., and Reuter, C. W. M. (2003) Therapeutic efficacy of prenylation inhibitors in the treatment of myeloid leukemia. Leukemia 17, 1482-1498
    • (2003) Leukemia , vol.17 , pp. 1482-1498
    • Morgan, H.E.1    Ganser, A.2    Reuter, C.W.M.3
  • 28
    • 0033963644 scopus 로고    scopus 로고
    • Inhibition of ras-targeted prenylation: Protein farnesyl transferase inhibitors revisited
    • Hill, B. T., Perrin, D., and Kruczynski, A. (2000) Inhibition of ras-targeted prenylation: protein farnesyl transferase inhibitors revisited. Crit. Rev. Oncol. Hematol. 33, 7-23
    • (2000) Crit. Rev. Oncol. Hematol. , vol.33 , pp. 7-23
    • Hill, B.T.1    Perrin, D.2    Kruczynski, A.3
  • 29
    • 12344264745 scopus 로고    scopus 로고
    • Targeting Ras and Rho GTPases as opportunities for cancer therapeutics
    • Walker, K., and Olson, M. F. (2005) Targeting Ras and Rho GTPases as opportunities for cancer therapeutics. Curr. Opin. Gen. Dev. 15, 62-68
    • (2005) Curr. Opin. Gen. Dev. , vol.15 , pp. 62-68
    • Walker, K.1    Olson, M.F.2
  • 30
    • 7544219925 scopus 로고    scopus 로고
    • Effects of statins and farnesyltransferase inhibitors on the development and progression of cancer
    • Graaf, M. R., Richel, D. J., van Noorden, J. F., and Guchelaar, H.-J. (2004) Effects of statins and farnesyltransferase inhibitors on the development and progression of cancer. Cancer Treat. Rev. 30, 609-641
    • (2004) Cancer Treat. Rev. , vol.30 , pp. 609-641
    • Graaf, M.R.1    Richel, D.J.2    van Noorden, J.F.3    Guchelaar, H.-J.4
  • 34
    • 0029099297 scopus 로고
    • Isolation of cDNA clones encoding eight different human G protein γ subunits, including three novel forms designated the γ4, γ10 and γ11 subunits
    • Ray, K., Kunsch, C., Bonner, L. M., and Robishaw, J. D. (1995) Isolation of cDNA clones encoding eight different human G protein γ subunits, including three novel forms designated the γ4, γ10 and γ11 subunits. J. Biol. Chem. 270, 21765-21771
    • (1995) J. Biol. Chem. , vol.270 , pp. 21765-21771
    • Ray, K.1    Kunsch, C.2    Bonner, L.M.3    Robishaw, J.D.4
  • 37
    • 0028799627 scopus 로고
    • Localization of various forms of the γ subunit of G protein in neural and nonneural tissues
    • Asano, T., Morishita, R., Ohashi, K., Nagahama, M., Miyake, T., and Kato, K. (1995) Localization of various forms of the γ subunit of G protein in neural and nonneural tissues. J. Neurochem. 64, 1267-1273
    • (1995) J. Neurochem. , vol.64 , pp. 1267-1273
    • Asano, T.1    Morishita, R.2    Ohashi, K.3    Nagahama, M.4    Miyake, T.5    Kato, K.6
  • 38
    • 0025155487 scopus 로고
    • G protein diversity is increased by association with a variety of γ subunits
    • Gautam, N., Northup, J., Tamir, H., and Simon, M. (1990) G protein diversity is increased by association with a variety of γ subunits. Proc. Natl. Acad. Sci. U. S. A. 87, 7973-7977
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 7973-7977
    • Gautam, N.1    Northup, J.2    Tamir, H.3    Simon, M.4
  • 39
    • 0026602928 scopus 로고
    • Characterization of the cDNA and genomic sequence of a G protein γ subunit
    • Fisher, K. J., and Aronson, N. N. (1992) Characterization of the cDNA and genomic sequence of a G protein γ subunit. Mol. Cell. Biol. 12 1585-1591
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1585-1591
    • Fisher, K.J.1    Aronson, N.N.2
  • 40
    • 0027056925 scopus 로고
    • Selective tissue distribution of G protein γ subunits, including a new form of the γ subunits identified by cDNA cloning
    • Cali, J. J., Balcueva, E. A., Rybalkin, I., and Robishaw, J. D. (1992) Selective tissue distribution of G protein γ subunits, including a new form of the γ subunits identified by cDNA cloning. J. Biol. Chem. 267, 24023-24027
    • (1992) J. Biol. Chem. , vol.267 , pp. 24023-24027
    • Cali, J.J.1    Balcueva, E.A.2    Rybalkin, I.3    Robishaw, J.D.4
  • 41
  • 42
    • 0029087152 scopus 로고
    • Determination of the complete covalent structure of the γ2 subunit of bovine brain G proteins by mass spectrometry
    • Wilcox, M. D., Schey, K. L., Busman, M., and Hildebrandt, J. D. (1995) Determination of the complete covalent structure of the γ2 subunit of bovine brain G proteins by mass spectrometry. Biochem. Biophys. Res. Commun. 212, 367-374
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 367-374
    • Wilcox, M.D.1    Schey, K.L.2    Busman, M.3    Hildebrandt, J.D.4
  • 43
    • 0035177020 scopus 로고    scopus 로고
    • Identification of a region in G protein γ subunits conserved across species but hypervariable among subunit isoforms
    • Cook, L. A., Schey, K. L., Cleator, J. H., Wilcox, M. D., Dingus, J., and Hildebrandt, J. D. (2001) Identification of a region in G protein γ subunits conserved across species but hypervariable among subunit isoforms. Protein Sci. 10, 2548-2555
    • (2001) Protein Sci. , vol.10 , pp. 2548-2555
    • Cook, L.A.1    Schey, K.L.2    Cleator, J.H.3    Wilcox, M.D.4    Dingus, J.5    Hildebrandt, J.D.6
  • 44
    • 0032168908 scopus 로고    scopus 로고
    • Heterogeneous processing of a G protein γ subunit at a site critical for protein and membrane interactions
    • Cook, L. A., Schey, K. L., Wilcox, M. D., Dingus, J., and Hildebrandt, J. D. (1998) Heterogeneous processing of a G protein γ subunit at a site critical for protein and membrane interactions. Biochemistry 37, 12280-12286
    • (1998) Biochemistry , vol.37 , pp. 12280-12286
    • Cook, L.A.1    Schey, K.L.2    Wilcox, M.D.3    Dingus, J.4    Hildebrandt, J.D.5
  • 46
    • 0024308815 scopus 로고
    • G protein subunit interactions. Studies with biotinylated G protein subunits
    • Kohnken, R. E., and Hildebrandt, J. D. (1989) G protein subunit interactions. Studies with biotinylated G protein subunits. J. Biol. Chem. 264, 20688-20696
    • (1989) J. Biol. Chem. , vol.264 , pp. 20688-20696
    • Kohnken, R.E.1    Hildebrandt, J.D.2
  • 47
    • 0021748090 scopus 로고
    • Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain
    • Sternweis, P. C., and Robishaw, J. D. (1984) Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain. J. Biol. Chem. 259, 13806-13813
    • (1984) J. Biol. Chem. , vol.259 , pp. 13806-13813
    • Sternweis, P.C.1    Robishaw, J.D.2
  • 49
    • 0035719122 scopus 로고    scopus 로고
    • Structural characterization of intact G protein γ subunits by mass spectrometry
    • Schey, K. L., Busman, M., Cook, L. A., Hamm, H. E., and Hildebrandt, J. D. (2002) Structural characterization of intact G protein γ subunits by mass spectrometry. Methods Enzymol. 344, 586-597
    • (2002) Methods Enzymol. , vol.344 , pp. 586-597
    • Schey, K.L.1    Busman, M.2    Cook, L.A.3    Hamm, H.E.4    Hildebrandt, J.D.5
  • 50
    • 0022876166 scopus 로고
    • The influence of bound GDP on the kinetics of guanine nucleotide binding to G proteins
    • Ferguson, K., Higashijima, T., Smigel, M., and Gilman, A. (1986) The influence of bound GDP on the kinetics of guanine nucleotide binding to G proteins. J. Biol. Chem. 261, 7393-7399
    • (1986) J. Biol. Chem. , vol.261 , pp. 7393-7399
    • Ferguson, K.1    Higashijima, T.2    Smigel, M.3    Gilman, A.4
  • 51
  • 52
    • 0027218189 scopus 로고
    • Identification of three forms of the γ subunit of G proteins isolated from bovine spleen
    • Morishita, R., Masuda, K., Niwa, M., Kato, K., and Asano, T. (1993) Identification of three forms of the γ subunit of G proteins isolated from bovine spleen. Biochem. Biophys. Res. Commun. 194, 1221-1227
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 1221-1227
    • Morishita, R.1    Masuda, K.2    Niwa, M.3    Kato, K.4    Asano, T.5
  • 55
    • 0026346215 scopus 로고
    • Methylation and demethylation reactions of guanine nucleotide-binding proteins of retinal rod outer segments
    • Perez-Sala, D., Tan, E. W., Canada, F. J., and Rando, R. R. (1991) Methylation and demethylation reactions of guanine nucleotide-binding proteins of retinal rod outer segments. Proc. Natl. Acad. Sci. U. S. A. 88, 3043-3046
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 3043-3046
    • Perez-Sala, D.1    Tan, E.W.2    Canada, F.J.3    Rando, R.R.4
  • 57
    • 2042544816 scopus 로고    scopus 로고
    • Post-translational processing of RhoA
    • Backlund, P. (1997) Post-translational processing of RhoA. J. Biol. Chem. 272, 33175-33180
    • (1997) J. Biol. Chem. , vol.272 , pp. 33175-33180
    • Backlund, P.1
  • 58
    • 0027983602 scopus 로고
    • Effects of carboxyl methylation of photoreceptor G protein γ-subunit in visual transduction
    • Fukada, Y., Matsuda, T., Kokame, K., Takao, T., Shimonishi, Y., Akino, T., and Yoshizawa, T. (1994) Effects of carboxyl methylation of photoreceptor G protein γ-subunit in visual transduction. J. Biol. Chem. 269, 5163-5170
    • (1994) J. Biol. Chem. , vol.269 , pp. 5163-5170
    • Fukada, Y.1    Matsuda, T.2    Kokame, K.3    Takao, T.4    Shimonishi, Y.5    Akino, T.6    Yoshizawa, T.7
  • 59
    • 0030564274 scopus 로고    scopus 로고
    • Isoprenylation/methylation of proteins enhances membrane association by a hydrophobic mechanism
    • Parish, G. A., and Rando, R. R. (1996) Isoprenylation/methylation of proteins enhances membrane association by a hydrophobic mechanism. Biochemistry 35, 8473-8477
    • (1996) Biochemistry , vol.35 , pp. 8473-8477
    • Parish, G.A.1    Rando, R.R.2
  • 60
    • 0029785706 scopus 로고    scopus 로고
    • G protein γ subunits with altered prenylation sequences are properly modified when expressed in Sf9 cells
    • Lindorfer, M. A., Sherman, N. E., Woodfork, K. A., Fletcher, J. E., Hunt, D. F., and Garrison, J. C. (1996) G protein γ subunits with altered prenylation sequences are properly modified when expressed in Sf9 cells. J. Biol. Chem. 271, 18582-18587
    • (1996) J. Biol. Chem. , vol.271 , pp. 18582-18587
    • Lindorfer, M.A.1    Sherman, N.E.2    Woodfork, K.A.3    Fletcher, J.E.4    Hunt, D.F.5    Garrison, J.C.6
  • 61
    • 0026640530 scopus 로고
    • Post-translational modifications of p21rho proteins
    • Adamson, P., Marshall, C. J., Hall, A., and Tilbrook, P. A. (1992) Post-translational modifications of p21rho proteins. J. Biol. Chem. 267, 20033-20038
    • (1992) J. Biol. Chem. , vol.267 , pp. 20033-20038
    • Adamson, P.1    Marshall, C.J.2    Hall, A.3    Tilbrook, P.A.4
  • 62
    • 0028920240 scopus 로고
    • CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB
    • Armstrong, S. A., Hannah, V. C., Goldstein, J. L., and Brown, M. S. (1995) CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB. J. Biol. Chem. 270, 7864-7868
    • (1995) J. Biol. Chem. , vol.270 , pp. 7864-7868
    • Armstrong, S.A.1    Hannah, V.C.2    Goldstein, J.L.3    Brown, M.S.4
  • 63
    • 0030916369 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors alter prenylation and growth-stimulating function of RhoB
    • Lebowitz, P. F., Casey, P. J., Prendergast, G. C., and Thissen, J. A. (1997) Farnesyltransferase inhibitors alter prenylation and growth-stimulating function of RhoB. J. Biol. Chem. 272, 15591-15594
    • (1997) J. Biol. Chem. , vol.272 , pp. 15591-15594
    • Lebowitz, P.F.1    Casey, P.J.2    Prendergast, G.C.3    Thissen, J.A.4
  • 64
    • 0028958919 scopus 로고
    • Polylysine and CVIM sequences of K-RasB dictate specificity of prenylation and confer resistance to benzodiazepine peptidomimetic in vitro
    • James, G. L., Goldstein, J. L., and Brown, M. S. (1995) Polylysine and CVIM sequences of K-RasB dictate specificity of prenylation and confer resistance to benzodiazepine peptidomimetic in vitro. J. Biol. Chem. 270, 6221-6226
    • (1995) J. Biol. Chem. , vol.270 , pp. 6221-6226
    • James, G.L.1    Goldstein, J.L.2    Brown, M.S.3
  • 65
    • 0030968859 scopus 로고    scopus 로고
    • Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo
    • Rowell, C. A., Kowalczyk, J. J., Lewis, M. D., and Garcia, A. M. (1997) Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo. J. Biol. Chem. 272, 14093-14097
    • (1997) J. Biol. Chem. , vol.272 , pp. 14093-14097
    • Rowell, C.A.1    Kowalczyk, J.J.2    Lewis, M.D.3    Garcia, A.M.4
  • 67
    • 0030943198 scopus 로고    scopus 로고
    • Characterization of Ha-Ras, N-Ras, Ki-Ras4A, and Ki-Ras4B as in vitro substrates for famesyl protein transferase and geranylgeranyl protein transferase type I
    • Zhang, F. L., Kirschmeier, P., Carr, D., James, L., Bond, R. W., Wang, L., Patton, R., Windsor, W. T., Syto, R., Zhang, R., and Bishop, W. R. (1997) Characterization of Ha-Ras, N-Ras, Ki-Ras4A, and Ki-Ras4B as in vitro substrates for famesyl protein transferase and geranylgeranyl protein transferase type I. J. Biol. Chem. 272, 10232-10239
    • (1997) J. Biol. Chem. , vol.272 , pp. 10232-10239
    • Zhang, F.L.1    Kirschmeier, P.2    Carr, D.3    James, L.4    Bond, R.W.5    Wang, L.6    Patton, R.7    Windsor, W.T.8    Syto, R.9    Zhang, R.10    Bishop, W.R.11
  • 68
    • 0031055466 scopus 로고    scopus 로고
    • Differential prenyl pyrophosphate binding to mammalian protein geranylgeranyltransferase-I and protein farnesyltransferase and its consequence on the specificity of protein prenylation
    • Yokoyama, K., Zimmerman, K., Scholten, J., and Gelb, M. H. (1997) Differential prenyl pyrophosphate binding to mammalian protein geranylgeranyltransferase-I and protein farnesyltransferase and its consequence on the specificity of protein prenylation. J. Biol. Chem. 272, 394403952
    • (1997) J. Biol. Chem. , vol.272 , pp. 394403952
    • Yokoyama, K.1    Zimmerman, K.2    Scholten, J.3    Gelb, M.H.4
  • 69
    • 0142211304 scopus 로고    scopus 로고
    • High affinity for farnesyltransferase and alternative prenylation contribute to K-Ras4B resistance to farnesyltransferase inhibitors
    • Fiordalis, J. J., Johnson, R. L., Weinbaum, C. A., Sakabe, K., Chem, Z., Casey, P., and Cox, A. D. (2003) High affinity for farnesyltransferase and alternative prenylation contribute to K-Ras4B resistance to farnesyltransferase inhibitors. J. Biol. Chem. 278, 41718-41727
    • (2003) J. Biol. Chem. , vol.278 , pp. 41718-41727
    • Fiordalis, J.J.1    Johnson, R.L.2    Weinbaum, C.A.3    Sakabe, K.4    Chem, Z.5    Casey, P.6    Cox, A.D.7
  • 71
    • 0028093624 scopus 로고
    • A farnesylated domain in the G protein γ subunit is a specific determinant of receptor coupling
    • Kisselev, O. G., Ermolaeva, M. V., and Gautam, N. (1994) A farnesylated domain in the G protein γ subunit is a specific determinant of receptor coupling. J. Biol. Chem. 269, 21399-21402
    • (1994) J. Biol. Chem. , vol.269 , pp. 21399-21402
    • Kisselev, O.G.1    Ermolaeva, M.V.2    Gautam, N.3
  • 72
    • 0029026880 scopus 로고
    • Receptor G protein coupling is established by a potential conformational switch in the β/γ complex
    • Kisselev, O., Pronin, A., Ermolaeva, M., and Gautam, N. (1995) Receptor G protein coupling is established by a potential conformational switch in the β/γ complex. Proc. Natl. Acad. Sci. U. S. A. 92, 9102-9106
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 9102-9106
    • Kisselev, O.1    Pronin, A.2    Ermolaeva, M.3    Gautam, N.4
  • 73
    • 0029746261 scopus 로고    scopus 로고
    • Role of the prenyl group on the G protein γ subunit in coupling trimeric G proteins to A1 adenosine receptors
    • Yasuda, H., Lindorfer, M. A., Woodfork, K. A., Fletcher, J. E., and Garrison, J. C. (1996) Role of the prenyl group on the G protein γ subunit in coupling trimeric G proteins to A1 adenosine receptors. J. Biol. Chem. 271, 18588-18595
    • (1996) J. Biol. Chem. , vol.271 , pp. 18588-18595
    • Yasuda, H.1    Lindorfer, M.A.2    Woodfork, K.A.3    Fletcher, J.E.4    Garrison, J.C.5
  • 74
    • 0028845341 scopus 로고
    • Efficient interaction with a receptor requires a specific type of prenyl group on the G protein γ subunit
    • Kisselev, O., Ermolaeva, M., and Gautam, N. (1995) Efficient interaction with a receptor requires a specific type of prenyl group on the G protein γ subunit. J. Biol. Chem. 270, 25356-25358
    • (1995) J. Biol. Chem. , vol.270 , pp. 25356-25358
    • Kisselev, O.1    Ermolaeva, M.2    Gautam, N.3
  • 75
    • 0030801368 scopus 로고    scopus 로고
    • Isolation and characterization of a prenylcysteine lyase from bovine brain
    • Zhang, L., Tschantz, W. R., and Casey, P. J. (1997) Isolation and characterization of a prenylcysteine lyase from bovine brain. J. Biol. Chem. 272, 23354-23359
    • (1997) J. Biol. Chem. , vol.272 , pp. 23354-23359
    • Zhang, L.1    Tschantz, W.R.2    Casey, P.J.3
  • 76
    • 0035951846 scopus 로고    scopus 로고
    • Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase
    • Tschantz, W. R., Digits, J. A., Pyon, H.-J., Coates, R. M., and Casey, P. (2001) Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase. J. Biol. Chem. 276, 2321-2324
    • (2001) J. Biol. Chem. , vol.276 , pp. 2321-2324
    • Tschantz, W.R.1    Digits, J.A.2    Pyon, H.-J.3    Coates, R.M.4    Casey, P.5
  • 78
    • 0033605596 scopus 로고    scopus 로고
    • Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells
    • Kim, E., Ambroziak, P., Otto, J. C., Taylor, B., Ashby, M., Shannon, K., Casey, P., and Young, S. G. (1999) Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells. J. Biol. Chem. 274, 8383-8390
    • (1999) J. Biol. Chem. , vol.274 , pp. 8383-8390
    • Kim, E.1    Ambroziak, P.2    Otto, J.C.3    Taylor, B.4    Ashby, M.5    Shannon, K.6    Casey, P.7    Young, S.G.8
  • 79
    • 1042266632 scopus 로고    scopus 로고
    • On the physiological importance of endoproteolysis of CAAX proteins. Heart-specific RCE1 knock-out mice develop a lethal cardiomyopathy
    • Bergo, M. O., Lieu, H. D., Gavino, B. J., Ambroziak, P., Otto, J. C., Casey, P., Walker, Q. M., and Young, S. G. (2004) On the physiological importance of endoproteolysis of CAAX proteins. Heart-specific RCE1 knock-out mice develop a lethal cardiomyopathy. J. Biol. Chem. 279, 4729-4736
    • (2004) J. Biol. Chem. , vol.279 , pp. 4729-4736
    • Bergo, M.O.1    Lieu, H.D.2    Gavino, B.J.3    Ambroziak, P.4    Otto, J.C.5    Casey, P.6    Walker, Q.M.7    Young, S.G.8
  • 80
    • 0026666233 scopus 로고
    • Farnesylcysteine, a constituent of the α and β subunits of rabbit skeletal muscle phosphorylase kinase: Localization by conversion to S-ethylcysteine and by tandem mass spectrometry
    • Heilmeyer, L. M. G., Serwe, M., Weber, C., Metzger, J., Hoffmann-Posorske, E., and Meyer, H. E. (1992) Farnesylcysteine, a constituent of the α and β subunits of rabbit skeletal muscle phosphorylase kinase: localization by conversion to S-ethylcysteine and by tandem mass spectrometry. Proc. Natl. Acad. Sci. U. S. A. 89, 9554-9558
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 9554-9558
    • Heilmeyer, L.M.G.1    Serwe, M.2    Weber, C.3    Metzger, J.4    Hoffmann-Posorske, E.5    Meyer, H.E.6
  • 81
    • 0014030335 scopus 로고
    • The heterogeneity of bovine serum albumin
    • Andersson, L. O. (1966) The heterogeneity of bovine serum albumin. Biochim. Biophys. Acta 117, 115-133
    • (1966) Biochim. Biophys. Acta , vol.117 , pp. 115-133
    • Andersson, L.O.1
  • 82
    • 0042974241 scopus 로고    scopus 로고
    • Sulfenic acid formation in human serum albumin by hydrogen peroxide and peroxynitrite
    • Carballal, S., Radi, R., Kirk, M., Barnes, S., Freemna, B. A., and Alvarez, B. (2003) Sulfenic acid formation in human serum albumin by hydrogen peroxide and peroxynitrite. Biochemistry 42, 9906-9914
    • (2003) Biochemistry , vol.42 , pp. 9906-9914
    • Carballal, S.1    Radi, R.2    Kirk, M.3    Barnes, S.4    Freemna, B.A.5    Alvarez, B.6
  • 83
    • 16444373712 scopus 로고    scopus 로고
    • Cysteinylation of maternal plasma albumin and its association with intrauterine growth restriction
    • Bar-Or, D., Heyborne, K. D., Bar-Or, R., Rael, L. T., Winkler, J. V., and Navot, D. (2005) Cysteinylation of maternal plasma albumin and its association with intrauterine growth restriction. Prenat. Diagn. 25, 245-249
    • (2005) Prenat. Diagn. , vol.25 , pp. 245-249
    • Bar-Or, D.1    Heyborne, K.D.2    Bar-Or, R.3    Rael, L.T.4    Winkler, J.V.5    Navot, D.6
  • 85
    • 0034903753 scopus 로고    scopus 로고
    • Potent inactivation of representative members of each PKC isozyme subfamily and PKD via S-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine
    • Chu, F., Ward, N. E., and O'Brian, C. A. (2001) Potent inactivation of representative members of each PKC isozyme subfamily and PKD via S-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine. Carcinogenesis 22, 1221-1229
    • (2001) Carcinogenesis , vol.22 , pp. 1221-1229
    • Chu, F.1    Ward, N.E.2    O'Brian, C.A.3
  • 86
    • 0037325938 scopus 로고    scopus 로고
    • PKC isozyme S-cysteinylation by cystine stimulates the pro-apoptotic isozyme PKC δ and inactivates the oncogenic PKC ε
    • Chu, F., Ward, N. E., and O'Brian, C. A. (2003) PKC isozyme S-cysteinylation by cystine stimulates the pro-apoptotic isozyme PKC δ and inactivates the oncogenic PKC ε. Carcinogenesis 24, 317-325
    • (2003) Carcinogenesis , vol.24 , pp. 317-325
    • Chu, F.1    Ward, N.E.2    O'Brian, C.A.3


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