메뉴 건너뛰기




Volumn 39, Issue 1, 1999, Pages 175-203

Expression of enzymes of covalent protein modification during regulated and dysregulated proliferation of mammary epithelial cells: PKA, PKC and NMT

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; CARRIER PROTEIN; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; GLYCYLPEPTIDE-N-MYRISTOYL TRANSFERASE; PROTEIN KINASE C; PROTEIN N MYRISTOYLTRANSFERASE; TUMOR PROTEIN;

EID: 0032879727     PISSN: 00652571     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-2571(98)00011-9     Document Type: Conference Paper
Times cited : (8)

References (88)
  • 1
    • 0019309120 scopus 로고
    • A scanning electron microscope study of myoepithelial cells in exocrine glands
    • T. NAGATO, H. YOSHIDA, A. YOSHIDA and Y. UEHARA, A scanning electron microscope study of myoepithelial cells in exocrine glands, Cell Tissue Res. 209, 1-10 (1980).
    • (1980) Cell Tissue Res. , vol.209 , pp. 1-10
    • Nagato, T.1    Yoshida, H.2    Yoshida, A.3    Uehara, Y.4
  • 2
    • 0020267629 scopus 로고
    • Development of the mammary gland
    • C. H. KNIGHT and M. PEAKER, Development of the mammary gland, J. Reprod. Fertil. 65, 521-536 (1982).
    • (1982) J. Reprod. Fertil. , vol.65 , pp. 521-536
    • Knight, C.H.1    Peaker, M.2
  • 3
    • 0002825985 scopus 로고
    • Development of the human mammary gland
    • (M. C. NEVILLE and C. W. DANIEL, eds.). Plenum Press, New York
    • J. RUSSO and I. H. RUSSO, Development of the human mammary gland, pp. 67-93 in The Mammary Gland: Development, Regulation and Function (M. C. NEVILLE and C. W. DANIEL, eds.). Plenum Press, New York (1987).
    • (1987) The Mammary Gland: Development, Regulation and Function , pp. 67-93
    • Russo, J.1    Russo, I.H.2
  • 4
    • 0029677184 scopus 로고    scopus 로고
    • The mammary gland: A unique organ for the study of development and tumorigenesis
    • D. MEDINA, The mammary gland: a unique organ for the study of development and tumorigenesis, J. Mammary Gland Biol. Neoplasia 1, 5-19 (1996).
    • (1996) J. Mammary Gland Biol. Neoplasia , vol.1 , pp. 5-19
    • Medina, D.1
  • 5
    • 0002586763 scopus 로고
    • Regulation of mammary gland development and lactation
    • (M. C. NEVILLE and M. R. NEIFERT, eds.). Plenum Press, New York
    • M. C. NEVILLE, Regulation of mammary gland development and lactation, pp. 103-140 in Lactation (M. C. NEVILLE and M. R. NEIFERT, eds.). Plenum Press, New York (1983).
    • (1983) Lactation , pp. 103-140
    • Neville, M.C.1
  • 6
    • 0028245542 scopus 로고
    • Development of the mammary gland and lactation
    • J. A. RILLEMA, Development of the mammary gland and lactation, TEM 5, 149-154 (1994).
    • (1994) TEM , vol.5 , pp. 149-154
    • Rillema, J.A.1
  • 7
    • 0032519554 scopus 로고    scopus 로고
    • Think globally, act locally: The making of a mouse mammary gland
    • L. HENNIGHAUSEN and G. W. ROBINSON, Think globally, act locally: the making of a mouse mammary gland, Genes and Dev. 12, 449-455 (1998).
    • (1998) Genes and Dev. , vol.12 , pp. 449-455
    • Hennighausen, L.1    Robinson, G.W.2
  • 8
    • 0030664779 scopus 로고    scopus 로고
    • AKAP expression in mammary gland
    • R. A. CLEGG, AKAP expression in mammary gland, Biochem. Soc. Trans. 25, S634 (1997).
    • (1997) Biochem. Soc. Trans. , vol.25
    • Clegg, R.A.1
  • 9
    • 18244411771 scopus 로고    scopus 로고
    • Expression of N-myristoyl transferase is developmentally regulated in mammary epithelial cells
    • R. A. CLEGG, Expression of N-myristoyl transferase is developmentally regulated in mammary epithelial cells, Biochem. Soc. Trans. 25, S680 (1997).
    • (1997) Biochem. Soc. Trans. , vol.25
    • Clegg, R.A.1
  • 10
    • 0028491081 scopus 로고
    • The cAMP-dependent protein kinases and cAMP signal transduction
    • S. J. BEEBE, The cAMP-dependent protein kinases and cAMP signal transduction, Seminars in Cancer Biology 5, 285-294 (1994).
    • (1994) Seminars in Cancer Biology , vol.5 , pp. 285-294
    • Beebe, S.J.1
  • 13
    • 0029737861 scopus 로고
    • Genetically lean mice result from targeted disruption of the RIIβ subunit of protein-kinase-A
    • D. E. CUMMINGS, E. P. BRANDON, J. V. PLANAS, K. MOTAMED, R. L. IDZERDA and G. S. MCKNIGHT, Genetically lean mice result from targeted disruption of the RIIβ subunit of protein-kinase-A, Nature 382, 622-626 (1986).
    • (1986) Nature , vol.382 , pp. 622-626
    • Cummings, D.E.1    Brandon, E.P.2    Planas, J.V.3    Motamed, K.4    Idzerda, R.L.5    Mcknight, G.S.6
  • 14
    • 0029980440 scopus 로고    scopus 로고
    • Molecular glue: Kinase anchoring and scaffold proteins
    • M. C. FAUX and J. D. SCOTT, Molecular glue: kinase anchoring and scaffold proteins, Cell 85, 9-12 (1996).
    • (1996) Cell , vol.85 , pp. 9-12
    • Faux, M.C.1    Scott, J.D.2
  • 15
    • 0028009991 scopus 로고
    • Localization of A-kinase through anchor proteins
    • J. D. SCOTT and S. MCCARTNEY, Localization of A-kinase through anchor proteins, Mol. Endocrinol. 8, 9-12 (1994).
    • (1994) Mol. Endocrinol. , vol.8 , pp. 9-12
    • Scott, J.D.1    Mccartney, S.2
  • 16
    • 0032486376 scopus 로고    scopus 로고
    • CE) of type I protein kinase A from Caenorhabditis elegans
    • CE) of type I protein kinase A from Caenorhabditis elegans, J Biol. Chem. 273, 14633-14643 (1998).
    • (1998) J Biol. Chem. , vol.273 , pp. 14633-14643
    • Angelo, R.1    Rubin, C.S.2
  • 17
    • 0030219389 scopus 로고    scopus 로고
    • More on target with protein phosphorylation: Conferring specificity by location
    • M. C. FAUX and J. D. SCOTT, More on target with protein phosphorylation: conferring specificity by location, TIBS 21, 312-315 (1996).
    • (1996) TIBS , vol.21 , pp. 312-315
    • Faux, M.C.1    Scott, J.D.2
  • 18
    • 0028588997 scopus 로고
    • A-kinase anchor proteins and the intracellular targeting of signals carried by cyclic AMP
    • C. S. RUBIN, A-kinase anchor proteins and the intracellular targeting of signals carried by cyclic AMP, Biochim. Biophys. Acta 1224, 467-479 (1994).
    • (1994) Biochim. Biophys. Acta , vol.1224 , pp. 467-479
    • Rubin, C.S.1
  • 19
    • 0028274544 scopus 로고
    • Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons
    • C. ROSENMUND, D. W. CARR, S. E. BERGESON, G. NILAVER, J. D. SCOTT and G. L. WESTBROOK, Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons, Nature 368, 853-856 (1994).
    • (1994) Nature , vol.368 , pp. 853-856
    • Rosenmund, C.1    Carr, D.W.2    Bergeson, S.E.3    Nilaver, G.4    Scott, J.D.5    Westbrook, G.L.6
  • 20
    • 0022154119 scopus 로고
    • Rapid and reversible translocation of the catalytic subunit of cAMP-dependent protein kinase type II from the Golgi complex to the nucleus
    • E. A. NIGG, H. HILZ, H. M. EPPENBERGER and F. DUTLY, Rapid and reversible translocation of the catalytic subunit of cAMP-dependent protein kinase type II from the Golgi complex to the nucleus, EMBO J. 4, 2801-2806 (1985).
    • (1985) EMBO J. , vol.4 , pp. 2801-2806
    • Nigg, E.A.1    Hilz, H.2    Eppenberger, H.M.3    Dutly, F.4
  • 21
    • 0027934704 scopus 로고
    • Differential phosphorylation of neuronal substrates of Aplysia cAMP-dependent protein kinase with alternative N-termini
    • R. G. PANCHAL, S. CHELEY and H. BAYLEY, Differential phosphorylation of neuronal substrates of Aplysia cAMP-dependent protein kinase with alternative N-termini, J. Biol. Chem. 269, 23722-23730 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 23722-23730
    • Panchal, R.G.1    Cheley, S.2    Bayley, H.3
  • 22
    • 0020201569 scopus 로고
    • 2-terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle
    • 2-terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle, Proc. Natl. Acad. Sci. USA 79, 6128-6131 (1982).
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6128-6131
    • Carr, S.A.1    Biemann, K.2    Shoji, S.3    Parmalee, D.C.4    Titani, K.5
  • 23
    • 0029098773 scopus 로고
    • Subcellular targeting of recombinant and mammalian Cα subunits of cAMP-dependent protein kinase
    • E. J. ADIE, P. H. THOMAS, M. R. MUNDAY and R. A. CLEGG, Subcellular targeting of recombinant and mammalian Cα subunits of cAMP-dependent protein kinase, Biochem. Soc. Trans. 23, 451S (1995).
    • (1995) Biochem. Soc. Trans. , vol.23
    • Adie, E.J.1    Thomas, P.H.2    Munday, M.R.3    Clegg, R.A.4
  • 24
    • 0025856049 scopus 로고
    • Cyclic AMP-dependent protein kinase in mammary epithelial cells - Activity and subcellular distribution are acutely modified by isoprenaline
    • R. A. CLEGG and K. CONNOR, Cyclic AMP-dependent protein kinase in mammary epithelial cells - activity and subcellular distribution are acutely modified by isoprenaline, Cell. Signalling 3, 201-208 (1991).
    • (1991) Cell. Signalling , vol.3 , pp. 201-208
    • Clegg, R.A.1    Connor, K.2
  • 25
    • 0024310170 scopus 로고
    • A mutation in the catalytic subunit of protein kinase A prevents myristylation but does not inhibit biological activity
    • C. H. CLEGG, W. RAN, M. D. UHLER and G. S. MCKNIGHT, A mutation in the catalytic subunit of protein kinase A prevents myristylation but does not inhibit biological activity, J. Biol. Chem. 264, 20140-20146 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 20140-20146
    • Clegg, C.H.1    Ran, W.2    Uhler, M.D.3    Mcknight, G.S.4
  • 26
    • 0027429591 scopus 로고
    • Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations
    • J. ZHENG, D. R. KNIGHTON, N.-H. XUONG, S. S. TAYLOR, J. M. SOWADSKI and L. F. TEN EYCK, Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations, Protein Sci. 2, 1559-1573 (1993).
    • (1993) Protein Sci. , vol.2 , pp. 1559-1573
    • Zheng, J.1    Knighton, D.R.2    Xuong, N.-H.3    Taylor, S.S.4    Sowadski, J.M.5    Ten Eyck, L.F.6
  • 27
    • 0024614795 scopus 로고
    • The cAMP-mediated stimulation of cell proliferation
    • J. E. DUMONT, J.-C. JAUNIAUX and P. P. ROGER, The cAMP-mediated stimulation of cell proliferation, TIBS 14, 67-71 (1989).
    • (1989) TIBS , vol.14 , pp. 67-71
    • Dumont, J.E.1    Jauniaux, J.-C.2    Roger, P.P.3
  • 28
    • 0029883790 scopus 로고    scopus 로고
    • Insulin, growth factors and cAMP. Antagonism in the signal transduction pathways
    • L. M. GRAVES and J. C. LAWRENCE, Insulin, growth factors and cAMP. Antagonism in the signal transduction pathways, TEM 7, 43-50 (1996).
    • (1996) TEM , vol.7 , pp. 43-50
    • Graves, L.M.1    Lawrence, J.C.2
  • 29
    • 0026736043 scopus 로고
    • CyclicAMP-dependent protein kinase type I mediates the inhibitory effects of cAMP on cell replication in human T-lymphocytes
    • B. S. SKÅLHEGG, B. F. LANDMARK, S. O. DØSKELAND, V. HANSSON, T. LEA and T. JAHNSEN, CyclicAMP-dependent protein kinase type I mediates the inhibitory effects of cAMP on cell replication in human T-lymphocytes, J. Biol. Chem. 267, 15704-15714 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 15704-15714
    • Skålhegg, B.S.1    Landmark, B.F.2    DØskeland, S.O.3    Hansson, V.4    Lea, T.5    Jahnsen, T.6
  • 30
    • 0026561844 scopus 로고
    • Suppression of malignancy: Targeting cyclic AMP signal transducing proteins
    • Y. S. CHO-CHUNG, Suppression of malignancy: targeting cyclic AMP signal transducing proteins, Biochem. Soc. Trans. 20, 425-430 (1992).
    • (1992) Biochem. Soc. Trans. , vol.20 , pp. 425-430
    • Cho-Chung, Y.S.1
  • 31
    • 0028797282 scopus 로고
    • Expression and activity of cell cycle regulators during proliferation and programmed cell death in the mammary gland
    • A. MARTI, Z. FENG, B. JEHN, V. DJONOV, G. CHICAIZA, H. J. ALTERMATT and R. JAGGI, Expression and activity of cell cycle regulators during proliferation and programmed cell death in the mammary gland, Cell Death and Differentiation 2, 277-283 (1995).
    • (1995) Cell Death and Differentiation , vol.2 , pp. 277-283
    • Marti, A.1    Feng, Z.2    Jehn, B.3    Djonov, V.4    Chicaiza, G.5    Altermatt, H.J.6    Jaggi, R.7
  • 32
    • 0030157818 scopus 로고    scopus 로고
    • Regulation of a physiological apoptosis: Mouse mammary involution
    • R. JAGGI, A. MARTI, K. GUO, Z. FENG and R. R. FRIIS, Regulation of a physiological apoptosis: mouse mammary involution, J. Dairy Sci. 79, 1074-1084 (1996).
    • (1996) J. Dairy Sci. , vol.79 , pp. 1074-1084
    • Jaggi, R.1    Marti, A.2    Guo, K.3    Feng, Z.4    Friis, R.R.5
  • 33
    • 0027153429 scopus 로고
    • Microinjected catalytic subunit of cAMP-dependent protein kinase induces apoptosis in myeloid leukemia (IPC-81) cells
    • O. K. VINTERMYR, B. T. GJERTSEN, M. LANOTTE and S. O. DØSKELAND, Microinjected catalytic subunit of cAMP-dependent protein kinase induces apoptosis in myeloid leukemia (IPC-81) cells, Exptl. Cell Res. 206, 157-161 (1993).
    • (1993) Exptl. Cell Res. , vol.206 , pp. 157-161
    • Vintermyr, O.K.1    Gjertsen, B.T.2    Lanotte, M.3    DØskeland, S.O.4
  • 34
    • 0018894321 scopus 로고
    • Growth factor- and cyclic nucleotide-induced proliferation of normal and malignant mammary epithelial cells in primary culture
    • J. YANG, R. GUZMAN, J. RICHARDS, W. IMAGAWA, K. MCCORMICK and S. NANDI, Growth factor- and cyclic nucleotide-induced proliferation of normal and malignant mammary epithelial cells in primary culture, Endocrinol. 107, 35-41 (1980).
    • (1980) Endocrinol. , vol.107 , pp. 35-41
    • Yang, J.1    Guzman, R.2    Richards, J.3    Imagawa, W.4    Mccormick, K.5    Nandi, S.6
  • 36
    • 0027969290 scopus 로고
    • Cyclic AMP-dependent protein kinase in rat mammary tissue: Expression of catalytic and regulatory subunits throughout pregnancy and lactation
    • R. A. GARDNER, M. T. TRAVERS, M. C. BARBER, W. R. MILLER and R. A. CLEGG, Cyclic AMP-dependent protein kinase in rat mammary tissue: expression of catalytic and regulatory subunits throughout pregnancy and lactation, Biochem. J. 301, 807-812 (1994).
    • (1994) Biochem. J. , vol.301 , pp. 807-812
    • Gardner, R.A.1    Travers, M.T.2    Barber, M.C.3    Miller, W.R.4    Clegg, R.A.5
  • 38
    • 0027993231 scopus 로고
    • Regulation of growth in a neoplastic B cell line by transfected subunits of 3′5′-cyclic adenosine monophosphate-dependent protein kinase
    • K. TASKEN, K. B. ANDERSSON, B. K. ERIKSTEIN, V. HANSSON, T. JAHNSEN and H. K. BLOMHOFF, Regulation of growth in a neoplastic B cell line by transfected subunits of 3′5′-cyclic adenosine monophosphate-dependent protein kinase, Endocrinol. 135, 2109-2119 (1994).
    • (1994) Endocrinol. , vol.135 , pp. 2109-2119
    • Tasken, K.1    Andersson, K.B.2    Erikstein, B.K.3    Hansson, V.4    Jahnsen, T.5    Blomhoff, H.K.6
  • 39
    • 0002636658 scopus 로고
    • Protein kinase C: A structurally related family of enzymes
    • (D. S. LESTER and R. M. EPAND, eds). Ellis Horwood, Chichester
    • P. J. PARKER, Protein kinase C: a structurally related family of enzymes, pp. 3-24 in Protein Kinase C: Current Concepts and Future Perspectives (D. S. LESTER and R. M. EPAND, eds). Ellis Horwood, Chichester (1992).
    • (1992) Protein Kinase C: Current Concepts and Future Perspectives , pp. 3-24
    • Parker, P.J.1
  • 40
    • 0001926779 scopus 로고
    • Lipid regulation of protein kinase C
    • (D. S. LESTER and R. M. EPAND, eds). Ellis Horwood, Chichester
    • D. J. BURNS and R. M. BELL, Lipid regulation of protein kinase C, pp. 25-40 in Protein Kinase C: Current Concepts and Future Perspectives (D. S. LESTER and R. M. EPAND, eds). Ellis Horwood, Chichester (1992).
    • (1992) Protein Kinase C: Current Concepts and Future Perspectives , pp. 25-40
    • Burns, D.J.1    Bell, R.M.2
  • 41
    • 0027287286 scopus 로고
    • Isoenzymes of protein kinase C in rat mammary tissue: Changes in properties and relative amounts during pregnancy and lactation
    • K. CONNOR and R. A. CLEGG, Isoenzymes of protein kinase C in rat mammary tissue: changes in properties and relative amounts during pregnancy and lactation, Biochem. J. 291, 817-824 (1993).
    • (1993) Biochem. J. , vol.291 , pp. 817-824
    • Connor, K.1    Clegg, R.A.2
  • 42
    • 0011966653 scopus 로고
    • Membrane-associated protein kinase C
    • (D. S. LESTER and R. M. EPAND, eds). Ellis Horwood, Chichester
    • D. S. LESTER, Membrane-associated protein kinase C, pp. 80-101 in Protein Kinase C: Current Concepts and Future Perspectives (D. S. LESTER and R. M. EPAND, eds). Ellis Horwood, Chichester (1992).
    • (1992) Protein Kinase C: Current Concepts and Future Perspectives , pp. 80-101
    • Lester, D.S.1
  • 43
    • 0025908315 scopus 로고
    • Identification of intracellular receptor proteins for activated protein kinase C
    • D. MOCHLY-ROSEN, H. KHANER and J. LOPEZ, Identification of intracellular receptor proteins for activated protein kinase C, Proc. Natl. Acad. Sci. USA 88, 3997-4000 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3997-4000
    • Mochly-Rosen, D.1    Khaner, H.2    Lopez, J.3
  • 44
    • 0026068576 scopus 로고
    • 'Crosstalk': A pivotal role for protein kinase C in modulating relationships between signal transducing pathways
    • M. D. HOUSLAY, 'Crosstalk': a pivotal role for protein kinase C in modulating relationships between signal transducing pathways, Eur. J. Biochem. 195, 9-27 (1991).
    • (1991) Eur. J. Biochem. , vol.195 , pp. 9-27
    • Houslay, M.D.1
  • 45
    • 0028917954 scopus 로고
    • Regulation of Ras-mediated signalling: More than one way to skin a cat
    • B. M. T. BURGERING and J. L. BOS, Regulation of Ras-mediated signalling: more than one way to skin a cat, TIBS 20, 18-22 (1995).
    • (1995) TIBS , vol.20 , pp. 18-22
    • Burgering, B.M.T.1    Bos, J.L.2
  • 47
    • 0029947711 scopus 로고    scopus 로고
    • Regulation by cAMP-dependent protein kinase of a G-protein-mediated phospholipase C
    • M. L. LIU and M. I. SIMON, Regulation by cAMP-dependent protein kinase of a G-protein-mediated phospholipase C, Nature 382, 83-87 (1996).
    • (1996) Nature , vol.382 , pp. 83-87
    • Liu, M.L.1    Simon, M.I.2
  • 49
    • 0029887701 scopus 로고    scopus 로고
    • Coordination of three signalling enzymes by AKAP79, a mammalian scaffold protein
    • T. M. KLAUCK, M. C. FAUX, K. LABUDDA, L. K. LANGEBERG, S. JAKEN and J. D. SCOTT, Coordination of three signalling enzymes by AKAP79, a mammalian scaffold protein, Science 271, 1589-1592 (1996).
    • (1996) Science , vol.271 , pp. 1589-1592
    • Klauck, T.M.1    Faux, M.C.2    Labudda, K.3    Langeberg, L.K.4    Jaken, S.5    Scott, J.D.6
  • 51
    • 0030639672 scopus 로고    scopus 로고
    • Perturbation of the expression of the catalytic subunit Cα of Cyclic AMP-dependent protein kinase inhibits TCR-triggered secretion of IL-2 by T helper hybridoma cells
    • H. SUGIYAMA, P. CHEN, M. G. HUNTER and M. V. SITKOVSKY, Perturbation of the expression of the catalytic subunit Cα of Cyclic AMP-dependent protein kinase inhibits TCR-triggered secretion of IL-2 by T helper hybridoma cells, J. Immunol. 158, 171-179 (1997).
    • (1997) J. Immunol. , vol.158 , pp. 171-179
    • Sugiyama, H.1    Chen, P.2    Hunter, M.G.3    Sitkovsky, M.V.4
  • 53
    • 0028278181 scopus 로고
    • Signal transduction and gene regulation: The nuclear response to cAMP
    • E. LALLI and P. SASSONE-CORSI, Signal transduction and gene regulation: the nuclear response to cAMP, J. Biol. Chem. 269, 17356-17362 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 17356-17362
    • Lalli, E.1    Sassone-Corsi, P.2
  • 54
    • 0028049921 scopus 로고
    • Conditional activation of cAMP signal transduction by protein kinase C. The effect of phorbol esters on adenylyl cyclase in permeabilized and intact cells
    • B. H. MORIMOTO and D. E. KOSHLAND JR., Conditional activation of cAMP signal transduction by protein kinase C. The effect of phorbol esters on adenylyl cyclase in permeabilized and intact cells, J. Biol. Chem. 269, 4065-4069 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 4065-4069
    • Morimoto, B.H.1    Koshland D.E., Jr.2
  • 56
    • 0025076172 scopus 로고
    • The fats of life: The importance and function of protein acylation
    • R. A. J. MCILHINNEY, The fats of life: the importance and function of protein acylation, TIBS 15, 386-390 (1990).
    • (1990) TIBS , vol.15 , pp. 386-390
    • Mcilhinney, R.A.J.1
  • 57
    • 0025167252 scopus 로고
    • Evidence for a non-myristoylated pool of the 80-kDa protein-kinase-C substrate of rat-brain
    • R. A. J. MCILHINNEY and K. MCGLONE, Evidence for a non-myristoylated pool of the 80-kDa protein-kinase-C substrate of rat-brain, Biochem. J. 271, 681-685 (1990).
    • (1990) Biochem. J. , vol.271 , pp. 681-685
    • Mcilhinney, R.A.J.1    Mcglone, K.2
  • 58
    • 0031007608 scopus 로고    scopus 로고
    • Myristoylated and nonmyristoylated pools of sea urchin sperm flagellar creatine kinase exist side-by-side: Myristoylation is necessary for efficient lipid association
    • A. F. G. QUEST, D. J. HARVEY and R. A. J. MCILHINNEY, Myristoylated and nonmyristoylated pools of sea urchin sperm flagellar creatine kinase exist side-by-side: Myristoylation is necessary for efficient lipid association, Biochemistry 36, 6993-7002 (1997).
    • (1997) Biochemistry , vol.36 , pp. 6993-7002
    • Quest, A.F.G.1    Harvey, D.J.2    Mcilhinney, R.A.J.3
  • 59
    • 0031019429 scopus 로고    scopus 로고
    • Understanding covalent modifications of proteins by lipids: Where cell biology and biophysics mingle
    • R. S. BHATNAGAR and J. I. GORDON, Understanding covalent modifications of proteins by lipids: where cell biology and biophysics mingle, Trends Cell Biol. 7, 14-20 (1997).
    • (1997) Trends Cell Biol. , vol.7 , pp. 14-20
    • Bhatnagar, R.S.1    Gordon, J.I.2
  • 60
    • 0027208292 scopus 로고
    • Identification of cellular proteins that bind to the human immunodeficiency virus type-I nef gene product in vitro - A role for myristylation
    • M. HARRIS and K. COATES, Identification of cellular proteins that bind to the human immunodeficiency virus type-I nef gene product in vitro - a role for myristylation, J. Gen. Virol. 74, 1581-1589 (1993).
    • (1993) J. Gen. Virol. , vol.74 , pp. 1581-1589
    • Harris, M.1    Coates, K.2
  • 63
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • M. D. RESH, Myristylation and palmitylation of Src family members: the fats of the matter, Cell 76, 411-413 (1994).
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 64
    • 0027432307 scopus 로고
    • Binding of acylated peptides and fatty acids to phospholipid vesicles: Pertinence to myristoylated proteins
    • R. M. PEITZSH and S. MCLAUGHLIN, Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins, Biochemistry 32, 10436-10443 (1993).
    • (1993) Biochemistry , vol.32 , pp. 10436-10443
    • Peitzsh, R.M.1    Mclaughlin, S.2
  • 65
    • 0029058605 scopus 로고    scopus 로고
    • The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions
    • S. MCLAUGHLIN and A. ADEREM, The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. TIBS, 20, 272-276.
    • TIBS , vol.20 , pp. 272-276
    • Mclaughlin, S.1    Aderem, A.2
  • 67
    • 0030948184 scopus 로고    scopus 로고
    • Myristoylation
    • J. A. BOUTIN, Myristoylation. Cell. Signal. 9, 15-35 (1997).
    • (1997) Cell. Signal. , vol.9 , pp. 15-35
    • Boutin, J.A.1
  • 68
    • 0028244655 scopus 로고
    • Isothermal titration calorimetric studies of Saccharomyces cerevisiae myristoyl-CoA: Protein N-myristoyltransferase: determinants of binding energy and catalytic discrimination among acyl-CoA and peptide ligands
    • R. S. BHATNAGAR, E. JACKSON-MACHELSKI, C. A. MCWHERTER and J. I. GORDON, Isothermal titration calorimetric studies of Saccharomyces cerevisiae myristoyl-CoA: protein N-myristoyltransferase: determinants of binding energy and catalytic discrimination among acyl-CoA and peptide ligands, J. Biol. Chem. 269, 11045-11053 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 11045-11053
    • Bhatnagar, R.S.1    Jackson-Machelski, E.2    Mcwherter, C.A.3    Gordon, J.I.4
  • 69
    • 0024590280 scopus 로고
    • Disruption of the yeast N-myristoyl transferase gene causes recessive lethality
    • R. J. DURONIO, D. A. TOWLER, R. O. HEUCKEROTH and J. I. GORDON, Disruption of the yeast N-myristoyl transferase gene causes recessive lethality, Science 243, 796-800 (1989).
    • (1989) Science , vol.243 , pp. 796-800
    • Duronio, R.J.1    Towler, D.A.2    Heuckeroth, R.O.3    Gordon, J.I.4
  • 70
    • 0030657584 scopus 로고    scopus 로고
    • Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction
    • C. J. GLOVER, K. D. HARTMAN and R. L. FELSTED, Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction, J. Biol. Chem. 272, 28680-28689 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 28680-28689
    • Glover, C.J.1    Hartman, K.D.2    Felsted, R.L.3
  • 71
    • 0032143539 scopus 로고    scopus 로고
    • Characterization of human and rat brain myristoyl-CoA:Protein N-myristoyltransferase: Evidence for an alternative splice variant of the enzyme
    • R. A. J. MCILHINNEY, K. YOUNG, M. EGERTON, R. CAMBLE, A. WHITE and A. SOLOVIEV, Characterization of human and rat brain myristoyl-CoA:protein N-myristoyltransferase: evidence for an alternative splice variant of the enzyme, Biochem. J. 333, 491-495 (1998).
    • (1998) Biochem. J. , vol.333 , pp. 491-495
    • Mcilhinney, R.A.J.1    Young, K.2    Egerton, M.3    Camble, R.4    White, A.5    Soloviev, A.6
  • 72
    • 0032549571 scopus 로고    scopus 로고
    • A second mammalian N-myristoyl transferase
    • D. K. GIANG and B. F. CRAVATT, A second mammalian N-myristoyl transferase, J. Biol. Chem. 273, 6595-6598 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 6595-6598
    • Giang, D.K.1    Cravatt, B.F.2
  • 73
    • 0031627047 scopus 로고    scopus 로고
    • Membrane targeting via protein N-myristoylation
    • (R. A. Clegg, ed.). Humana Press, Totowa
    • R. A. J. MCILHINNEY, Membrane targeting via protein N-myristoylation, pp. 211-225 in Protein Targeting Protocols (R. A. Clegg, ed.). Humana Press, Totowa (1998).
    • (1998) Protein Targeting Protocols , pp. 211-225
    • Mcilhinney, R.A.J.1
  • 74
    • 0031846663 scopus 로고    scopus 로고
    • Myristoyl-CoA:Protein N-myristoyltransferase from bovine cardiac muscle: Molecular cloning, kinetic analysis, and in vitro proteolytic cleavage by m-calpain
    • R. V. S. RAJU, R. KAKKAR, R. S. S. DATLA, J. RADHI and R. K. SHARMA, Myristoyl-CoA:protein N-myristoyltransferase from bovine cardiac muscle: molecular cloning, kinetic analysis, and in vitro proteolytic cleavage by m-calpain, Exptl. Cell Res. 241, 23-35 (1998).
    • (1998) Exptl. Cell Res. , vol.241 , pp. 23-35
    • Raju, R.V.S.1    Kakkar, R.2    Datla, R.S.S.3    Radhi, J.4    Sharma, R.K.5
  • 75
    • 0028972680 scopus 로고
    • Increased N-myristoyltransferase activity observed in rat and human colonic tumours
    • B. A. MAGNUSON, R. V. S. RAJU, T. N. MOYANA and R. K. SHARMA, Increased N-myristoyltransferase activity observed in rat and human colonic tumours, J. Natl. Cancer Inst. 87, 1630-1635 (1995).
    • (1995) J. Natl. Cancer Inst. , vol.87 , pp. 1630-1635
    • Magnuson, B.A.1    Raju, R.V.S.2    Moyana, T.N.3    Sharma, R.K.4
  • 76
    • 0028828067 scopus 로고
    • Protein N-myristoylation as a chemotherapeutic target for cancer
    • R. L. FELSTED, C. J. GLOVER and K. HARTMAN, Protein N-myristoylation as a chemotherapeutic target for cancer, J. Natl. Cancer Inst. 87, 1571-1573 (1995).
    • (1995) J. Natl. Cancer Inst. , vol.87 , pp. 1571-1573
    • Felsted, R.L.1    Glover, C.J.2    Hartman, K.3
  • 77
    • 0024819250 scopus 로고
    • Expression of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli
    • L. W. SLICE and S. S. TAYLOR, Expression of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli, J. Biol. Chem. 264, 20940-20946 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 20940-20946
    • Slice, L.W.1    Taylor, S.S.2
  • 78
    • 0018447907 scopus 로고
    • A new cAMP affinity matrix for the rapid purification of protein kinase regulatory subunits
    • W. WEBER, C.-W. VOGEL and H. HILTZ, A new cAMP affinity matrix for the rapid purification of protein kinase regulatory subunits, FEBS Lett. 99, 62-66 (1979).
    • (1979) FEBS Lett. , vol.99 , pp. 62-66
    • Weber, W.1    Vogel, C.-W.2    Hiltz, H.3
  • 79
    • 0000939974 scopus 로고    scopus 로고
    • Elevation of protein kinase A and protein kinase C activities in malignant as compared with normal human breast tissue
    • P. C. GORDGE, M. J. HULME and W. R. MILLER, Elevation of protein kinase A and protein kinase C activities in malignant as compared with normal human breast tissue, Eur. J. Cancer 32a, 2120-2126 (1996).
    • (1996) Eur. J. Cancer , vol.32 A , pp. 2120-2126
    • Gordge, P.C.1    Hulme, M.J.2    Miller, W.R.3
  • 80
    • 0025013002 scopus 로고
    • Cyclic AMP-dependent protein kinase in mammary tissue of the lactating rat. Activity ratio and responsiveness of the target enzymes acetyl-CoA carboxylase and glycogen phosphorylase to β-adrenergic stimulation
    • R. A. CLEGG and K. A. OTTEY, Cyclic AMP-dependent protein kinase in mammary tissue of the lactating rat. Activity ratio and responsiveness of the target enzymes acetyl-CoA carboxylase and glycogen phosphorylase to β-adrenergic stimulation, Biochem. J. 265, 769-775 (1990).
    • (1990) Biochem. J. , vol.265 , pp. 769-775
    • Clegg, R.A.1    Ottey, K.A.2
  • 81
    • 0025128519 scopus 로고
    • Characterization of a myristoyl CoA:Glycylpeptide N-myristoyl transferase activity in rat brain: Subcellular and regional distribution
    • R. A. J. MCILHINNEY and K. MCGLONE, Characterization of a myristoyl CoA:glycylpeptide N-myristoyl transferase activity in rat brain: subcellular and regional distribution, J. Neurochem. 54, 110-117 (1990).
    • (1990) J. Neurochem. , vol.54 , pp. 110-117
    • Mcilhinney, R.A.J.1    Mcglone, K.2
  • 82
    • 0031577590 scopus 로고    scopus 로고
    • N-myristoylation of the catalytic subunit of cAMP-dependent protein kinase in the free-living nematode Caenorhabditis elegans
    • R. A. ASPBURY, M. J. FISHER, H. H. REES and R. A. CLEGG, N-myristoylation of the catalytic subunit of cAMP-dependent protein kinase in the free-living nematode Caenorhabditis elegans, Biochem. Biophys. Res. Commun. 238, 523-527 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 523-527
    • Aspbury, R.A.1    Fisher, M.J.2    Rees, H.H.3    Clegg, R.A.4
  • 84
    • 0029876931 scopus 로고    scopus 로고
    • Immunocytochemical characterization and subcellular localization of human myristoyl-CoA:Protein N-myristoyl transferase in HeLa cells
    • R. A. J. MCILHINNEY and K. MCGLONE, Immunocytochemical characterization and subcellular localization of human myristoyl-CoA:protein N-myristoyl transferase in HeLa cells, Exptl. Cell Res. 223, 348-356 (1996).
    • (1996) Exptl. Cell Res. , vol.223 , pp. 348-356
    • Mcilhinney, R.A.J.1    Mcglone, K.2
  • 85
    • 0031630680 scopus 로고    scopus 로고
    • Overlay, ligand blotting and band-shift techniques to study kinase anchoring
    • (R. A. CLEGG, ed.). Humana Press, Totowa
    • Z. E. HAUSKEN, V. M. COGHLAN and J. D. SCOTT, Overlay, ligand blotting and band-shift techniques to study kinase anchoring, pp. 47-64 in Protein Targeting Protocols (R. A. CLEGG, ed.). Humana Press, Totowa (1998).
    • (1998) Protein Targeting Protocols , pp. 47-64
    • Hausken, Z.E.1    Coghlan, V.M.2    Scott, J.D.3
  • 86
    • 0026680801 scopus 로고
    • Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain
    • D. W. CARR, Z. E. HAUSKEN, I. D. C. FRASER, R. D. CONE and J. D. SCOTT, Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain, J. Biol. Chem. 267, 13376-13382 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 13376-13382
    • Carr, D.W.1    Hausken, Z.E.2    Fraser, I.D.C.3    Cone, R.D.4    Scott, J.D.5
  • 87
    • 0022404103 scopus 로고
    • Fate of immunoprecipitable protein kinase C in GH3 cells treated with phorbol-12-myristate-13-acetate
    • R. BALLESTER and O. M. ROSEN, Fate of immunoprecipitable protein kinase C in GH3 cells treated with phorbol-12-myristate-13-acetate, J. Biol. Chem. 260, 15194-15199 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 15194-15199
    • Ballester, R.1    Rosen, O.M.2
  • 88
    • 0022386766 scopus 로고
    • Acute change in the cyclic AMP content of rat mammary acini in vitro. Influence of physiological and pharmacological agents
    • R. A. CLEGG and I. MULLANEY, Acute change in the cyclic AMP content of rat mammary acini in vitro. Influence of physiological and pharmacological agents, Biochem. J. 230, 239-246 (1985).
    • (1985) Biochem. J. , vol.230 , pp. 239-246
    • Clegg, R.A.1    Mullaney, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.