메뉴 건너뛰기




Volumn 14, Issue 1, 1993, Pages 40-58

Regulation of the cell cycle by calcium and calmodulin

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALMODULIN; COMPLEMENTARY DNA; CYCLINE; PROTEIN KINASE;

EID: 0027467864     PISSN: 0163769X     EISSN: 0163769X     Source Type: Journal    
DOI: 10.1210/edrv-14-1-40     Document Type: Article
Times cited : (272)

References (215)
  • 1
    • 0025320398 scopus 로고
    • Calcium and cell cycle
    • Whitaker M, Patel R 1990 Calcium and cell cycle. Development 108:525-542
    • (1990) Development , vol.108 , pp. 525-542
    • Whitaker, M.1    Patel, R.2
  • 6
    • 0023006881 scopus 로고    scopus 로고
    • Isolation of the yeast calmodulin gene: Calmodulin is an essential protein
    • Davis TN, Urdea MS, Masiarz FR, Thorner J 1986 Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47:423-431
    • Cell
    • Davis, T.N.1    Urdea, M.S.2    Masiarz, F.R.3    Thorner, J.4
  • 7
    • 0023197157 scopus 로고
    • Analysis and
    • Takeda T, Yamamoto M 1987 Analysis and in vivo disruption of the gene encoding for calmodulin in Schizosaccharomyces pombe. Proc Natl Acad Sci USA 84:3580-3584
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3580-3584
    • Takeda, T.1    Yamamoto, M.2
  • 8
    • 0024989875 scopus 로고
    • Characterization and expression of the unique calmodulin gene of
    • Rasmussen CD, Means RL, Lu KP, May GS, Means AR 1990 Characterization and expression of the unique calmodulin gene of Aspergillus nidulans. J Biol Chem 265:1367-13775
    • (1993) J Biol Chem , vol.265 , pp. 1367-13775
    • Rasmussen, C.D.1    Means, R.L.2    Lu, K.P.3    May, G.S.4    Means, A.R.5
  • 9
    • 0023661342 scopus 로고
    • Calmodulin is involved in regulation of cell proliferation
    • Rasmussen CD, Means AR 1987 Calmodulin is involved in regulation of cell proliferation. EMBO J 6:3961-3968
    • (1987) EMBO J , vol.6 , pp. 3961-3968
    • Rasmussen, C.D.1    Means, A.R.2
  • 10
    • 0024440855 scopus 로고
    • Calmodulin is required for cell cycle progression during Gi and mitosis
    • Rasmussen CD, Means AR 1989 Calmodulin is required for cell cycle progression during Gi and mitosis. EMBO J 8:73-82
    • (1989) EMBO J , vol.8 , pp. 73-82
    • Rasmussen, C.D.1    Means, A.R.2
  • 11
    • 0023758446 scopus 로고
    • The abundance of calmodulin mRNAs is regulated in phosphorylase kinase-deficient skeletal muscle
    • Bender PK, Dedman JR, Emerson CP 1988 The abundance of calmodulin mRNAs is regulated in phosphorylase kinase-deficient skeletal muscle. J Biol Chem 263:9733-9737
    • (1988) J Biol Chem , vol.263 , pp. 9733-9737
    • Bender, P.K.1    Dedman, J.R.2    Emerson, C.P.3
  • 13
    • 0024370325 scopus 로고
    • Structural organization of multiple rat calmodulin genes
    • Nojima H 1989 Structural organization of multiple rat calmodulin genes. J Mol Biol 208:269-282
    • (1989) J Mol Biol , vol.208 , pp. 269-282
    • Nojima, H.1
  • 14
    • 0025789649 scopus 로고
    • The increase of calmodulin in PC12 cells induced by NGF is caused by differential expression of multiple mRNAs for calmodulin
    • Bai G, Weiss B 1991 The increase of calmodulin in PC12 cells induced by NGF is caused by differential expression of multiple mRNAs for calmodulin. J Cell Physiol 149:414-421
    • (1991) J Cell Physiol , vol.149 , pp. 414-421
    • Bai, G.1    Weiss, B.2
  • 16
    • 0025855885 scopus 로고
    • Cell cycle control by calcium and calmodulin in
    • Anraku Y, Ohya Y, Iida H 1991 Cell cycle control by calcium and calmodulin in Saccharomyces cerevisiae. Biochim Biophys Acta 1093:169-177
    • (1991) Biochim Biophys Acta , vol.1093 , pp. 169-177
    • Anraku, Y.1    Ohya, Y.2    Iida, H.3
  • 17
    • 0024425274 scopus 로고
    • Dominoes and clocks: The union of two views of the cell cycle
    • Murray AW, Kirschner MW 1989 Dominoes and clocks: the union of two views of the cell cycle. Science 246:614-621
    • (1989) Science , vol.246 , pp. 614-621
    • Murray, A.W.1    Kirschner, M.W.2
  • 18
    • 0025022102 scopus 로고
    • Controls of cell proliferation in yeast and animals
    • Norbury C, Nurse P 1990 Controls of cell proliferation in yeast and animals. Ciba Found Symp 150:168-177
    • (1990) Ciba Found Symp , vol.150 , pp. 168-177
    • Norbury, C.1    Nurse, P.2
  • 19
    • 0025787953 scopus 로고
    • Cell cycle regulation in the
    • Forsbury SL, Nurse P 1991 Cell cycle regulation in the Saccharomyces cerevisiae and Schizosaccharomyces pombe. Annu Rev Cell Biol 7:227-256
    • (1991) Annu Rev Cell Biol , vol.7 , pp. 227-256
    • Forsbury, S.L.1    Nurse, P.2
  • 20
    • 0025351481 scopus 로고
    • Lower eukaryotic cell cycle: Perspectives on mitosis from the fungi
    • Morris NR 1990 Lower eukaryotic cell cycle: perspectives on mitosis from the fungi. Curr Opin Cell Biol 2:252-257
    • (1990) Curr Opin Cell Biol , vol.2 , pp. 252-257
    • Morris, N.R.1
  • 21
    • 0017084282 scopus 로고    scopus 로고
    • Mutual potentiation by magnesium and calcium of growth in animal cells
    • Rubin H, Koide T 1976 Mutual potentiation by magnesium and calcium of growth in animal cells. Proc Natl Acad Sci USA 73:168172
    • Proc Natl Acad Sci USA
    • Rubin, H.1    Koide, T.2
  • 23
    • 0017889940 scopus 로고
    • Calcium requirements for the proliferation of cells infected with a temperature-sensitive mutant of rous sarcoma virus
    • Boynton AL, Whitfield JF 1978 Calcium requirements for the proliferation of cells infected with a temperature-sensitive mutant of rous sarcoma virus. Cancer Res 38:1237-1240
    • (1978) Cancer Res , vol.38 , pp. 1237-1240
    • Boynton, A.L.1    Whitfield, J.F.2
  • 25
    • 0018613064 scopus 로고
    • Calcium, magnesium and growth control in the WI-38 fibroblast cell
    • Hazelton B, Mitchell B, Tupper J 1979 Calcium, magnesium and growth control in the WI-38 fibroblast cell. J Cell Biol 83:487-498
    • (1979) J Cell Biol , vol.83 , pp. 487-498
    • Hazelton, B.1    Mitchell, B.2    Tupper, J.3
  • 26
    • 0019287552 scopus 로고
    • Related effects of calcium and serum on the G phase of human WI 38 fibroblasts
    • Tupper JT, Kaufman L, Bodine PV 1980 Related effects of calcium and serum on the G phase of human WI 38 fibroblasts. J Cell Physiol 104:97-103
    • (1980) J Cell Physiol , vol.104 , pp. 97-103
    • Tupper, J.T.1    Kaufman, L.2    Bodine, P.V.3
  • 27
  • 28
    • 0025392622 scopus 로고
    • The stimulatory effect of heavy metal cations on the proliferation of aortic smooth muscle cells
    • Lu KP, Chao SH, Wang DS 1990 The stimulatory effect of heavy metal cations on the proliferation of aortic smooth muscle cells. Sci China (B) 33:303-310
    • (1990) Sci China (B) , vol.33 , pp. 303-310
    • Lu, K.P.1    Chao, S.H.2    Wang, D.S.3
  • 29
    • 0017640414 scopus 로고
    • The control of human Wi-38 cell proliferation by extracellular calcium and its elimination by SV-40 virus-induced proliferative transformation
    • Boynton AL, Whitfield JF, Isaacs RJ, Tremblay R 1977 The control of human Wi-38 cell proliferation by extracellular calcium and its elimination by SV-40 virus-induced proliferative transformation. J Cell Physiol 92:241-248
    • (1977) J Cell Physiol , vol.92 , pp. 241-248
    • Boynton, A.L.1    Whitfield, J.F.2    Isaacs, R.J.3    Tremblay, R.4
  • 33
    • 0026609630 scopus 로고
    • 2+ pump of the plasma membrane
    • 2+ pump of the plasma membrane. J Biol Chem 267:2115-2118
    • (1992) J Biol Chem , vol.267 , pp. 2115-2118
    • Carafoli, E.1
  • 34
    • 0023025201 scopus 로고
    • Early signals in the mitogenic response
    • Rozengurt E 1986 Early signals in the mitogenic response. Science 234:161-166
    • (1986) Science , vol.234 , pp. 161-166
    • Rozengurt, E.1
  • 35
    • 0025283839 scopus 로고
    • Calcium oscillations in electrically non-excitable cells
    • Jacob R 1990 Calcium oscillations in electrically non-excitable cells. Biochim Biophys Acta 1052:427-438
    • (1990) Biochim Biophys Acta , vol.1052 , pp. 427-438
    • Jacob, R.1
  • 36
    • 0024453294 scopus 로고
    • Inositol phosphates and cell signalling
    • Berridge MJ, Irvin RF 1989 Inositol phosphates and cell signalling. Nature 341:197-205
    • (1989) Nature , vol.341 , pp. 197-205
    • Berridge, M.J.1    Irvin, R.F.2
  • 37
    • 0025350112 scopus 로고
    • Calcium oscillations
    • Berridge MJ 1990 Calcium oscillations. J Biol Chem 265:95839586
    • (1990) J Biol Chem , vol.9583-9586 , pp. 265
    • Berridge, M.J.1
  • 38
    • 0024811662 scopus 로고
    • Calcium transients during mitosis: Observation in flux
    • Hepler PK 1989 Calcium transients during mitosis: observation in flux. J Cell Biol 109:2576-2573
    • (1989) J Cell Biol , vol.109 , pp. 2576-2573
    • Hepler, P.K.1
  • 39
    • 0025297818 scopus 로고
    • Calcium and cellular clocks orchestrate cell division
    • Silver RB 1990 Calcium and cellular clocks orchestrate cell division. Ann NY Acad Sci 582:207-221
    • (1990) Ann NY Acad Sci , vol.582 , pp. 207-221
    • Silver, R.B.1
  • 40
    • 0018834707 scopus 로고
    • Isolation of mitotic apparatus containing vesicles with calcium sequestration activity
    • Silver RB, Cole RD, Cande WZ 1980 Isolation of mitotic apparatus containing vesicles with calcium sequestration activity. Cell 19:505-516
    • (1980) Cell , vol.19 , pp. 505-516
    • Silver, R.B.1    Cole, R.D.2    Cande, W.Z.3
  • 41
    • 0019421929 scopus 로고
    • Studies of the
    • Kiehart DP 1981 Studies of the in vivo sensitivity of spindle microtubules to calcium ions and evidence for a vascular calciumsequestering system. J Cell Biol 88:604-616
    • (1981) J Cell Biol , vol.88 , pp. 604-616
    • Kiehart, D.P.1
  • 42
    • 0019598810 scopus 로고    scopus 로고
    • The coincident distribution of calcium-rich membranes and kinetochore fibers at metaphase in living endosperm cells of
    • Wolniak SM, Hepler PK, Jackson WT 1981 The coincident distribution of calcium-rich membranes and kinetochore fibers at metaphase in living endosperm cells of Haemanthus. Eur J Cell Biol 25:171-174
    • Eur J Cell Biol
    • Wolniak, S.M.1    Hepler, P.K.2    Jackson, W.T.3
  • 43
    • 0021646561 scopus 로고    scopus 로고
    • Membranes in the mitotic apparatus: Their structure and function
    • Hepler PK, Wolniak SM 1984 Membranes in the mitotic apparatus: their structure and function. Int Rev Cytol 90:169-238
    • Int Rev Cytol
    • Hepler, P.K.1    Wolniak, S.M.2
  • 44
    • 0021840109 scopus 로고
    • Changes of free calcium levels with stages of the cell division cycle
    • Poenie M, Alderton J, Tsien RY, Steinhardt RA 1985 Changes of free calcium levels with stages of the cell division cycle. Nature 315:147-149
    • (1985) Nature , vol.315 , pp. 147-149
    • Poenie, M.1    Alderton, J.2    Tsien, R.Y.3    Steinhardt, R.A.4
  • 46
    • 0022468347 scopus 로고
    • Calcium rises abruptly and briefly throughout the cell at the onset of anaphase
    • Poenie M, Alderton J, Steinhardt RA, Tsien RY 1986 Calcium rises abruptly and briefly throughout the cell at the onset of anaphase. Science 233:886-899
    • (1986) Science , vol.233 , pp. 886-899
    • Poenie, M.1    Alderton, J.2    Steinhardt, R.A.3    Tsien, R.Y.4
  • 47
    • 0025194832 scopus 로고
    • Active involvement of Ca2+ in mitotic progression of Swiss 3T3 fibroblasts
    • Kao JPY, Alderton JM, Tsien RY, Steinhardt RA 1990 Active involvement of Ca2+ in mitotic progression of Swiss 3T3 fibroblasts. J Cell Biol 111:183-196
    • (1990) J Cell Biol , vol.111 , pp. 183-196
    • Kao, J.1    Alderton, J.M.2    Tsien, R.Y.3    Steinhardt, R.A.4
  • 48
    • 0020964486 scopus 로고
    • The role of calcium ion during mitosis: Calcium participitates in the anaphase trigger
    • Izant JG 1983 The role of calcium ion during mitosis: calcium participitates in the anaphase trigger. Chromosoma 88:1-10
    • (1983) Chromosoma , vol.88 , pp. 1-10
    • Izant, J.G.1
  • 49
    • 0023882072 scopus 로고
    • Intracellular free calcium rise triggers nuclear envelope breakdown in the sea urchin embryo
    • Steinhardt RA, Alderton J 1988 Intracellular free calcium rise triggers nuclear envelope breakdown in the sea urchin embryo. Nature 332:364-366
    • (1988) Nature , vol.332 , pp. 364-366
    • Steinhardt, R.A.1    Alderton, J.2
  • 50
    • 0024295662 scopus 로고
    • 3-induced chromatin condensation during the early cell cycles of sea urchin embryos
    • 3-induced chromatin condensation during the early cell cycles of sea urchin embryos. Nature 332:366-369
    • (1988) Nature , vol.332 , pp. 366-369
    • Twigg, J.1    Patel, R.2    Whitaker, M.J.3
  • 51
    • 0014934492 scopus 로고
    • Cyclic 3’, 5’-nucleotide phosphodiesterase: Demonstration of an activator
    • Cheung WY 1970 Cyclic 3’, 5’-nucleotide phosphodiesterase: demonstration of an activator. Biochem Biophys Res Commun 38:533-538
    • (1970) Biochem Biophys Res Commun , vol.38 , pp. 533-538
    • Cheung, W.Y.1
  • 52
    • 0014938577 scopus 로고
    • Calcium dependent phosphodiesterase activity and its activating factor (PAF) from brain: Studies on cyclic 3’, 5’-nucleotide phosphodiesterase (III)
    • Kakiuchi S, Yamazaki R 1970 Calcium dependent phosphodiesterase activity and its activating factor (PAF) from brain: studies on cyclic 3’, 5’-nucleotide phosphodiesterase (III). Biochem Biophys Res Commun 41:1104-1110
    • (1970) Biochem Biophys Res Commun , vol.41 , pp. 1104-1110
    • Kakiuchi, S.1    Yamazaki, R.2
  • 54
    • 0018872612 scopus 로고
    • Calmodulin plays a pivotal role in cellular regulation
    • Cheung WY 1980 Calmodulin plays a pivotal role in cellular regulation. Science 207:19-27
    • (1980) Science , vol.207 , pp. 19-27
    • Cheung, W.Y.1
  • 55
    • 0019319345 scopus 로고
    • Calmodulin-an intracellular calcium receptor
    • Means AR, Dedman JR 1980 Calmodulin-an intracellular calcium receptor. Nature 285:73-77
    • (1980) Nature , vol.285 , pp. 73-77
    • Means, A.R.1    Dedman, J.R.2
  • 57
    • 0024196034 scopus 로고
    • Molecular mechanism of action of calmodulin
    • Means AR 1988 Molecular mechanism of action of calmodulin. Recent Prog Horm Res 44:223-262
    • (1988) Recent Prog Horm Res , vol.44 , pp. 223-262
    • Means, A.R.1
  • 59
    • 0015919772 scopus 로고
    • Carp muscle calcium-binding protein. II. Structure determination and general description
    • Kretsinger RH, Nockolds CE 1973 Carp muscle calcium-binding protein. II. Structure determination and general description. J Biol Chem 248:3313-3326
    • (1973) J Biol Chem , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 60
    • 0016716829 scopus 로고
    • Protein activator of cyclic 3’, 5’-nucleotide phosphodiesterase of bovine or rat brain also activates its adenyl cyclase
    • Cheung WY, Bradham LS, Lynch TJ, Lin YM, Tallant EA 1975 Protein activator of cyclic 3’, 5’-nucleotide phosphodiesterase of bovine or rat brain also activates its adenyl cyclase. Biochem Biophys Res Commun 66:1055-1062
    • (1975) Biochem Biophys Res Commun , vol.66 , pp. 1055-1062
    • Cheung, W.Y.1    Bradham, L.S.2    Lynch, T.J.3    Lin, Y.M.4    Tallant, E.A.5
  • 61
    • 0016436371 scopus 로고
    • Identification of a calcium-binding protein as a calcium-dependent regulator of brain adenylate cyclase
    • Brostrom CO, Huang YC, Breckenridge BM 1975 Identification of a calcium-binding protein as a calcium-dependent regulator of brain adenylate cyclase. Proc Natl Acad Sci USA 72:64-68
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 64-68
    • Brostrom, C.O.1    Huang, Y.C.2    Breckenridge, B.M.3
  • 62
    • 0017622160 scopus 로고
    • 2+ ATPase activator from human erythrocytes: Its similarity to the activator of 3’, 5’-cyclic nucleotide phosphodiesterase
    • 2+ ATPase activator from human erythrocytes: its similarity to the activator of 3’, 5’-cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun 77:1210-1216
    • (1977) Biochem Biophys Res Commun , vol.77 , pp. 1210-1216
    • Jarret, H.W.1    Penniston, J.T.2
  • 64
    • 0018764505 scopus 로고
    • Calcium transport across the plasma membrane: Stimulation by calmoudlin
    • Larson FL, Vincenzi FF 1979 Calcium transport across the plasma membrane: stimulation by calmoudlin. Science 204:306-309
    • (1979) Science , vol.204 , pp. 306-309
    • Larson, F.L.1    Vincenzi, F.F.2
  • 65
    • 0018092098 scopus 로고
    • Phosphodiesterase protein activator stimulates calcium transport in cardiac microsomal preparations enriched in sarcoplasmic reticulum
    • Katz S, Remtulla MA 1978 Phosphodiesterase protein activator stimulates calcium transport in cardiac microsomal preparations enriched in sarcoplasmic reticulum. Biochem Biophys Res Commun 83:1373-1379
    • (1978) Biochem Biophys Res Commun , vol.83 , pp. 1373-1379
    • Katz, S.1    Remtulla, M.A.2
  • 67
    • 0017854367 scopus 로고
    • Stimulation of brain membrane protein phosphorylation by calcium and an endogenous heatstable protein
    • Schulman H, Greengard P 1978 Stimulation of brain membrane protein phosphorylation by calcium and an endogenous heatstable protein. Nature 271:478-479
    • (1978) Nature , vol.271 , pp. 478-479
    • Schulman, H.1    Greengard, P.2
  • 69
    • 0018800226 scopus 로고
    • Tion and characterization of an inhibitor protein of brain adenylate cyclase and cyclic nucleotide phosphodiesterase
    • Wallace RW, Lynch TJ, Tallant EA, Cheung WY 1979 Purification and characterization of an inhibitor protein of brain adenylate cyclase and cyclic nucleotide phosphodiesterase. J Biol Chem 254:377-382
    • (1993) J Biol Chem , vol.254 , pp. 377-382
    • Wallace, R.W.1    Lynch, T.J.2    Tallant, E.A.3    Cheung, W.Y.4
  • 70
    • 0018800864 scopus 로고
    • Purification and subunit structure of bovine brain modulator binding protein
    • Shrma RK, Desai R, Waisman DM, Wang JH 1979 Purification and subunit structure of bovine brain modulator binding protein. J Biol Chem 254:4276-4282
    • (1979) J Biol Chem , vol.254 , pp. 4276-4282
    • Shrma, R.K.1    Desai, R.2    Waisman, D.M.3    Wang, J.H.4
  • 71
    • 0001018554 scopus 로고
    • Calcineurin: A calciumand calmodulin-binding protein of nervous system
    • Klee CB, Crouch TH, Krinks MH 1979 Calcineurin: a calciumand calmodulin-binding protein of nervous system. Proc Natl Acad Sci USA 76:6270-6273
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 6270-6273
    • Klee, C.B.1    Crouch, T.H.2    Krinks, M.H.3
  • 72
    • 0023244022 scopus 로고
    • Calcium-calmodulin stimulates inositol 1, 4, 5-trisphosphate kinase activity from insulin-secreting RINm5F cells
    • Biden TJ, Comte M, Cox JA, Wollheim CB 1987 Calcium-calmodulin stimulates inositol 1, 4, 5-trisphosphate kinase activity from insulin-secreting RINm5F cells. J Biol Chem 262:9437-9440
    • (1987) J Biol Chem , vol.262 , pp. 9437-9440
    • Biden, T.J.1    Comte, M.2    Cox, J.A.3    Wollheim, C.B.4
  • 73
    • 0023655190 scopus 로고
    • Calmodulin stimulates inositol 1, 4, 5-trisphosphate 3-kinase activity in pig aortic smooth muscle
    • Yamaquchi K, Hirata M, Kuriyama H 1987 Calmodulin stimulates inositol 1, 4, 5-trisphosphate 3-kinase activity in pig aortic smooth muscle. Biochem J 244:787-791
    • (1987) Biochem J , vol.244 , pp. 787-791
    • Yamaquchi, K.1    Hirata, M.2    Kuriyama, H.3
  • 74
    • 0025191219 scopus 로고
    • Isolation of nitric oxide synthetase: A calmodulin-requiring enzyme
    • Bredt DS, Snyder SH 1990 Isolation of nitric oxide synthetase: a calmodulin-requiring enzyme. Proc Natl Acad Sci USA 87:682685
    • (1990) Proc Natl Acad Sci USA , vol.682-685 , pp. 87
    • Bredt, D.S.1    Snyder, S.H.2
  • 75
    • 0025572626 scopus 로고
    • Purification of a
    • +/calmodulin-dependent nitric oxide synthase from porcine cerebellum: cofactor-role of tetrahydrobiopterin. FEBS Lett 277:215-219
    • (1990) FEBS Lett , vol.277 , pp. 215-219
    • Mayer, B.1    John, M.2    Bohme, E.3
  • 77
    • 0020062918 scopus 로고
    • Calmodulin and the cell cycle: Involvement in regulation of cell cycle progression
    • Chafouleas JG, Bolton WE, Boyd III AE, Means AR 1982 Calmodulin and the cell cycle: involvement in regulation of cell cycle progression. Cell 28:41-50
    • (1982) Cell , vol.28 , pp. 41-50
    • Chafouleas, J.G.1    Bolton, W.E.2    Boyd, I.3    Means, A.R.4
  • 81
    • 0023680159 scopus 로고
    • Cell cycle dependent variation of calmodulin in
    • Singh J, Chatterjee S 1988 Cell cycle dependent variation of calmodulin in Tetrahymena. Cytobios 55:95-103
    • (1988) Cytobios , vol.55 , pp. 95-103
    • Singh, J.1    Chatterjee, S.2
  • 82
    • 0024957663 scopus 로고
    • Cell cycle-dependent regulation of calmodulin levels in
    • Uno I, Ohya Y, Anraku Y, Ishikawa T 1989 Cell cycle-dependent regulation of calmodulin levels in Saccharomyces cerevisiae. J Gen Appl Microbiol 35:59-63
    • (1989) J Gen Appl Microbiol , vol.35 , pp. 59-63
    • Uno, I.1    Ohya, Y.2    Anraku, Y.3    Ishikawa, T.4
  • 83
    • 85003102019 scopus 로고
    • Calmodulin: A possible regulatory factor in the proliferation of vascular smooth muscle cells
    • Lu KP, Chao SH, Wang DS 1989 Calmodulin: a possible regulatory factor in the proliferation of vascular smooth muscle cells. Chin Sci Bull 34:174-175
    • (1989) Chin Sci Bull , vol.34 , pp. 174-175
    • Lu, K.P.1    Chao, S.H.2    Wang, D.S.3
  • 84
    • 0017062914 scopus 로고
    • Calcium-dependent regulatory protein of cyclic nucleotide metabolism in normal and transformed chicken embryo fiblasts
    • Watterson DM, Van Eldik LJ, Smith RE, Vanaman TC 1976 Calcium-dependent regulatory protein of cyclic nucleotide metabolism in normal and transformed chicken embryo fiblasts. Proc Natl Acad Sci USA 73:2711-2715
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 2711-2715
    • Watterson, D.M.1    Van Eldik, L.J.2    Smith, R.E.3    Vanaman, T.C.4
  • 86
    • 0018390793 scopus 로고
    • Relationship between changes in the calcium dependent regulatory protein and adenylate cylase during viral transformation
    • LaPorte DC, Gidwitz S, Weber MJ, Storm DR 1979 Relationship between changes in the calcium dependent regulatory protein and adenylate cylase during viral transformation. Biochem Biophys Res Commun 86:1169-1173
    • (1979) Biochem Biophys Res Commun , vol.86 , pp. 1169-1173
    • Laporte, D.C.1    Gidwitz, S.2    Weber, M.J.3    Storm, D.R.4
  • 87
    • 0039489189 scopus 로고
    • Calciumdependent regulator protein: Localization in the mitotic spindle of eukaryotic cells
    • Welsh MJ, Dedman JR, Brinkley BR, Means AR 1978 Calciumdependent regulator protein: localization in the mitotic spindle of eukaryotic cells. Proc Natl Acad Sci USA 75:1867-1871
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 1867-1871
    • Welsh, M.J.1    Dedman, J.R.2    Brinkley, B.R.3    Means, A.R.4
  • 88
    • 0018746497 scopus 로고
    • Tubulin and calcium-dependent regulator protein: Effects of microtubule and microfilament inhibitors on localization in the mitotic apparatus
    • Welsh MJ, Dedman JR, Brinkley BR, Means AR 1979 Tubulin and calcium-dependent regulator protein: effects of microtubule and microfilament inhibitors on localization in the mitotic apparatus. J Cell Biol 81:624-634
    • (1979) J Cell Biol , vol.81 , pp. 624-634
    • Welsh, M.J.1    Dedman, J.R.2    Brinkley, B.R.3    Means, A.R.4
  • 89
    • 0021959299 scopus 로고
    • Induction of chromosome condensation in tsBN2, a temperature-sensitive mutant of BHK21, is inhibited by the calmodulin antagonist, W-7
    • Nishimoto T, Ajiro K, Hirata M, Yamashita K, Sekiguchi M 1985 Induction of chromosome condensation in tsBN2, a temperature-sensitive mutant of BHK21, is inhibited by the calmodulin antagonist, W-7. Exp Cell Res 156:351-358
    • (1985) Exp Cell Res , vol.156 , pp. 351-358
    • Nishimoto, T.1    Ajiro, K.2    Hirata, M.3    Yamashita, K.4    Sekiguchi, M.5
  • 90
    • 0020666378 scopus 로고
    • N-(6-Aminohexyl)-5chloro-l-naphthalenesulfonamide (W7), a calmodulin antagonist, also inhibits phospholipid-sensitive calcium-dependent protein kinase
    • Schatzman RC, Raynor RL, Kuo JF 1983 N-(6-Aminohexyl)-5chloro-l-naphthalenesulfonamide (W7), a calmodulin antagonist, also inhibits phospholipid-sensitive calcium-dependent protein kinase. Biochim Biophys Acta 755:144-147
    • (1983) Biochim Biophys Acta , vol.755 , pp. 144-147
    • Schatzman, R.C.1    Raynor, R.L.2    Kuo, J.F.3
  • 91
    • 0024443792 scopus 로고
    • Calmodulin, cell growth and gene expression
    • Rasmussen CD, Means AR 1989 Calmodulin, cell growth and gene expression. Trends Neurosci 12:433-438
    • (1989) Trends Neurosci , vol.12 , pp. 433-438
    • Rasmussen, C.D.1    Means, A.R.2
  • 93
    • 0022999043 scopus 로고
    • Calmodulin: Regulation of the cholinergic receptor in rat heart during ontogeny and senescence
    • Ho AK, Shang K, Duffield R 1986 Calmodulin: regulation of the cholinergic receptor in rat heart during ontogeny and senescence. Mech Ageing Dev 36:143-154
    • (1986) Mech Ageing Dev , vol.36 , pp. 143-154
    • Ho, A.K.1    Shang, K.2    Duffield, R.3
  • 95
    • 0023114145 scopus 로고
    • Multiple calmodulin mRNA species are derived from two distinct genes
    • Nojima H, Kishi K, Sokabe H 1987 Multiple calmodulin mRNA species are derived from two distinct genes. Mol Cell Biol 7:18731880
    • (1987) Mol Cell Biol , vol.1873-1880 , pp. 7
    • Nojima, H.1    Kishi, K.2    Sokabe, H.3
  • 97
    • 0024448762 scopus 로고
    • Analysis of expression of multiple genes encoding calmodulin during spermatogenesis
    • Slaughter GR, Means AR 1989 Analysis of expression of multiple genes encoding calmodulin during spermatogenesis. Mol Endocrinol 3:1569-1578
    • (1989) Mol Endocrinol , vol.3 , pp. 1569-1578
    • Slaughter, G.R.1    Means, A.R.2
  • 100
    • 0024313794 scopus 로고
    • Vertebrate and yeast calmodulin, despite significant sequence divergence, are functionally interchangeable
    • Davis TN, Thorner J 1989 Vertebrate and yeast calmodulin, despite significant sequence divergence, are functionally interchangeable. Proc Natl Acad Sci USA 86:7909-7913
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 7909-7913
    • Davis, T.N.1    Thorner, J.2
  • 101
    • 0023478561 scopus 로고
    • Yeast calmodulin: Structural and functional differences compared with vertebrate calmodulin
    • Luan Y, Matsuura I, Yazawa M, Nakamura T, Yagi K 1987 Yeast calmodulin: structural and functional differences compared with vertebrate calmodulin. J Biochem (Tokyo) 102:1531-1537
    • (1987) J Biochem (Tokyo) , vol.102 , pp. 1531-1537
    • Luan, Y.1    Matsuura, I.2    Yazawa, M.3    Nakamura, T.4    Yagi, K.5
  • 104
    • 0023429054 scopus 로고
    • Purification and biochemical properties of calmodulin from
    • Ohya Y, Uno I, Ishikawa T, Anraku Y 1987 Purification and biochemical properties of calmodulin from Saccharomyces cerevisiae. Eur J Biochem 168:13-19
    • (1987) Eur J Biochem , vol.168 , pp. 13-19
    • Ohya, Y.1    Uno, I.2    Ishikawa, T.3    Anraku, Y.4
  • 105
    • 0026518437 scopus 로고
    • Identification and molecular characterization of the calmodulin-binding subunit gene (CMP1) of protein phosphatase 2B from
    • Ye RR, Bretscher A 1992 Identification and molecular characterization of the calmodulin-binding subunit gene (CMP1) of protein phosphatase 2B from Saccharomyces cerevisiae: an a-factor inducible gene. Eur J Biochem 204:713-723
    • (1992) Eur J Biochem , vol.204 , pp. 713-723
    • Ye, R.R.1    Bretscher, A.2
  • 106
    • 0025768945 scopus 로고
    • Half-calmodulin is sufficient for cell proliferation: Expression of Nand C-terminal halves of calmodulin in the yeast
    • Sun GH, Ohya Y, Anraku Y 1991 Half-calmodulin is sufficient for cell proliferation: expression of Nand C-terminal halves of calmodulin in the yeast Saccharomyces cerevisiae. J Biol Chem 266:7008-7015
    • (1991) J Biol Chem , vol.266 , pp. 7008-7015
    • Sun, G.H.1    Ohya, Y.2    Anraku, Y.3
  • 107
    • 0026027633 scopus 로고
    • Calmodulins with deletions in the central helix functionally replace the native protein in yeast cells
    • Persechini A, Kretsinger RH, Davis TN 1991 Calmodulins with deletions in the central helix functionally replace the native protein in yeast cells. Proc Natl Acad Sci USA 88:449-452
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 449-452
    • Persechini, A.1    Kretsinger, R.H.2    Davis, T.N.3
  • 108
    • 0018967724 scopus 로고
    • Positive cooperative binding of calcium to bovine brain calmodulin
    • Crouch TH, Klee CB 1980 Positive cooperative binding of calcium to bovine brain calmodulin. Biochemistry 19:3692-3698
    • (1980) Biochemistry , vol.19 , pp. 3692-3698
    • Crouch, T.H.1    Klee, C.B.2
  • 109
    • 0019406008 scopus 로고
    • Effect of cations on affinity of calcium for calmodulin: Ordered binding of calcium ions allows the specific activation of calmodulin-stimulated enzyme
    • Haiech J, Klee CB, Demaille JG 1981 Effect of cations on affinity of calcium for calmodulin: ordered binding of calcium ions allows the specific activation of calmodulin-stimulated enzyme. Biochemistry 20:3890-3894
    • (1981) Biochemistry , vol.20 , pp. 3890-3894
    • Haiech, J.1    Klee, C.B.2    Demaille, J.G.3
  • 114
    • 0025745205 scopus 로고
    • In vivo regulation of granulosa cell type I insulin-like growth factor receptors: Evidence for an inhibitory role for the putative endogenous ligand(s) of the ovarian gonadotropin-releasing hormone receptor
    • Adashi EY, Resnick CE, Vera A, Hernandez E 1991 In vivo regulation of granulosa cell type I insulin-like growth factor receptors: evidence for an inhibitory role for the putative endogenous ligand(s) of the ovarian gonadotropin-releasing hormone receptor. Endocrinology 128:3130
    • (1991) Endocrinology , vol.128 , pp. 3130
    • Adashi, E.Y.1    Resnick, C.E.2    Vera, A.3    Hernandez, E.4
  • 116
    • 0025234725 scopus 로고
    • Calmodulin activation of target enzymes: Consequences of deletions in the central helix
    • VanBerkum MFA, George SE, Means AR 1990 Calmodulin activation of target enzymes: consequences of deletions in the central helix. J Biol Chem 265:3750-3756
    • (1990) J Biol Chem , vol.265 , pp. 3750-3756
    • Vanberkum, M.1    George, S.E.2    Means, A.R.3
  • 117
    • 0025854636 scopus 로고
    • Restoration of the calcium binding activity of mutant calmodulins toward normal by the presence of a calmodulin binding structure
    • Haiech J, Kilhoffer MC, Lukas TJ, Craig TA, Watterson DW 1991 Restoration of the calcium binding activity of mutant calmodulins toward normal by the presence of a calmodulin binding structure. J Biol Chem 266:3427-3431
    • (1991) J Biol Chem , vol.266 , pp. 3427-3431
    • Haiech, J.1    Kilhoffer, M.C.2    Lukas, T.J.3    Craig, T.A.4    Watterson, D.W.5
  • 118
    • 0020630774 scopus 로고
    • Calcium transport driven by a proton motive force in vacuolar membrane vesicles of
    • Ohsumi Y, Anraku Y 1983 Calcium transport driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae. J Biol Chem 258:5614-5617
    • (1983) J Biol Chem , vol.258 , pp. 5614-5617
    • Ohsumi, Y.1    Anraku, Y.2
  • 119
    • 0025762643 scopus 로고
    • Rose MD, Vallen EA 1991 Acid loops fail the acid test. Cell 65:919-920
    • (1991) Cell , vol.65 , pp. 919-920
    • Rose, M.D.1    Vallen, E.A.2
  • 121
    • 0024555855 scopus 로고    scopus 로고
    • Functional expression of chicken calmodulin in yeast
    • Ohya Y, Anraku Y 1989 Functional expression of chicken calmodulin in yeast. Biochem Biophys Res Commun 158:541-547
    • Biochem Biophys Res Commun
    • Ohya, Y.1    Anraku, Y.2
  • 124
    • 0025836296 scopus 로고
    • Two yeast genes encoding calmodulin-dependent protein kinases: Isolation, sequencing and bacterial expressions of CMK1 and CMK2
    • Ohya Y, Kawasaki H, Suzuki K, Londesborough J, Anraku Y 1991 Two yeast genes encoding calmodulin-dependent protein kinases: isolation, sequencing and bacterial expressions of CMK1 and CMK2. J Biol Chem 266:12784-12794
    • (1991) J Biol Chem , vol.266 , pp. 12784-12794
    • Ohya, Y.1    Kawasaki, H.2    Suzuki, K.3    Londesborough, J.4    Anraku, Y.5
  • 125
    • 0025882163 scopus 로고
    • Multiple Ca2+/calmodulin-dependent protein kinase genes in a unicellular eukaryote
    • Pausch MH, Kaim D, Kunisawa R, Admon A, Thorner J 1991 Multiple Ca2+/calmodulin-dependent protein kinase genes in a unicellular eukaryote. EMBO J 10:1511-1522
    • (1991) EMBO J , vol.10 , pp. 1511-1522
    • Pausch, M.H.1    Kaim, D.2    Kunisawa, R.3    Admon, A.4    Thorner, J.5
  • 126
    • 0025913953 scopus 로고
    • Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase
    • Cyert MS, Kunisawa R, Kaim D, Thorner J 1991 Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase. Proc Natl Acad Sci USA 88:7376-7380
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7376-7380
    • Cyert, M.S.1    Kunisawa, R.2    Kaim, D.3    Thorner, J.4
  • 131
    • 0024834127 scopus 로고
    • An essential G1 function for cyclin-like proteins in yeast
    • Richardson HE, Wittenberg C, Cross F, Reed SI 1989 An essential G1 function for cyclin-like proteins in yeast. Cell 59:1127-1133
    • (1989) Cell , vol.59 , pp. 1127-1133
    • Richardson, H.E.1    Wittenberg, C.2    Cross, F.3    Reed, S.I.4
  • 132
    • 0024835839 scopus 로고    scopus 로고
    • Substitution at position
    • Takeda T, Imai Y, Yamamoto M 1989 Substitution at position 116 of Schizosaccharomyces pombe calmodulin decreases its stability under nitrogen starvation and results in a sporulation-deficient phenotype. Proc Natl Acad Sci USA 86:9737-9741
    • Proc Natl Acad Sci USA
    • Takeda, T.1    Imai, Y.2    Yamamoto, M.3
  • 133
    • 0021790702 scopus 로고
    • Specific recognition of calmodulin from
    • Gregori L, Marriott D, West CM, Chau V 1985 Specific recognition of calmodulin from Dictyostelium discoideum by the ATP, ubiquitin-dependent degradative pathway. J Biol Chem 260:52325235
    • (1985) J Biol Chem , vol.5232-5235 , pp. 260
    • Gregori, L.1    Marriott, D.2    West, C.M.3    Chau, V.4
  • 134
    • 0023217988 scopus 로고
    • Bacterially synthesized vertebrate calmodulin is a specific substrate for ubiquitination
    • Gregori L, Marriott D, Putkey JA, Means AR, Chau V 1987 Bacterially synthesized vertebrate calmodulin is a specific substrate for ubiquitination. J Biol Chem 262:2562-2567
    • (1987) J Biol Chem , vol.262 , pp. 2562-2567
    • Gregori, L.1    Marriott, D.2    Putkey, J.A.3    Means, A.R.4    Chau, V.5
  • 135
    • 85003156487 scopus 로고
    • The genetics of
    • Smith JE, Patemen JA, Academic Press Inc, New York
    • Cove DJ 1977 The genetics of Aspergillus nidulans. In: Smith JE, Patemen JA (eds) The Genetics and Physiology of Aspergillus nidulans. Academic Press Inc, New York, pp 81-95
    • (1993) The Genetics and Physiology Of , pp. 81-95
    • Cove, D.J.1
  • 136
    • 0024361083 scopus 로고
    • Genetic engineering of filamentous fungi
    • Timberlake WE, Marshall MA 1989 Genetic engineering of filamentous fungi. Science 244:1313-1317
    • (1989) Science , vol.244 , pp. 1313-1317
    • Timberlake, W.E.1    Marshall, M.A.2
  • 137
    • 0024390791 scopus 로고
    • Characterization of an inducible expression system in
    • Waring RB, May GS, Morris NR 1989 Characterization of an inducible expression system in Aspergillus nidulans using alcA and tubulin coding genes. Gene 79:119-130
    • (1989) Gene , vol.79 , pp. 119-130
    • Waring, R.B.1    May, G.S.2    Morris, N.R.3
  • 139
    • 0021086457 scopus 로고
    • Kinetics of the nuclear division cycle of
    • Bergen LG, Morris NR 1983 Kinetics of the nuclear division cycle of Aspergillus nidulans. J Bacteriol 156:155-160
    • (1983) J Bacteriol , vol.156 , pp. 155-160
    • Bergen, L.G.1    Morris, N.R.2
  • 140
    • 0016789438 scopus 로고
    • Mitotic mutants of
    • Morris NR 1976 Mitotic mutants of Aspergillus nidulans. Genet Res 26:237-254
    • (1976) Genet Res , vol.26 , pp. 237-254
    • Morris, N.R.1
  • 141
    • 0343967482 scopus 로고
    • Activation of the cell cycle regulated NIMA protein kinase at G
    • Lu KP, Osmani SA, Means AR 1991 Activation of the cell cycle regulated NIMA protein kinase at G2 required calcium/calmodulin. J Cell Biol 115:426 (Abstract)
    • (1991) J Cell Biol , vol.115 , pp. 426
    • Lu, K.P.1    Osmani, S.A.2    Means, A.R.3
  • 142
    • 0020961333 scopus 로고
    • Cyclin: A protein specified maternal mRNA in sea urchin eggs that is destroyed at each cleavage division
    • Evans TE, Rosenthal J, Youngbloom K, Distel K, Hunt T 1983 Cyclin: a protein specified maternal mRNA in sea urchin eggs that is destroyed at each cleavage division. Cell 33:389-396
    • (1983) Cell , vol.33 , pp. 389-396
    • Evans, T.E.1    Rosenthal, J.2    Youngbloom, K.3    Distel, K.4    Hunt, T.5
  • 143
    • 0022915860 scopus 로고
    • The clam embryo protein cyclin A induces entry into M and the resumption of meiosis
    • Swenson KI, Farell KM, Ruderman JV 1986 The clam embryo protein cyclin A induces entry into M and the resumption of meiosis. Cell 47:861-870
    • (1986) Cell , vol.47 , pp. 861-870
    • Swenson, K.I.1    Farell, K.M.2    Ruderman, J.V.3
  • 144
    • 0024978344 scopus 로고
    • The role of cyclin synthesis and degradation in the control of maturation promoting factor activity
    • Murray AW, Solomon MJ, Kirschner MW 1989 The role of cyclin synthesis and degradation in the control of maturation promoting factor activity. Nature 339:280-286
    • (1989) Nature , vol.339 , pp. 280-286
    • Murray, A.W.1    Solomon, M.J.2    Kirschner, M.W.3
  • 145
    • 0026551634 scopus 로고
    • Cooperative regulation of cell proliferation by calcium and calmodulin in As
    • Lu KP, Rasmussen CD, May GS, Means AR 1992 Cooperative regulation of cell proliferation by calcium and calmodulin in Aspergillus nidulans. Mol Endocrinol 6:365-374
    • (1992) Mol Endocrinol , vol.6 , pp. 365-374
    • Lu, K.P.1    Rasmussen, C.D.2    May, G.S.3    Means, A.R.4
  • 146
    • 0019182299 scopus 로고
    • Activation of skeletal muscle myosin light chain kinase by calcium and calmodulin
    • Blumenthal DK, Stull JT 1980 Activation of skeletal muscle myosin light chain kinase by calcium and calmodulin. Biochemistry 19:5608-5614
    • (1980) Biochemistry , vol.19 , pp. 5608-5614
    • Blumenthal, D.K.1    Stull, J.T.2
  • 147
    • 0025861473 scopus 로고
    • Activation of the
    • Osmani AH, O’Donnell K, Pu RT, Osmani SA 1991 Activation of the nimA protein kinase plays a unique role during mitosis that cannot be bypassed by absence of the bimE checkpoint. EMBO J 10:2669-2679
    • (1991) EMBO J , vol.10 , pp. 2669-2679
    • Osmani, A.H.1    O’donnell, K.2    Pu, R.T.3    Osmani, S.A.4
  • 148
    • 0020383408 scopus 로고
    • Functionally homologous cell cycle control genes in budding and fission yeast
    • Beach D, Durkacz B, Nurse P 1982 Functionally homologous cell cycle control genes in budding and fission yeast. Nature 300:706709
    • (1982) Nature , vol.706-709 , pp. 300
    • Beach, D.1    Durkacz, B.2    Nurse, P.3
  • 149
    • 0023647143 scopus 로고
    • Complementation used to clone a human homologue of the fission yeast cell cycle control gene
    • Lee MG, Nurse P 1987 Complementation used to clone a human homologue of the fission yeast cell cycle control gene cdc2. Nature 327:31-35
    • (1987) Nature , vol.327 , pp. 31-35
    • Lee, M.G.1    Nurse, P.2
  • 150
    • 0025246110 scopus 로고
    • Universal control mechanism regulating onset of Mphase
    • Nurse P 1990 Universal control mechanism regulating onset of Mphase. Nature 344:503-508
    • (1990) Nature , vol.344 , pp. 503-508
    • Nurse, P.1
  • 151
    • 0025281829 scopus 로고
    • Driving the cell cycle: M protein kinase, its partners, and substrates
    • Lewin B 1990 Driving the cell cycle: M protein kinase, its partners, and substrates. Cell 61:743-752
    • (1990) Cell , vol.61 , pp. 743-752
    • Lewin, B.1
  • 153
    • 0021749901 scopus 로고
    • Sequence of the ell division gene cdc2+ from
    • Hindley J, Phear GA 1984 Sequence of the ell division gene cdc2+ from Schizosaccharmyces prombe: patterns of splicing and homology to protein kinase. Gene 31:129-134
    • (1984) Gene , vol.31 , pp. 129-134
    • Hindley, J.1    Phear, G.A.2
  • 154
    • 0022542621 scopus 로고
    • The cell cycle control gene cdc2+ of fission yeast encodes a protein kinase potentially regulated by phosphorylation
    • Simanis V, Nurse PM 1986 The cell cycle control gene cdc2+ of fission yeast encodes a protein kinase potentially regulated by phosphorylation. Cell 45:261-268
    • (1986) Cell , vol.45 , pp. 261-268
    • Simanis, V.1    Nurse, P.M.2
  • 155
    • 0023735159 scopus 로고
    • Activation of cdc2 protein kinase during mitosis in human cells: Cell cycle dpendent phosphorylation and subunit rearrangement
    • Draetta G, Beach D 1988 Activation of cdc2 protein kinase during mitosis in human cells: cell cycle dpendent phosphorylation and subunit rearrangement. Cell 54:17-26
    • (1988) Cell , vol.54 , pp. 17-26
    • Draetta, G.1    Beach, D.2
  • 156
    • 0024294002 scopus 로고
    • 1988 cdc2 is a component of the M phase-specific histone HI kinase: Evidence for identity withMPF
    • Arion D, Meijer L, Brizuela L, Beach D 1988 cdc2 is a component of the M phase-specific histone HI kinase: evidence for identity withMPF. Cell 55:317-318
    • (1993) Cell , vol.55 , pp. 317-318
    • Arion, D.1    Meijer, L.2    Brizuela, L.3
  • 157
    • 0024299475 scopus 로고
    • Purified maturation-promoting factor contains the product of a
    • Gautier J, Norbury C, Lorbury C, Nurse PM, Maller J 1988 Purified maturation-promoting factor contains the product of a Xenopus homolog of fission yeast cell cycle control gene cdc2+. Cell 54:433-439
    • (1988) Cell , vol.54 , pp. 433-439
    • Gautier, J.1    Norbury, C.2    Lorbury, C.3    Nurse, P.M.4    Maller, J.5
  • 159
    • 0025745205 scopus 로고
    • In vivo regulation of granulosa cell type I insulin-like growth factor receptors: Evidence for an inhibitory role for the putative endogenous ligand(s) of the ovarian gonadotropin-releasing hormone receptor
    • Adashi EY, Resnick CE, Vera A, Hernandez E 1991 In vivo regulation of granulosa cell type I insulin-like growth factor receptors: Evidence for an inhibitory role for the putative endogenous ligand(s) of the ovarian gonadotropin-releasing hormone receptor. Endocrinology 128:3130
    • (1991) Endocrinology , vol.128 , pp. 3130
    • Adashi, E.Y.1    Resnick, C.E.2    Vera, A.3    Hernandez, E.4
  • 160
    • 0024470772 scopus 로고
    • Beach D Cyclin is a component of the sea urchin egg M-phase specific histone HI kinase
    • Meijer L, Arion D, Golsteyn R, Brizuela L, Hunt T, Beach D Cyclin is a component of the sea urchin egg M-phase specific histone HI kinase. EMBO J 8:2275-2282
    • (1993) EMBO J , vol.8 , pp. 2275-2282
    • Meijer, L.1    Arion, D.2    Golsteyn, R.3    Brizuela, L.4    Hunt, T.5
  • 162
    • 0024349663 scopus 로고
    • The fission yeast cdc2/cdcl3/sucl protein kinase: Regulation of catalytic activity and nuclear localization
    • Booher RN, Alfa CE, Hyams JS, Beach D 1989 The fission yeast cdc2/cdcl3/sucl protein kinase: regulation of catalytic activity and nuclear localization. Cell 58:485-497
    • (1989) Cell , vol.58 , pp. 485-497
    • Booher, R.N.1    Alfa, C.E.2    Hyams, J.S.3    Beach, D.4
  • 163
    • 0348217634 scopus 로고
    • Activation of human cdc2 protein as a histone HI kinase is associated with complex formation with the p62 subunit
    • Brizuela L, Draetta G, Beach D 1989 Activation of human cdc2 protein as a histone HI kinase is associated with complex formation with the p62 subunit. Proc Natl Acad Sci USA 86:4362-4366
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 4362-4366
    • Brizuela, L.1    Draetta, G.2    Beach, D.3
  • 168
    • 0025885070 scopus 로고
    • Isolation of the human
    • Tsai LH, Harlow E, Meyerson M 1991 Isolation of the human cdk2 gene that encodes the cyclin Aand adenovirus ElA-associated p33 kinase. Nature 353:174-177
    • (1991) Nature , vol.353 , pp. 174-177
    • Tsai, L.H.1    Harlow, E.2    Meyerson, M.3
  • 169
    • 0025831974 scopus 로고
    • Evidence that the Gl-S and G2-M transitions are controlled by different cdc2 proteins in higher eukaryotes
    • Fang F, Newport JW 1991 Evidence that the Gl-S and G2-M transitions are controlled by different cdc2 proteins in higher eukaryotes. Cell 66:731-742
    • (1991) Cell , vol.66 , pp. 731-742
    • Fang, F.1    Newport, J.W.2
  • 170
    • 0025893161 scopus 로고
    • Cell cycle regulation of the E2F transcription factor involves an interation with cyclin A
    • Mudryj M, Devoto SH, Hiebert SW, Hunter T, Pines J, Nevins JR 1991 Cell cycle regulation of the E2F transcription factor involves an interation with cyclin A. Cell 65:1243-1253
    • (1991) Cell , vol.65 , pp. 1243-1253
    • Mudryj, M.1    Devoto, S.H.2    Hiebert, S.W.3    Hunter, T.4    Pines, J.5    Nevins, J.R.6
  • 171
    • 0025894942 scopus 로고
    • A new human p34 protein kinase, CDK2, identified by complementation of a
    • Elledge SJ, Spottswood MR 1991 A new human p34 protein kinase, CDK2, identified by complementation of a cdc28 mutation in Saccharomyces cerevisiae, is a homolog of Xenopus Egl. EMBO J 10:2653-2659
    • (1991) EMBO J , vol.10 , pp. 2653-2659
    • Elledge, S.J.1    Spottswood, M.R.2
  • 172
    • 0024978338 scopus 로고
    • Cyclin synthesis drives the early embryonic cell cycle
    • Murray AW, Kirschner MW 1989 Cyclin synthesis drives the early embryonic cell cycle. Nature 339:275-286
    • (1989) Nature , vol.339 , pp. 275-286
    • Murray, A.W.1    Kirschner, M.W.2
  • 173
    • 0024959919 scopus 로고
    • Tyrosine phosphorylation of the fission yeast
    • Gould KL, Nurse P 1989 Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis. Nature 342:39-45
    • (1989) Nature , vol.342 , pp. 39-45
    • Gould, K.L.1    Nurse, P.2
  • 174
    • 0025821565 scopus 로고
    • cdc2 for tyrosine phosphorylation
    • cdc2 for tyrosine phosphorylation. EMBO J 10:1545-1554
    • (1991) EMBO J , vol.10 , pp. 1545-1554
    • Meijer, L.1    Azzi, L.2    Wang, J.3
  • 176
    • 0025924328 scopus 로고
    • weel mitotic inhibitor is a tyrosine/serine kinase
    • weel mitotic inhibitor is a tyrosine/serine kinase. Nature 349:808-811
    • (1991) Nature , vol.349 , pp. 808-811
    • Featherstone, C.1    Russel, P.2
  • 177
    • 0026035524 scopus 로고
    • 1991 mikl and weel cooperate in the inhibitory tyrosine phosphorylation of cdc2
    • Lundgren K, Walworth N, Booher R, Dembski M, Kirschner MW, Beach D 1991 mikl and weel cooperate in the inhibitory tyrosine phosphorylation of cdc2. Cell 64:1111-1122
    • (1993) Cell , vol.64 , pp. 1111-1122
    • Lundgren, K.1    Walworth, N.2    Booher, R.3    Dembski, M.4    Kirschner, M.W.5
  • 178
    • 0026319225 scopus 로고
    • Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: Evidence for multiple roles of mitotic cyclins
    • Galaktionov K, Beach D 1991 Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins. Cell 67:1181-1194
    • (1991) Cell , vol.67 , pp. 1181-1194
    • Galaktionov, K.1    Beach, D.2
  • 179
    • 0026719599 scopus 로고
    • Regulation of the cdc25 protein during the cell cycle in
    • Kumagai A, Dunphy WG 1992 Regulation of the cdc25 protein during the cell cycle in Xenopus extracts. Cell 70:139-151
    • (1992) Cell , vol.70 , pp. 139-151
    • Kumagai, A.1    Dunphy, W.G.2
  • 180
    • 0024390591 scopus 로고
    • Reversible tyrosine phosphorylation of cdc2: Dephosphorylation accompanies activation entry into mitosis
    • Morla AO, Draetta G, Beach D, Wang JYJ 1989 Reversible tyrosine phosphorylation of cdc2: dephosphorylation accompanies activation entry into mitosis. Cell 58:193-203
    • (1989) Cell , vol.58 , pp. 193-203
    • Morla, A.O.1    Draetta, G.2    Beach, D.3    Wang, J.4
  • 181
    • 0024395110 scopus 로고
    • Fission yeast pl3 blocks mitotic activation and tyrosine dephosphorylation of the Xenopus
    • Dunphy WG, Newport JW 1989 Fission yeast pl3 blocks mitotic activation and tyrosine dephosphorylation of the Xenopus cdc2 protein kinase. Cell 58:181-191
    • (1989) Cell , vol.58 , pp. 181-191
    • Dunphy, W.G.1    Newport, J.W.2
  • 184
  • 185
    • 0026006392 scopus 로고
    • Mutations of p34
    • cdc2 kinase activation in vertebrates. EMBO J 10:33313341
    • (1991) EMBO J , vol.3331-3341 , pp. 10
    • Krek, W.1    Nigg, E.A.2
  • 186
    • 0026027660 scopus 로고
    • Differential phosphorylation of vertebrate p34
    • cdc2 kinase at the Gl/S and G2/M transitions of the cell cycle: identification of major phosphorylation sites. EMBO J 10:305-316
    • (1991) EMBO J , vol.10 , pp. 305-316
    • Krek, W.1    Nigg, E.A.2
  • 187
    • 0026569665 scopus 로고
    • The cdc25 M-phase inducer: An unconventional protein phosphatase
    • Millar JBA, Russel P 1992 The cdc25 M-phase inducer: an unconventional protein phosphatase. Cell 68:407-410
    • (1992) Cell , vol.68 , pp. 407-410
    • Millar, J.1    Russel, P.2
  • 189
    • 0026070261 scopus 로고
    • Phosphorylation at Thrl67 is required for
    • Gould KL, Moreno S, Owen DJ, Sazer S, Nurse P 1991 Phosphorylation at Thrl67 is required for Schizosaccharomyces pombe p34 function. EMBO J 10:3297-3309
    • (1991) EMBO J , vol.10 , pp. 3297-3309
    • Gould, K.L.1    Moreno, S.2    Owen, D.J.3    Sazer, S.4    Nurse, P.5
  • 191
    • 0026048594 scopus 로고
    • Parallel activation of the NIMA and p34
    • cdc2 cell cycle-regulated protein kinases is required to initiate mitosis in A. nidulans. Cell 67:283-291
    • (1991) Cell , vol.67 , pp. 283-291
    • Osmani, A.H.1    McGuire, S.L.2    Osmani, S.A.3
  • 192
    • 0023238668 scopus 로고
    • Regulation of the mRNA level of nimA, a gene required for the G2-M transition in
    • Osmani SA, May GS, Morris NR 1987 Regulation of the mRNA level of nimA, a gene required for the G2-M transition in Aspergillus nidulans. J Cell Biol 104:1495-1504
    • (1987) J Cell Biol , vol.104 , pp. 1495-1504
    • Osmani, S.A.1    May, G.S.2    Morris, N.R.3
  • 193
    • 0024294395 scopus 로고
    • Mitotic induction and maintenance by overexpression of a G2-specific gene that encodes a potential protein kinase
    • Osmani SA, Pu RT, Morris NR 1988 Mitotic induction and maintenance by overexpression of a G2-specific gene that encodes a potential protein kinase. Cell 53:237-244
    • (1988) Cell , vol.53 , pp. 237-244
    • Osmani, S.A.1    Pu, R.T.2    Morris, N.R.3
  • 194
    • 0025058599 scopus 로고
    • Cdc2 HI kinase is negatively regulated by a type 2A phosphatase in the
    • Felix MA, Cohen P, Karsenti E 1990 Cdc2 HI kinase is negatively regulated by a type 2A phosphatase in the Xenopus early embryonic cell cycle: evidence from the effects of okadaic acid. EMBO J 9:675-683
    • (1990) EMBO J , vol.9 , pp. 675-683
    • Felix, M.A.1    Cohen, P.2    Karsenti, E.3
  • 195
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzer M, Murray AW, Kirschner MW 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
  • 198
    • 0343203330 scopus 로고
    • Mitosis specific monoclonal antibody MPM-2 inhibits Xenopus oocyte maturation and depletes maturation promoting activity
    • Kuang J, Zhao J-Y, Wright DA, Saunders GF, Rao PN 1989 Mitosis specific monoclonal antibody MPM-2 inhibits Xenopus oocyte maturation and depletes maturation promoting activity. Proc Natl Acad Sci USA 86:4982-4986
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 4982-4986
    • Kuang, J.1    Zhao, J.-Y.2    Wright, D.A.3    Saunders, G.F.4    Rao, P.N.5
  • 200
    • 0026554801 scopus 로고
    • Cloning and sequence determination of a cDNA encoding
    • Kornstein LB, Gaiso ML, Hammell RL, Bartelt DC 1992 Cloning and sequence determination of a cDNA encoding Aspergillus nidulans calmodulin-dependent multifunctional protein kinase. Gene 113:75-82
    • (1992) Gene , vol.113 , pp. 75-82
    • Kornstein, L.B.1    Gaiso, M.L.2    Hammell, R.L.3    Bartelt, D.C.4
  • 201
    • 0025980359 scopus 로고
    • The cdc25 protein controls tyrosine dephosphorylation of the cdc
    • Kumagai A, Dunphy WG 1991 The cdc25 protein controls tyrosine dephosphorylation of the cdc2 protein in a cell-free system. Cell 64:903-914
    • (1991) Cell , vol.64 , pp. 903-914
    • Kumagai, A.1    Dunphy, W.G.2
  • 204
    • 0026569334 scopus 로고
    • Expression of a constituitive form of Ca
    • +/calmodulin-dependent protein kinase II leads to G2 arrest. EMBO J 11:507-517
    • (1992) EMBO J , vol.11 , pp. 507-517
    • Planas-Silva, M.D.1    Means, A.R.2
  • 206
    • 0017760162 scopus 로고
    • Ca and Mg control of cytostatic factors from
    • Meyerhof PG, Masui Y 1977 Ca and Mg control of cytostatic factors from Rana pipiens oocytes which cause metaphase and cleavage arrest. Dev Biol 61:214-229
    • (1977) Dev Biol , vol.61 , pp. 214-229
    • Meyerhof, P.G.1    Masui, Y.2
  • 207
    • 0023747302 scopus 로고
    • Stabilization and enhancement of primary cytostatic factor (CSF) by ATP and NaF in amphibian egg cytosols
    • Shibuya EK, Masui Y 1988 Stabilization and enhancement of primary cytostatic factor (CSF) by ATP and NaF in amphibian egg cytosols. Dev Biol 129:253-264
    • (1988) Dev Biol , vol.129 , pp. 253-264
    • Shibuya, E.K.1    Masui, Y.2
  • 208
    • 0024313534 scopus 로고
    • The c
    • Sagata N, Watanabe N, Vande Woude GF, Ikawa Y 1989 The cmos proto-oncogene product is a cytostatic factor responsible for meiotic arrest in vertebrate eggs. Nature 342:512-518
    • (1989) Nature , vol.342 , pp. 512-518
    • Sagata, N.1    Watanabe, N.2    Vande Woude, G.F.3    Ikawa, Y.4
  • 209
    • 0024326801 scopus 로고
    • Specific proteolysis of the c
    • Watanabe N, Vande Woude GF, Ikawa Y, Sagata N 1989 Specific proteolysis of the c-mos proto-oncogene product by calpain on fertilization of Xenopus eggs. Nature 342:505-511
    • (1989) Nature , vol.342 , pp. 505-511
    • Watanabe, N.1    Vande Woude, G.F.2    Ikawa, Y.3    Sagata, N.4
  • 210
    • 0019758643 scopus 로고
    • Induction of its activation potential by an increase in intracellular calcium in eggs of the frog
    • Cross NL 1981 Induction of its activation potential by an increase in intracellular calcium in eggs of the frog Rana pipiens. Dev Biol 85:380-384
    • (1981) Dev Biol , vol.85 , pp. 380-384
    • Cross, N.L.1
  • 211
    • 85003158611 scopus 로고
    • Elemental composition of the pervitelline fluid in early
    • Jaffe LF 1983 Elemental composition of the pervitelline fluid in early Drosophila embryos. Dev Biol 95: 265-276
    • (1983) Dev Biol , vol.95 , pp. 265-276
    • Jaffe, L.F.1
  • 212
    • 0021960243 scopus 로고
    • 2+ wave follows fertilization in eggs of the frog
    • 2+ wave follows fertilization in eggs of the frog Xenopus laevis. J Cell Biol 100:1325-1329
    • (1985) J Cell Biol , vol.100 , pp. 1325-1329
    • Busa, W.B.1    Nucitelli, R.2
  • 215


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.