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1
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0030447434
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Polo kinase: The choreographer of the mitotic stage?
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Glover DM, Ohkura H, Tavares A. Polo kinase: the choreographer of the mitotic stage? J Cell Biol. 135:1996;1681-1684.
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J Cell Biol
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Glover, D.M.1
Ohkura, H.2
Tavares, A.3
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2
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0031081209
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Cell-cycle control: Polo-like kinases join the outer circle
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Lane HA, Nigg EA. Cell-cycle control: polo-like kinases join the outer circle. Trends Cell Biol. 7:1997;63-68.
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Trends Cell Biol
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Lane, H.A.1
Nigg, E.A.2
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3
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0023804548
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Polo, a mitotic mutant of Drosophila displaying abnormal spindle poles
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Sunkel CE, Glover DM. polo, a mitotic mutant of Drosophila displaying abnormal spindle poles. J Cell Sci. 89:1988;25-38.
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(1988)
J Cell Sci
, vol.89
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Sunkel, C.E.1
Glover, D.M.2
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4
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0026665462
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Identification of an early-growth-response gene encoding a novel putative protein kinase
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Simmons DL, Neel BG, Stevens R, Evett G, Erikson RL. Identification of an early-growth-response gene encoding a novel putative protein kinase. Mol Cell Biol. 12:1992;4164-4169.
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(1992)
Mol Cell Biol
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Simmons, D.L.1
Neel, B.G.2
Stevens, R.3
Evett, G.4
Erikson, R.L.5
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5
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0028960192
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Identification by targeted differential display of an immediate early gene encoding a putative serine/threonine kinase
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Donohue PJ, Alberts GF, Guo Y, Winkles JA. Identification by targeted differential display of an immediate early gene encoding a putative serine/threonine kinase. J Biol Chem. 270:1995;10351-10357.
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J Biol Chem
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Donohue, P.J.1
Alberts, G.F.2
Guo, Y.3
Winkles, J.A.4
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6
-
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0029770725
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Prk, a cytokine-inducible human protein serine/threonine kinase whose expression appears to be down-regulated in lung carcinomas
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Li B, Ouyang B, Pan H, Reissmann PT, Slamon DJ, Arceci R, Lu L, Dai W. Prk, a cytokine-inducible human protein serine/threonine kinase whose expression appears to be down-regulated in lung carcinomas. J Biol Chem. 271:1996;19402-19408.
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(1996)
J Biol Chem
, vol.271
, pp. 19402-19408
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Li, B.1
Ouyang, B.2
Pan, H.3
Reissmann, P.T.4
Slamon, D.J.5
Arceci, R.6
Lu, L.7
Dai, W.8
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7
-
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0032144088
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Expression and phosphorylation of fibroblast-growth-factor-inducible kinase (Fnk) during cell-cycle progression
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of special interest. The fibroblast-growth-factor-inducible kinase (Fnk) protein is shown to be present in quiescent cells, and to fluctuate moderately as cells progress through the cell cycle, reaching a peak in M phase. Interestingly, Fnk is phosphorylated both during M phase, concomitant with its increased activity, and subsequent to stimulation of cells with mitogenic growth factors. The authors speculate that Fnk may function during mitosis as well as upon entry of cells into the cell cycle. See also annotation to [8].
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Chase D, Feng Y, Hanshew B, Winkles JA, Longo DL, Ferris DK. Expression and phosphorylation of fibroblast-growth-factor-inducible kinase (Fnk) during cell-cycle progression. of special interest Biochem J. 333:1998;655-660 The fibroblast-growth-factor-inducible kinase (Fnk) protein is shown to be present in quiescent cells, and to fluctuate moderately as cells progress through the cell cycle, reaching a peak in M phase. Interestingly, Fnk is phosphorylated both during M phase, concomitant with its increased activity, and subsequent to stimulation of cells with mitogenic growth factors. The authors speculate that Fnk may function during mitosis as well as upon entry of cells into the cell cycle. See also annotation to [8].
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(1998)
Biochem J
, vol.333
, pp. 655-660
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Chase, D.1
Feng, Y.2
Hanshew, B.3
Winkles, J.A.4
Longo, D.L.5
Ferris, D.K.6
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8
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0030695943
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Human Prk is a conserved protein serine/threonine kinase involved in regulating M phase functions
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2. On the basis of in vitro phosphorylation data and antisense experiments performed with Xenopus oocytes, the authors propose that Prk may activate Cdc25C, but the use of heterologous probes makes the latter experiments difficult to interpret. See also annotations to [7,9].
-
2. On the basis of in vitro phosphorylation data and antisense experiments performed with Xenopus oocytes, the authors propose that Prk may activate Cdc25C, but the use of heterologous probes makes the latter experiments difficult to interpret. See also annotations to [7,9].
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(1997)
J Biol Chem
, vol.272
, pp. 28646-28651
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Ouyang, B.1
Pan, H.2
Lu, L.3
Li, J.4
Stambrook, P.5
Li, B.6
Dai, W.7
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9
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0030924977
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Plk is a functional homolog of Saccharomyces cerevisiae Cdc5, and elevated Plk activity induces multiple septation structures
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of special interest. A cdc5 ts mutant is complemented by murine polo-like kinase (Plk1), emphasizing the functional similarity between these kinases. In addition, replacement of Thr 210 by an acidic residue (aspartic acid) is shown to enhance Plk1 activity, suggesting that Thr 210 may be a site for activating phosphorylation events. Finally, overexpression of hyperactive Plk1 in budding yeast results in the deposition of multiple septation structures, consistent with the idea that Plks may play a role in cytokinesis. See also annotation to [8].
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Lee KS, Erikson RL. Plk is a functional homolog of Saccharomyces cerevisiae Cdc5, and elevated Plk activity induces multiple septation structures. of special interest Mol Cell Biol. 17:1997;3408-3417 A cdc5 ts mutant is complemented by murine polo-like kinase (Plk1), emphasizing the functional similarity between these kinases. In addition, replacement of Thr 210 by an acidic residue (aspartic acid) is shown to enhance Plk1 activity, suggesting that Thr 210 may be a site for activating phosphorylation events. Finally, overexpression of hyperactive Plk1 in budding yeast results in the deposition of multiple septation structures, consistent with the idea that Plks may play a role in cytokinesis. See also annotation to [8].
-
(1997)
Mol Cell Biol
, vol.17
, pp. 3408-3417
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Lee, K.S.1
Erikson, R.L.2
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10
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0029079267
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Cell cycle regulation of the activity and subcellular localization of Plk1, a human protein kinase implicated in mitotic spindle function
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Golsteyn RM, Mundt KE, Fry AM, Nigg EA. Cell cycle regulation of the activity and subcellular localization of Plk1, a human protein kinase implicated in mitotic spindle function. J Cell Biol. 129:1995;1617-1628.
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(1995)
J Cell Biol
, vol.129
, pp. 1617-1628
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Golsteyn, R.M.1
Mundt, K.E.2
Fry, A.M.3
Nigg, E.A.4
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11
-
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0029134127
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Polo-like kinase is a cell cycle-regulated kinase activated during mitosis
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Hamanaka R, Smith MR, O'Connor PM, Maloid S, Mihalic K, Spivak JL, Longo DL, Ferris DK. Polo-like kinase is a cell cycle-regulated kinase activated during mitosis. J Biol Chem. 270:1995;21086-21091.
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(1995)
J Biol Chem
, vol.270
, pp. 21086-21091
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-
Hamanaka, R.1
Smith, M.R.2
O'Connor, P.M.3
Maloid, S.4
Mihalic, K.5
Spivak, J.L.6
Longo, D.L.7
Ferris, D.K.8
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12
-
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0028884602
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Plk is an M-phase-specific protein kinase and interacts with a kinesin- like protein, CHO1/MKLP-1
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Lee KS, Yuan YL, Kuriyama R, Erikson RL. Plk is an M-phase-specific protein kinase and interacts with a kinesin- like protein, CHO1/MKLP-1. Mol Cell Biol. 15:1995;7143-7151.
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(1995)
Mol Cell Biol
, vol.15
, pp. 7143-7151
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Lee, K.S.1
Yuan, Y.L.2
Kuriyama, R.3
Erikson, R.L.4
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13
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0031581099
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On the regulation and function of human polo-like kinase 1 (PLK1): Effects of overexpression on cell cycle progression
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of special interest. This study reports that maximal activity of polo-like kinase 1 (PLK1) during M phase correlates with Plk1 phosphorylation, that the carboxyl terminus of Plk1 negatively regulates Plk1 activity, and that overexpression of Plk1 in mammalian cells causes a multinucleation phenotype consistent with a role of Plk1 in cytokinesis.
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Mundt KE, Golsteyn RM, Lane HA, Nigg EA. On the regulation and function of human polo-like kinase 1 (PLK1): effects of overexpression on cell cycle progression. of special interest Biochem Biophys Res Commun. 239:1997;377-385 This study reports that maximal activity of polo-like kinase 1 (PLK1) during M phase correlates with Plk1 phosphorylation, that the carboxyl terminus of Plk1 negatively regulates Plk1 activity, and that overexpression of Plk1 in mammalian cells causes a multinucleation phenotype consistent with a role of Plk1 in cytokinesis.
-
(1997)
Biochem Biophys Res Commun
, vol.239
, pp. 377-385
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Mundt, K.E.1
Golsteyn, R.M.2
Lane, H.A.3
Nigg, E.A.4
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14
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0032415593
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GFP tagging reveals human Polo-like kinase 1 at the kinetochore/centromere region of mitotic chromosomes
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Both green fluorescent protein (GFP)-tagged human Plk1 and endogenous Plk1 are shown to colocalize with centromere protein B (CENP-B) at the kinetochore/centromere region of human chromosomes. See also annotation to [17]. of special interest
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Arnaud L, Pines J, Nigg EA. GFP tagging reveals human Polo-like kinase 1 at the kinetochore/centromere region of mitotic chromosomes. of special interest Chromosoma. 1998; Both green fluorescent protein (GFP)-tagged human Plk1 and endogenous Plk1 are shown to colocalize with centromere protein B (CENP-B) at the kinetochore/centromere region of human chromosomes. See also annotation to [17].
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(1998)
Chromosoma
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Arnaud, L.1
Pines, J.2
Nigg, E.A.3
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15
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0027280212
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A conserved mitotic kinase active at late anaphase-telophase in syncytial Drosophila embryos
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Fenton B, Glover DM. A conserved mitotic kinase active at late anaphase-telophase in syncytial Drosophila embryos. Nature. 363:1993;637-640.
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(1993)
Nature
, vol.363
, pp. 637-640
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Fenton, B.1
Glover, D.M.2
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16
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0032523956
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Pavarotti encodes a kinesin-like protein required to organize the central spindle and contractile ring for cytokinesis
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of outstanding interest. This study characterizes Drosophila Pavarotti, a kinesin-related motor similar to mammalian MKLP-1. Pavarotti and Polo co-localize extensively, correct Polo localization depends on Pavarotti function, and biochemical data suggest a close relationship between these two proteins. The authors speculate that Polo might be transported by Pavarotti, and discuss the possible role of these proteins in cytokinesis.
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Adams RR, Tavares AAM, Salzberg A, Bellen HJ, Glover DM. Pavarotti encodes a kinesin-like protein required to organize the central spindle and contractile ring for cytokinesis. of outstanding interest Genes Dev. 12:1998;1483-1494 This study characterizes Drosophila Pavarotti, a kinesin-related motor similar to mammalian MKLP-1. Pavarotti and Polo co-localize extensively, correct Polo localization depends on Pavarotti function, and biochemical data suggest a close relationship between these two proteins. The authors speculate that Polo might be transported by Pavarotti, and discuss the possible role of these proteins in cytokinesis.
-
(1998)
Genes Dev
, vol.12
, pp. 1483-1494
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Adams, R.R.1
Tavares, A.A.M.2
Salzberg, A.3
Bellen, H.J.4
Glover, D.M.5
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17
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0031790268
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The Drosophila POLO kinase localises to multiple compartments of the mitotic apparatus and is required for the phosphorylation of MPM2 reactive epitopes
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2 epitopes, and to localize to multiple locations, including the kinetochore/centromere region on mitotic chromosomes. See also annotation to [14]. of special interest
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Logarinho E, Sunkel CE. The Drosophila POLO kinase localises to multiple compartments of the mitotic apparatus and is required for the phosphorylation of MPM2 reactive epitopes. of special interest J Cell Sci. 1998; Polo is shown to be able to generate MPM-2 epitopes, and to localize to multiple locations, including the kinetochore/centromere region on mitotic chromosomes. See also annotation to [14].
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(1998)
J Cell Sci
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Logarinho, E.1
Sunkel, C.E.2
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18
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0029838630
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The conserved mitotic kinase polo is regulated by phosphorylation and has preferred microtubule-associated substrates in Drosophila embryo extracts
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Tavares AA, Glover DM, Sunkel CE. The conserved mitotic kinase polo is regulated by phosphorylation and has preferred microtubule-associated substrates in Drosophila embryo extracts. EMBO J. 15:1996;4873-4883.
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(1996)
EMBO J
, vol.15
, pp. 4873-4883
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Tavares, A.A.1
Glover, D.M.2
Sunkel, C.E.3
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19
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0031850551
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2/M-phase transition of the cell cycle in Xenopus eggs
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2→M transition in Xenopus egg extracts. Conversely, activated Cdc2 - cyclin B (but not Cdc2 - cyclin A) triggers Plx1 activation in interphase extracts, indicating the existence of a positive-feedback loop. See also annotation to [20].
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2→M transition in Xenopus egg extracts. Conversely, activated Cdc2 - cyclin B (but not Cdc2 - cyclin A) triggers Plx1 activation in interphase extracts, indicating the existence of a positive-feedback loop. See also annotation to [20].
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(1998)
J Cell Sci
, vol.111
, pp. 1751-1757
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-
Abrieu, A.1
Brassac, T.2
Galas, S.3
Fisher, D.4
Labbé, J.C.5
Dorée, M.6
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20
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0031806809
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Activated polo-like kinase Plx1 is required at multiple points during mitosis in Xenopus laevis
-
of outstanding interest. A strong case is made that Plx1 functions in the activation of Cdc25C during Xenopus oocyte maturation. First, endogenous Plx1 is itself activated at about the same time as Cdc25C. Second, the rate of activation of Cdc25C is augmented when oocytes are injected with wild-type Plx1, but reduced by catalytically inactive Plx1 or anti-Plx1 antibody. Conversely, injection of Cdc25C causes activation of Plx1, suggesting the existence of a positive-feedback loop. See also annotation to [19].
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Qian Y-W, Erikson E, Li C, Maller JL. Activated polo-like kinase Plx1 is required at multiple points during mitosis in Xenopus laevis. of outstanding interest Mol Cell Biol. 18:1998;4262-4271 A strong case is made that Plx1 functions in the activation of Cdc25C during Xenopus oocyte maturation. First, endogenous Plx1 is itself activated at about the same time as Cdc25C. Second, the rate of activation of Cdc25C is augmented when oocytes are injected with wild-type Plx1, but reduced by catalytically inactive Plx1 or anti-Plx1 antibody. Conversely, injection of Cdc25C causes activation of Plx1, suggesting the existence of a positive-feedback loop. See also annotation to [19].
-
(1998)
Mol Cell Biol
, vol.18
, pp. 4262-4271
-
-
Qian Y-W1
Erikson, E.2
Li, C.3
Maller, J.L.4
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21
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0029968996
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A novel role for Cdc5p in DNA replication
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of special interest. Cdc5p is shown to be able to bind and phosphorylate Dbf4p, a protein required for S phase entry in budding yeast. The authors propose that the action of Cdc5p in late mitosis may be important for events occurring at the subsequent S phase.
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Hardy CFJ, Pautz A. A novel role for Cdc5p in DNA replication. of special interest Mol Cell Biol. 16:1997;6775-6782 Cdc5p is shown to be able to bind and phosphorylate Dbf4p, a protein required for S phase entry in budding yeast. The authors propose that the action of Cdc5p in late mitosis may be important for events occurring at the subsequent S phase.
-
(1997)
Mol Cell Biol
, vol.16
, pp. 6775-6782
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-
Hardy, C.F.J.1
Pautz, A.2
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22
-
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0032560029
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The polo-related kinase cdc5 activates and is destroyed by the mitotic cyclin destruction machinery in S. cerevisiae
-
of outstanding interest. of special interest. Cdc5p is identified as both an activator and a substrate of the mitotic destruction machinery in budding yeast. See also annotation to [23].
-
of outstanding interest Charles JF, Jaspersen SL, Tinker-Kulberg RL, Hwang L, Szidon A, Morgan DO. The polo-related kinase cdc5 activates and is destroyed by the mitotic cyclin destruction machinery in S. cerevisiae. of special interest Curr Biol. 8:1998;497-507 Cdc5p is identified as both an activator and a substrate of the mitotic destruction machinery in budding yeast. See also annotation to [23].
-
(1998)
Curr Biol
, vol.8
, pp. 497-507
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-
Charles, J.F.1
Jaspersen, S.L.2
Tinker-Kulberg, R.L.3
Hwang, L.4
Szidon, A.5
Morgan, D.O.6
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23
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0032473568
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The Polo-like kinase Cdc5p and the WD-repeat protein Cdc20p/fizzy are regulators and substrates of the anaphase promoting complex in Saccharomyces cerevisiae
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of special interest. of outstanding interest. This paper analyses the roles of Cdc5p and Cdc20p (the yeast homologue of Drosophila fizzy) in relation to the anaphase promoting complex/centrosome (APC/C) in budding yeast. Cdc5p is identified as both a regulator of APC/C and a target of APC/C. Interestingly, Cdc5p is required for proteolytic degradation of mitotic cyclins, and hence exit from mitosis, but not for degradation of Pds1p and anaphase onset. Whether the same holds true in metazoan organisms remains to be determined. See also annotations to [22,41,42].
-
of special interest Shirayama M, Zachariae W, Ciosk R, Nasmyth K. The Polo-like kinase Cdc5p and the WD-repeat protein Cdc20p/fizzy are regulators and substrates of the anaphase promoting complex in Saccharomyces cerevisiae. of outstanding interest EMBO J. 17:1998;1336-1349 This paper analyses the roles of Cdc5p and Cdc20p (the yeast homologue of Drosophila fizzy) in relation to the anaphase promoting complex/centrosome (APC/C) in budding yeast. Cdc5p is identified as both a regulator of APC/C and a target of APC/C. Interestingly, Cdc5p is required for proteolytic degradation of mitotic cyclins, and hence exit from mitosis, but not for degradation of Pds1p and anaphase onset. Whether the same holds true in metazoan organisms remains to be determined. See also annotations to [22,41,42].
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(1998)
EMBO J
, vol.17
, pp. 1336-1349
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Shirayama, M.1
Zachariae, W.2
Ciosk, R.3
Nasmyth, K.4
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24
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25744459215
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Role of fission yeast polo kinase in selecting the site of cell division
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A careful analysis of the phenotype of temperature-sensitive plo1 mutants in Schizosaccharomyces. pombe. The data reported support the view that polo-like kinase play an important role in septation in fission yeast (and by extension in cytokinesis in metazoan organisms). of special interest
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Bähler J, Steever AB, Wheatley S, Wang Y-I, Pringle JR, Gould KL, McCollum D. Role of fission yeast polo kinase in selecting the site of cell division. of special interest J Cell Biol. 1998; A careful analysis of the phenotype of temperature-sensitive plo1 mutants in Schizosaccharomyces. pombe. The data reported support the view that polo-like kinase play an important role in septation in fission yeast (and by extension in cytokinesis in metazoan organisms).
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(1998)
J Cell Biol
-
-
Bähler, J.1
Steever, A.B.2
Wheatley, S.3
Wang Y-I4
Pringle, J.R.5
Gould, K.L.6
McCollum, D.7
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25
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0032482986
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Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk
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of special interest. A mutation within the polo-box is shown to render murine polo-like kinase (Plk1) nonfunctional and mislocalized in budding yeast.
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Lee KS, Grenfell TZ, Yarm FR, Erikson RL. Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk. of special interest Proc Natl Acad Sci USA. 95:1998;9301-9306 A mutation within the polo-box is shown to render murine polo-like kinase (Plk1) nonfunctional and mislocalized in budding yeast.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 9301-9306
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Lee, K.S.1
Grenfell, T.Z.2
Yarm, F.R.3
Erikson, R.L.4
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26
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0029993727
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Active and inactive protein kinases: Structural basis for regulation
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Johnson LN, Noble MEM, Owen DJ. Active and inactive protein kinases: structural basis for regulation. Cell. 85:1996;149-158.
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(1996)
Cell
, vol.85
, pp. 149-158
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Johnson, L.N.1
Noble, M.E.M.2
Owen, D.J.3
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27
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0029821131
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Purification and molecular cloning of Plx1, a Cdc25-stimulatory kinase from Xenopus egg extracts
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Kumagai A, Dunphy WG. Purification and molecular cloning of Plx1, a Cdc25-stimulatory kinase from Xenopus egg extracts. Science. 273:1996;1377-1380.
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(1996)
Science
, vol.273
, pp. 1377-1380
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Kumagai, A.1
Dunphy, W.G.2
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29
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0032031634
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The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins
-
of outstanding interest. of special interest. A biochemical study showing extensive overlap in the proteins that are recognized by MPM-2 antibody and those that are bound by the peptidyl-prolyl isomerase Pin1. In many instances, protein binding by Pin1 requires phosphorylation at serine/threonine-proline sites. Pin1 is shown to bind to several important mitotic regulators, including Plk1. See also annotations to [31,32].
-
of outstanding interest Shen M, Stukenberg PT, Kirschner MW, Lu KP. The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. of special interest Genes Dev. 12:1998;706-720 A biochemical study showing extensive overlap in the proteins that are recognized by MPM-2 antibody and those that are bound by the peptidyl-prolyl isomerase Pin1. In many instances, protein binding by Pin1 requires phosphorylation at serine/threonine-proline sites. Pin1 is shown to bind to several important mitotic regulators, including Plk1. See also annotations to [31,32].
-
(1998)
Genes Dev
, vol.12
, pp. 706-720
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Shen, M.1
Stukenberg, P.T.2
Kirschner, M.W.3
Lu, K.P.4
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30
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0031149841
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Systematic identification of mitotic phosphoproteins
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of outstanding interest. This paper describes a functional screen of expression libraries, based on in vitro transcription and translation of pooled cDNAs. Used here to identify candidate mitotic phosphoproteins, adaptations of this type of screen may have a wide utility.
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Stukenberg PT, Lustig KD, McGarry TJ, King RW, Kuang J, Kirschner MW. Systematic identification of mitotic phosphoproteins. of outstanding interest Curr Biol. 7:1997;338-348 This paper describes a functional screen of expression libraries, based on in vitro transcription and translation of pooled cDNAs. Used here to identify candidate mitotic phosphoproteins, adaptations of this type of screen may have a wide utility.
-
(1997)
Curr Biol
, vol.7
, pp. 338-348
-
-
Stukenberg, P.T.1
Lustig, K.D.2
McGarry, T.J.3
King, R.W.4
Kuang, J.5
Kirschner, M.W.6
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31
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0031438929
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Sequence-specific and phosphorylation-dependent proline isomerization: A potential mitotic regulatory mechanism
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of outstanding interest. This paper shows that Pin1 is a phosphorylation-dependent peptidyl-prolyl isomerase that specifically recognizes phosphorylated serine/threonine-proline sites. As many such sites are produced during mitosis, this raises the possibility that phosphorylation-dependent proline isomerization may represent a novel mechanism for regulating the activity of mitotic phosphoproteins.
-
Yaffe MB, Schutkowski M, Shen M, Zhou XZ, Stukenberg PT, Rahfeld JU, Xu J, Kuang J, Kirschner MW, Fischer G, et al. Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism. of outstanding interest Science. 278:1997;1957-1960 This paper shows that Pin1 is a phosphorylation-dependent peptidyl-prolyl isomerase that specifically recognizes phosphorylated serine/threonine-proline sites. As many such sites are produced during mitosis, this raises the possibility that phosphorylation-dependent proline isomerization may represent a novel mechanism for regulating the activity of mitotic phosphoproteins.
-
(1997)
Science
, vol.278
, pp. 1957-1960
-
-
Yaffe, M.B.1
Schutkowski, M.2
Shen, M.3
Zhou, X.Z.4
Stukenberg, P.T.5
Rahfeld, J.U.6
Xu, J.7
Kuang, J.8
Kirschner, M.W.9
Fischer, G.10
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32
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0032473350
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The mitotic peptidyl prolyl isomerase, Pin1, interacts with Cdc25 and Plx1
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of special interest. The authors propose that Pin1 may modulate mitotic progression through binding Cdc25 and Plx1. Whereas only the mitotically phosphorylated, active form of Cdc25 was bound by Pin1, it is noteworthy that Plx1 binding did not seem to require phosphorylation. See also annotation to [29].
-
Crenshaw DG, Yang J, Means AR, Kornbluth S. The mitotic peptidyl prolyl isomerase, Pin1, interacts with Cdc25 and Plx1. of special interest EMBO J. 17:1998;1315-1327 The authors propose that Pin1 may modulate mitotic progression through binding Cdc25 and Plx1. Whereas only the mitotically phosphorylated, active form of Cdc25 was bound by Pin1, it is noteworthy that Plx1 binding did not seem to require phosphorylation. See also annotation to [29].
-
(1998)
EMBO J
, vol.17
, pp. 1315-1327
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-
Crenshaw, D.G.1
Yang, J.2
Means, A.R.3
Kornbluth, S.4
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33
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0025840258
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Polo encodes a protein kinase homolog required for mitosis in Drosophila
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41
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0032473421
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The polo-like kinase Plx1 is required for M phase exit and destruction of mitotic regulators in Xenopus egg extracts
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of special interest. of outstanding interest. By a dominant-negative approach and immunodepletion-reconstitution experiments, Plx1 is shown to be required for the activation of the ubiquitin dependent proteolytic degradation machinery upon M phase exit of Xenopus egg extracts. This paper points to Plx1 as as essential regulator of anaphase promoting complex/cyclosome (APC/C) activity. See also annotations to [22,23,42].
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of special interest Descombes P, Nigg EA. The polo-like kinase Plx1 is required for M phase exit and destruction of mitotic regulators in Xenopus egg extracts. of outstanding interest EMBO J. 17:1998;1328-1335 By a dominant-negative approach and immunodepletion-reconstitution experiments, Plx1 is shown to be required for the activation of the ubiquitin dependent proteolytic degradation machinery upon M phase exit of Xenopus egg extracts. This paper points to Plx1 as as essential regulator of anaphase promoting complex/cyclosome (APC/C) activity. See also annotations to [22,23,42].
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(1998)
EMBO J
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Descombes, P.1
Nigg, E.A.2
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42
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0031991880
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PKA and MPF-activated polo-like kinase regulate anaphase-promoting complex activity and mitosis progression
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of special interest. of outstanding interest. This provocative study suggests that Plk1 may activate APC/C by direct phosphorylation of APC/C subunits. Interestingly, in these experiments Plk1 had first to be incubated with Cdk1/cyclin B in order to be active on APC/C subunits. See also annotations to [22,23,41].
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of special interest Kotani S, Tugendreich S, Fuji M, Jorgensen P-M, Watanabe N, Hoog C, Hieter P, Todokoro K. PKA and MPF-activated polo-like kinase regulate anaphase-promoting complex activity and mitosis progression. of outstanding interest Mol Cell. 1:1998;371-380 This provocative study suggests that Plk1 may activate APC/C by direct phosphorylation of APC/C subunits. Interestingly, in these experiments Plk1 had first to be incubated with Cdk1/cyclin B in order to be active on APC/C subunits. See also annotations to [22,23,41].
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(1998)
Mol Cell
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Kotani, S.1
Tugendreich, S.2
Fuji, M.3
Jorgensen P-M4
Watanabe, N.5
Hoog, C.6
Hieter, P.7
Todokoro, K.8
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43
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Anaphase initiation in Saccharomyces cerevisiae is controlled by the APC-dependent degradation of the anaphase inhibitor Pds1p
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Cohen-Fix O, Peters JM, Kirschner MW, Koshland D. Anaphase initiation in Saccharomyces cerevisiae is controlled by the APC-dependent degradation of the anaphase inhibitor Pds1p. Genes Dev. 10:1996;3081-3093.
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Peters, J.M.2
Kirschner, M.W.3
Koshland, D.4
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44
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0030013594
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Cut2 proteolysis required for sister-chromatid seperation in fission yeast
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Funabiki H, Yamano H, Kumada K, Nagao K, Hunt T, Yanagida M. Cut2 proteolysis required for sister-chromatid seperation in fission yeast. Nature. 381:1996;438-441.
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Funabiki, H.1
Yamano, H.2
Kumada, K.3
Nagao, K.4
Hunt, T.5
Yanagida, M.6
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46
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0031911931
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Fission yeast cut mutations revisited: Control of anaphase
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of special interest. A comprehensive review of the cut mutant gene products of Schizosaccharomyces pombe, with particular emphasis on their relevance to proteolytic degradation and anaphase onset.
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Yanagida M. Fission yeast cut mutations revisited: control of anaphase. of special interest Trends Cell Biol. 8:1998;144-149 A comprehensive review of the cut mutant gene products of Schizosaccharomyces pombe, with particular emphasis on their relevance to proteolytic degradation and anaphase onset.
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Trends Cell Biol
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Yanagida, M.1
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47
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0030835478
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Drosophila fizzy-related down-regulates mitotic cyclins and is required for cell proliferation arrest and entry into endocyles
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2 preceding salivary gland endoreduplication), whereas fzy is required for cyclin destruction during M phase.
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2 preceding salivary gland endoreduplication), whereas fzy is required for cyclin destruction during M phase.
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Cell
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Sigrist, S.J.1
Lehner, C.F.2
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48
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Glotzer M, Murray AW, Kirschner MW. Cyclin is degraded by the ubiquitin pathway. Nature. 349:1991;132-138.
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49
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0028243084
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Cell cycle analysis and chromosomal localization of human Plk1, a putative homologue of the mitotic kinases Drosophila polo and Saccharomyces cerevisiae Cdc5
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Golsteyn RM, Schultz SJ, Bartek J, Ziemiecki A, Ried T, Nigg EA. Cell cycle analysis and chromosomal localization of human Plk1, a putative homologue of the mitotic kinases Drosophila polo and Saccharomyces cerevisiae Cdc5. J Cell Sci. 107:1994;1509-1517.
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Golsteyn, R.M.1
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Bartek, J.3
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50
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0030046306
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Meiotic metaphase arrest in animal oocytes: Its mechanisms and biological significance
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Sagata N. Meiotic metaphase arrest in animal oocytes: its mechanisms and biological significance. Trends Cell Biol. 6:1996;22-28.
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Murray AW. Cell cycle extracts. Methods Cell Biol. 36:1991;581-605.
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52
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The dmf1/mid1 gene is essential for correct positioning of the division septum in fission yeast
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Sohrmann M, Fankhauser C, Brodbeck C, Simanis V. The dmf1/mid1 gene is essential for correct positioning of the division septum in fission yeast. Genes Dev. 10:1996;2707-2719.
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Sohrmann, M.1
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Simanis, V.4
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53
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0030040263
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Isolation and characterization of fission yeast mutants defective in the assembly and placement of the contractile actin ring
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Chang F, Woollard A, Nurse P. Isolation and characterization of fission yeast mutants defective in the assembly and placement of the contractile actin ring. J Cell Sci. 109:1996;131-142.
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Chang, F.1
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54
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0030718601
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The control of septum formation in fission yeast
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of special interest. A comprehensive review of septum formation in S. pombe. Genetic dissection of septation in fission yeast is expected to provide insight into the mechanisms underlying cytokinesis in metazoan organisms.
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Gould KL, Simanis V. The control of septum formation in fission yeast. of special interest Genes Dev. 11:1997;2939-2951 A comprehensive review of septum formation in S. pombe. Genetic dissection of septation in fission yeast is expected to provide insight into the mechanisms underlying cytokinesis in metazoan organisms.
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(1997)
Genes Dev
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Gould, K.L.1
Simanis, V.2
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55
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0023020417
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Establishment of the mechanism of cytokinesis in animal cells
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Rappaport R. Establishment of the mechanism of cytokinesis in animal cells. Int Rev Cytol. 105:1986;245-281.
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Rappaport, R.1
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56
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0030912088
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Rappaport rules: Cleavage furrow induction in animal cells
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of special interest. A review of recent studies on cytokinesis, from the perspective of the pioneering work performed by Rappaport.
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Oegema K, Mitchison TJ. Rappaport rules: cleavage furrow induction in animal cells. of special interest Proc Natl Acad Sci USA. 94:1997;4817-4820 A review of recent studies on cytokinesis, from the perspective of the pioneering work performed by Rappaport.
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(1997)
Proc Natl Acad Sci USA
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, pp. 4817-4820
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Oegema, K.1
Mitchison, T.J.2
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57
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0032476579
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Drosophila Polo kinase is required for cytokinesis
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A detailed re-investigation of the phenotype of polo mutants in Drosophila, with particular emphasis on spermatogenesis. The data indicate a predominance of cytokinesis defects at various stages of spermatogenesis, consistent with the view that Polo-like kinases are important regulators of cytokinesis. of special interest
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Carmena M, Riparbelli MG, Minestrini G, Tavares AM, Adams R, Callaini G, Glover DM. Drosophila Polo kinase is required for cytokinesis. of special interest J Cell Biol. 1998; A detailed re-investigation of the phenotype of polo mutants in Drosophila, with particular emphasis on spermatogenesis. The data indicate a predominance of cytokinesis defects at various stages of spermatogenesis, consistent with the view that Polo-like kinases are important regulators of cytokinesis.
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(1998)
J Cell Biol
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Carmena, M.1
Riparbelli, M.G.2
Minestrini, G.3
Tavares, A.M.4
Adams, R.5
Callaini, G.6
Glover, D.M.7
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58
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0031578244
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Malignant transformation of mammalian cells initiated by constitutive expression of the polo-like kinase
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of special interest. Microinjection of polo-like kinase (Plk1) mRNA into NIH-3T3 cells is reported to drive quiescent cells into the cell cycle. Furthermore, constitutive over-expression of Plk1 causes malignant transformation of NIH-3T3 cells, as measured by soft-agar growth and tumor formation in nude mice.
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Smith MR, Wilson ML, Hamanaka R, Chase D, Kung H, Longo DL, Ferris DK. Malignant transformation of mammalian cells initiated by constitutive expression of the polo-like kinase. of special interest Biochem Biophys Res Commun. 234:1997;397-405 Microinjection of polo-like kinase (Plk1) mRNA into NIH-3T3 cells is reported to drive quiescent cells into the cell cycle. Furthermore, constitutive over-expression of Plk1 causes malignant transformation of NIH-3T3 cells, as measured by soft-agar growth and tumor formation in nude mice.
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(1997)
Biochem Biophys Res Commun
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, pp. 397-405
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Smith, M.R.1
Wilson, M.L.2
Hamanaka, R.3
Chase, D.4
Kung, H.5
Longo, D.L.6
Ferris, D.K.7
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59
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1842372659
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Polo-like kinase, a novel marker for cellular proliferation
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of special interest. Polo-like kinase (Plk1) protein levels in tumors are studied by immunocyto-chemistry. Elevated proliferative activity of the cells is found to be correlated with the upregulation of Plk1 expression, whereas in vitro differentiation of leukemic cell types is accompanied by downregulation of Plk1. The authors propose Plk1 as a marker for diagnosis and prognosis of cancer patients and as a potential target for cancer chemotherapy.
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Yuan J, Horlin A, Hock B, Stutte HJ, Rubsamen-Waigmann H, Strebhardt K. Polo-like kinase, a novel marker for cellular proliferation. of special interest Am J Pathol. 150:1997;1165-1172 Polo-like kinase (Plk1) protein levels in tumors are studied by immunocyto-chemistry. Elevated proliferative activity of the cells is found to be correlated with the upregulation of Plk1 expression, whereas in vitro differentiation of leukemic cell types is accompanied by downregulation of Plk1. The authors propose Plk1 as a marker for diagnosis and prognosis of cancer patients and as a potential target for cancer chemotherapy.
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(1997)
Am J Pathol
, vol.150
, pp. 1165-1172
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Yuan, J.1
Horlin, A.2
Hock, B.3
Stutte, H.J.4
Rubsamen-Waigmann, H.5
Strebhardt, K.6
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60
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0031051218
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Prognostic significance of polo-like kinase (PLK) expression in non-small cell lung cancer
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of special interest. A detailed study on polo-like kinase (Plk1) mRNA levels in non-small cell lung cancer tissues suggests that high Plk1 levels correlate with poor survival. This leads the authors to propose that Plk1 expression might be used as a prognostic indicator for patients with this disease.
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Wolf G, Elez R, Doermer A, Holtrich U, Ackermann H, Stutte HJ, Altmannsberger HM, Rubsamen-Waigmann H, Strebhardt K. Prognostic significance of polo-like kinase (PLK) expression in non-small cell lung cancer. of special interest Oncogene. 14:1997;543-549 A detailed study on polo-like kinase (Plk1) mRNA levels in non-small cell lung cancer tissues suggests that high Plk1 levels correlate with poor survival. This leads the authors to propose that Plk1 expression might be used as a prognostic indicator for patients with this disease.
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(1997)
Oncogene
, vol.14
, pp. 543-549
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Wolf, G.1
Elez, R.2
Doermer, A.3
Holtrich, U.4
Ackermann, H.5
Stutte, H.J.6
Altmannsberger, H.M.7
Rubsamen-Waigmann, H.8
Strebhardt, K.9
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61
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0031015299
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What does Mos do in oocytes and somatic cells?
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of special interest. An excellent review of the function of the mos proto-oncogene.
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Sagata N. What does Mos do in oocytes and somatic cells? of special interest Bioessays. 19:1997;13-21 An excellent review of the function of the mos proto-oncogene.
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Bioessays
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Sagata, N.1
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62
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0028134981
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A MAP kinase-dependent spindle assembly checkpoint in Xenopus egg extracts
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Minshull J, Sun H, Tonks NK, Murray AW. A MAP kinase-dependent spindle assembly checkpoint in Xenopus egg extracts. Cell. 79:1994;475-486.
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Cell
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Minshull, J.1
Sun, H.2
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Murray, A.W.4
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63
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0030898893
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MAP kinase is required for the spindle assembly checkpoint but is dispensable for the normal M phase entry and exit in Xenopus egg cell cycle extracts
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of outstanding interest. By immunodepletion of Xenopus egg extracts, mitogen-activated protein (MAP) kinase is shown to be dispensible for normal M phase entry and exit in vitro. In contrast, the nocodazole-sensitive spindle checkpoint is not operational in such extracts, but can be restored by addition of recombinant MAP kinase. This confirms and extends an earlier study [62], indicating that MAP kinase is required for the spindle checkpoint. See also annotation to [64].
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Takenaka K, Gotoh Y, Nishida E. MAP kinase is required for the spindle assembly checkpoint but is dispensable for the normal M phase entry and exit in Xenopus egg cell cycle extracts. of outstanding interest J Cell Biol. 136:1997;1091-1097 By immunodepletion of Xenopus egg extracts, mitogen-activated protein (MAP) kinase is shown to be dispensible for normal M phase entry and exit in vitro. In contrast, the nocodazole-sensitive spindle checkpoint is not operational in such extracts, but can be restored by addition of recombinant MAP kinase. This confirms and extends an earlier study [62], indicating that MAP kinase is required for the spindle checkpoint. See also annotation to [64].
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(1997)
J Cell Biol
, vol.136
, pp. 1091-1097
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Takenaka, K.1
Gotoh, Y.2
Nishida, E.3
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64
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0344647981
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A role for mitogen-activated protein kinase in the spindle assembly checkpoint in XTC cells
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of outstanding interest. Microinjection of a mitogen activated protein (MAP)-kinase specific phosphatase into cultured Xenopus cells is shown to abrogate the spindle checkpoint, arguing that MAP kinase function is required for this checkpoint. See also annotation to [63].
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Wang XM, Xhai Y, Ferrell JE Jr. A role for mitogen-activated protein kinase in the spindle assembly checkpoint in XTC cells. of outstanding interest J Cell Biol. 137:1997;433-443 Microinjection of a mitogen activated protein (MAP)-kinase specific phosphatase into cultured Xenopus cells is shown to abrogate the spindle checkpoint, arguing that MAP kinase function is required for this checkpoint. See also annotation to [63].
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(1997)
J Cell Biol
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Wang, X.M.1
Xhai, Y.2
Ferrell J.E., Jr.3
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65
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0030885666
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CDC5 and CKII control adaptation to the yeast DNA damage checkpoint
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of outstanding interest. The budding yeast polo-like kinase (Plk) homologue, Cdc5, is shown to be required for adaptation to a DNA damage checkpoint. In wild-type cells, a double-stranded DNA break will trigger a checkpoint causing cell cycle arrest; if the damage cannot be repaired, wild-type yeast cells will eventually override this arrest (i.e. adapt to it). This adaptation is shown to require Cdc5 function. Considering that the DNA damage checkpoint arrests cells prior to anaphase onset, this suggests that Cdc5 has a (nonessential) role at a time prior to its essential role during late mitosis.
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Toczyski DP, Galgoczy DJ, Hartwell LH. CDC5 and CKII control adaptation to the yeast DNA damage checkpoint. of outstanding interest Cell. 90:1997;1097-1106 The budding yeast polo-like kinase (Plk) homologue, Cdc5, is shown to be required for adaptation to a DNA damage checkpoint. In wild-type cells, a double-stranded DNA break will trigger a checkpoint causing cell cycle arrest; if the damage cannot be repaired, wild-type yeast cells will eventually override this arrest (i.e. adapt to it). This adaptation is shown to require Cdc5 function. Considering that the DNA damage checkpoint arrests cells prior to anaphase onset, this suggests that Cdc5 has a (nonessential) role at a time prior to its essential role during late mitosis.
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(1997)
Cell
, vol.90
, pp. 1097-1106
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Toczyski, D.P.1
Galgoczy, D.J.2
Hartwell, L.H.3
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66
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0032545661
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Characterisation of a polo-like protein kinase gene homologue from an evolutionary divergent eukaryote, Trypanosoma brucei
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of special interest. This study reports the molecular characterization of a polo-like kinase (Plk) from Trypanosoma brucei. The identification of a Plk in this evolutionary divergent eukaryote underscores the extensive conservation of this kinase, consistent with a key role for Plks in cell cycle control.
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Graham TM, Tait A, Hide G. Characterisation of a polo-like protein kinase gene homologue from an evolutionary divergent eukaryote, Trypanosoma brucei. of special interest Gene. 207:1998;71-77 This study reports the molecular characterization of a polo-like kinase (Plk) from Trypanosoma brucei. The identification of a Plk in this evolutionary divergent eukaryote underscores the extensive conservation of this kinase, consistent with a key role for Plks in cell cycle control.
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(1998)
Gene
, vol.207
, pp. 71-77
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Graham, T.M.1
Tait, A.2
Hide, G.3
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