Papers associated with egg (and rasgrf1)

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	Increases in cyclin A/Cdk activity and in PP2A-B55 inhibition by FAM122A are key mitosis-inducing events., Lacroix B., EMBO J. March 1, 2024; 43 (6): 993-1014.
	Bora phosphorylation substitutes in trans for T-loop phosphorylation in Aurora A to promote mitotic entry., Tavernier N., Nat Commun. March 26, 2021; 12 (1): 1899.
	Bistable, Biphasic Regulation of PP2A-B55 Accounts for the Dynamics of Mitotic Substrate Phosphorylation., Kamenz J., Curr Biol. February 22, 2021; 31 (4): 794-808.e6.
	Managing the Oocyte Meiotic Arrest-Lessons from Frogs and Jellyfish., Jessus C., Cells. May 7, 2020; 9 (5):
	A robust and tunable mitotic oscillator in artificial cells., Guan Y., Elife. April 5, 2018; 7
	Protein interactomes of protein phosphatase 2A B55 regulatory subunits reveal B55-mediated regulation of replication protein A under replication stress., Wang F., Sci Rep. February 8, 2018; 8 (1): 2683.
	RSK promotes G2/M transition through activating phosphorylation of Cdc25A and Cdc25B., Wu CF., Oncogene. May 1, 2014; 33 (18): 2385-94.
	Changes in oscillatory dynamics in the cell cycle of early Xenopus laevis embryos., Tsai TY., PLoS Biol. February 1, 2014; 12 (2): e1001788.
	Budding yeast greatwall and endosulfines control activity and spatial regulation of PP2A(Cdc55) for timely mitotic progression., Juanes MA., PLoS Genet. January 1, 2013; 9 (7): e1003575.
	Protein phosphatase 2A controls the order and dynamics of cell-cycle transitions., Krasinska L., Mol Cell. November 4, 2011; 44 (3): 437-50.
	Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis., Mochida S., Science. December 17, 2010; 330 (6011): 1670-3.
	Direct roles of the signaling kinase RSK2 in Cdc25C activation during Xenopus oocyte maturation., Wang R., Proc Natl Acad Sci U S A. November 16, 2010; 107 (46): 19885-90.
	Roles of Greatwall kinase in the regulation of cdc25 phosphatase., Zhao Y., Mol Biol Cell. April 1, 2008; 19 (4): 1317-27.
	Differences in regulation of the first two M-phases in Xenopus laevis embryo cell-free extracts., Chesnel F., Dev Biol. September 15, 2005; 285 (2): 358-75.
	Inhibition of translation and induction of apoptosis by Bunyaviral nonstructural proteins bearing sequence similarity to reaper., Colón-Ramos DA., Mol Biol Cell. October 1, 2003; 14 (10): 4162-72.
	Regulation of EDEN-dependent deadenylation of Aurora A/Eg2-derived mRNA via phosphorylation and dephosphorylation in Xenopus laevis egg extracts., Detivaud L., J Cell Sci. July 1, 2003; 116 (Pt 13): 2697-705.
	Timing of events in mitosis., Georgi AB., Curr Biol. January 22, 2002; 12 (2): 105-14.
	Characterization of vertebrate cohesin complexes and their regulation in prophase., Sumara I., J Cell Biol. November 13, 2000; 151 (4): 749-62.
	Requirement of the prolyl isomerase Pin1 for the replication checkpoint., Winkler KE., Science. March 3, 2000; 287 (5458): 1644-7.
	Inactivation of p42 mitogen-activated protein kinase is required for exit from M-phase after cyclin destruction., Chau AS., J Biol Chem. November 5, 1999; 274 (45): 32085-90.
	A maternal form of the phosphatase Cdc25A regulates early embryonic cell cycles in Xenopus laevis., Kim SH., Dev Biol. August 15, 1999; 212 (2): 381-91.
	The Xenopus Chk1 protein kinase mediates a caffeine-sensitive pathway of checkpoint control in cell-free extracts., Kumagai A., J Cell Biol. September 21, 1998; 142 (6): 1559-69.
	The polo-like kinase Plx1 is required for M phase exit and destruction of mitotic regulators in Xenopus egg extracts., Descombes P., EMBO J. March 2, 1998; 17 (5): 1328-35.
	The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1., Crenshaw DG., EMBO J. March 2, 1998; 17 (5): 1315-27.
	14-3-3 proteins act as negative regulators of the mitotic inducer Cdc25 in Xenopus egg extracts., Kumagai A., Mol Biol Cell. February 1, 1998; 9 (2): 345-54.
	Induction of a G2-phase arrest in Xenopus egg extracts by activation of p42 mitogen-activated protein kinase., Walter SA., Mol Biol Cell. November 1, 1997; 8 (11): 2157-69.
	Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from Xenopus egg extracts., Kumagai A., Science. September 6, 1996; 273 (5280): 1377-80.
	Phosphorylation and activation of the Xenopus Cdc25 phosphatase in the absence of Cdc2 and Cdk2 kinase activity., Izumi T., Mol Biol Cell. February 1, 1995; 6 (2): 215-26.
	A role for cAMP-dependent protein kinase in early embryonic divisions., Grieco D., Proc Natl Acad Sci U S A. October 11, 1994; 91 (21): 9896-900.
	Cell cycle regulation of the p34cdc2 inhibitory kinases., Atherton-Fessler S., Mol Biol Cell. September 1, 1994; 5 (9): 989-1001.
	cdc25 is one of the MPM-2 antigens involved in the activation of maturation-promoting factor., Kuang J., Mol Biol Cell. February 1, 1994; 5 (2): 135-45.
	Dephosphorylation of cdc25-C by a type-2A protein phosphatase: specific regulation during the cell cycle in Xenopus egg extracts., Clarke PR., Mol Biol Cell. April 1, 1993; 4 (4): 397-411.
	Phosphorylation and activation of human cdc25-C by cdc2--cyclin B and its involvement in the self-amplification of MPF at mitosis., Hoffmann I., EMBO J. January 1, 1993; 12 (1): 53-63.
	Cdc25 regulates the phosphorylation and activity of the Xenopus cdk2 protein kinase complex., Gabrielli BG., J Biol Chem. September 5, 1992; 267 (25): 18040-6.
	Cyclin A potentiates maturation-promoting factor activation in the early Xenopus embryo via inhibition of the tyrosine kinase that phosphorylates cdc2., Devault A., J Cell Biol. September 1, 1992; 118 (5): 1109-20.
	Periodic changes in phosphorylation of the Xenopus cdc25 phosphatase regulate its activity., Izumi T., Mol Biol Cell. August 1, 1992; 3 (8): 927-39.
	DNA replication and progression through the cell cycle., Dasso M., Ciba Found Symp. January 1, 1992; 170 161-80; discussion 180-6.
	cdc25 is a specific tyrosine phosphatase that directly activates p34cdc2., Gautier J., Cell. October 4, 1991; 67 (1): 197-211.

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