Scaffold Subunit Aalpha of PP2A Is Essential for Female Meiosis and Fertility in Mice1
Abstract
Ppp2r1a encodes the scaffold subunit Aalpha of protein phosphatase 2A (PP2A), which is an important and ubiquitously expressed serine threonine phosphatase family and plays a critical role in many fundamental cellular processes. To identify the physiological role of PP2A in female germ cell meiosis, we selectively disrupted Ppp2r1a expression in oocytes by using the Cre-Loxp conditional knockout system. Here we report for the first time that oocyte-specific deletion of Ppp2r1a led to severe female subfertility without affecting follicle survival, growth, and ovulation. PP2A-Aalpha was essential for regulating oocyte meiotic maturation because depletion of PP2A-Aalpha facilitated germinal vesicle breakdown, causing elongation of the MII spindle and precocious separation of sister chromatids. The resulting eggs had high risk of aneuploidy, though they could be fertilized, leading to defective embryonic development and thus subfertility. Our findings provide strong evidence that PP2A-Aalpha within the oocyte plays an indispensable role in oocyte meiotic maturation, though it is dispensable for folliculogenesis in the mouse ovary.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In these mice, a meiotic maturation defect was observed: normal meiosis-I, but abnormal elongated spindle formation during meiosis-II, precocious sister chromatid separation due to loss of centromeric cohesion, and increased germinal vesicle breakdown.
“Again, a meiotic maturation defect was observed, with in this case, a normal meiosis-I, but abnormal elongated spindle formation during meiosis-II, precocious sister chromatid separation due to loss of centromeric cohesion, and increased germinal vesicle breakdown.”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [29]
Fertilization was followed by impaired embryonic development: at E0.5 efficient pronuclear formation was defective, and at E4.0 the blastocyst stage was rarely reached and signs of apoptosis were seen.
“Fertilization was however followed by impaired embryonic development.At E0.5, efficient pronuclear formation was defective, and at E4.0, the blastocyst stage was rarely reached and signs of apoptosis were seen.”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [29]
Cites
To err (meiotically) is human: the genesis of human aneuploidy
Hassold, T. J., & Hunt, P. A. (2001) · Nature Reviews Genetics · doi:10.1038/35066065 · Cited by 2,456 · see citing works
Development of Follicles in the Mammalian Ovary
Hirshfield, A. N. (1991) · International review of cytology · doi:10.1016/s0074-7696(08)61524-7 · Cited by 1,281 · see citing works
Cyclin synthesis drives the early embryonic cell cycle
Murray, A. W., & Kirschner, M. W. (1989) · Nature · doi:10.1038/339275a0 · Cited by 1,177 · see citing works
PROPOSAL FOR A CLASSIFICATION OF OOCYTES AND FOLLICLES IN THE MOUSE OVARY
PEDERSEN, T., & PETERS, H. (1968) · Reproduction · doi:10.1530/jrf.0.0170555 · Cited by 1,141 · see citing works
Oocyte-Specific Deletion of Pten Causes Premature Activation of the Primordial Follicle Pool
Reddy, P., Liu, L., Adhikari, D., Jagarlamudi, K., Singareddy, R., Shen, Y., Du, C., Tang, W., Hämäläinen, T. M., Peng, S. L., et al. (2008) · Science · doi:10.1126/science.1152257 · Cited by 854 · see citing works
Regulation of protein kinase cascades by protein phosphatase 2A
Millward, T. A., Zołnierowicz, S., & Hemmings, B. A. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01375-4 · Cited by 793 · see citing works
Petronczki, M. P., Siomos, M. F., & Nasmyth, K. (2003) · Cell · doi:10.1016/s0092-8674(03)00083-7 · Cited by 704 · see citing works
Shugoshin collaborates with protein phosphatase 2A to protect cohesin
Kitajima, T. S., Sakuno, T., Ishiguro, K., Iemura, S., Natsume, T., Kawashima, S. A., & Watanabe, Y. (2006) · Nature · doi:10.1038/nature04663 · Cited by 597 · see citing works
Tsc/mTORC1 signaling in oocytes governs the quiescence and activation of primordial follicles
Adhikari, D., Zheng, W., Shen, Y., Gorre, N., Hämäläinen, T. M., Cooney, A. J., Huhtaniemi, I. T., Lan, Z., & Liu, K. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp483 · Cited by 370 · see citing works
From Cdc2 to Cdk1: when did the cell cycle kinase join its cyclin partner?
Dorée, M., & Hunt, T. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.12.2461 · Cited by 277 · see citing works
Mochida, S., Ikeo, S., Gannon, J., & Hunt, T. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.238 · Cited by 276 · see citing works
Unified mode of centromeric protection by shugoshin in mammalian oocytes and somatic cells
Lee, J., Kitajima, T. S., Tanno, Y., Yoshida, K., Morita, T., Miyano, T., Miyake, M., & Watanabe, Y. (2007) · Nature Cell Biology · doi:10.1038/ncb1667 · Cited by 263 · see citing works
Hemmings, B. A., Adams-Pearson, C., Maurer, F., Mueller, P., Goris, J., Merlevede, W., Hofsteenge, J., & Stone, S. R. (1990) · Biochemistry · doi:10.1021/bi00465a002 · Cited by 243 · see citing works
Ovarian follicle counts – not as simple as 1, 2, 3
Tilly, J. L. (2003) · Reproductive Biology and Endocrinology · doi:10.1186/1477-7827-1-11 · Cited by 227 · see citing works
Calin, G. A., di Iasio, M. G., Caprini, E., Vorechovsky, I., Natali, P. G., Sozzi, G., Croce, C. M., Barbanti-Brodano, G., Russo, G., & Negrini, M. (2000) · Oncogene · doi:10.1038/sj.onc.1203389 · Cited by 219 · see citing works
Type 2A protein phosphatase, the complex regulator of numerous signaling pathways
Zołnierowicz, S. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(00)00424-x · Cited by 200 · see citing works
Distinct roles of PP1 and PP2A‐like phosphatases in control of microtubule dynamics during mitosis
Tournebize, R., Andersen, S. S. L., Verde, F., Dorée, M., Karsenti, E., & Hyman, A. A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.18.5537 · Cited by 192 · see citing works
Kremmer, E., Ohst, K., Kiefer, J., Brewis, N., & Walter, G. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.3.1692 · Cited by 175 · see citing works
Towards a new understanding on the regulation of mammalian oocyte meiosis resumption
Sun, Q., Miao, Y., & Schatten, H. (2009) · Cell Cycle · doi:10.4161/cc.8.17.9471 · Cited by 161 · see citing works
Self-citationMARF1 Regulates Essential Oogenic Processes in Mice
Su, Y., Sugiura, K., Sun, F., Pendola, J. K., Cox, G. A., Handel, M. A., Schimenti, J. C., & Eppig, J. J. (2012) · Science · doi:10.1126/science.1214680 · Cited by 111 · see citing works
Karaı̈skou, A., Jessus, C., Brassac, T., & Ozon, R. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.21.3747 · Cited by 101 · see citing works
Ruediger, R., Ruiz, J., & Walter, G. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05744-11 · Cited by 98 · see citing works
ZHOU, J., PHAM, H. T., RUEDIGER, R., & WALTER, G. (2003) · Biochemical Journal · doi:10.1042/bj20021244 · Cited by 95 · see citing works
The PP2A Inhibitor I2PP2A Is Essential for Sister Chromatid Segregation in Oocyte Meiosis II
Chambon, J., Touati, S. A., Berneau, S., Cladière, D., Hebras, C., Groeme, R., McDougall, A., & Wassmann, K. (2013) · Current Biology · doi:10.1016/j.cub.2013.02.004 · Cited by 83 · see citing works
Sun, Q., Wu, G., Lai, L., Bonk, A., Cabot, R. A., Park, K., Day, B. N., Prather, R. S., & Schatten, H. (2002) · Biology of Reproduction · doi:10.1095/biolreprod66.3.580 · Cited by 81 · see citing works
Self-citationRattani, A., Wolna, M., Ploquin, M. J.-Y., Helmhart, W., Morrone, S. R., Mayer, B., Godwin, J., Xu, W., Stemmann, O., Pendás, A. M., et al. (2013) · eLife · doi:10.7554/elife.01133 · Cited by 77 · see citing works
Pleiotropic effect of okadaic acid on maturing mouse oocytes
Alexandre, H., Cauwenberge, A. V., Tsukitani, Y., & Mulnard, J. (1991) · Development · doi:10.1242/dev.112.4.971 · Cited by 71 · see citing works
Zhang, D., Ma, W., Li, Y.-H., Hou, Y., Li, S., Meng, X., Sun, X., Sun, Q., & Wang, W. (2004) · Biology of Reproduction · doi:10.1095/biolreprod.104.028282 · Cited by 60 · see citing works
Self-citationEffects of Regulatory Subunits on the Kinetics of Protein Phosphatase 2A
Price, N. E., & Mumby, M. C. (2000) · Biochemistry · doi:10.1021/bi0008478 · Cited by 57 · see citing works
Mailhes, J. B., Hilliard, C., Fuseler, J. W., & London, S. N. (2003) · Chromosome Research · doi:10.1023/a:1024909119593 · Cited by 54 · see citing works
Lu, Q. R., Dunn, R. L., Angeles, R., & Smith, G. D. (2002) · Biology of Reproduction · doi:10.1095/biolreprod66.1.29 · Cited by 51 · see citing works
Initial activation of cyclin‐B1–cdc2 kinase requires phosphorylation of cyclin B1
Peter, M., Peuch, C. J. L., Labbé, J., Meyer, A. N., Donoghue, D. J., & Dorée, M. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf111 · Cited by 47 · see citing works
Molecular insights into mechanisms regulating faithful chromosome separation in female meiosis
Yin, S., Sun, X., Schatten, H., & Sun, Q. (2008) · Cell Cycle · doi:10.4161/cc.7.19.6809 · Cited by 45 · see citing works
Self-citationQi, S., Wang, Z.-B., Ouyang, Y., Zhang, Q.-H., Hu, M., Huang, X., Ge, Z., Guo, L., Wang, Y.-P., Hou, Y., et al. (2013) · Journal of Cell Science · doi:10.1242/jcs.116541 · Cited by 42 · see citing works
Self-citationChang, H.-Y., Jennings, P. C., Stewart, J., Verrills, N. M., & Jones, K. T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.193227 · Cited by 39 · see citing works
Swain, J. E., Wang, X., Saunders, T. L., Dunn, R. L., & Smith, G. D. (2003) · Molecular Reproduction and Development · doi:10.1002/mrd.10258 · Cited by 36 · see citing works
Hu, M., Wang, Z., Schatten, H., & Sun, Q. (2012) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2012.01.004 · Cited by 20 · see citing works
Self-citationRegulation of p34 cdc2 Protein Kinase Activity by Phosphorylation and Cyclin Binding
Nigg, E. A., Gallant, P., & Krek, W. (2007) · Novartis Foundation symposium · doi:10.1002/9780470514320.ch6 · Cited by 13 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Physiologic functions of PP2A: Lessons from genetically modified mice
Reynhout, S., & Janssens, V. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.07.010 · Cited by 124 · see citing works
Regulation of chromosome segregation in oocytes and the cellular basis for female meiotic errors
Greaney, J., Wei, Z., & Homer, H. A. (2017) · Human Reproduction Update · doi:10.1093/humupd/dmx035 · Cited by 111 · see citing works
Causative Mutations and Mechanism of Androgenetic Hydatidiform Moles
Nguyen, N. M., Ge, Z., Reddy, R., Fahiminiya, S., Sauthier, P. G., Bagga, R., Şahin, F. İ., Mahadevan, S. K., Osmond, M., Bréguet, M., et al. (2018) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2018.10.007 · Cited by 113 · see citing works
PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer
(2019) · Advances in Cancer Research · doi:10.1016/bs.acr.2019.03.009 · Cited by 93 · see citing works
Yu, C. Y., Ji, S., Sha, Q., Sun, Q., & Fan, H. (2015) · Nature Communications · doi:10.1038/ncomms9017 · Cited by 81 · see citing works
Self-citationLiu, Q., Li, Y., Feng, Y., Liu, C., Ma, J., Li, Y., Xiang, H., Ji, Y., Cao, Y., Tong, X., et al. (2016) · Scientific Reports · doi:10.1038/srep39638 · Cited by 80 · see citing works
Rahimi, M., Bakhtiarizadeh, M. R., & Mohammadi‐Sangcheshmeh, A. (2016) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2016.11.028 · Cited by 73 · see citing works
Meiotic spindle formation in mammalian oocytes: implications for human infertility†
Namgoong, S., & Kim, N. (2018) · Biology of Reproduction · doi:10.1093/biolre/iox145 · Cited by 61 · see citing works
Biased holoenzyme assembly of protein phosphatase 2A (PP2A): From cancer to small molecules
Haanen, T. J., O’Connor, C. M., & Narla, G. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102656 · Cited by 36 · see citing works
FAM122A, a new endogenous inhibitor of protein phosphatase 2A
Fan, L., Liu, M.-H., Guo, M., Hu, C. X., Yan, Z.-W., Chen, J., Chen, G., & Huang, Y. (2016) · Oncotarget · doi:10.18632/oncotarget.11698 · Cited by 33 · see citing works
PP2A regulates kinetochore-microtubule attachment during meiosis I in oocyte
Tang, A., Shi, P., Song, A., Zou, D., Zhou, Y., Gu, P., Huang, Z., Wang, Q., Lin, Z., & Gao, X. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1175256 · Cited by 29 · see citing works
Genome-wide DNA methylation dynamics during epigenetic reprogramming in the porcine germline
Gómez‐Redondo, I., Planells, B., Cánovas, S., Ivanova, E., Kelsey, G., & Gutiérrez‐Adán, A. (2021) · Clinical Epigenetics · doi:10.1186/s13148-021-01003-x · Cited by 29 · see citing works
Fan, H., & Sun, Q. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813209-8.00012-1 · Cited by 26 · see citing works
Self-citationWang, Y., Pattarawat, P., Zhang, J., Kim, E., Zhang, D., Fang, M., Jannaman, E. A., Yuan, Y., Chatterjee, S., Kim, J.-Y. J., et al. (2023) · Environmental Health Perspectives · doi:10.1289/ehp12034 · Cited by 25 · see citing works
Protein phosphatase 6 is a key factor regulating spermatogenesis
Lei, W., Han, F., Hu, M., Liang, Q., Meng, T., Zhou, Q., Ouyang, Y., Hou, Y., Schatten, H., Wang, Z., et al. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0472-9 · Cited by 22 · see citing works
Self-citationTranscriptome profiling of human oocytes experiencing recurrent total fertilization failure
Suo, L., Zhou, Y., Jia, L. L., Wu, H. B., Zheng, J., Lyu, Q., Sun, L. H., Sun, H., & Kuang, Y. (2018) · Scientific Reports · doi:10.1038/s41598-018-36275-6 · Cited by 23 · see citing works
Protein Phosphatase 6 Protects Prophase I-Arrested Oocytes by Safeguarding Genomic Integrity
Hu, M., Meng, T., Jiang, Z., Dong, M., Schatten, H., Xu, X., Wang, Z., & Sun, Q. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006513 · Cited by 22 · see citing works
Self-citationHu, M., Wang, Z., Teng, Y., Jiang, Z., Ma, X., Hou, N., Cheng, X., Schatten, H., Xu, X., Yang, X. Y., et al. (2015) · Journal of Cell Science · doi:10.1242/jcs.173179 · Cited by 20 · see citing works
Self-citationSexual Dimorphism in Mouse Meiosis
Hua, R., & Liu, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.670599 · Cited by 19 · see citing works
Jang, J. K., Gladstein, A. C., Das, A., Shapiro, J. G., Sisco, Z., & McKim, K. S. (2021) · Journal of Cell Science · doi:10.1242/jcs.254037 · Cited by 18 · see citing works
Li, X., Yao, X., Xie, H., Zhang, G., Deng, M., Deng, K., Gao, X., Bao, Y., Li, K., & Wang, F. (2021) · Theriogenology · doi:10.1016/j.theriogenology.2021.09.026 · Cited by 16 · see citing works
Rad9a is involved in chromatin decondensation and post-zygotic embryo development in mice
Huang, L., Meng, T., Ma, X., Wang, Z.-B., Qi, S., Chen, Q., Zhang, Q.-H., Liang, Q., Wang, Z.-W., Hu, M., et al. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0181-9 · Cited by 15 · see citing works
Self-citationWong, A. Y. W., Oikonomou, V., Paolicelli, G., LUCA, A. D., Pariano, M., Frič, J., Tay, H. S., Ricciardi‐Castagnoli, P., & Zelante, T. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00210 · Cited by 15 · see citing works
Dong, M., Ouyang, Y., Gao, S.-C., Gu, L., Guo, J.-N., Sun, S., Wang, Z., & Sun, Q. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07051-4 · Cited by 13 · see citing works
Self-citationCritical Functions of PP2A-Like Protein Phosphotases in Regulating Meiotic Progression
Lei, W., Qian, W., & Sun, Q. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.638559 · Cited by 11 · see citing works
Self-citationBRG1 promotes progression of B-cell acute lymphoblastic leukemia by disrupting PPP2R1A transcription
Kang, Q., Ma, D., Zhao, P., Chai, X., Huang, Y., Gao, R., Zhang, T., Liu, P., Deng, B., Feng, C., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06996-w · Cited by 11 · see citing works
Wang, Z., Ma, X., Hu, M., Jiang, Z., Meng, T., Dong, M., Fan, L., Ouyang, Y., Snapper, S. B., Schatten, H., et al. (2016) · Molecular Human Reproduction · doi:10.1093/molehr/gaw046 · Cited by 11 · see citing works
Self-citationLlanses, M., Nan, K., Bao, Z., Bacchetti, R., Yuan, S., Tyler, J. J., Guezennec, X. L., Bard, F., & Rainero, E. (2024) · PLoS Biology · doi:10.1371/journal.pbio.3002930 · Cited by 10 · see citing works
Targeting PP2A in cancer: an underrated option
Sarais, F., Krempien, F., Koehn, C., Brewing, L., Classen, C. F., Walter, M., & Shokraie, O. (2025) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-025-03560-y · Cited by 8 · see citing works
Effects of post‐ovulatory aging on centromeric cohesin protection in murine MII oocytes
Shimoi, G., Wakabayashi, R., Ishikawa, R., & Kameyama, Y. (2021) · Reproductive Medicine and Biology · doi:10.1002/rmb2.12433 · Cited by 8 · see citing works
Protein Phosphatase Signaling in Cardiac Myocytes
Abdallah, D., Malhotra, N., & Refaey, M. E. (2022) · Springer eBooks · doi:10.1007/978-3-031-08309-9_5 · Cited by 6 · see citing works
Xu, M., Che, L., Wang, D., Yang, Z., Zhang, P., Lin, Y., Fang, Z., Che, L., Li, J., Chen, D., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135514 · Cited by 6 · see citing works
OTSSP167 leads to follicular dysplasia and negatively affects oocyte quality in mice
Zhang, X.-R., Ouyang, Y., Meng, T., Zhang, H.-Y., Yue, W., Yan, F.-Z., Xue, Y., Schatten, H., Wang, Z., & Sun, Q. (2022) · Toxicology · doi:10.1016/j.tox.2022.153243 · Cited by 6 · see citing works
Self-citationFan, F., Zhao, J., Liu, Y., Zhao, H., Weng, L., Li, Q., Chen, G., & Xu, Y. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.04.135 · Cited by 4 · see citing works
Internalisation of integrin-bound extracellular matrix modulates invasive carcinoma cell migrationPreprint
Llanses, M., Nan, K., Bao, Z., Bacchetti, R., Yuan, S., Tyler, J. J., Guezennec, X. L., Bard, F., & Rainero, E. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.11.575153 · Cited by 4 · see citing works
Bai, Y., Bo, D., Bi, Y., Areb, E., Zhu, H., Pan, C., & Lan, X. (2024) · Animal Reproduction Science · doi:10.1016/j.anireprosci.2024.107544 · Cited by 3 · see citing works
Cytoplasmic granules in bovine oocytes do not affect embryonic or fetal development
Rosa, P. M. D. S., Guedes, P. H. E., Garcia, J. M., & Oliveira, C. S. (2023) · Zygote · doi:10.1017/s0967199423000576 · Cited by 3 · see citing works
PPP6R3-mediated dephosphorylation regulates mRNA translation during spermatogonial differentiation
Fang, Q., Liu, B., Cen, J., Li, T.-T., Ji, S.-H., Li, W.-Q., Lu, G., Chen, Z.-J., Wang, X., Bao, J.-Q., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-08539-1 · Cited by 2 · see citing works
Oscillations in PP1 activity are essential for accurate progression through mammalian oocyte meiosis
Camlin, N. J., Venkatachalam, I., & Evans, J. P. (2023) · Cell Cycle · doi:10.1080/15384101.2023.2225924 · Cited by 2 · see citing works
Uterine secretome: What do the proteins say about maternal-fetal communication in buffaloes?
Codognoto, V. M., de Souza, F. F., Cataldi, T. R., Labate, C. A., de Camargo, L. S., Scott, C., Filho, R. R. D. R., Carvalho, N. A. T., & Oba, E. (2023) · Journal of Proteomics · doi:10.1016/j.jprot.2023.105023 · Cited by 1 · see citing works
Yan, X., & Zhu, X. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1188604 · Cited by 1 · see citing works
Schubert, C. (2014) · Biology of Reproduction · doi:10.1095/biolreprod.114.125294
Gómez‐Redondo, I., Planells, B., Cánovas, S., Ivanova, E., Kelsey, G., & Gutiérrez-Adán, A. (2021) · Figshare · doi:10.6084/m9.figshare.13710749
Gómez‐Redondo, I., Planells, B., Cánovas, S., Ivanova, E., Kelsey, G., & Gutiérrez-Adán, A. (2021) · Figshare · doi:10.6084/m9.figshare.13710731
Gómez‐Redondo, I., Planells, B., Cánovas, S., Ivanova, E., Kelsey, G., & Gutiérrez-Adán, A. (2021) · Figshare · doi:10.6084/m9.figshare.13710740
Gómez‐Redondo, I., Planells, B., Cánovas, S., Ivanova, E., Kelsey, G., & Gutiérrez-Adán, A. (2021) · Figshare · doi:10.6084/m9.figshare.13710734
Gómez‐Redondo, I., Planells, B., Cánovas, S., Ivanova, E., Kelsey, G., & Gutiérrez‐Adán, A. (2021) · Figshare · doi:10.6084/m9.figshare.13710737
- Authors
- Hu, M.-W., Wang, Z.-B., Jiang, Z.-Z., Qi, S.-T., Huang, L., Liang, Q.-X., Schatten, H., & Sun, Q.-Y.
- Affiliations
- Chinese Academy of Sciences (CN)
- University of Missouri (US)
- Corresponding author
- Sun, Qing-Yuan
- Venue
- Biology of Reproduction
- Publisher
- Oxford University Press (OUP)
- Published
- 2014-07-01
- Volume
- 91
- Issue
- 1
- Pages
- 19-19
- ISSN
- 0006-3363 (ISSN-L)
- 1529-7268
- OpenAlex
- W2129736177
- Cited by
- 48
- References
- 38
- Citations by year
- 2025: 2 · 2024: 5 · 2023: 4 · 2022: 3 · 2021: 12 · 2019: 2 · 2018: 8 · 2017: 1 · 2016: 7 · 2015: 3 · 2014: 1
- FWCI
- 3.96
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biology of Reproduction (publishedVersion)
- PubMed (publishedVersion)
- BioOne Complete (BioOne) (submittedVersion)
- Funders
- Chinese Academy of Sciences
- Topics
- Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Reproductive Biology and Fertility
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Reproductive biology and impacts on aquatic species
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- protein phosphatase 2A, PPP2R1A, oocyte maturation, female fertility, subfertility, germinal vesicle breakdown, aneuploidy, sister chromatid separation, folliculogenesis, embryonic development
- MeSH terms
- Animals, Female, Fertility, Meiosis, Oocytes, Oogenesis, Ovulation, Mice, Knockout, Protein Subunits, Mice, Protein Phosphatase 2
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review