Artículos de revistas sobre el tema "Phosphorylation of histone H3 at threonine 3"
Crea una cita precisa en los estilos APA, MLA, Chicago, Harvard y otros
Consulte los 50 mejores artículos de revistas para su investigación sobre el tema "Phosphorylation of histone H3 at threonine 3".
Junto a cada fuente en la lista de referencias hay un botón "Agregar a la bibliografía". Pulsa este botón, y generaremos automáticamente la referencia bibliográfica para la obra elegida en el estilo de cita que necesites: APA, MLA, Harvard, Vancouver, Chicago, etc.
También puede descargar el texto completo de la publicación académica en formato pdf y leer en línea su resumen siempre que esté disponible en los metadatos.
Explore artículos de revistas sobre una amplia variedad de disciplinas y organice su bibliografía correctamente.
Polioudaki, Hara, Yolanda Markaki, Niki Kourmouli, George Dialynas, Panayiotis A. Theodoropoulos, Prim B. Singh y Spyros D. Georgatos. "Mitotic phosphorylation of histone H3 at threonine 3". FEBS Letters 560, n.º 1-3 (4 de febrero de 2004): 39–44. http://dx.doi.org/10.1016/s0014-5793(04)00060-2.
Texto completoHurd, Paul J., Andrew J. Bannister, Karen Halls, Mark A. Dawson, Michiel Vermeulen, Jesper V. Olsen, Heba Ismail et al. "Phosphorylation of Histone H3 Thr-45 Is Linked to Apoptosis". Journal of Biological Chemistry 284, n.º 24 (10 de abril de 2009): 16575–83. http://dx.doi.org/10.1074/jbc.m109.005421.
Texto completoWang, Zhen, Juan Armando Casas-Mollano, Jianping Xu, Jean-Jack M. Riethoven, Chi Zhang y Heriberto Cerutti. "Osmotic stress induces phosphorylation of histone H3 at threonine 3 in pericentromeric regions of Arabidopsis thaliana". Proceedings of the National Academy of Sciences 112, n.º 27 (22 de junio de 2015): 8487–92. http://dx.doi.org/10.1073/pnas.1423325112.
Texto completoŻabka, Aneta, Natalia Gocek, Konrad Winnicki, Paweł Szczeblewski, Tomasz Laskowski y Justyna Teresa Polit. "Changes in Epigenetic Patterns Related to DNA Replication in Vicia faba Root Meristem Cells under Cadmium-Induced Stress Conditions". Cells 10, n.º 12 (3 de diciembre de 2021): 3409. http://dx.doi.org/10.3390/cells10123409.
Texto completoYoshida, Makoto M., Lily Ting, Steven P. Gygi y Yoshiaki Azuma. "SUMOylation of DNA topoisomerase IIα regulates histone H3 kinase Haspin and H3 phosphorylation in mitosis". Journal of Cell Biology 213, n.º 6 (20 de junio de 2016): 665–78. http://dx.doi.org/10.1083/jcb.201511079.
Texto completoKarakkat, Jimsheena V., Suneesh Kaimala, Sreejisha P. Sreedharan, Princy Jayaprakash, Ernest A. Adeghate, Suraiya A. Ansari, Ernesto Guccione, Eric P. K. Mensah-Brown y Bright Starling Emerald. "The metabolic sensor PASK is a histone 3 kinase that also regulates H3K4 methylation by associating with H3K4 MLL2 methyltransferase complex". Nucleic Acids Research 47, n.º 19 (16 de septiembre de 2019): 10086–103. http://dx.doi.org/10.1093/nar/gkz786.
Texto completoKang, Hyoeun, Yong Seok Park, Dong-Hyung Cho, Jae-Sung Kim y Jeong Su Oh. "Dynamics of histone H3 phosphorylation at threonine 3 during meiotic maturation in mouse oocytes". Biochemical and Biophysical Research Communications 458, n.º 2 (marzo de 2015): 280–86. http://dx.doi.org/10.1016/j.bbrc.2015.01.099.
Texto completoWang, Fangwei, Natalia P. Ulyanova, John R. Daum, Debasis Patnaik, Anna V. Kateneva, Gary J. Gorbsky y Jonathan M. G. Higgins. "Haspin inhibitors reveal centromeric functions of Aurora B in chromosome segregation". Journal of Cell Biology 199, n.º 2 (15 de octubre de 2012): 251–68. http://dx.doi.org/10.1083/jcb.201205106.
Texto completoQuadri, Roberto, Sarah Sertic, Anna Ghilardi, Diego Rondelli, Guido Roberto Gallo, Luca Del Giacco y Marco Muzi-Falconi. "Phosphorylation of H3-Thr3 by Haspin Is Required for Primary Cilia Regulation". International Journal of Molecular Sciences 22, n.º 14 (20 de julio de 2021): 7753. http://dx.doi.org/10.3390/ijms22147753.
Texto completoNguyen, A. L., A. S. Gentilello, A. Z. Balboula, V. Shrivastava, J. Ohring y K. Schindler. "Phosphorylation of threonine 3 on histone H3 by haspin kinase is required for meiosis I in mouse oocytes". Journal of Cell Science 127, n.º 23 (14 de octubre de 2014): 5066–78. http://dx.doi.org/10.1242/jcs.158840.
Texto completoCao, Zubing, Tengteng Xu, Xu Tong, Dandan Zhang, Chengxue Liu, Yiqing Wang, Di Gao et al. "HASPIN kinase mediates histone deacetylation to regulate oocyte meiotic maturation in pigs". Reproduction 157, n.º 6 (junio de 2019): 501–10. http://dx.doi.org/10.1530/rep-18-0447.
Texto completoEdgerton, Heather, Marnie Johansson, Daniel Keifenheim, Soumya Mukherjee, Jeremy M. Chacón, Jeff Bachant, Melissa K. Gardner y Duncan J. Clarke. "A noncatalytic function of the topoisomerase II CTD in Aurora B recruitment to inner centromeres during mitosis". Journal of Cell Biology 213, n.º 6 (20 de junio de 2016): 651–64. http://dx.doi.org/10.1083/jcb.201511080.
Texto completoKarimi-Ashtiyani, Raheleh y Andreas Houben. "In Vitro Phosphorylation of Histone H3 at Threonine 3 by Arabidopsis Haspin Is Strongly Influenced by Posttranslational Modifications of Adjacent Amino Acids". Molecular Plant 6, n.º 2 (marzo de 2013): 574–76. http://dx.doi.org/10.1093/mp/sss149.
Texto completoFujimura, Akiko, Yuki Hayashi, Kazashi Kato, Yuichiro Kogure, Mutsuro Kameyama, Haruka Shimamoto, Hiroaki Daitoku, Akiyoshi Fukamizu, Toru Hirota y Keiji Kimura. "Identification of a novel nucleolar protein complex required for mitotic chromosome segregation through centromeric accumulation of Aurora B". Nucleic Acids Research 48, n.º 12 (1 de junio de 2020): 6583–96. http://dx.doi.org/10.1093/nar/gkaa449.
Texto completoThakar, Sumukh, Yash T. Katakia, Shyam Kumar Ramakrishnan, Niyati Pandya Thakkar y Syamantak Majumder. "Intermittent High Glucose Elevates Nuclear Localization of EZH2 to Cause H3K27me3-Dependent Repression of KLF2 Leading to Endothelial Inflammation". Cells 10, n.º 10 (26 de septiembre de 2021): 2548. http://dx.doi.org/10.3390/cells10102548.
Texto completoNishida-Fukuda, Hisayo, Keizo Tokuhiro, Yukio Ando, Hiroaki Matsushita, Morimasa Wada y Hiromitsu Tanaka. "Evaluation of the antiproliferative effects of the HASPIN inhibitor CHR-6494 in breast cancer cell lines". PLOS ONE 16, n.º 4 (14 de abril de 2021): e0249912. http://dx.doi.org/10.1371/journal.pone.0249912.
Texto completoHoek, Maarten, Michael P. Myers y Bruce Stillman. "An Analysis of CAF-1-interacting Proteins Reveals Dynamic and Direct Interactions with the KU Complex and 14-3-3 Proteins". Journal of Biological Chemistry 286, n.º 12 (5 de enero de 2011): 10876–87. http://dx.doi.org/10.1074/jbc.m110.217075.
Texto completoRobert, F., C. Verschraegen, H. Hurwitz, H. Uronis, R. Advani, A. Chen, P. Taverna, M. Wollman, J. Fox y G. Michelson. "A phase I trial of sns-314, a novel and selective pan-aurora kinase inhibitor, in advanced solid tumor patients". Journal of Clinical Oncology 27, n.º 15_suppl (20 de mayo de 2009): 2536. http://dx.doi.org/10.1200/jco.2009.27.15_suppl.2536.
Texto completoKristeleit, R., H. Calvert, H. Arkenau, D. Olmos, J. Adam, E. R. Plummer, V. Lock, M. Squires, L. Fazal y I. Judson. "A phase I study of AT9283, an aurora kinase inhibitor, in patients with refractory solid tumors". Journal of Clinical Oncology 27, n.º 15_suppl (20 de mayo de 2009): 2566. http://dx.doi.org/10.1200/jco.2009.27.15_suppl.2566.
Texto completoHammond, Sharra, Stephanie Byrum, Sarita Namjoshi, Hilary Graves, briana Dennehey, Alan J. Tackett y Jessica Tyler. "Mitotic phosphorylation of histone H3 threonine 80". Cell Cycle 13, n.º 3 (25 de noviembre de 2013): 440–52. http://dx.doi.org/10.4161/cc.27269.
Texto completoOkabe, Seiichi, Tetsuzo Tauchi, Yuko Tanaka, Toshihiko Kitahara y Kazuma Ohyashiki. "Efficacy Of The Polo-Like Kinase Inhibitor, Rigosertib Alone Or In Combination With ABL Tyrosine Kinase Inhibitor Against BCR-ABL-Positive Leukemia Cells". Blood 122, n.º 21 (15 de noviembre de 2013): 3985. http://dx.doi.org/10.1182/blood.v122.21.3985.3985.
Texto completoFong, Jerry J., Brenda L. Nguyen, Robert Bridger, Estela E. Medrano, Lance Wells, Shujuan Pan y Richard N. Sifers. "β-N-Acetylglucosamine (O-GlcNAc) Is a Novel Regulator of Mitosis-specific Phosphorylations on Histone H3". Journal of Biological Chemistry 287, n.º 15 (27 de febrero de 2012): 12195–203. http://dx.doi.org/10.1074/jbc.m111.315804.
Texto completoMahadevan, Daruka, Wenqing Qi, Laurence Cooke, Xiabing Lui, Daniel Oscar Persky, Lisa M. Rimsza y Thomas P. Miller. "Targeting Aurora Kinase in Aggressive B-Cell Non-Hodgkin's Lymphomas." Blood 114, n.º 22 (20 de noviembre de 2009): 284. http://dx.doi.org/10.1182/blood.v114.22.284.284.
Texto completoMartinez, Danielle R., Hunter W. Richards, Qiushi Lin, Carlos A. Torres-Cabala, Victor G. Prieto, Jonathan L. Curry y Estela E. Medrano. "H3K79me3T80ph is a Novel Histone Dual Modification and a Mitotic Indicator in Melanoma". Journal of Skin Cancer 2012 (2012): 1–9. http://dx.doi.org/10.1155/2012/823534.
Texto completoXie, Jing, Matthew Wooten, Vuong Tran, Bi-Chang Chen, Caitlin Pozmanter, Christine Simbolon, Eric Betzig y Xin Chen. "Histone H3 Threonine Phosphorylation Regulates Asymmetric Histone Inheritance in the Drosophila Male Germline". Cell 163, n.º 4 (noviembre de 2015): 920–33. http://dx.doi.org/10.1016/j.cell.2015.10.002.
Texto completoZeitlin, S. G., C. M. Barber, C. D. Allis y K. Sullivan. "Differential regulation of CENP-A and histone H3 phosphorylation in G2/M". Journal of Cell Science 114, n.º 4 (15 de febrero de 2001): 653–61. http://dx.doi.org/10.1242/jcs.114.4.653.
Texto completoChen, Lisa S., William G. Wierda, Sanjeev Redkar, David J. Bearss y Varsha Gandhi. "Pim Kinase Inhibitor, SGI-1776, Induces Apoptosis in CLL Lymphocytes". Blood 112, n.º 11 (16 de noviembre de 2008): 4199. http://dx.doi.org/10.1182/blood.v112.11.4199.4199.
Texto completoSun, Guangyan C., Anna C. Shvab, Bin C. Li, Felipe C. Beckedorff, Guy Jacques Leclerc, Ramin Shiekhattar y Julio C. Barredo. "Acadesine Elicits a Rapid Epigenetic Reprograming of Immediate Early Genes through the Protein Kinase D1 Pathway in Acute Lymphoblastic Leukemia Cells Undergoing Energy/Metabolic Stress". Blood 132, Supplement 1 (29 de noviembre de 2018): 1321. http://dx.doi.org/10.1182/blood-2018-99-112678.
Texto completoBui, H. T., V. T. Nguyen, T. Wakayama y T. Miyano. "123 HISTONE H3 MODIFICATIONS IN PIG OOCYTES DURING GROWTH, MATURATION, AND ACTIVATION". Reproduction, Fertility and Development 18, n.º 2 (2006): 170. http://dx.doi.org/10.1071/rdv18n2ab123.
Texto completoWaterborg, Jakob H. "Evolution of histone H3: emergence of variants and conservation of post-translational modification sites1This article is part of Special Issue entitled Asilomar Chromatin and has undergone the Journal’s usual peer review process." Biochemistry and Cell Biology 90, n.º 1 (febrero de 2012): 79–95. http://dx.doi.org/10.1139/o11-036.
Texto completoWalter, Wendy, David Clynes, Yong Tang, Ronen Marmorstein, Jane Mellor y Shelley L. Berger. "14-3-3 Interaction with Histone H3 Involves a Dual Modification Pattern of Phosphoacetylation". Molecular and Cellular Biology 28, n.º 8 (11 de febrero de 2008): 2840–49. http://dx.doi.org/10.1128/mcb.01457-07.
Texto completoBui Hong, T., L. G. Villa-Diaz, E. Yamaoka y T. Miyano. "309CHROMOSOME CONDENSATION IS CORRELATED WITH HISTONE H3 PHOSPHORYLATION WITHOUT CDC2 KINASE AND MAP KINASE ACTIVITIES IN PIG OOCYTES". Reproduction, Fertility and Development 16, n.º 2 (2004): 273. http://dx.doi.org/10.1071/rdv16n1ab309.
Texto completoOkabe, Seiichi, Tetsuzo Tauchi, Seiichiro Katagiri, Yuko Tanaka y Kazuma Ohyashiki. "Activity of the Aurora Kinase Inhibitor, MLN8237 (alisertib) Alone or in Combination with Ponatinib Against Imatinib-Resistant BCR-ABL-Positive Cells". Blood 120, n.º 21 (16 de noviembre de 2012): 1333. http://dx.doi.org/10.1182/blood.v120.21.1333.1333.
Texto completoMetzger, Eric, Na Yin, Melanie Wissmann, Natalia Kunowska, Kristin Fischer, Nicolaus Friedrichs, Debasis Patnaik et al. "Phosphorylation of histone H3 at threonine 11 establishes a novel chromatin mark for transcriptional regulation". Nature Cell Biology 10, n.º 1 (9 de diciembre de 2007): 53–60. http://dx.doi.org/10.1038/ncb1668.
Texto completoTan, Ee Phie, Sarah Caro, Anish Potnis, Christopher Lanza y Chad Slawson. "O-Linked N-Acetylglucosamine Cycling Regulates Mitotic Spindle Organization". Journal of Biological Chemistry 288, n.º 38 (14 de agosto de 2013): 27085–99. http://dx.doi.org/10.1074/jbc.m113.470187.
Texto completoNiedzialkowska, Ewa, Fangwei Wang, Przemyslaw J. Porebski, Wladek Minor, Jonathan M. G. Higgins y P. Todd Stukenberg. "Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogues at inner centromeres". Molecular Biology of the Cell 23, n.º 8 (15 de abril de 2012): 1457–66. http://dx.doi.org/10.1091/mbc.e11-11-0904.
Texto completoDastidar, Eeshita G., Kristina Dzeyk, Jeroen Krijgsveld, Nicholas A. Malmquist, Christian Doerig, Artur Scherf y Jose-Juan Lopez-Rubio. "Comprehensive Histone Phosphorylation Analysis and Identification of Pf14-3-3 Protein as a Histone H3 Phosphorylation Reader in Malaria Parasites". PLoS ONE 8, n.º 1 (7 de enero de 2013): e53179. http://dx.doi.org/10.1371/journal.pone.0053179.
Texto completoParwani, Kiran, Jennifer Spangle, Leon McSwain, Ramona Haji Seyed Javadi, Anna Kenney y David Yu. "DNAR-06. LOSS OF HISTONE H3 THREONINE 45 PHOSPHORYLATION DECREASES H3K36ME3 TO ABROGATE THE RADIATION-INDUCED DNA DAMAGE IN GLIOBLASTOMA MULTIFORME". Neuro-Oncology 24, Supplement_7 (1 de noviembre de 2022): vii91. http://dx.doi.org/10.1093/neuonc/noac209.338.
Texto completoEspinos, Estelle, Agathe Le Van Thaï, Christelle Pomiès y Michel J. Weber. "Cooperation between Phosphorylation and Acetylation Processes in Transcriptional Control". Molecular and Cellular Biology 19, n.º 5 (1 de mayo de 1999): 3474–84. http://dx.doi.org/10.1128/mcb.19.5.3474.
Texto completoHarrison, J. G. y A. Clerk. "Phosphorylation of Histone 3 (H3) in cardiac myocytes subjected to hyperosmotic shock". Biochemical Society Transactions 28, n.º 5 (1 de octubre de 2000): A429. http://dx.doi.org/10.1042/bst028a429a.
Texto completoWeissmann, Frank, Inhua Muyrers-Chen, Tanja Musch, Dirk Stach, Manfred Wiessler, Renato Paro y Frank Lyko. "DNA Hypermethylation in Drosophila melanogaster Causes Irregular Chromosome Condensation and Dysregulation of Epigenetic Histone Modifications". Molecular and Cellular Biology 23, n.º 7 (1 de abril de 2003): 2577–86. http://dx.doi.org/10.1128/mcb.23.7.2577-2586.2003.
Texto completoSmith, James A. H., Tertius A. Kohn, Ashley K. Chetty y Edward O. Ojuka. "CaMK activation during exercise is required for histone hyperacetylation and MEF2A binding at the MEF2 site on the Glut4 gene". American Journal of Physiology-Endocrinology and Metabolism 295, n.º 3 (septiembre de 2008): E698—E704. http://dx.doi.org/10.1152/ajpendo.00747.2007.
Texto completoKelly, Alexander E., Cristina Ghenoiu, John Z. Xue, Christian Zierhut, Hiroshi Kimura y Hironori Funabiki. "Survivin Reads Phosphorylated Histone H3 Threonine 3 to Activate the Mitotic Kinase Aurora B". Science 330, n.º 6001 (12 de agosto de 2010): 235–39. http://dx.doi.org/10.1126/science.1189505.
Texto completoChandrasekaran, V., G. Katona, M. I. Bokarewa, K. M. Andersson, M. C. Erlandsson, M. Jensen, N. Oparina y A. Damdimopoulos. "POS0397 AGGREGATED SURVIVIN BINDING AROUND HISTONE H3 EPIGENETIC MODIFICATIONS IN RISK LOCI ASSOCIATED WITH RHEUMATOID ARTHRITIS". Annals of the Rheumatic Diseases 80, Suppl 1 (19 de mayo de 2021): 428.1–428. http://dx.doi.org/10.1136/annrheumdis-2021-eular.3212.
Texto completoPancholi, Vijaykumar y Vincent A. Fischetti. "Regulation of the Phosphorylation of Human Pharyngeal Cell Proteins by Group A Streptococcal Surface Dehydrogenase: Signal Transduction between Streptococci and Pharyngeal Cells". Journal of Experimental Medicine 186, n.º 10 (17 de noviembre de 1997): 1633–43. http://dx.doi.org/10.1084/jem.186.10.1633.
Texto completoLucero, Héctor A., Néstor Cortez y Rubén H. Vallejos. "Light modulation of serine and threonine phosphorylation in histone III by thylakoids". Biochimica et Biophysica Acta (BBA) - Bioenergetics 890, n.º 1 (enero de 1987): 77–81. http://dx.doi.org/10.1016/0005-2728(87)90070-3.
Texto completoHappel, Nicole, Stefan Stoldt, Bernhard Schmidt y Detlef Doenecke. "M Phase-Specific Phosphorylation of Histone H1.5 at Threonine 10 by GSK-3". Journal of Molecular Biology 386, n.º 2 (febrero de 2009): 339–50. http://dx.doi.org/10.1016/j.jmb.2008.12.047.
Texto completoChandrasekaran, V., M. I. Bokarewa, N. Oparina, K. M. Andersson, G. Katona, M. Erlandsson, M. Jensen y A. Damdimopoulos. "POS0032 FUNCTIONAL ROLE OF SURVIVIN IN ORGANIZATION OF BIVALENT CHROMATIN REGIONS AND CONSEQUENCE FOR ARTHRITIS-RELEVANT GENE EXPRESSION". Annals of the Rheumatic Diseases 81, Suppl 1 (23 de mayo de 2022): 231.3–231. http://dx.doi.org/10.1136/annrheumdis-2022-eular.4856.
Texto completoFeizbakhsh, Omid, Florian Pontheaux, Virginie Glippa, Julia Morales, Sandrine Ruchaud, Patrick Cormier y Fernando Roch. "A Peak of H3T3 Phosphorylation Occurs in Synchrony with Mitosis in Sea Urchin Early Embryos". Cells 9, n.º 4 (7 de abril de 2020): 898. http://dx.doi.org/10.3390/cells9040898.
Texto completoLi, Ji, Peili Chen, Natasha Sinogeeva, Myriam Gorospe, Robert P. Wersto, Francis J. Chrest, Janice Barnes y Yusen Liu. "Arsenic Trioxide Promotes Histone H3 Phosphoacetylation at the Chromatin ofCASPASE-10in Acute Promyelocytic Leukemia Cells". Journal of Biological Chemistry 277, n.º 51 (17 de octubre de 2002): 49504–10. http://dx.doi.org/10.1074/jbc.m207836200.
Texto completo