Artigos de revistas sobre o tema "Phosphorylation of histone H3 at threonine 3"
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Polioudaki, Hara, Yolanda Markaki, Niki Kourmouli, George Dialynas, Panayiotis A. Theodoropoulos, Prim B. Singh e Spyros D. Georgatos. "Mitotic phosphorylation of histone H3 at threonine 3". FEBS Letters 560, n.º 1-3 (4 de fevereiro de 2004): 39–44. http://dx.doi.org/10.1016/s0014-5793(04)00060-2.
Texto completo da fonteHurd, 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 completo da fonteWang, Zhen, Juan Armando Casas-Mollano, Jianping Xu, Jean-Jack M. Riethoven, Chi Zhang e 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 junho de 2015): 8487–92. http://dx.doi.org/10.1073/pnas.1423325112.
Texto completo da fonteŻabka, Aneta, Natalia Gocek, Konrad Winnicki, Paweł Szczeblewski, Tomasz Laskowski e 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 dezembro de 2021): 3409. http://dx.doi.org/10.3390/cells10123409.
Texto completo da fonteYoshida, Makoto M., Lily Ting, Steven P. Gygi e 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 junho de 2016): 665–78. http://dx.doi.org/10.1083/jcb.201511079.
Texto completo da fonteKarakkat, Jimsheena V., Suneesh Kaimala, Sreejisha P. Sreedharan, Princy Jayaprakash, Ernest A. Adeghate, Suraiya A. Ansari, Ernesto Guccione, Eric P. K. Mensah-Brown e 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 setembro de 2019): 10086–103. http://dx.doi.org/10.1093/nar/gkz786.
Texto completo da fonteKang, Hyoeun, Yong Seok Park, Dong-Hyung Cho, Jae-Sung Kim e 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 (março de 2015): 280–86. http://dx.doi.org/10.1016/j.bbrc.2015.01.099.
Texto completo da fonteWang, Fangwei, Natalia P. Ulyanova, John R. Daum, Debasis Patnaik, Anna V. Kateneva, Gary J. Gorbsky e 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 outubro de 2012): 251–68. http://dx.doi.org/10.1083/jcb.201205106.
Texto completo da fonteQuadri, Roberto, Sarah Sertic, Anna Ghilardi, Diego Rondelli, Guido Roberto Gallo, Luca Del Giacco e 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 julho de 2021): 7753. http://dx.doi.org/10.3390/ijms22147753.
Texto completo da fonteNguyen, A. L., A. S. Gentilello, A. Z. Balboula, V. Shrivastava, J. Ohring e 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 outubro de 2014): 5066–78. http://dx.doi.org/10.1242/jcs.158840.
Texto completo da fonteCao, 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 (junho de 2019): 501–10. http://dx.doi.org/10.1530/rep-18-0447.
Texto completo da fonteEdgerton, Heather, Marnie Johansson, Daniel Keifenheim, Soumya Mukherjee, Jeremy M. Chacón, Jeff Bachant, Melissa K. Gardner e 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 junho de 2016): 651–64. http://dx.doi.org/10.1083/jcb.201511080.
Texto completo da fonteKarimi-Ashtiyani, Raheleh, e 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 (março de 2013): 574–76. http://dx.doi.org/10.1093/mp/sss149.
Texto completo da fonteFujimura, Akiko, Yuki Hayashi, Kazashi Kato, Yuichiro Kogure, Mutsuro Kameyama, Haruka Shimamoto, Hiroaki Daitoku, Akiyoshi Fukamizu, Toru Hirota e 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 junho de 2020): 6583–96. http://dx.doi.org/10.1093/nar/gkaa449.
Texto completo da fonteThakar, Sumukh, Yash T. Katakia, Shyam Kumar Ramakrishnan, Niyati Pandya Thakkar e 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 setembro de 2021): 2548. http://dx.doi.org/10.3390/cells10102548.
Texto completo da fonteNishida-Fukuda, Hisayo, Keizo Tokuhiro, Yukio Ando, Hiroaki Matsushita, Morimasa Wada e 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 completo da fonteHoek, Maarten, Michael P. Myers e 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 janeiro de 2011): 10876–87. http://dx.doi.org/10.1074/jbc.m110.217075.
Texto completo da fonteRobert, F., C. Verschraegen, H. Hurwitz, H. Uronis, R. Advani, A. Chen, P. Taverna, M. Wollman, J. Fox e 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 maio de 2009): 2536. http://dx.doi.org/10.1200/jco.2009.27.15_suppl.2536.
Texto completo da fonteKristeleit, R., H. Calvert, H. Arkenau, D. Olmos, J. Adam, E. R. Plummer, V. Lock, M. Squires, L. Fazal e 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 maio de 2009): 2566. http://dx.doi.org/10.1200/jco.2009.27.15_suppl.2566.
Texto completo da fonteHammond, Sharra, Stephanie Byrum, Sarita Namjoshi, Hilary Graves, briana Dennehey, Alan J. Tackett e Jessica Tyler. "Mitotic phosphorylation of histone H3 threonine 80". Cell Cycle 13, n.º 3 (25 de novembro de 2013): 440–52. http://dx.doi.org/10.4161/cc.27269.
Texto completo da fonteOkabe, Seiichi, Tetsuzo Tauchi, Yuko Tanaka, Toshihiko Kitahara e 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 novembro de 2013): 3985. http://dx.doi.org/10.1182/blood.v122.21.3985.3985.
Texto completo da fonteFong, Jerry J., Brenda L. Nguyen, Robert Bridger, Estela E. Medrano, Lance Wells, Shujuan Pan e 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 fevereiro de 2012): 12195–203. http://dx.doi.org/10.1074/jbc.m111.315804.
Texto completo da fonteMahadevan, Daruka, Wenqing Qi, Laurence Cooke, Xiabing Lui, Daniel Oscar Persky, Lisa M. Rimsza e Thomas P. Miller. "Targeting Aurora Kinase in Aggressive B-Cell Non-Hodgkin's Lymphomas." Blood 114, n.º 22 (20 de novembro de 2009): 284. http://dx.doi.org/10.1182/blood.v114.22.284.284.
Texto completo da fonteMartinez, Danielle R., Hunter W. Richards, Qiushi Lin, Carlos A. Torres-Cabala, Victor G. Prieto, Jonathan L. Curry e 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 completo da fonteXie, Jing, Matthew Wooten, Vuong Tran, Bi-Chang Chen, Caitlin Pozmanter, Christine Simbolon, Eric Betzig e Xin Chen. "Histone H3 Threonine Phosphorylation Regulates Asymmetric Histone Inheritance in the Drosophila Male Germline". Cell 163, n.º 4 (novembro de 2015): 920–33. http://dx.doi.org/10.1016/j.cell.2015.10.002.
Texto completo da fonteZeitlin, S. G., C. M. Barber, C. D. Allis e K. Sullivan. "Differential regulation of CENP-A and histone H3 phosphorylation in G2/M". Journal of Cell Science 114, n.º 4 (15 de fevereiro de 2001): 653–61. http://dx.doi.org/10.1242/jcs.114.4.653.
Texto completo da fonteChen, Lisa S., William G. Wierda, Sanjeev Redkar, David J. Bearss e Varsha Gandhi. "Pim Kinase Inhibitor, SGI-1776, Induces Apoptosis in CLL Lymphocytes". Blood 112, n.º 11 (16 de novembro de 2008): 4199. http://dx.doi.org/10.1182/blood.v112.11.4199.4199.
Texto completo da fonteSun, Guangyan C., Anna C. Shvab, Bin C. Li, Felipe C. Beckedorff, Guy Jacques Leclerc, Ramin Shiekhattar e 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 novembro de 2018): 1321. http://dx.doi.org/10.1182/blood-2018-99-112678.
Texto completo da fonteBui, H. T., V. T. Nguyen, T. Wakayama e 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 completo da fonteWaterborg, 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 (fevereiro de 2012): 79–95. http://dx.doi.org/10.1139/o11-036.
Texto completo da fonteWalter, Wendy, David Clynes, Yong Tang, Ronen Marmorstein, Jane Mellor e 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 fevereiro de 2008): 2840–49. http://dx.doi.org/10.1128/mcb.01457-07.
Texto completo da fonteBui Hong, T., L. G. Villa-Diaz, E. Yamaoka e 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 completo da fonteOkabe, Seiichi, Tetsuzo Tauchi, Seiichiro Katagiri, Yuko Tanaka e 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 novembro de 2012): 1333. http://dx.doi.org/10.1182/blood.v120.21.1333.1333.
Texto completo da fonteMetzger, 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 dezembro de 2007): 53–60. http://dx.doi.org/10.1038/ncb1668.
Texto completo da fonteTan, Ee Phie, Sarah Caro, Anish Potnis, Christopher Lanza e 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 completo da fonteNiedzialkowska, Ewa, Fangwei Wang, Przemyslaw J. Porebski, Wladek Minor, Jonathan M. G. Higgins e 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 completo da fonteDastidar, Eeshita G., Kristina Dzeyk, Jeroen Krijgsveld, Nicholas A. Malmquist, Christian Doerig, Artur Scherf e 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 janeiro de 2013): e53179. http://dx.doi.org/10.1371/journal.pone.0053179.
Texto completo da fonteParwani, Kiran, Jennifer Spangle, Leon McSwain, Ramona Haji Seyed Javadi, Anna Kenney e 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 novembro de 2022): vii91. http://dx.doi.org/10.1093/neuonc/noac209.338.
Texto completo da fonteEspinos, Estelle, Agathe Le Van Thaï, Christelle Pomiès e Michel J. Weber. "Cooperation between Phosphorylation and Acetylation Processes in Transcriptional Control". Molecular and Cellular Biology 19, n.º 5 (1 de maio de 1999): 3474–84. http://dx.doi.org/10.1128/mcb.19.5.3474.
Texto completo da fonteHarrison, J. G., e A. Clerk. "Phosphorylation of Histone 3 (H3) in cardiac myocytes subjected to hyperosmotic shock". Biochemical Society Transactions 28, n.º 5 (1 de outubro de 2000): A429. http://dx.doi.org/10.1042/bst028a429a.
Texto completo da fonteWeissmann, Frank, Inhua Muyrers-Chen, Tanja Musch, Dirk Stach, Manfred Wiessler, Renato Paro e 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 completo da fonteSmith, James A. H., Tertius A. Kohn, Ashley K. Chetty e 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 (setembro de 2008): E698—E704. http://dx.doi.org/10.1152/ajpendo.00747.2007.
Texto completo da fonteKelly, Alexander E., Cristina Ghenoiu, John Z. Xue, Christian Zierhut, Hiroshi Kimura e 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 completo da fonteChandrasekaran, V., G. Katona, M. I. Bokarewa, K. M. Andersson, M. C. Erlandsson, M. Jensen, N. Oparina e 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 maio de 2021): 428.1–428. http://dx.doi.org/10.1136/annrheumdis-2021-eular.3212.
Texto completo da fontePancholi, Vijaykumar, e 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 novembro de 1997): 1633–43. http://dx.doi.org/10.1084/jem.186.10.1633.
Texto completo da fonteLucero, Héctor A., Néstor Cortez e 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 (janeiro de 1987): 77–81. http://dx.doi.org/10.1016/0005-2728(87)90070-3.
Texto completo da fonteHappel, Nicole, Stefan Stoldt, Bernhard Schmidt e Detlef Doenecke. "M Phase-Specific Phosphorylation of Histone H1.5 at Threonine 10 by GSK-3". Journal of Molecular Biology 386, n.º 2 (fevereiro de 2009): 339–50. http://dx.doi.org/10.1016/j.jmb.2008.12.047.
Texto completo da fonteChandrasekaran, V., M. I. Bokarewa, N. Oparina, K. M. Andersson, G. Katona, M. Erlandsson, M. Jensen e 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 maio de 2022): 231.3–231. http://dx.doi.org/10.1136/annrheumdis-2022-eular.4856.
Texto completo da fonteFeizbakhsh, Omid, Florian Pontheaux, Virginie Glippa, Julia Morales, Sandrine Ruchaud, Patrick Cormier e 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 completo da fonteLi, Ji, Peili Chen, Natasha Sinogeeva, Myriam Gorospe, Robert P. Wersto, Francis J. Chrest, Janice Barnes e 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 outubro de 2002): 49504–10. http://dx.doi.org/10.1074/jbc.m207836200.
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