Статті в журналах з теми "PIP5K1"
Оформте джерело за APA, MLA, Chicago, Harvard та іншими стилями
Ознайомтеся з топ-50 статей у журналах для дослідження на тему "PIP5K1".
Біля кожної праці в переліку літератури доступна кнопка «Додати до бібліографії». Скористайтеся нею – і ми автоматично оформимо бібліографічне посилання на обрану працю в потрібному вам стилі цитування: APA, MLA, «Гарвард», «Чикаго», «Ванкувер» тощо.
Також ви можете завантажити повний текст наукової публікації у форматі «.pdf» та прочитати онлайн анотацію до роботи, якщо відповідні параметри наявні в метаданих.
Переглядайте статті в журналах для різних дисциплін та оформлюйте правильно вашу бібліографію.
Kawase, Atsushi, Yuta Inoue, Miho Hirosoko, Yuka Sugihara, Hiroaki Shimada, and Masahiro Iwaki. "Decrease in Multidrug Resistance-associated Protein 2 Activities by Knockdown of Phosphatidylinositol 4-phosphate 5-kinase in Hepatocytes and Cancer Cells." Journal of Pharmacy & Pharmaceutical Sciences 22 (November 19, 2019): 576–84. http://dx.doi.org/10.18433/jpps30444.
Повний текст джерелаWright, Brittany D., Catherine Simpson, Michael Stashko, Dmitri Kireev, Emily A. Hull-Ryde, Mark J. Zylka, and William P. Janzen. "Development of a High-Throughput Screening Assay to Identify Inhibitors of the Lipid Kinase PIP5K1C." Journal of Biomolecular Screening 20, no. 5 (December 22, 2014): 655–62. http://dx.doi.org/10.1177/1087057114564057.
Повний текст джерелаKhadka, Bijendra, and Radhey S. Gupta. "Novel Molecular Signatures in the PIP4K/PIP5K Family of Proteins Specific for Different Isozymes and Subfamilies Provide Important Insights into the Evolutionary Divergence of this Protein Family." Genes 10, no. 4 (April 21, 2019): 312. http://dx.doi.org/10.3390/genes10040312.
Повний текст джерелаWang, Yanfeng, Lurong Lian, Aae Suzuki, Rustem I. Litvinov, Timothy J. Stalker, Alec A. Schmaier, Lawrence F. Brass, John Weisel, and Charles S. Abrams. "Loss of Individual PIP5KI Isoforms Demonstrate That Spatial PIP2 Synthesis Is Required for Platelet Second Messenger Formation & Integrity of the Actin Cytoskeleton." Blood 112, no. 11 (November 16, 2008): 109. http://dx.doi.org/10.1182/blood.v112.11.109.109.
Повний текст джерелаPadrón, David, Ying Jie Wang, Masaya Yamamoto, Helen Yin та Michael G. Roth. "Phosphatidylinositol phosphate 5-kinase Iβ recruits AP-2 to the plasma membrane and regulates rates of constitutive endocytosis". Journal of Cell Biology 162, № 4 (11 серпня 2003): 693–701. http://dx.doi.org/10.1083/jcb.200302051.
Повний текст джерелаClarke, Jonathan H., Piers C. Emson та Robin F. Irvine. "Localization of phosphatidylinositol phosphate kinase IIγ in kidney to a membrane trafficking compartment within specialized cells of the nephron". American Journal of Physiology-Renal Physiology 295, № 5 (листопад 2008): F1422—F1430. http://dx.doi.org/10.1152/ajprenal.90310.2008.
Повний текст джерелаBultsma, Yvette, Willem-Jan Keune та Nullin Divecha. "PIP4Kβ interacts with and modulates nuclear localization of the high-activity PtdIns5P-4-kinase isoform PIP4Kα". Biochemical Journal 430, № 2 (13 серпня 2010): 223–35. http://dx.doi.org/10.1042/bj20100341.
Повний текст джерелаChen, Xinsheng, Yanfeng Wang, Tami L. Bach, Lurong Lian, Rustem I. Litvinov, John W. Weisel та Charles S. Abrams. "Mice Lacking PIP5Kβ or PIP5Kγ Have Unique Cytoskeletal Changes within Their Megakaryocytes & Platelets." Blood 106, № 11 (16 листопада 2005): 380. http://dx.doi.org/10.1182/blood.v106.11.380.380.
Повний текст джерелаWang, Yanfeng, Aae Suzuki, Lurong Lian, Rustem I. Litvinov, Timothy J. Stalker, John K. Choi, John W. Weisel, Lawrence F. Brass та Charles S. Abrams. "Platelets Lacking PIP5KIγ Have Impaired Cytoskeletal Dynamics and Adhesion, but No Defect in Integrin Activation." Blood 114, № 22 (20 листопада 2009): 772. http://dx.doi.org/10.1182/blood.v114.22.772.772.
Повний текст джерелаDrake, J. M., and J. Huang. "PIP5K1 inhibition as a therapeutic strategy for prostate cancer." Proceedings of the National Academy of Sciences 111, no. 35 (August 12, 2014): 12578–79. http://dx.doi.org/10.1073/pnas.1413363111.
Повний текст джерелаAikawa, Yoshikatsu, and Thomas F. J. Martin. "ARF6 regulates a plasma membrane pool of phosphatidylinositol(4,5)bisphosphate required for regulated exocytosis." Journal of Cell Biology 162, no. 4 (August 18, 2003): 647–59. http://dx.doi.org/10.1083/jcb.200212142.
Повний текст джерелаFairn, Gregory D., Koji Ogata, Roberto J. Botelho, Philip D. Stahl, Richard A. Anderson, Pietro De Camilli, Tobias Meyer, Shoshana Wodak, and Sergio Grinstein. "An electrostatic switch displaces phosphatidylinositol phosphate kinases from the membrane during phagocytosis." Journal of Cell Biology 187, no. 5 (November 30, 2009): 701–14. http://dx.doi.org/10.1083/jcb.200909025.
Повний текст джерелаWang, Yanfeng, Rustem Litvinov, John W. Weisel, John H. Hartwig та Charles S. Abrams. "PIP5KIγ Knockout Megakaryocytes Have Defects in Their Cytoskeleton & Demarcation Membrane System, yet Form Proplatlets & Platelets." Blood 108, № 11 (16 листопада 2006): 1793. http://dx.doi.org/10.1182/blood.v108.11.1793.1793.
Повний текст джерелаZeng, Xuankun, Arzu Uyar, Dexin Sui, Nazanin Donyapour, Dianqing Wu, Alex Dickson та Jian Hu. "Structural insights into lethal contractural syndrome type 3 (LCCS3) caused by a missense mutation of PIP5Kγ". Biochemical Journal 475, № 14 (25 липня 2018): 2257–69. http://dx.doi.org/10.1042/bcj20180326.
Повний текст джерелаHassan, Bassem A., Sergei N. Prokopenko, Sebastian Breuer, Bing Zhang, Achim Paululat, and Hugo J. Bellen. "skittles, a Drosophila Phosphatidylinositol 4-Phosphate 5-Kinase, Is Required for Cell Viability, Germline Development and Bristle Morphology, But Not for Neurotransmitter Release." Genetics 150, no. 4 (December 1, 1998): 1527–37. http://dx.doi.org/10.1093/genetics/150.4.1527.
Повний текст джерелаKuroda, Ryo, Mariko Kato, Tomohiko Tsuge, and Takashi Aoyama. "Arabidopsis phosphatidylinositol 4‐phosphate 5‐kinase genes PIP5K7 , PIP5K8 , and PIP5K9 are redundantly involved in root growth adaptation to osmotic stress." Plant Journal 106, no. 4 (April 5, 2021): 913–27. http://dx.doi.org/10.1111/tpj.15207.
Повний текст джерелаParkhitko, Andrey A., Arashdeep Singh, Sharon Hsieh, Yanhui Hu, Richard Binari, Christopher J. Lord, Sridhar Hannenhalli, Colm J. Ryan, and Norbert Perrimon. "Cross-species identification of PIP5K1-, splicing- and ubiquitin-related pathways as potential targets for RB1-deficient cells." PLOS Genetics 17, no. 2 (February 16, 2021): e1009354. http://dx.doi.org/10.1371/journal.pgen.1009354.
Повний текст джерелаWang, Xiaoxiang, Lan Yu, Xing Xiong, Yao Chen, and Bo Men. "Bone Marrow Mesenchymal Stem Cells (BMSCs) Transplantation Alleviates Acute Pancreatitis Through Inhibiting Inflammation and Promoting Caspase-8 Apoptosis Pathway." Journal of Biomaterials and Tissue Engineering 12, no. 5 (May 1, 2022): 1034–39. http://dx.doi.org/10.1166/jbt.2022.2969.
Повний текст джерелаWang, Yanfeng, Lurong Lian, Tami L. Bach, Xinsheng Chen, Qing-Min Chen та Charles S. Abrams. "PIP5Kγ-Null Mutation Induces Cytoskeletal Changes within Megakaryocytes." Blood 104, № 11 (16 листопада 2004): 629. http://dx.doi.org/10.1182/blood.v104.11.629.629.
Повний текст джерелаChen, Xinsheng, Yanfeng Wang, Edward K. Williamson, Timothy J. Stalker, Lawrence F. Brass, Morris J. Birnbaum, John H. Harwig та Charles S. Abrams. "Loss of PIP5KIβ Causes a Defect in Lamellipodia Formation and Shear Resistant Adhesion." Blood 108, № 11 (16 листопада 2006): 141. http://dx.doi.org/10.1182/blood.v108.11.141.141.
Повний текст джерелаSemenas, J., A. Hedblom, R. R. Miftakhova, M. Sarwar, R. Larsson, L. Shcherbina, M. E. Johansson, P. Harkonen, O. Sterner, and J. L. Persson. "The role of PI3K/AKT-related PIP5K1 and the discovery of its selective inhibitor for treatment of advanced prostate cancer." Proceedings of the National Academy of Sciences 111, no. 35 (July 28, 2014): E3689—E3698. http://dx.doi.org/10.1073/pnas.1405801111.
Повний текст джерелаLiu, Aizhuo, Dexin Sui, Dianqing Wu, and Jian Hu. "The activation loop of PIP5K functions as a membrane sensor essential for lipid substrate processing." Science Advances 2, no. 11 (November 2016): e1600925. http://dx.doi.org/10.1126/sciadv.1600925.
Повний текст джерелаCarpenter, C. L. "Btk-dependent regulation of phosphoinositide synthesis." Biochemical Society Transactions 32, no. 2 (April 1, 2004): 326–29. http://dx.doi.org/10.1042/bst0320326.
Повний текст джерелаEl Sayegh, T. Y., P. D. Arora, K. Ling, C. Laschinger, P. A. Janmey, R. A. Anderson та C. A. McCulloch. "Phosphatidylinositol-4,5 Bisphosphate Produced by PIP5KIγ Regulates Gelsolin, Actin Assembly, and Adhesion Strength of N-Cadherin Junctions". Molecular Biology of the Cell 18, № 8 (серпень 2007): 3026–38. http://dx.doi.org/10.1091/mbc.e06-12-1159.
Повний текст джерелаZarza, Xavier, Ringo Van Wijk, Lana Shabala, Anna Hunkeler, Matthew Lefebvre, Antia Rodriguez‐Villalón, Sergey Shabala, Antonio F. Tiburcio, Ingo Heilmann, and Teun Munnik. "Lipid kinases PIP5K7 and PIP5K9 are required for polyamine‐triggered K + efflux in Arabidopsis roots." Plant Journal 104, no. 2 (August 19, 2020): 416–32. http://dx.doi.org/10.1111/tpj.14932.
Повний текст джерелаWang, Ying Jie, Wen Hong Li, Jing Wang, Ke Xu, Ping Dong, Xiang Luo та Helen L. Yin. "Critical role of PIP5KIγ87 in InsP3-mediated Ca2+ signaling". Journal of Cell Biology 167, № 6 (20 грудня 2004): 1005–10. http://dx.doi.org/10.1083/jcb.200408008.
Повний текст джерелаZhao, Xiaoying, Penglei Cui, Guoli Hu, Chuandong Wang, Lei Jiang, Jingyu Zhao, Jiake Xu та Xiaoling Zhang. "PIP5k1β controls bone homeostasis through modulating both osteoclast and osteoblast differentiation". Journal of Molecular Cell Biology 12, № 1 (16 квітня 2019): 55–70. http://dx.doi.org/10.1093/jmcb/mjz028.
Повний текст джерелаRen, X. D., G. M. Bokoch, A. Traynor-Kaplan, G. H. Jenkins, R. A. Anderson, and M. A. Schwartz. "Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells." Molecular Biology of the Cell 7, no. 3 (March 1996): 435–42. http://dx.doi.org/10.1091/mbc.7.3.435.
Повний текст джерелаAbajy, Mohammad Y., Jolanta Kopeć, Katarzyna Schiwon, Michal Burzynski, Mike Döring, Christine Bohn, and Elisabeth Grohmann. "A Type IV-Secretion-Like System Is Required for Conjugative DNA Transport of Broad-Host-Range Plasmid pIP501 in Gram-Positive Bacteria." Journal of Bacteriology 189, no. 6 (January 5, 2007): 2487–96. http://dx.doi.org/10.1128/jb.01491-06.
Повний текст джерелаMao, Yuntao S., Masaki Yamaga, Xiaohui Zhu, Yongjie Wei, Hui-Qiao Sun, Jing Wang, Mia Yun та ін. "Essential and unique roles of PIP5K-γ and -α in Fcγ receptor-mediated phagocytosis". Journal of Cell Biology 184, № 2 (19 січня 2009): 281–96. http://dx.doi.org/10.1083/jcb.200806121.
Повний текст джерелаPoli, Alessandro, Shidqiyyah Abdul-Hamid, Antonio Enrico Zaurito, Francesca Campagnoli, Valeria Bevilacqua, Bhavwanti Sheth, Roberta Fiume, Massimiliano Pagani, Sergio Abrignani, and Nullin Divecha. "PIP4Ks impact on PI3K, FOXP3, and UHRF1 signaling and modulate human regulatory T cell proliferation and immunosuppressive activity." Proceedings of the National Academy of Sciences 118, no. 31 (July 26, 2021): e2010053118. http://dx.doi.org/10.1073/pnas.2010053118.
Повний текст джерелаShimada, Takashi L., Shigeyuki Betsuyaku, Noriko Inada, Kazuo Ebine, Masaru Fujimoto, Tomohiro Uemura, Yoshitaka Takano, Hiroo Fukuda, Akihiko Nakano, and Takashi Ueda. "Enrichment of Phosphatidylinositol 4,5-Bisphosphate in the Extra-Invasive Hyphal Membrane Promotes Colletotrichum Infection of Arabidopsis thaliana." Plant and Cell Physiology 60, no. 7 (April 15, 2019): 1514–24. http://dx.doi.org/10.1093/pcp/pcz058.
Повний текст джерелаGoessweiner-Mohr, Nikolaus, Markus Eder, Gerhard Hofer, Christian Fercher, Karsten Arends, Ruth Birner-Gruenberger, Elisabeth Grohmann, and Walter Keller. "Structure of the double-stranded DNA-binding type IV secretion protein TraN fromEnterococcus." Acta Crystallographica Section D Biological Crystallography 70, no. 9 (August 29, 2014): 2376–89. http://dx.doi.org/10.1107/s1399004714014187.
Повний текст джерелаXie, Zhongjian, Sandra M. Chang, Sally D. Pennypacker, Er-Yuan Liao та Daniel D. Bikle. "Phosphatidylinositol-4-phosphate 5-kinase 1α Mediates Extracellular Calcium-induced Keratinocyte Differentiation". Molecular Biology of the Cell 20, № 6 (15 березня 2009): 1695–704. http://dx.doi.org/10.1091/mbc.e08-07-0756.
Повний текст джерелаZhang, Jiping, Ruihua Luo, Heqing Wu, Shunhui Wei, Weiping Han та GuoDong Li. "Role of Type Iα Phosphatidylinositol-4-Phosphate 5-Kinase in Insulin Secretion, Glucose Metabolism, and Membrane Potential in INS-1 β-Cells". Endocrinology 150, № 5 (30 грудня 2008): 2127–35. http://dx.doi.org/10.1210/en.2008-0516.
Повний текст джерелаChakrabarti, Rajarshi, Sulagna Sanyal, Amit Ghosh, Kaushik Bhar, Chandrima Das та Anirban Siddhanta. "Phosphatidylinositol-4-phosphate 5-Kinase 1α Modulates Ribosomal RNA Gene Silencing through Its Interaction with Histone H3 Lysine 9 Trimethylation and Heterochromatin Protein HP1-α". Journal of Biological Chemistry 290, № 34 (7 липня 2015): 20893–903. http://dx.doi.org/10.1074/jbc.m114.633727.
Повний текст джерелаSerror, Pascale, Golnar Ilami, Hichem Chouayekh, S. Dusko Ehrlich, and Emmanuelle Maguin. "Transposition in Lactobacillus delbrueckii subsp. bulgaricus: identification of two thermosensitive replicons and two functional insertion sequences." Microbiology 149, no. 6 (June 1, 2003): 1503–11. http://dx.doi.org/10.1099/mic.0.25827-0.
Повний текст джерелаKurenbach, Brigitta, Jolanta Kopeć, Marion Mägdefrau, Kristin Andreas, Walter Keller, Christine Bohn, Mouhammad Y. Abajy, and Elisabeth Grohmann. "The TraA relaxase autoregulates the putative type IV secretion-like system encoded by the broad-host-range Streptococcus agalactiae plasmid pIP501." Microbiology 152, no. 3 (March 1, 2006): 637–45. http://dx.doi.org/10.1099/mic.0.28468-0.
Повний текст джерелаWong, Ka-Wing, та Ralph R. Isberg. "Arf6 and Phosphoinositol-4-Phosphate-5-Kinase Activities Permit Bypass of the Rac1 Requirement for β1 Integrin–mediated Bacterial Uptake". Journal of Experimental Medicine 198, № 4 (18 серпня 2003): 603–14. http://dx.doi.org/10.1084/jem.20021363.
Повний текст джерелаSANTONI, Véronique, Joëlle VINH, Delphine PFLIEGER, Nicolas SOMMERER, and Christophe MAUREL. "A proteomic study reveals novel insights into the diversity of aquaporin forms expressed in the plasma membrane of plant roots." Biochemical Journal 373, no. 1 (July 1, 2003): 289–96. http://dx.doi.org/10.1042/bj20030159.
Повний текст джерелаKumari, Aastha, Avishek Ghosh, Sourav Kolay, and Padinjat Raghu. "Septins tune lipid kinase activity and PI(4,5)P2 turnover during G-protein–coupled PLC signalling in vivo." Life Science Alliance 5, no. 6 (March 11, 2022): e202101293. http://dx.doi.org/10.26508/lsa.202101293.
Повний текст джерелаWang, Y., X. Chen, L. Lian, T. Tang, T. J. Stalker, T. Sasaki, L. F. Brass, J. K. Choi, J. H. Hartwig, and C. S. Abrams. "Loss of PIP5KI demonstrates that PIP5KI isoform-specific PIP2 synthesis is required for IP3 formation." Proceedings of the National Academy of Sciences 105, no. 37 (September 4, 2008): 14064–69. http://dx.doi.org/10.1073/pnas.0804139105.
Повний текст джерелаHoraud, T., G. de Céspèdes, and P. Trieu-Cuot. "Chromosomal gentamicin resistance transposon Tn3706 in Streptococcus agalactiae B128." Antimicrobial Agents and Chemotherapy 40, no. 5 (May 1996): 1085–90. http://dx.doi.org/10.1128/aac.40.5.1085.
Повний текст джерелаYamamoto, Masaya, Donald H. Hilgemann, Siyi Feng, Haruhiko Bito, Hisamitsu Ishihara, Yoshikazu Shibasaki, and Helen L. Yin. "Phosphatidylinositol 4,5-Bisphosphate Induces Actin Stress-Fiber Formation and Inhibits Membrane Ruffling in Cv1 Cells." Journal of Cell Biology 152, no. 5 (February 26, 2001): 867–76. http://dx.doi.org/10.1083/jcb.152.5.867.
Повний текст джерелаvan den Bout, Iman, David R. Jones, Zahid H. Shah, Jonathan R. Halstead, Willem-Jan Keune, Shabaz Mohammed, Clive S. D’Santos, and Nullin Divecha. "Collaboration of AMPK and PKC to induce phosphorylation of Ser413 on PIP5K1B resulting in decreased kinase activity and reduced PtdIns(4,5)P2 synthesis in response to oxidative stress and energy restriction." Biochemical Journal 455, no. 3 (October 10, 2013): 347–58. http://dx.doi.org/10.1042/bj20130259.
Повний текст джерелаKarlsson, Richard, Per Larsson, Regina Miftakhova, Azharuddin Sajid Syed Khaja, Martuza Sarwar, Julius Semenas, Sa Chen та ін. "Establishment of Prostate Tumor Growth and Metastasis Is Supported by Bone Marrow Cells and Is Mediated by PIP5K1α Lipid Kinase". Cancers 12, № 9 (22 вересня 2020): 2719. http://dx.doi.org/10.3390/cancers12092719.
Повний текст джерелаYamamoto, A., D. B. DeWald, I. V. Boronenkov, R. A. Anderson, S. D. Emr, and D. Koshland. "Novel PI(4)P 5-kinase homologue, Fab1p, essential for normal vacuole function and morphology in yeast." Molecular Biology of the Cell 6, no. 5 (May 1995): 525–39. http://dx.doi.org/10.1091/mbc.6.5.525.
Повний текст джерелаGough, N. R. "Inhibition of PIP5K by Apoptotic Stresses." Science's STKE 2006, no. 354 (September 19, 2006): tw332. http://dx.doi.org/10.1126/stke.3542006tw332.
Повний текст джерелаToda, Atsushi, Hisataka Kayahara, Hitomi Yasuhira, and Junichi Sikigichi. "Conjugal Transfer of pIP501 fromEnterococcus faecalistoPediococcus halophilus." Agricultural and Biological Chemistry 53, no. 12 (December 1989): 3317–18. http://dx.doi.org/10.1080/00021369.1989.10869865.
Повний текст джерелаSarwar, Martuza, Azharuddin Sajid Syed Khaja, Mohammed Aleskandarany, Richard Karlsson, Maryam Althobiti, Niels Ødum, Nigel P. Mongan та ін. "The role of PIP5K1α/pAKT and targeted inhibition of growth of subtypes of breast cancer using PIP5K1α inhibitor". Oncogene 38, № 3 (13 серпня 2018): 375–89. http://dx.doi.org/10.1038/s41388-018-0438-2.
Повний текст джерела