Статті в журналах з теми "Inositol polyphosphate phosphatases"
Оформте джерело за APA, MLA, Chicago, Harvard та іншими стилями
Ознайомтеся з топ-50 статей у журналах для дослідження на тему "Inositol polyphosphate phosphatases".
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.
Eramo, Matthew J., and Christina A. Mitchell. "Regulation of PtdIns(3,4,5)P3/Akt signalling by inositol polyphosphate 5-phosphatases." Biochemical Society Transactions 44, no. 1 (February 9, 2016): 240–52. http://dx.doi.org/10.1042/bst20150214.
Повний текст джерелаZhang, Qingxiu, and Francois X. Claret. "Phosphatases: The New Brakes for Cancer Development?" Enzyme Research 2012 (October 31, 2012): 1–11. http://dx.doi.org/10.1155/2012/659649.
Повний текст джерелаJia, Qi, Defeng Kong, Qinghua Li, Song Sun, Junliang Song, Yebao Zhu, Kangjing Liang, Qingming Ke, Wenxiong Lin, and Jinwen Huang. "The Function of Inositol Phosphatases in Plant Tolerance to Abiotic Stress." International Journal of Molecular Sciences 20, no. 16 (August 16, 2019): 3999. http://dx.doi.org/10.3390/ijms20163999.
Повний текст джерелаAstle, Megan V., Kristy A. Horan, Lisa M. Ooms, and Christina A. Mitchell. "The inositol polyphosphate 5-phosphatases: traffic controllers, waistline watchers and tumour suppressors?" Biochemical Society Symposia 74 (January 12, 2007): 161–81. http://dx.doi.org/10.1042/bss2007c15.
Повний текст джерелаChellapandi, Paulchamy, and Jayachandrabal Balachandramohan. "Computational Evaluation of Designed Phosphatase from Conserved Sequence Scratch for Diverse Substrate Specificity." International Journal Bioautomation 26, no. 3 (September 2022): 297–310. http://dx.doi.org/10.7546/ijba.2022.26.3.000553.
Повний текст джерелаMitchell, Christina A., Rajendra Gurung, Anne M. Kong, Jennifer M. Dyson, April Tan, and Lisa M. Ooms. "Inositol Polyphosphate 5-Phosphatases: Lipid Phosphatases With Flair." IUBMB Life (International Union of Biochemistry and Molecular Biology: Life) 53, no. 1 (January 1, 2002): 25–36. http://dx.doi.org/10.1080/15216540210815.
Повний текст джерелаMitchell, C. A. "THE REGULATION OF INOSITOL TRISPHOSPHATE BY INOSITOL POLYPHOSPHATE 5-PHOSPHATASES." Biochemical Society Transactions 24, no. 4 (November 1, 1996): 621S. http://dx.doi.org/10.1042/bst024621sa.
Повний текст джерелаNoakes, Christopher J., Grace Lee, and Martin Lowe. "The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling in the endocytic pathway." Molecular Biology of the Cell 22, no. 5 (March 2011): 606–23. http://dx.doi.org/10.1091/mbc.e10-08-0730.
Повний текст джерелаDrayer, A. L., X. Pesesse, F. De Smedt, D. Communi, C. Moreau, and C. Erneux. "The family of inositol and phosphatidylinositol polyphosphate 5-phosphatases." Biochemical Society Transactions 24, no. 4 (November 1, 1996): 1001–5. http://dx.doi.org/10.1042/bst0241001.
Повний текст джерелаAntibus, Robert K., Robert L. Sinsabaugh, and Arthur E. Linkins. "Phosphatase activities and phosphorus uptake from inositol phosphate by ectomycorrhizal fungi." Canadian Journal of Botany 70, no. 4 (April 1, 1992): 794–801. http://dx.doi.org/10.1139/b92-101.
Повний текст джерелаOoms, Lisa M., Kristy A. Horan, Parvin Rahman, Gillian Seaton, Rajendra Gurung, Dharini S. Kethesparan, and Christina A. Mitchell. "The role of the inositol polyphosphate 5-phosphatases in cellular function and human disease." Biochemical Journal 419, no. 1 (March 13, 2009): 29–49. http://dx.doi.org/10.1042/bj20081673.
Повний текст джерелаErneux, Christophe, Somadri Ghosh, Ana Raquel Ramos, and William`s Elong Edimo. "New Functions of the Inositol Polyphosphate 5-Phosphatases in Cancer." Current Pharmaceutical Design 22, no. 16 (April 27, 2016): 2309–14. http://dx.doi.org/10.2174/1381612822666160226132512.
Повний текст джерелаAstle, Megan, Gillian Seaton, Elizabeth Davies, Clare Fedele, Parvin Rahman, Laima Arsala, and Christina Mitchell. "Regulation of phosphoinositide signaling by the inositol polyphosphate 5-phosphatases." IUBMB Life (International Union of Biochemistry and Molecular Biology: Life) 58, no. 8 (August 1, 2006): 451–56. http://dx.doi.org/10.1080/15216540600871159.
Повний текст джерелаMitchell, C. A., S. Brown, J. K. Campbell, A. D. Munday, and C. J. Speed. "Regulation of second messengers by the inositol polyphosphate 5-phosphatases." Biochemical Society Transactions 24, no. 4 (November 1, 1996): 994–1000. http://dx.doi.org/10.1042/bst0240994.
Повний текст джерелаBraun, Werner, and Catherine H. Schein. "Membrane Interaction and Functional Plasticity of Inositol Polyphosphate 5-Phosphatases." Structure 22, no. 5 (May 2014): 664–66. http://dx.doi.org/10.1016/j.str.2014.04.008.
Повний текст джерелаO'MALLEY, Cindy J., Brad K. McCOLL, Anne M. KONG, Sarah L. ELLIS, A. Primrose W. WIJAYARATNAM, Joe SAMBROOK, and Christina A. MITCHELL. "Mammalian inositol polyphosphate 5-phosphatase II can compensate for the absence of all three yeast Sac1-like-domain-containing 5-phosphatases." Biochemical Journal 355, no. 3 (April 24, 2001): 805–17. http://dx.doi.org/10.1042/bj3550805.
Повний текст джерелаZhang, Zaibao, Yuting Li, Zhaoyi Luo, Shuwei Kong, Yilin Zhao, Chi Zhang, Wei Zhang, Hongyu Yuan, and Lin Cheng. "Expansion and Functional Divergence of Inositol Polyphosphate 5-Phosphatases in Angiosperms." Genes 10, no. 5 (May 22, 2019): 393. http://dx.doi.org/10.3390/genes10050393.
Повний текст джерелаErneux, Christophe, Cédric Govaerts, David Communi, and Xavier Pesesse. "The diversity and possible functions of the inositol polyphosphate 5-phosphatases." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1436, no. 1-2 (December 1998): 185–99. http://dx.doi.org/10.1016/s0005-2760(98)00132-5.
Повний текст джерелаJefferson, Anne Bennett, and Philip W. Majerus. "Mutation of the Conserved Domains of Two Inositol Polyphosphate 5-Phosphatases†." Biochemistry 35, no. 24 (January 1996): 7890–94. http://dx.doi.org/10.1021/bi9602627.
Повний текст джерелаHoran, Kristy A., Megan V. Astle, Lisa M. Ooms, and Christina A. Mitchell. "The inositol polyphosphate 5-phosphatases: traffic controllers, waistline watchers and tumour suppressors?" Biochemical Society Symposium 74, no. 1 (December 1, 2007): 161. http://dx.doi.org/10.1042/bss0740161.
Повний текст джерелаWhisstock, J. C., F. Wiradjaja, J. E. Waters, and R. Gurung. "The Structure and Function of Catalytic Domains Within Inositol Polyphosphate 5-Phosphatases." IUBMB Life (International Union of Biochemistry and Molecular Biology: Life) 53, no. 1 (January 1, 2002): 15–23. http://dx.doi.org/10.1080/15216540210814.
Повний текст джерелаStolz, Leslie E., Chau V. Huynh, Jeremy Thorner, and John D. York. "Identification and Characterization of an Essential Family of Inositol Polyphosphate 5-Phosphatases (INP51, INP52 and INP53 Gene Products) in the Yeast Saccharomyces cerevisiae." Genetics 148, no. 4 (April 1, 1998): 1715–29. http://dx.doi.org/10.1093/genetics/148.4.1715.
Повний текст джерелаBertelli, Daniela F., Eliana P. Araújo, Maristela Cesquini, Graziela R. Stoppa, Miriam Gasparotto-Contessotto, Marcos H. Toyama, Jorge V. C. Felix, et al. "Phosphoinositide-Specific Inositol Polyphosphate 5-Phosphatase IV Inhibits Inositide Trisphosphate Accumulation in Hypothalamus and Regulates Food Intake and Body Weight." Endocrinology 147, no. 11 (November 1, 2006): 5385–99. http://dx.doi.org/10.1210/en.2006-0280.
Повний текст джерелаNakajima, Toshio, Shun Hosoyamada, Takehiko Kobayashi, and Yukio Mukai. "Secreted acid phosphatases maintain replicative lifespan via inositol polyphosphate metabolism in budding yeast." FEBS Letters 596, no. 2 (December 5, 2021): 189–98. http://dx.doi.org/10.1002/1873-3468.14245.
Повний текст джерелаGunesekera, Bhadra, Javad Torabinejad, Jamille Robinson, and Glenda E. Gillaspy. "Inositol Polyphosphate 5-Phosphatases 1 and 2 Are Required for Regulating Seedling Growth." Plant Physiology 143, no. 3 (January 19, 2007): 1408–17. http://dx.doi.org/10.1104/pp.106.089474.
Повний текст джерелаConduit, Sarah E., Jennifer M. Dyson, and Christina A. Mitchell. "Inositol polyphosphate 5-phosphatases; new players in the regulation of cilia and ciliopathies." FEBS Letters 586, no. 18 (July 21, 2012): 2846–57. http://dx.doi.org/10.1016/j.febslet.2012.07.037.
Повний текст джерелаMaeda, Akito, Mari Kurosaki, Masao Ono, Toshiyuki Takai, and Tomohiro Kurosaki. "Requirement of SH2-containing Protein Tyrosine Phosphatases SHP-1 and SHP-2 for Paired Immunoglobulin-like Receptor B (PIR-B)–mediated Inhibitory Signal." Journal of Experimental Medicine 187, no. 8 (April 20, 1998): 1355–60. http://dx.doi.org/10.1084/jem.187.8.1355.
Повний текст джерелаOoms, Lisa M., Brad K. McColl, Fenny Wiradjaja, A. P. W. Wijayaratnam, Paul Gleeson, Mary Jane Gething, Joe Sambrook, and Christina A. Mitchell. "The Yeast Inositol Polyphosphate 5-Phosphatases Inp52p and Inp53p Translocate to Actin Patches following Hyperosmotic Stress: Mechanism for Regulating Phosphatidylinositol 4,5-Bisphosphate at Plasma Membrane Invaginations." Molecular and Cellular Biology 20, no. 24 (December 15, 2000): 9376–90. http://dx.doi.org/10.1128/mcb.20.24.9376-9390.2000.
Повний текст джерелаMcConnell, F. M., L. R. Stephens, and S. B. Shears. "Multiple isomers of inositol pentakisphosphate in Epstein-Barr-virus- transformed (T5-1) B-lymphocytes. Identification of inositol 1,3,4,5,6-pentakisphosphate, d-inositol 1,2,4,5,6-pentakisphosphate and l-inositol 1,2,4,5,6-pentakisphosphate." Biochemical Journal 280, no. 2 (December 1, 1991): 323–29. http://dx.doi.org/10.1042/bj2800323.
Повний текст джерелаHejna, James A., Hiroshi Saito, Louise S. Merkens, Thomas V. Tittle, Petra M. Jakobs, Michael A. Whitney, Markus Grompe, Andrew S. Friedberg, and Robb E. Moses. "Cloning and Characterization of a Human cDNA (INPPL1) Sharing Homology with Inositol Polyphosphate Phosphatases." Genomics 29, no. 1 (September 1995): 285–87. http://dx.doi.org/10.1006/geno.1995.1247.
Повний текст джерелаSitaram, Uyemura, Malarkannan, and Riese. "Beyond the Cell Surface: Targeting Intracellular Negative Regulators to Enhance T cell Anti-Tumor Activity." International Journal of Molecular Sciences 20, no. 23 (November 20, 2019): 5821. http://dx.doi.org/10.3390/ijms20235821.
Повний текст джерелаBatty, Ian H., Jeroen van der Kaay, Alex Gray, Joan F. Telfer, Miles J. Dixon, and C. Peter Downes. "The control of phosphatidylinositol 3,4-bisphosphate concentrations by activation of the Src homology 2 domain containing inositol polyphosphate 5-phosphatase 2, SHIP2." Biochemical Journal 407, no. 2 (September 25, 2007): 255–66. http://dx.doi.org/10.1042/bj20070558.
Повний текст джерелаOoms, Lisa M., Clare G. Fedele, Megan V. Astle, Ivan Ivetac, Vanessa Cheung, Richard B. Pearson, Meredith J. Layton, Ariel Forrai, Harshal H. Nandurkar, and Christina A. Mitchell. "The Inositol Polyphosphate 5-Phosphatase, PIPP, Is a Novel Regulator of Phosphoinositide 3-Kinase-dependent Neurite Elongation." Molecular Biology of the Cell 17, no. 2 (February 2006): 607–22. http://dx.doi.org/10.1091/mbc.e05-05-0469.
Повний текст джерелаPöhlmann, Jennifer, and Ursula Fleig. "Asp1, a Conserved 1/3 Inositol Polyphosphate Kinase, Regulates the Dimorphic Switch in Schizosaccharomyces pombe." Molecular and Cellular Biology 30, no. 18 (July 12, 2010): 4535–47. http://dx.doi.org/10.1128/mcb.00472-10.
Повний текст джерелаWang, Ruobing, Yan Jiao, Yanqing Li, Siyang Ye, Guoqiang Pan, Shanshan Qin, Fang Hua, and Yahui Liu. "The Prediction and Prognostic Significance of INPP5K Expression in Patients with Liver Cancer." BioMed Research International 2020 (April 27, 2020): 1–9. http://dx.doi.org/10.1155/2020/9519235.
Повний текст джерелаMalbec, Odile, Dana C. Fong, Martin Turner, Victor L. J. Tybulewicz, John C. Cambier, Wolf H. Fridman та Marc Daëron. "Fcε Receptor I-Associated lyn-Dependent Phosphorylation of Fcγ Receptor IIB During Negative Regulation of Mast Cell Activation". Journal of Immunology 160, № 4 (15 лютого 1998): 1647–58. http://dx.doi.org/10.4049/jimmunol.160.4.1647.
Повний текст джерелаJia, Qi, Song Sun, Defeng Kong, Junliang Song, Lumei Wu, Zhen Yan, Lin Zuo, et al. "Ectopic Expression of Gs5PTase8, a Soybean Inositol Polyphosphate 5-Phosphatase, Enhances Salt Tolerance in Plants." International Journal of Molecular Sciences 21, no. 3 (February 4, 2020): 1023. http://dx.doi.org/10.3390/ijms21031023.
Повний текст джерелаTrésaugues, Lionel, Camilla Silvander, Susanne Flodin, Martin Welin, Tomas Nyman, Susanne Gräslund, Martin Hammarström, Helena Berglund, and Pär Nordlund. "Structural Basis for Phosphoinositide Substrate Recognition, Catalysis, and Membrane Interactions in Human Inositol Polyphosphate 5-Phosphatases." Structure 22, no. 5 (May 2014): 744–55. http://dx.doi.org/10.1016/j.str.2014.01.013.
Повний текст джерелаMarshall, Aaron J., Sen Hou, Xun Wu, and Hongzhao Li. "Control of B cell activation and migration by PI 3-kinase: role of inositol polyphosphate 4-phosphatases." Journal of Immunology 196, no. 1_Supplement (May 1, 2016): 198.5. http://dx.doi.org/10.4049/jimmunol.196.supp.198.5.
Повний текст джерелаCsolle, Mariah P., Lisa M. Ooms, Antonella Papa, and Christina A. Mitchell. "PTEN and Other PtdIns(3,4,5)P3 Lipid Phosphatases in Breast Cancer." International Journal of Molecular Sciences 21, no. 23 (December 2, 2020): 9189. http://dx.doi.org/10.3390/ijms21239189.
Повний текст джерелаGurung, Rajendra, April Tan, Lisa M. Ooms, Meagan J. McGrath, Richard D. Huysmans, Adam D. Munday, Mark Prescott, James C. Whisstock, and Christina A. Mitchell. "Identification of a Novel Domain in Two Mammalian Inositol-polyphosphate 5-Phosphatases That Mediates Membrane Ruffle Localization." Journal of Biological Chemistry 278, no. 13 (January 20, 2003): 11376–85. http://dx.doi.org/10.1074/jbc.m209991200.
Повний текст джерелаZhong, Ruiqin, and Zheng-Hua Ye. "Molecular and Biochemical Characterization of Three WD-Repeat-Domain-containing Inositol Polyphosphate 5-Phosphatases in Arabidopsis thaliana." Plant and Cell Physiology 45, no. 11 (November 15, 2004): 1720–28. http://dx.doi.org/10.1093/pcp/pch187.
Повний текст джерелаAcquistapace, Isabella M., Monika A. Zi¸etek, Arthur W. H. Li, Melissa Salmon, Imke Kühn, Mike R. Bedford, Charles A. Brearley, and Andrew M. Hemmings. "Snapshots during the catalytic cycle of a histidine acid phytase reveal an induced-fit structural mechanism." Journal of Biological Chemistry 295, no. 51 (October 14, 2020): 17724–37. http://dx.doi.org/10.1074/jbc.ra120.015925.
Повний текст джерелаWhisstock, James C., Susana Romero, Rajendra Gurung, Harshal Nandurkar, Lisa M. Ooms, Stephen P. Bottomley, and Christina A. Mitchell. "The Inositol Polyphosphate 5-Phosphatases and the Apurinic/Apyrimidinic Base Excision Repair Endonucleases Share a Common Mechanism for Catalysis." Journal of Biological Chemistry 275, no. 47 (August 28, 2000): 37055–61. http://dx.doi.org/10.1074/jbc.m006244200.
Повний текст джерелаZhang, Yanyan, Anne-Sophie Wavreille, Andrew R. Kunys, and Dehua Pei. "The SH2 Domains of Inositol Polyphosphate 5-Phosphatases SHIP1 and SHIP2 Have Similar Ligand Specificity but Different Binding Kinetics." Biochemistry 48, no. 46 (November 24, 2009): 11075–83. http://dx.doi.org/10.1021/bi9012462.
Повний текст джерелаCOMMUNI, David, and Christophe ERNEUX. "Identification of an active site cysteine residue in human type I Ins(1,4,5)P3 5-phosphatase by chemical modification and site-directed mutagenesis." Biochemical Journal 320, no. 1 (November 15, 1996): 181–86. http://dx.doi.org/10.1042/bj3200181.
Повний текст джерелаDionisio, Giuseppe, Preben B. Holm, and Henrik Brinch-Pedersen. "Wheat (Triticum aestivum L.) and barley (Hordeum vulgare L.) multiple inositol polyphosphate phosphatases (MINPPs) are phytases expressed during grain filling and germination." Plant Biotechnology Journal 5, no. 2 (March 2007): 325–38. http://dx.doi.org/10.1111/j.1467-7652.2007.00244.x.
Повний текст джерелаMarjanovic, Jasna, Brad Rumancik, Luke Weber, Felix Wangmang, Dane Fickes, Dmitri Postnov, Dung Nguyen, Yoon Lee, Richard Ngo-Lam, and Monita Wilson. "Phosphatidylinositol-3,4-Bisphosphate-Akt Signaling Pathway Promotes Platelet Activation." Blood 132, Supplement 1 (November 29, 2018): 1131. http://dx.doi.org/10.1182/blood-2018-99-115066.
Повний текст джерелаChi, Hongbo, Xiaonian Yang, Paul D. Kingsley, Regis J. O'Keefe, J. Edward Puzas, Randy N. Rosier, Stephen B. Shears, and Paul R. Reynolds. "Targeted Deletion of Minpp1 Provides New Insight into the Activity of Multiple Inositol Polyphosphate Phosphatase In Vivo." Molecular and Cellular Biology 20, no. 17 (September 1, 2000): 6496–507. http://dx.doi.org/10.1128/mcb.20.17.6496-6507.2000.
Повний текст джерелаHoran, Kristy A., Ken-ichi Watanabe, Anne M. Kong, Charles G. Bailey, John E. J. Rasko, Takehiko Sasaki та Christina A. Mitchell. "Regulation of FcγR-stimulated phagocytosis by the 72-kDa inositol polyphosphate 5-phosphatase: SHIP1, but not the 72-kDa 5-phosphatase, regulates complement receptor 3–mediated phagocytosis by differential recruitment of these 5-phosphatases to the phagocytic cup". Blood 110, № 13 (15 грудня 2007): 4480–91. http://dx.doi.org/10.1182/blood-2007-02-073874.
Повний текст джерела