Artículos de revistas sobre el tema "Tyrosine"
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Hunter, Tony. "THE CROONIAN LECTURE 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and disease". Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 353, n.º 1368 (29 de abril de 1998): 583–605. http://dx.doi.org/10.1098/rstb.1998.0228.
Texto completoLongmore, Gregory D., Yun You, Jaime Molden, Kathleen D. Liu, Aki Mikami, Stephen Y. Lai, Pamela Pharr y Mark A. Goldsmith. "Redundant and Selective Roles for Erythropoietin Receptor Tyrosines in Erythropoiesis In Vivo". Blood 91, n.º 3 (1 de febrero de 1998): 870–78. http://dx.doi.org/10.1182/blood.v91.3.870.
Texto completoLongmore, Gregory D., Yun You, Jaime Molden, Kathleen D. Liu, Aki Mikami, Stephen Y. Lai, Pamela Pharr y Mark A. Goldsmith. "Redundant and Selective Roles for Erythropoietin Receptor Tyrosines in Erythropoiesis In Vivo". Blood 91, n.º 3 (1 de febrero de 1998): 870–78. http://dx.doi.org/10.1182/blood.v91.3.870.870_870_878.
Texto completoMarumo, K. y J. H. Waite. "Optimization of hydroxylation of tyrosine and tyrosine-containing peptides by mushroom tyrosinase". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 872, n.º 1-2 (julio de 1986): 98–103. http://dx.doi.org/10.1016/0167-4838(86)90152-4.
Texto completoHansen, J. A., L. H. Hansen, X. Wang, J. J. Kopchick, F. Gouilleux, B. Groner, J. H. Nielsen, A. Møldrup, E. D. Galsgaard y N. Billestrup. "The role of GH receptor tyrosine phosphorylation in Stat5 activation". Journal of Molecular Endocrinology 18, n.º 3 (junio de 1997): 213–21. http://dx.doi.org/10.1677/jme.0.0180213.
Texto completoKing, M. J. y G. J. Sale. "Dephosphorylation of insulin-receptor autophosphorylation sites by particulate and soluble phosphotyrosyl-protein phosphatases". Biochemical Journal 266, n.º 1 (15 de febrero de 1990): 251–59. http://dx.doi.org/10.1042/bj2660251.
Texto completoPao, Lily I., Sara J. Famiglietti y John C. Cambier. "Asymmetrical Phosphorylation and Function of Immunoreceptor Tyrosine-Based Activation Motif Tyrosines in B Cell Antigen Receptor Signal Transduction". Journal of Immunology 160, n.º 7 (1 de abril de 1998): 3305–14. http://dx.doi.org/10.4049/jimmunol.160.7.3305.
Texto completoArgetsinger, Lawrence S., Jean-Louis K. Kouadio, Hanno Steen, Allan Stensballe, Ole N. Jensen y Christin Carter-Su. "Autophosphorylation of JAK2 on Tyrosines 221 and 570 Regulates Its Activity". Molecular and Cellular Biology 24, n.º 11 (1 de junio de 2004): 4955–67. http://dx.doi.org/10.1128/mcb.24.11.4955-4967.2004.
Texto completoDeng, Kaiping, Jason R. Mock, Steven Greenberg, Nicolai S. C. van Oers y Eric J. Hansen. "Haemophilus ducreyi LspA Proteins Are Tyrosine Phosphorylated by Macrophage-Encoded Protein Tyrosine Kinases". Infection and Immunity 76, n.º 10 (4 de agosto de 2008): 4692–702. http://dx.doi.org/10.1128/iai.00513-08.
Texto completoGIBSON, Spencer, Ken TRUITT, Yiling LU, Ruth LAPUSHIN, Humera KHAN, B. John IMBODEN y B. Gordon MILLS. "Efficient CD28 signalling leads to increases in the kinase activities of the TEC family tyrosine kinase EMT/ITK/TSK and the SRC family tyrosine kinase LCK". Biochemical Journal 330, n.º 3 (15 de marzo de 1998): 1123–28. http://dx.doi.org/10.1042/bj3301123.
Texto completoZhang, Juan, Teruaki Kimura y Reuben P. Siraganian. "Mutations in the Activation Loop Tyrosines of Protein Tyrosine Kinase Syk Abrogate Intracellular Signaling But Not Kinase Activity". Journal of Immunology 161, n.º 8 (15 de octubre de 1998): 4366–74. http://dx.doi.org/10.4049/jimmunol.161.8.4366.
Texto completoKing, P. D., A. Sadra, J. M. Teng, L. Xiao-Rong, A. Han, A. Selvakumar, A. August y B. Dupont. "Analysis of CD28 cytoplasmic tail tyrosine residues as regulators and substrates for the protein tyrosine kinases, EMT and LCK." Journal of Immunology 158, n.º 2 (15 de enero de 1997): 580–90. http://dx.doi.org/10.4049/jimmunol.158.2.580.
Texto completode Castro, Rodrigo Orlandini. "Regulation and Function of Syk Tyrosine Kinase in Mast Cell Signaling and Beyond". Journal of Signal Transduction 2011 (12 de mayo de 2011): 1–9. http://dx.doi.org/10.1155/2011/507291.
Texto completoXia, Kai, Robert S. Lee, Radha P. Narsimhan, Nishit K. Mukhopadhyay, Benjamin G. Neel y Thomas M. Roberts. "Tyrosine Phosphorylation of the Proto-Oncoprotein Raf-1 Is Regulated by Raf-1 Itself and the Phosphatase Cdc25A". Molecular and Cellular Biology 19, n.º 7 (1 de julio de 1999): 4819–24. http://dx.doi.org/10.1128/mcb.19.7.4819.
Texto completoHead, Julie A., Dongyan Jiang, Min Li, Lynda J. Zorn, Erik M. Schaefer, J. Thomas Parsons y Scott A. Weed. "Cortactin Tyrosine Phosphorylation Requires Rac1 Activity and Association with the Cortical Actin Cytoskeleton". Molecular Biology of the Cell 14, n.º 8 (agosto de 2003): 3216–29. http://dx.doi.org/10.1091/mbc.e02-11-0753.
Texto completoMatos, Maria João, Lourdes Santana, Eugenio Uriarte, Silvia Serra, Marcella Corda, Maria Benedetta Fadda, Benedetta Era y Antonella Fais. "Tyrosine-like condensed derivatives as tyrosinase inhibitors". Journal of Pharmacy and Pharmacology 64, n.º 5 (21 de febrero de 2012): 742–46. http://dx.doi.org/10.1111/j.2042-7158.2012.01467.x.
Texto completoTripathi, R. K., C. Chaya Devi y A. Ramaiah. "pH-dependent interconversion of two forms of tyrosinase in human skin". Biochemical Journal 252, n.º 2 (1 de junio de 1988): 481–87. http://dx.doi.org/10.1042/bj2520481.
Texto completoMitchell, MA, MM Huang, P. Chien, ZK Indik, XQ Pan y AD Schreiber. "Substitutions and deletions in the cytoplasmic domain of the phagocytic receptor Fc gamma RIIA: effect on receptor tyrosine phosphorylation and phagocytosis [published erratum appears in Blood 1994 Nov 1;84(9):3252]". Blood 84, n.º 6 (15 de septiembre de 1994): 1753–59. http://dx.doi.org/10.1182/blood.v84.6.1753.1753.
Texto completoMitchell, MA, MM Huang, P. Chien, ZK Indik, XQ Pan y AD Schreiber. "Substitutions and deletions in the cytoplasmic domain of the phagocytic receptor Fc gamma RIIA: effect on receptor tyrosine phosphorylation and phagocytosis [published erratum appears in Blood 1994 Nov 1;84(9):3252]". Blood 84, n.º 6 (15 de septiembre de 1994): 1753–59. http://dx.doi.org/10.1182/blood.v84.6.1753.bloodjournal8461753.
Texto completoSlominski, Andrzej y John Pawelek. "MSH binding in bomirski amelanotic hamster melanoma cells is stimulated by L-tyrosine". Bioscience Reports 7, n.º 12 (1 de diciembre de 1987): 949–54. http://dx.doi.org/10.1007/bf01122128.
Texto completoKimura, T., H. Sakamoto, E. Appella y R. P. Siraganian. "Conformational changes induced in the protein tyrosine kinase p72syk by tyrosine phosphorylation or by binding of phosphorylated immunoreceptor tyrosine-based activation motif peptides." Molecular and Cellular Biology 16, n.º 4 (abril de 1996): 1471–78. http://dx.doi.org/10.1128/mcb.16.4.1471.
Texto completoSlominski, A., G. Moellmann y E. Kuklinska. "MSH inhibits growth in a line of amelanotic hamster melanoma cells and induces increases in cyclic AMP levels and tyrosinase activity without inducing melanogenesis". Journal of Cell Science 92, n.º 4 (1 de abril de 1989): 551–59. http://dx.doi.org/10.1242/jcs.92.4.551.
Texto completoZhang, Juan, Elsa Berenstein y Reuben P. Siraganian. "Phosphorylation of Tyr342 in the Linker Region of Syk Is Critical for FcεRI Signaling in Mast Cells". Molecular and Cellular Biology 22, n.º 23 (1 de diciembre de 2002): 8144–54. http://dx.doi.org/10.1128/mcb.22.23.8144-8154.2002.
Texto completoRagab, Ashraf, Sonia Séverin, Marie-Pierre Gratacap, Enrique Aguado, Marie Malissen, Martine Jandrot-Perrus, Bernard Malissen, Jeannie Ragab-Thomas y Bernard Payrastre. "Roles of the C-terminal tyrosine residues of LAT in GPVI-induced platelet activation: insights into the mechanism of PLCγ2 activation". Blood 110, n.º 7 (1 de octubre de 2007): 2466–74. http://dx.doi.org/10.1182/blood-2007-02-075432.
Texto completoNaish-Byfield, S. y P. A. Riley. "Oxidation of monohydric phenol substrates by tyrosinase. An oximetric study". Biochemical Journal 288, n.º 1 (15 de noviembre de 1992): 63–67. http://dx.doi.org/10.1042/bj2880063.
Texto completoBarber, Dwayne L., Bryan K. Beattie, Jacqueline M. Mason, Melody H. H. Nguyen, Monique Yoakim, Benjamin G. Neel, Alan D. D'Andrea y David A. Frank. "A common epitope is shared by activated signal transducer and activator of transcription-5 (STAT5) and the phosphorylated erythropoietin receptor: implications for the docking model of STAT activation". Blood 97, n.º 8 (15 de abril de 2001): 2230–37. http://dx.doi.org/10.1182/blood.v97.8.2230.
Texto completoSlominski, A., G. Moellmann, E. Kuklinska, A. Bomirski y J. Pawelek. "Positive regulation of melanin pigmentation by two key substrates of the melanogenic pathway, L-tyrosine and L-dopa". Journal of Cell Science 89, n.º 3 (1 de marzo de 1988): 287–96. http://dx.doi.org/10.1242/jcs.89.3.287.
Texto completoSuwunwong, T., T. Kobkeatthawin, K. Chanawanno, N. Saewan, P. Wisitsak y Suchada Chantrapromma. "Tyrosinase Inhibitory Activity of Pyrazole Derivatives". Advanced Materials Research 506 (abril de 2012): 194–97. http://dx.doi.org/10.4028/www.scientific.net/amr.506.194.
Texto completoHeffetz, D., W. J. Rutter y Y. Zick. "The insulinomimetic agents H2O2 and vanadate stimulate tyrosine phosphorylation of potential target proteins for the insulin receptor kinase in intact cells". Biochemical Journal 288, n.º 2 (1 de diciembre de 1992): 631–35. http://dx.doi.org/10.1042/bj2880631.
Texto completoGobert, S., F. Porteu, S. Pallu, O. Muller, M. Sabbah, I. Dusanter-Fourt, G. Courtois, C. Lacombe, S. Gisselbrecht y P. Mayeux. "Tyrosine phosphorylation of the erythropoietin receptor: role for differentiation and mitogenic signal transduction". Blood 86, n.º 2 (15 de julio de 1995): 598–606. http://dx.doi.org/10.1182/blood.v86.2.598.bloodjournal862598.
Texto completoRybalchenko I.V., Krylov V. I. "Synthesis of O-tyrosine Phosphorylated Adducts of Methylphosphonic and Phosphoric Acid Derivatives as Reference Compounds for the Analysis of Biomedical Samples". Journal of NBC Protection Corps 3, n.º 2 (2019): 103–10. http://dx.doi.org/10.35825/2587-5728-2019-3-2-103-110.
Texto completoBinns, Kathleen L., Paul P. Taylor, Frank Sicheri, Tony Pawson y Sacha J. Holland. "Phosphorylation of Tyrosine Residues in the Kinase Domain and Juxtamembrane Region Regulates the Biological and Catalytic Activities of Eph Receptors". Molecular and Cellular Biology 20, n.º 13 (1 de julio de 2000): 4791–805. http://dx.doi.org/10.1128/mcb.20.13.4791-4805.2000.
Texto completoSadra, Ali, Tomas Cinek, Jerry L. Arellano, Jia Shi, Kenneth E. Truitt y John B. Imboden. "Identification of Tyrosine Phosphorylation Sites in the CD28 Cytoplasmic Domain and Their Role in the Costimulation of Jurkat T Cells". Journal of Immunology 162, n.º 4 (15 de febrero de 1999): 1966–73. http://dx.doi.org/10.4049/jimmunol.162.4.1966.
Texto completoCastro, Rodrigo, Juan Zhang, Maria Jamur, Constance Oliver y Reuben Siraganian. "Tyrosines in the carboxy-terminal region regulate Syk function (86.18)". Journal of Immunology 184, n.º 1_Supplement (1 de abril de 2010): 86.18. http://dx.doi.org/10.4049/jimmunol.184.supp.86.18.
Texto completoMusch, M. W., F. M. McConnell, L. Goldstein y M. Field. "Tyrosine transport in winter flounder intestine: interaction with Na+-K+-2Cl- cotransport". American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 253, n.º 2 (1 de agosto de 1987): R264—R269. http://dx.doi.org/10.1152/ajpregu.1987.253.2.r264.
Texto completoNagatsu, Toshiharu, Akira Nakashima, Hirohisa Watanabe, Shosuke Ito y Kazumasa Wakamatsu. "Neuromelanin in Parkinson’s Disease: Tyrosine Hydroxylase and Tyrosinase". International Journal of Molecular Sciences 23, n.º 8 (10 de abril de 2022): 4176. http://dx.doi.org/10.3390/ijms23084176.
Texto completoKeshvara, Lakhu M., Christina C. Isaacson, Thomas M. Yankee, Radmila Sarac, Marietta L. Harrison y Robert L. Geahlen. "Syk- and Lyn-Dependent Phosphorylation of Syk on Multiple Tyrosines Following B Cell Activation Includes a Site That Negatively Regulates Signaling". Journal of Immunology 161, n.º 10 (15 de noviembre de 1998): 5276–83. http://dx.doi.org/10.4049/jimmunol.161.10.5276.
Texto completoGauen, L. K., Y. Zhu, F. Letourneur, Q. Hu, J. B. Bolen, L. A. Matis, R. D. Klausner y A. S. Shaw. "Interactions of p59fyn and ZAP-70 with T-cell receptor activation motifs: defining the nature of a signalling motif". Molecular and Cellular Biology 14, n.º 6 (junio de 1994): 3729–41. http://dx.doi.org/10.1128/mcb.14.6.3729-3741.1994.
Texto completoGauen, L. K., Y. Zhu, F. Letourneur, Q. Hu, J. B. Bolen, L. A. Matis, R. D. Klausner y A. S. Shaw. "Interactions of p59fyn and ZAP-70 with T-cell receptor activation motifs: defining the nature of a signalling motif." Molecular and Cellular Biology 14, n.º 6 (junio de 1994): 3729–41. http://dx.doi.org/10.1128/mcb.14.6.3729.
Texto completoSlominski, Andrzej, Pawel Jastreboff y John Pawelek. "L-Tyrosine stimulates induction of tyrosinase activity by MSH and reduces cooperative interactions between MSH receptors in hamster melanoma cells". Bioscience Reports 9, n.º 5 (1 de octubre de 1989): 579–86. http://dx.doi.org/10.1007/bf01119801.
Texto completoMüller, Günter, Susanne Wied y Wendelin Frick. "Cross Talk of pp125FAK and pp59Lyn Non-Receptor Tyrosine Kinases to Insulin-Mimetic Signaling in Adipocytes". Molecular and Cellular Biology 20, n.º 13 (1 de julio de 2000): 4708–23. http://dx.doi.org/10.1128/mcb.20.13.4708-4723.2000.
Texto completoKurzer, Jason H., Lawrence S. Argetsinger, Yong-Jie Zhou, Jean-Louis K. Kouadio, John J. O'Shea y Christin Carter-Su. "Tyrosine 813 Is a Site of JAK2 Autophosphorylation Critical for Activation of JAK2 by SH2-Bβ". Molecular and Cellular Biology 24, n.º 10 (15 de mayo de 2004): 4557–70. http://dx.doi.org/10.1128/mcb.24.10.4557-4570.2004.
Texto completoSaitoh, Shin-ichiroh, Sandra Odom, Gregorio Gomez, Connie L. Sommers, Howard A. Young, Juan Rivera y Lawrence E. Samelson. "The Four Distal Tyrosines Are Required for LAT-dependent Signaling in FcεRI-mediated Mast Cell Activation". Journal of Experimental Medicine 198, n.º 5 (1 de septiembre de 2003): 831–43. http://dx.doi.org/10.1084/jem.20030574.
Texto completoREILAND, Jane, Vanessa L. OTT, Connie S. LEBAKKEN, Charles YEAMAN, James McCARTHY y Alan C. RAPRAEGER. "Pervanadate activation of intracellular kinases leads to tyrosine phosphorylation and shedding of syndecan-1". Biochemical Journal 319, n.º 1 (1 de octubre de 1996): 39–47. http://dx.doi.org/10.1042/bj3190039.
Texto completoKulathu, Yogesh, Christa Zuern, Jianying Yang y Michael Reth. "Synthetic biology of B cell activation: understanding signal amplification at the B cell antigen receptor using a rebuilding approach". Biological Chemistry 400, n.º 4 (24 de abril de 2019): 555–63. http://dx.doi.org/10.1515/hsz-2018-0308.
Texto completoTauchi, T., JE Damen, K. Toyama, GS Feng, HE Broxmeyer y G. Krystal. "Tyrosine 425 within the activated erythropoietin receptor binds Syp, reduces the erythropoietin required for Syp tyrosine phosphorylation, and promotes mitogenesis". Blood 87, n.º 11 (1 de junio de 1996): 4495–501. http://dx.doi.org/10.1182/blood.v87.11.4495.bloodjournal87114495.
Texto completoCONLON, J. MICHAEL. "Peptide Tyrosine-Tyrosine (PYY) — An Evolutionary Perspective". American Zoologist 35, n.º 6 (diciembre de 1995): 466–73. http://dx.doi.org/10.1093/icb/35.6.466.
Texto completoRocchi, Stéphane, Sophie Tartare-Deckert, Joseph Murdaca, Marina Holgado-Madruga, Albert J. Wong y Emmanuel Van Obberghen. "Determination of Gab1 (Grb2-Associated Binder-1) Interaction with Insulin Receptor-Signaling Molecules". Molecular Endocrinology 12, n.º 7 (1 de julio de 1998): 914–23. http://dx.doi.org/10.1210/mend.12.7.0141.
Texto completoSun, Biyun, A. Daryl Ariawan, Holly Warren, Sophia C. Goodchild, Marc in het Panhuis, Lars M. Ittner y Adam D. Martin. "Programmable enzymatic oxidation of tyrosine–lysine tetrapeptides". Journal of Materials Chemistry B 8, n.º 15 (2020): 3104–12. http://dx.doi.org/10.1039/d0tb00250j.
Texto completoBacker, J. M., S. E. Shoelson, M. A. Weiss, Q. X. Hua, R. B. Cheatham, E. Haring, D. C. Cahill y M. F. White. "The insulin receptor juxtamembrane region contains two independent tyrosine/beta-turn internalization signals." Journal of Cell Biology 118, n.º 4 (15 de agosto de 1992): 831–39. http://dx.doi.org/10.1083/jcb.118.4.831.
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