Статті в журналах з теми "Src homology 2 domain (SH2 domain)"
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Ознайомтеся з топ-50 статей у журналах для дослідження на тему "Src homology 2 domain (SH2 domain)".
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Tian, M., and G. S. Martin. "The role of the Src homology domains in morphological transformation by v-src." Molecular Biology of the Cell 8, no. 7 (July 1997): 1183–93. http://dx.doi.org/10.1091/mbc.8.7.1183.
Повний текст джерелаKoch, C. A., M. F. Moran, D. Anderson, X. Q. Liu, G. Mbamalu, and T. Pawson. "Multiple SH2-mediated interactions in v-src-transformed cells." Molecular and Cellular Biology 12, no. 3 (March 1992): 1366–74. http://dx.doi.org/10.1128/mcb.12.3.1366-1374.1992.
Повний текст джерелаKoch, C. A., M. F. Moran, D. Anderson, X. Q. Liu, G. Mbamalu, and T. Pawson. "Multiple SH2-mediated interactions in v-src-transformed cells." Molecular and Cellular Biology 12, no. 3 (March 1992): 1366–74. http://dx.doi.org/10.1128/mcb.12.3.1366.
Повний текст джерелаSong, X., X. Shang, T. Ju, R. Cerny, W. Niu, and J. Guo. "A photoactivatable Src homology 2 (SH2) domain." RSC Advances 6, no. 56 (2016): 51120–24. http://dx.doi.org/10.1039/c6ra06211c.
Повний текст джерелаKlippel, A., J. A. Escobedo, W. J. Fantl, and L. T. Williams. "The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platelet-derived growth factor beta receptor." Molecular and Cellular Biology 12, no. 4 (April 1992): 1451–59. http://dx.doi.org/10.1128/mcb.12.4.1451-1459.1992.
Повний текст джерелаKlippel, A., J. A. Escobedo, W. J. Fantl, and L. T. Williams. "The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platelet-derived growth factor beta receptor." Molecular and Cellular Biology 12, no. 4 (April 1992): 1451–59. http://dx.doi.org/10.1128/mcb.12.4.1451.
Повний текст джерелаXing, Z., H. C. Chen, J. K. Nowlen, S. J. Taylor, D. Shalloway, and J. L. Guan. "Direct interaction of v-Src with the focal adhesion kinase mediated by the Src SH2 domain." Molecular Biology of the Cell 5, no. 4 (April 1994): 413–21. http://dx.doi.org/10.1091/mbc.5.4.413.
Повний текст джерелаBibbins, K. B., H. Boeuf, and H. E. Varmus. "Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides." Molecular and Cellular Biology 13, no. 12 (December 1993): 7278–87. http://dx.doi.org/10.1128/mcb.13.12.7278-7287.1993.
Повний текст джерелаBibbins, K. B., H. Boeuf, and H. E. Varmus. "Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides." Molecular and Cellular Biology 13, no. 12 (December 1993): 7278–87. http://dx.doi.org/10.1128/mcb.13.12.7278.
Повний текст джерелаSongyang, Z., S. E. Shoelson, J. McGlade, P. Olivier, T. Pawson, X. R. Bustelo, M. Barbacid, H. Sabe, H. Hanafusa, and T. Yi. "Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav." Molecular and Cellular Biology 14, no. 4 (April 1994): 2777–85. http://dx.doi.org/10.1128/mcb.14.4.2777-2785.1994.
Повний текст джерелаSongyang, Z., S. E. Shoelson, J. McGlade, P. Olivier, T. Pawson, X. R. Bustelo, M. Barbacid, H. Sabe, H. Hanafusa, and T. Yi. "Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav." Molecular and Cellular Biology 14, no. 4 (April 1994): 2777–85. http://dx.doi.org/10.1128/mcb.14.4.2777.
Повний текст джерелаJoseph, Raji E., Nathaniel D. Ginder, Julie A. Hoy, Jay C. Nix, D. Bruce Fulton, Richard B. Honzatko, and Amy H. Andreotti. "Structure of the interleukin-2 tyrosine kinase Src homology 2 domain; comparison between X-ray and NMR-derived structures." Acta Crystallographica Section F Structural Biology and Crystallization Communications 68, no. 2 (January 25, 2012): 145–53. http://dx.doi.org/10.1107/s1744309111049761.
Повний текст джерелаShe, H. Y., S. Rockow, J. Tang, R. Nishimura, E. Y. Skolnik, M. Chen, B. Margolis, and W. Li. "Wiskott-Aldrich syndrome protein is associated with the adapter protein Grb2 and the epidermal growth factor receptor in living cells." Molecular Biology of the Cell 8, no. 9 (September 1997): 1709–21. http://dx.doi.org/10.1091/mbc.8.9.1709.
Повний текст джерелаKoch, C. A., M. Moran, I. Sadowski, and T. Pawson. "The common src homology region 2 domain of cytoplasmic signaling proteins is a positive effector of v-fps tyrosine kinase function." Molecular and Cellular Biology 9, no. 10 (October 1989): 4131–40. http://dx.doi.org/10.1128/mcb.9.10.4131-4140.1989.
Повний текст джерелаKoch, C. A., M. Moran, I. Sadowski, and T. Pawson. "The common src homology region 2 domain of cytoplasmic signaling proteins is a positive effector of v-fps tyrosine kinase function." Molecular and Cellular Biology 9, no. 10 (October 1989): 4131–40. http://dx.doi.org/10.1128/mcb.9.10.4131.
Повний текст джерелаStoica, Bogdan, Karen E. DeBell, Laurie Graham, Barbara L. Rellahan, Maria A. Alava, Jorge Laborda та Ezio Bonvini. "The Amino-Terminal Src Homology 2 Domain of Phospholipase Cγ1 Is Essential for TCR-Induced Tyrosine Phosphorylation of Phospholipase Cγ1". Journal of Immunology 160, № 3 (1 лютого 1998): 1059–66. http://dx.doi.org/10.4049/jimmunol.160.3.1059.
Повний текст джерелаDuplay, P., M. Thome, F. Hervé, and O. Acuto. "p56lck interacts via its src homology 2 domain with the ZAP-70 kinase." Journal of Experimental Medicine 179, no. 4 (April 1, 1994): 1163–72. http://dx.doi.org/10.1084/jem.179.4.1163.
Повний текст джерелаSeidel-Dugan, C., B. E. Meyer, S. M. Thomas, and J. S. Brugge. "Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src." Molecular and Cellular Biology 12, no. 4 (April 1992): 1835–45. http://dx.doi.org/10.1128/mcb.12.4.1835-1845.1992.
Повний текст джерелаSeidel-Dugan, C., B. E. Meyer, S. M. Thomas, and J. S. Brugge. "Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src." Molecular and Cellular Biology 12, no. 4 (April 1992): 1835–45. http://dx.doi.org/10.1128/mcb.12.4.1835.
Повний текст джерелаNorthrop, J. P., M. J. Pustelnik, A. T. Lu, and J. R. Grove. "Characterization of the roles of SH2 domain-containing proteins in T-lymphocyte activation by using dominant negative SH2 domains." Molecular and Cellular Biology 16, no. 5 (May 1996): 2255–63. http://dx.doi.org/10.1128/mcb.16.5.2255.
Повний текст джерелаSchüller, Annika C., Zamal Ahmed, James A. Levitt, Kin M. Suen, Klaus Suhling, and John E. Ladbury. "Indirect recruitment of the signalling adaptor Shc to the fibroblast growth factor receptor 2 (FGFR2)." Biochemical Journal 416, no. 2 (November 12, 2008): 189–99. http://dx.doi.org/10.1042/bj20080887.
Повний текст джерелаHorstmann, Martin A., and Peter Nollau. "Src Homology 2 Domain Binding as a Phosphoproteomic Approach to Signaling in Acute Lymphoblastic Leukemia." Blood 104, no. 11 (November 16, 2004): 4442. http://dx.doi.org/10.1182/blood.v104.11.4442.4442.
Повний текст джерелаWaksman, Gabriel, Sangaralingam Kumaran, and Olga Lubman. "SH2 domains: role, structure and implications for molecular medicine." Expert Reviews in Molecular Medicine 6, no. 3 (January 30, 2004): 1–18. http://dx.doi.org/10.1017/s1462399404007331.
Повний текст джерелаYogo, Keiichiro, Megumi Mizutamari, Kazuta Mishima, Hiromi Takenouchi, Norihiro Ishida-Kitagawa, Takehiko Sasaki, and Tatsuo Takeya. "Src Homology 2 (SH2)-Containing 5′-Inositol Phosphatase Localizes to Podosomes, and the SH2 Domain Is Implicated in the Attenuation of Bone Resorption in Osteoclasts." Endocrinology 147, no. 7 (July 1, 2006): 3307–17. http://dx.doi.org/10.1210/en.2005-1309.
Повний текст джерелаTridandapani, Susheela, Madhura Pradhan, James R. LaDine, Stacey Garber, Clark L. Anderson та K. Mark Coggeshall. "Protein Interactions of Src Homology 2 (SH2) Domain-Containing Inositol Phosphatase (SHIP): Association with Shc Displaces SHIP from FcγRIIb in B Cells". Journal of Immunology 162, № 3 (1 лютого 1999): 1408–14. http://dx.doi.org/10.4049/jimmunol.162.3.1408.
Повний текст джерелаRIORDAN, Stephen M., Sukhwinderjit LIDDER, Roger WILLIAMS та George G. SKOUTERIS. "The β-subunit of the hepatocyte growth factor/scatter factor (HGF/SF) receptor phosphorylates and associates with CrkII: expression of CrkII enhances HGF/SF-induced mitogenesis". Biochemical Journal 350, № 3 (8 вересня 2000): 925–32. http://dx.doi.org/10.1042/bj3500925.
Повний текст джерелаMeng, Li, JinPing Luo, Chunhua Li, and William H. Kinsey. "Role of Src homology 2 domain-mediated PTK signaling in mouse zygotic development." Reproduction 132, no. 3 (September 2006): 413–21. http://dx.doi.org/10.1530/rep.1.01151.
Повний текст джерелаde Araujo, Elvin D., Anna Orlova, Heidi A. Neubauer, Dávid Bajusz, Hyuk-Soo Seo, Sirano Dhe-Paganon, György M. Keserű, Richard Moriggl, and Patrick T. Gunning. "Structural Implications of STAT3 and STAT5 SH2 Domain Mutations." Cancers 11, no. 11 (November 8, 2019): 1757. http://dx.doi.org/10.3390/cancers11111757.
Повний текст джерелаDombrosky-Ferlan, Patrice, Anatoly Grishin, Roberto J. Botelho, Matthew Sampson, Lin Wang, William A. Rudert, Sergio Grinstein, and Seth J. Corey. "Felic (CIP4b), a novel binding partner with the Src kinase Lyn and Cdc42, localizes to the phagocytic cup." Blood 101, no. 7 (April 1, 2003): 2804–9. http://dx.doi.org/10.1182/blood-2002-03-0851.
Повний текст джерелаKOTANI, Kei, Peter WILDEN та Tahir S. PILLAY. "SH2-Bα is an insulin-receptor adapter protein and substrate that interacts with the activation loop of the insulin-receptor kinase". Biochemical Journal 335, № 1 (1 жовтня 1998): 103–9. http://dx.doi.org/10.1042/bj3350103.
Повний текст джерелаTu, Yizeng, Fugang Li, and Chuanyue Wu. "Nck-2, a Novel Src Homology2/3-containing Adaptor Protein That Interacts with the LIM-only Protein PINCH and Components of Growth Factor Receptor Kinase-signaling Pathways." Molecular Biology of the Cell 9, no. 12 (December 1998): 3367–82. http://dx.doi.org/10.1091/mbc.9.12.3367.
Повний текст джерелаMuller, A. J., J. C. Young, A. M. Pendergast, M. Pondel, N. R. Landau, D. R. Littman, and O. N. Witte. "BCR first exon sequences specifically activate the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias." Molecular and Cellular Biology 11, no. 4 (April 1991): 1785–92. http://dx.doi.org/10.1128/mcb.11.4.1785-1792.1991.
Повний текст джерелаMuller, A. J., J. C. Young, A. M. Pendergast, M. Pondel, N. R. Landau, D. R. Littman, and O. N. Witte. "BCR first exon sequences specifically activate the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias." Molecular and Cellular Biology 11, no. 4 (April 1991): 1785–92. http://dx.doi.org/10.1128/mcb.11.4.1785.
Повний текст джерелаSchlaepfer, D. D., M. A. Broome, and T. Hunter. "Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: involvement of the Grb2, p130cas, and Nck adaptor proteins." Molecular and Cellular Biology 17, no. 3 (March 1997): 1702–13. http://dx.doi.org/10.1128/mcb.17.3.1702.
Повний текст джерелаJu, Tong, Wei Niu, and Jiantao Guo. "Evolution of Src Homology 2 (SH2) Domain to Recognize Sulfotyrosine." ACS Chemical Biology 11, no. 9 (July 21, 2016): 2551–57. http://dx.doi.org/10.1021/acschembio.6b00555.
Повний текст джерелаCooper, J. A., and A. Kashishian. "In vivo binding properties of SH2 domains from GTPase-activating protein and phosphatidylinositol 3-kinase." Molecular and Cellular Biology 13, no. 3 (March 1993): 1737–45. http://dx.doi.org/10.1128/mcb.13.3.1737-1745.1993.
Повний текст джерелаCooper, J. A., and A. Kashishian. "In vivo binding properties of SH2 domains from GTPase-activating protein and phosphatidylinositol 3-kinase." Molecular and Cellular Biology 13, no. 3 (March 1993): 1737–45. http://dx.doi.org/10.1128/mcb.13.3.1737.
Повний текст джерелаVerderame, M. F. "pp60v-src transformation of rat cells but not chicken cells strongly correlates with low-affinity phosphopeptide binding by the SH2 domain." Molecular Biology of the Cell 8, no. 5 (May 1997): 843–54. http://dx.doi.org/10.1091/mbc.8.5.843.
Повний текст джерелаWARNER, Andrea J., Jennifer LOPEZ-DEE, Emma L. KNIGHT, James R. FERAMISCO, and Sally A. PRIGENT. "The Shc-related adaptor protein, Sck, forms a complex with the vascular-endothelial-growth-factor receptor KDR in transfected cells." Biochemical Journal 347, no. 2 (April 10, 2000): 501–9. http://dx.doi.org/10.1042/bj3470501.
Повний текст джерелаSACI, Abdelhafid, Wang-Qing LIU, Michel VIDAL, Christiane GARBAY, Francine RENDU, and Christilla BACHELOT-LOZA. "Differential effect of the inhibition of Grb2–SH3 interactions in platelet activation induced by thrombin and by Fc receptor engagement." Biochemical Journal 363, no. 3 (April 24, 2002): 717–25. http://dx.doi.org/10.1042/bj3630717.
Повний текст джерелаTakagi, Norio, Herman H. Cheung, Nankie Bissoon, Lucy Teves, M. Christopher Wallace, and James W. Gurd. "The Effect of Transient Global Ischemia on the Interaction of Src and Fyn with the N-Methyl-d-Aspartate Receptor and Postsynaptic Densities: Possible Involvement of Src Homology 2 Domains." Journal of Cerebral Blood Flow & Metabolism 19, no. 8 (August 1999): 880–88. http://dx.doi.org/10.1097/00004647-199908000-00007.
Повний текст джерелаFujioka, Y., T. Matozaki, T. Noguchi, A. Iwamatsu, T. Yamao, N. Takahashi, M. Tsuda, T. Takada, and M. Kasuga. "A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion." Molecular and Cellular Biology 16, no. 12 (December 1996): 6887–99. http://dx.doi.org/10.1128/mcb.16.12.6887.
Повний текст джерелаDeBell, Karen, Laurie Graham, Ilona Reischl, Carmen Serrano, Ezio Bonvini та Barbara Rellahan. "Intramolecular Regulation of Phospholipase C-γ1 by Its C-Terminal Src Homology 2 Domain". Molecular and Cellular Biology 27, № 3 (20 листопада 2006): 854–63. http://dx.doi.org/10.1128/mcb.01400-06.
Повний текст джерелаVisperas, Patrick R., Jonathan A. Winger, Timothy M. Horton, Neel H. Shah, Diane J. Aum, Alyssa Tao, Tiago Barros, et al. "Modification by covalent reaction or oxidation of cysteine residues in the tandem-SH2 domains of ZAP-70 and Syk can block phosphopeptide binding." Biochemical Journal 465, no. 1 (December 12, 2014): 149–61. http://dx.doi.org/10.1042/bj20140793.
Повний текст джерелаVelazquez, Laura, Gerald D. Gish, Peter van der Geer, Lorne Taylor, Johanna Shulman, and Tony Pawson. "The Shc adaptor protein forms interdependent phosphotyrosine-mediated protein complexes in mast cells stimulated with interleukin 3." Blood 96, no. 1 (July 1, 2000): 132–38. http://dx.doi.org/10.1182/blood.v96.1.132.
Повний текст джерелаVelazquez, Laura, Gerald D. Gish, Peter van der Geer, Lorne Taylor, Johanna Shulman, and Tony Pawson. "The Shc adaptor protein forms interdependent phosphotyrosine-mediated protein complexes in mast cells stimulated with interleukin 3." Blood 96, no. 1 (July 1, 2000): 132–38. http://dx.doi.org/10.1182/blood.v96.1.132.013k13_132_138.
Повний текст джерелаHirai, H., and H. E. Varmus. "Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src." Molecular and Cellular Biology 10, no. 4 (April 1990): 1307–18. http://dx.doi.org/10.1128/mcb.10.4.1307-1318.1990.
Повний текст джерелаHirai, H., and H. E. Varmus. "Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src." Molecular and Cellular Biology 10, no. 4 (April 1990): 1307–18. http://dx.doi.org/10.1128/mcb.10.4.1307.
Повний текст джерелаMuller, A. J., A. M. Pendergast, M. H. Havlik, L. Puil, T. Pawson, and O. N. Witte. "A limited set of SH2 domains binds BCR through a high-affinity phosphotyrosine-independent interaction." Molecular and Cellular Biology 12, no. 11 (November 1992): 5087–93. http://dx.doi.org/10.1128/mcb.12.11.5087-5093.1992.
Повний текст джерелаMuller, A. J., A. M. Pendergast, M. H. Havlik, L. Puil, T. Pawson, and O. N. Witte. "A limited set of SH2 domains binds BCR through a high-affinity phosphotyrosine-independent interaction." Molecular and Cellular Biology 12, no. 11 (November 1992): 5087–93. http://dx.doi.org/10.1128/mcb.12.11.5087.
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