Статті в журналах з теми "SH2 domain family"
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Panchamoorthy, G., T. Fukazawa, L. Stolz, G. Payne, K. Reedquist, S. Shoelson, Z. Songyang, L. Cantley, C. Walsh, and H. Band. "Physical and functional interactions between SH2 and SH3 domains of the Src family protein tyrosine kinase p59fyn." Molecular and Cellular Biology 14, no. 9 (September 1994): 6372–85. http://dx.doi.org/10.1128/mcb.14.9.6372-6385.1994.
Повний текст джерелаPanchamoorthy, G., T. Fukazawa, L. Stolz, G. Payne, K. Reedquist, S. Shoelson, Z. Songyang, L. Cantley, C. Walsh, and H. Band. "Physical and functional interactions between SH2 and SH3 domains of the Src family protein tyrosine kinase p59fyn." Molecular and Cellular Biology 14, no. 9 (September 1994): 6372–85. http://dx.doi.org/10.1128/mcb.14.9.6372.
Повний текст джерелаRichard, S., D. Yu, K. J. Blumer, D. Hausladen, M. W. Olszowy, P. A. Connelly, and A. S. Shaw. "Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1." Molecular and Cellular Biology 15, no. 1 (January 1995): 186–97. http://dx.doi.org/10.1128/mcb.15.1.186.
Повний текст джерелаDumas, Caroline, Anna Schmoker, Shannon Bennett, Amara Chittenden, Chelsea Darwin, Helena Gaffney, Hannah Lewis, et al. "Novel Interactors of the SH2 Domain of the Signaling Adaptors CRK and CRKL Identified in Neuro2A Cells." American Journal of Undergraduate Research 19, no. 3 (December 31, 2022): 47–55. http://dx.doi.org/10.33697/ajur.2022.068.
Повний текст джерелаLi, Minghua, Zhiqin Li, David L. Morris та Liangyou Rui. "Identification of SH2B2β as an Inhibitor for SH2B1- and SH2B2α-Promoted Janus Kinase-2 Activation and Insulin Signaling". Endocrinology 148, № 4 (1 квітня 2007): 1615–21. http://dx.doi.org/10.1210/en.2006-1010.
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 джерелаMayer, B. J., and D. Baltimore. "Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase." Molecular and Cellular Biology 14, no. 5 (May 1994): 2883–94. http://dx.doi.org/10.1128/mcb.14.5.2883-2894.1994.
Повний текст джерелаMayer, B. J., and D. Baltimore. "Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase." Molecular and Cellular Biology 14, no. 5 (May 1994): 2883–94. http://dx.doi.org/10.1128/mcb.14.5.2883.
Повний текст джерелаMargolis, Ben. "The GRB family of SH2 domain proteins." Progress in Biophysics and Molecular Biology 62, no. 3 (January 1994): 223–44. http://dx.doi.org/10.1016/0079-6107(94)90013-2.
Повний текст джерелаWang, Bing, Serge Lemay, Schickwann Tsai, and André Veillette. "SH2 Domain-Mediated Interaction of Inhibitory Protein Tyrosine Kinase Csk with Protein Tyrosine Phosphatase-HSCF." Molecular and Cellular Biology 21, no. 4 (February 15, 2001): 1077–88. http://dx.doi.org/10.1128/mcb.21.4.1077-1088.2001.
Повний текст джерелаKurzer, Jason H., Pipsa Saharinen, Olli Silvennoinen, and Christin Carter-Su. "Binding of SH2-B Family Members within a Potential Negative Regulatory Region Maintains JAK2 in an Active State." Molecular and Cellular Biology 26, no. 17 (September 1, 2006): 6381–94. http://dx.doi.org/10.1128/mcb.00570-06.
Повний текст джерелаMatthews, R. J., D. B. Bowne, E. Flores, and M. L. Thomas. "Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences." Molecular and Cellular Biology 12, no. 5 (May 1992): 2396–405. http://dx.doi.org/10.1128/mcb.12.5.2396-2405.1992.
Повний текст джерелаMatthews, R. J., D. B. Bowne, E. Flores, and M. L. Thomas. "Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences." Molecular and Cellular Biology 12, no. 5 (May 1992): 2396–405. http://dx.doi.org/10.1128/mcb.12.5.2396.
Повний текст джерелаBerg, Angela, Martin Gräber, Sebastian Schmutzler, Ralf Hoffmann, and Thorsten Berg. "A High-Throughput Fluorescence Polarization-Based Assay for the SH2 Domain of STAT4." Methods and Protocols 5, no. 6 (November 23, 2022): 93. http://dx.doi.org/10.3390/mps5060093.
Повний текст джерелаPatsoukis, Nikolaos, Jonathan Duke-Cohan, Apoorvi Chaudhri, Eunyoung Park, Council Asia, Anders Berg, Gordon J. Freeman, Michael Eck, and Vassiliki A. Boussiotis. "The Two SH2 Domains of SHP-2 Bridge Two PD-1 Molecules Resulting in SHP-2 Activation and PD-1-Mediated Inhibition." Blood 132, Supplement 1 (November 29, 2018): 862. http://dx.doi.org/10.1182/blood-2018-99-117486.
Повний текст джерелаShen, Kexin, Jamie A. Moroco, Ravi K. Patel, Haibin Shi, John R. Engen, Heather R. Dorman, and Thomas E. Smithgall. "The Src family kinase Fgr is a transforming oncoprotein that functions independently of SH3-SH2 domain regulation." Science Signaling 11, no. 553 (October 23, 2018): eaat5916. http://dx.doi.org/10.1126/scisignal.aat5916.
Повний текст джерелаWang, Lawrence L., Julie Blasioli, David R. Plas, Matthew L. Thomas, and Wayne M. Yokoyama. "Specificity of the SH2 Domains of SHP-1 in the Interaction with the Immunoreceptor Tyrosine-Based Inhibitory Motif-Bearing Receptor gp49B." Journal of Immunology 162, no. 3 (February 1, 1999): 1318–23. http://dx.doi.org/10.4049/jimmunol.162.3.1318.
Повний текст джерелаMayoral-Varo, Víctor, María Pilar Sánchez-Bailón, Annarica Calcabrini, Marta García-Hernández, Valerio Frezza, María Elena Martín, Víctor M. González, and Jorge Martín-Pérez. "The Relevance of the SH2 Domain for c-Src Functionality in Triple-Negative Breast Cancer Cells." Cancers 13, no. 3 (January 26, 2021): 462. http://dx.doi.org/10.3390/cancers13030462.
Повний текст джерелаWeerawarna, Pathum M., and Timothy I. Richardson. "Lyn Kinase Structure, Regulation, and Involvement in Neurodegenerative Diseases: A Mini Review." Kinases and Phosphatases 1, no. 1 (January 23, 2023): 23–38. http://dx.doi.org/10.3390/kinasesphosphatases1010004.
Повний текст джерелаSheets, Michael P., Usha P. Warrior, Hosup Yoon, Karl W. Mollison, Stevan W. Djuric, and James M. Trevillyan. "A High-Capacity Scintillation Proximity Assay for the Discovery and Evaluation of ZAP-70 Tandem SH2 Domain Antagonists." Journal of Biomolecular Screening 3, no. 2 (March 1998): 139–44. http://dx.doi.org/10.1177/108705719800300208.
Повний текст джерелаKan, Yagmur, YiTing Paung, Markus A. Seeliger, and W. Todd Miller. "Domain Architecture of the Nonreceptor Tyrosine Kinase Ack1." Cells 12, no. 6 (March 15, 2023): 900. http://dx.doi.org/10.3390/cells12060900.
Повний текст джерелаAHMED, Zamal, Beverley J. SMITH, Kei KOTANI, Peter WILDEN, and Tahir S. PILLAY. "APS, an adapter protein with a PH and SH2 domain, is a substrate for the insulin receptor kinase." Biochemical Journal 341, no. 3 (July 26, 1999): 665–68. http://dx.doi.org/10.1042/bj3410665.
Повний текст джерелаGe, Liang, Bo Wu, Youjia Zhang, Jiarong Wang, Hongxin Zhao, and Junfeng Wang. "Biochemical and NMR characterization of the interactions of Vav2–SH2 domain with lipids and the EphA2 juxtamembrane region on membrane." Biochemical Journal 477, no. 19 (October 12, 2020): 3791–801. http://dx.doi.org/10.1042/bcj20200300.
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 джерелаAhmed, Z., and T. S. Pillay. "Functional effects of APS and SH2-B on insulin receptor signalling." Biochemical Society Transactions 29, no. 4 (August 1, 2001): 529–34. http://dx.doi.org/10.1042/bst0290529.
Повний текст джерелаAsada, Hiroshi, Naoto Ishii, Yoshiteru Sasaki, Kazuhiro Endo, Hirotake Kasai, Nobuyuki Tanaka, Toshikazu Takeshita, Shigeru Tsuchiya, Tasuke Konno, and Kazuo Sugamura. "Grf40, A Novel Grb2 Family Member, Is Involved in T Cell Signaling through Interaction with SLP-76 and LAT." Journal of Experimental Medicine 189, no. 9 (May 3, 1999): 1383–90. http://dx.doi.org/10.1084/jem.189.9.1383.
Повний текст джерелаNishi, Masahiro, Eric D. Werner, Byung-Chul Oh, J. Daniel Frantz, Sirano Dhe-Paganon, Lone Hansen, Jongsoon Lee, and Steven E. Shoelson. "Kinase Activation through Dimerization by Human SH2-B." Molecular and Cellular Biology 25, no. 7 (April 1, 2005): 2607–21. http://dx.doi.org/10.1128/mcb.25.7.2607-2621.2005.
Повний текст джерелаMehlmann, Lisa M., and Laurinda A. Jaffe. "SH2 domain-mediated activation of an SRC family kinase is not required to initiate Ca2+ release at fertilization in mouse eggs." Reproduction 129, no. 5 (May 2005): 557–64. http://dx.doi.org/10.1530/rep.1.00638.
Повний текст джерелаJiao, H., K. Berrada, W. Yang, M. Tabrizi, L. C. Platanias, and T. Yi. "Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1." Molecular and Cellular Biology 16, no. 12 (December 1996): 6985–92. http://dx.doi.org/10.1128/mcb.16.12.6985.
Повний текст джерелаKohmura, N., T. Yagi, Y. Tomooka, M. Oyanagi, R. Kominami, N. Takeda, J. Chiba, Y. Ikawa, and S. Aizawa. "A novel nonreceptor tyrosine kinase, Srm: cloning and targeted disruption." Molecular and Cellular Biology 14, no. 10 (October 1994): 6915–25. http://dx.doi.org/10.1128/mcb.14.10.6915-6925.1994.
Повний текст джерелаKohmura, N., T. Yagi, Y. Tomooka, M. Oyanagi, R. Kominami, N. Takeda, J. Chiba, Y. Ikawa, and S. Aizawa. "A novel nonreceptor tyrosine kinase, Srm: cloning and targeted disruption." Molecular and Cellular Biology 14, no. 10 (October 1994): 6915–25. http://dx.doi.org/10.1128/mcb.14.10.6915.
Повний текст джерелаCobb, B. S., M. D. Schaller, T. H. Leu, and J. T. Parsons. "Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK." Molecular and Cellular Biology 14, no. 1 (January 1994): 147–55. http://dx.doi.org/10.1128/mcb.14.1.147-155.1994.
Повний текст джерелаCobb, B. S., M. D. Schaller, T. H. Leu, and J. T. Parsons. "Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK." Molecular and Cellular Biology 14, no. 1 (January 1994): 147–55. http://dx.doi.org/10.1128/mcb.14.1.147.
Повний текст джерелаChen, Riyan, Sylvain Latour, Xiaochu Shi, and André Veillette. "Association between SAP and FynT: Inducible SH3 Domain-Mediated Interaction Controlled by Engagement of the SLAM Receptor." Molecular and Cellular Biology 26, no. 15 (August 1, 2006): 5559–68. http://dx.doi.org/10.1128/mcb.00357-06.
Повний текст джерелаLavens, Delphine, Peter Ulrichts, Dominiek Catteeuw, Kris Gevaert, Joël Vandekerckhove, Frank Peelman, Sven Eyckerman, and Jan Tavernier. "The C-terminus of CIS defines its interaction pattern." Biochemical Journal 401, no. 1 (December 11, 2006): 257–67. http://dx.doi.org/10.1042/bj20060242.
Повний текст джерелаIsakov, N., R. L. Wange, W. H. Burgess, J. D. Watts, R. Aebersold, and L. E. Samelson. "ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs: the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity." Journal of Experimental Medicine 181, no. 1 (January 1, 1995): 375–80. http://dx.doi.org/10.1084/jem.181.1.375.
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 джерелаNika, Konstantina, Lutz Tautz, Yutaka Arimura, Torkel Vang, Scott Williams, and Tomas Mustelin. "A Weak Lck Tail Bite Is Necessary for Lck Function in T Cell Antigen Receptor Signaling." Journal of Biological Chemistry 282, no. 49 (September 26, 2007): 36000–36009. http://dx.doi.org/10.1074/jbc.m702779200.
Повний текст джерелаHowell, B. W., and J. A. Cooper. "Csk suppression of Src involves movement of Csk to sites of Src activity." Molecular and Cellular Biology 14, no. 8 (August 1994): 5402–11. http://dx.doi.org/10.1128/mcb.14.8.5402-5411.1994.
Повний текст джерелаHowell, B. W., and J. A. Cooper. "Csk suppression of Src involves movement of Csk to sites of Src activity." Molecular and Cellular Biology 14, no. 8 (August 1994): 5402–11. http://dx.doi.org/10.1128/mcb.14.8.5402.
Повний текст джерелаTanaka, M., R. Gupta, and B. J. Mayer. "Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins." Molecular and Cellular Biology 15, no. 12 (December 1995): 6829–37. http://dx.doi.org/10.1128/mcb.15.12.6829.
Повний текст джерелаHELLYER, Nathan J., Kunrong CHENG, and John G. KOLAND. "ErbB3 (HER3) interaction with the p85 regulatory subunit of phosphoinositide 3-kinase." Biochemical Journal 333, no. 3 (August 1, 1998): 757–63. http://dx.doi.org/10.1042/bj3330757.
Повний текст джерелаYang, Edward, Zilong Wen, Richard L. Haspel, Jue J. Zhang, and James E. Darnell. "The Linker Domain of Stat1 Is Required for Gamma Interferon-Driven Transcription." Molecular and Cellular Biology 19, no. 7 (July 1, 1999): 5106–12. http://dx.doi.org/10.1128/mcb.19.7.5106.
Повний текст джерелаCampbell, S. J., and R. M. Jackson. "Diversity in the SH2 domain family phosphotyrosyl peptide binding site." Protein Engineering, Design and Selection 16, no. 3 (March 2003): 217–27. http://dx.doi.org/10.1093/proeng/gzg025.
Повний текст джерелаLiao, Yi-Chun, Lizhen Si, Ralph W. deVere White, and Su Hao Lo. "The phosphotyrosine-independent interaction of DLC-1 and the SH2 domain of cten regulates focal adhesion localization and growth suppression activity of DLC-1." Journal of Cell Biology 176, no. 1 (December 26, 2006): 43–49. http://dx.doi.org/10.1083/jcb.200608015.
Повний текст джерелаJahn, Thomas, Petra Seipel, Susanne Urschel, Christian Peschel, and Justus Duyster. "Role for the Adaptor Protein Grb10 in the Activation of Akt." Molecular and Cellular Biology 22, no. 4 (February 15, 2002): 979–91. http://dx.doi.org/10.1128/mcb.22.4.979-991.2002.
Повний текст джерелаZhang, Tong, Wei Hua Kee, Kah Tong Seow, Winnie Fung, and Xinmin Cao. "The Coiled-Coil Domain of Stat3 Is Essential for Its SH2 Domain-Mediated Receptor Binding and Subsequent Activation Induced by Epidermal Growth Factor and Interleukin-6." Molecular and Cellular Biology 20, no. 19 (October 1, 2000): 7132–39. http://dx.doi.org/10.1128/mcb.20.19.7132-7139.2000.
Повний текст джерелаCourtneidge, Sara A., Stefano Fumagalli, Manfred Koegl, Giulio Superti-Furga, and Geraldine M. Twamley-Stein. "The Src family of protein tyrosine kinases: regulation and functions." Development 119, Supplement (December 1, 1993): 57–64. http://dx.doi.org/10.1242/dev.119.supplement.57.
Повний текст джерелаWolf, Ingrid, Brendan J. Jenkins, Yan Liu, Martina Seiffert, Joseph M. Custodio, Paul Young, and Larry R. Rohrschneider. "Gab3, a New DOS/Gab Family Member, Facilitates Macrophage Differentiation." Molecular and Cellular Biology 22, no. 1 (January 1, 2002): 231–44. http://dx.doi.org/10.1128/mcb.22.1.231-244.2002.
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