BLNK Required for Coupling Syk to PLCγ2 and Rac1-JNK in B Cells

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617 · see citing works

A new generation of Ca2+ indicators with greatly improved fluorescence properties.

Grynkiewicz, G., Poenie, M., & Tsien, R. Y. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83641-4 · Cited by 21,722 · see citing works

The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling

Lowenstein, E. J., Daly, R. J., Batzer, A., Li, W., Margolis, B. L., Lammers, R., Ullrich, A., Skolnik, E. Y., Bar‐Sagi, D., & Schlessinger, J. (1992) · Cell · doi:10.1016/0092-8674(92)90167-b · Cited by 1,632 · see citing works

LAT

Zhang, W., Sloan‐Lancaster, J., Kitchen, J., Trible, R. P., & Samelson, L. E. (1998) · Cell · doi:10.1016/s0092-8674(00)80901-0 · Cited by 1,269 · see citing works

Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product

Crespo, P., Schuebel, K. E., Ostrom, A. A., Gutkind, J. S., & Bustelo, X. R. (1997) · Nature · doi:10.1038/385169a0 · Cited by 755 · see citing works

SH2 and SH3 domains

Pawson, T. J., & Schlessingert, J. (1993) · Current Biology · doi:10.1016/0960-9822(93)90350-w · Cited by 698 · see citing works

Tyrosine kinases Lyn and Syk regulate B cell receptor‐coupled Ca2+ mobilization through distinct pathways.

Takata, M., Sabe, H., Hata, A., Inazu, T., Homma, Y., Nukada, T., Yamamura, H., & Kurosaki, T. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06387.x · Cited by 650 · see citing works

Increase of the Catalytic Activity of Phospholipase C-γ1 by Tyrosine Phosphorylation

Nishibe, S., Wahl, M. I., Hernández‐Sotomayor, S. M. T., Tonks, N. K., Rhee, S. G., & Carpenter, G. F. (1990) · Science · doi:10.1126/science.1700866 · Cited by 635 · see citing works

Alternative membrane forms of Fc gamma RIII(CD16) on human natural killer cells and neutrophils. Cell type-specific expression of two genes that differ in single nucleotide substitutions.

Ravetch, J. V., & PERUSSIA, B. (1989) · The Journal of Experimental Medicine · doi:10.1084/jem.170.2.481 · Cited by 577 · see citing works

Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase.

Salim, K., Bottomley, M. J., Querfurth, E., Zvelebil, M., Gout, I. T., Scaife, R. M., Margolis, R. L., Gigg, R., Smith, C. I., Driscoll, P. C., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01014.x · Cited by 558 · see citing works

Untitled work

Fu (1998) · doi:10.1016/s1074-7613(00)80591-9 · Cited by 518 · see citing works

Deletion of SHIP or SHP-1 Reveals Two Distinct Pathways for Inhibitory Signaling

Ono, M., Okada, H., Bolland, S. M., Yanagi, S., Kurosaki, T., & Ravetch, J. V. (1997) · Cell · doi:10.1016/s0092-8674(00)80337-2 · Cited by 488 · see citing works

A role for Bruton's tyrosine kinase in B cell antigen receptor-mediated activation of phospholipase C-gamma 2.

Takata, M., & Kurosaki, T. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.1.31 · Cited by 487 · see citing works

A Comparative Analysis of the Phosphoinositide Binding Specificity of Pleckstrin Homology Domains

Rameh, L. E., Arvidsson, A., Carraway, K. L., Couvillon, A. D., Rathbun, G. A., Crompton, A. M., VanRenterghem, B., Czech, M., Ravichandran, K. S., Burakoff, S. J., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22059 · Cited by 460 · see citing works

INITIATION AND PROCESSING OF SIGNALS FROM THE B CELL ANTIGEN RECEPTOR

Reth, M. G., & Wienands, J. (1997) · Annual Review of Immunology · doi:10.1146/annurev.immunol.15.1.453 · Cited by 436 · see citing works

Uncoupling of Nonreceptor Tyrosine Kinases from PLC-γ1 in an SLP-76-Deficient T Cell

Yablonski, D., Kuhné, M. R., Kadlecek, T. A., & Weiss, A. (1998) · Science · doi:10.1126/science.281.5375.413 · Cited by 413 · see citing works

Btk/Tec kinases regulate sustained increases in intracellular Ca2+ following B‐cell receptor activation

Fluckiger, A.-C., Li, Z., Kato, R. M., Wahl, M. I., Ochs, H. D., Longnecker, R., Kinet, J.-P., Witte, O. N., Scharenberg, A. M., & Rawlings, D. J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.7.1973 · Cited by 403 · see citing works

SHIP Modulates Immune Receptor Responses by Regulating Membrane Association of Btk

Bolland, S. M., Pearse, R. N., Kurosaki, T., & Ravetch, J. V. (1998) · Immunity · doi:10.1016/s1074-7613(00)80555-5 · Cited by 384 · see citing works

Cell cycle-dependent activation of Ras

Taylor, S. J., & Shalloway, D. I. (1996) · Current Biology · doi:10.1016/s0960-9822(02)70785-9 · Cited by 383 · see citing works

Vav and SLP-76 Interact and Functionally Cooperate in IL-2 Gene Activation

Wu, J., Motto, D. G., Koretzky, G. A., & Weiss, A. (1996) · Immunity · doi:10.1016/s1074-7613(00)80485-9 · Cited by 333 · see citing works

Molecular Cloning of SLP-76, a 76-kDa Tyrosine Phosphoprotein Associated with Grb2 in T Cells

Jackman, J. K., Motto, D. G., Sun, Q., Tanemoto, M., Turck, C. W., Peltz, G., Koretzky, G. A., & Findell, P. R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7029 · Cited by 326 · see citing works

The complexity of signaling pathways activated by the BCR

DeFranco, A. L. (1997) · Current Opinion in Immunology · doi:10.1016/s0952-7915(97)80074-x · Cited by 318 · see citing works

POSITIVE VERSUS NEGATIVE SIGNALING BY LYMPHOCYTE ANTIGEN RECEPTORS

Healy, J. I., & Goodnow, C. C. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.645 · Cited by 317 · see citing works

The nucleotide sequence of the chick cytoplasmic β-actin gene

Kost, T. A., Theodorakis, N. D., & Hughes, S. H. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.23.8287 · Cited by 316 · see citing works

Syk Protein-tyrosine Kinase Is Regulated by Tyrosine-phosphorylated Iga/Ig/3 Immunoreceptor Tyrosine Activation Motif Binding and Autophosphorylation

Rowleyt, R. B., Burkhardtt, A. L., Chao, H.-G., Matsueda, G. R., & Bolen, J. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.19.11590 · Cited by 274 · see citing works

SLP-65: A New Signaling Component in B Lymphocytes which Requires Expression of the Antigen Receptor for Phosphorylation

Wienands, J., Schweikert, J., Wollscheid, B., Jumaa, H., Nielsen, P. J., & Reth, M. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.4.791 · Cited by 271 · see citing works

Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling.

Kurosaki, T., Johnson, S. A., Pao, L. I., Sada, K., Yamamura, H., & Cambier, J. C. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.182.6.1815 · Cited by 261 · see citing works

Phospholipase C-γ1 Interacts with Conserved Phosphotyrosyl Residues in the Linker Region of Syk and Is a Substrate for Syk

Law, C., Chandran, K. A., Sidorenko, S. P., & Clark, E. A. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.4.1305 · Cited by 225 · see citing works

Regulation of Vav–SLP-76 Binding by ZAP-70 and Its Relevance to TCRζ/CD3 Induction of Interleukin-2

Raab, M., da Silva, A. J., Findell, P. R., & Rudd, C. E. (1997) · Immunity · doi:10.1016/s1074-7613(00)80422-7 · Cited by 222 · see citing works

The B-cell antigen receptor complex

Reth, M. G., Hombach, J., Wienands, J., et al. (1991) · Immunology Today · doi:10.1016/0167-5699(91)90053-v · Cited by 208 · see citing works

B lymphocyte activation is accompanied by phosphorylation of a 72-kDa protein-tyrosine kinase

Hutchcroft, J. E., Harrison, M. L., & Geahlen, R. L. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98549-2 · Cited by 203 · see citing works

The B-cell antigen receptor complex: structure and signal transduction

Pleiman, C. M., D’Ambrosio, D., & Cambier, J. C. (1994) · Immunology Today · doi:10.1016/0167-5699(94)90267-4 · Cited by 200 · see citing works

Involvement of Guanosine Triphosphatases and Phospholipase C-γ2 in Extracellular Signal–regulated Kinase, c-Jun NH2-terminal Kinase, and p38 Mitogen-activated Protein Kinase Activation by the B Cell Antigen Receptor

Hashimoto, A., Okada, H., Jiang, A., Kurosaki, M., Greenberg, S., Clark, E. A., & Kurosaki, T. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.7.1287 · Cited by 199 · see citing works

Molecular mechanisms in B cell antigen receptor signaling

Kurosaki, T. (1997) · Current Opinion in Immunology · doi:10.1016/s0952-7915(97)80075-1 · Cited by 192 · see citing works

Requirement of phospholipase C-gamma 2 activation in surface immunoglobulin M-induced B cell apoptosis.

Takata, M., Homma, Y., & Kurosaki, T. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.182.4.907 · Cited by 190 · see citing works

The SH3 Domain-binding T Cell Tyrosyl Phosphoprotein p120

Fukazawa, T., Reedquist, K. A., Trüb, T., Soltoff, S. P., Panchamoorthy, G., Druker, B. J., Cantley, L. C., Shoelson, S. E., & Band, H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.19141 · Cited by 184 · see citing works

Molecular cloning and chromosomal localization of the human T-cell receptor zeta chain: distinction from the molecular CD3 complex.

Weissman, A. M., Hou, D., Orloff, D. G., et al. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.24.9709 · Cited by 179 · see citing works

p120 Is a Major Substrate of Tyrosine Phosphorylation upon B Cell Antigen Receptor Stimulation and Interacts in Vivo with Fyn and Syk Tyrosine Kinases, Grb2 and Shc Adaptors, and the p85 Subunit of Phosphatidylinositol 3-Kinase

Panchamoorthy, G., Fukazawa, T., Miyake, S., Soltoff, S. P., Reedquist, K. A., Druker, B. J., Shoelson, S. E., Cantley, L. C., & Band, H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.6.3187 · Cited by 171 · see citing works

Different Protein Tyrosine Kinases Are Required for B Cell Antigen Receptor–mediated Activation of Extracellular Signal–Regulated kinase, c-Jun NH2-terminal Kinase 1, and p38 Mitogen-activated Protein Kinase

Jiang, A., Craxton, A., Kurosaki, T., & Clark, E. A. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.7.1297 · Cited by 170 · see citing works

B cell antigen receptor cross-linking induces phosphorylation of the p21 <i>ras</i> oncoprotein activators SHC and mSOS1 as well as assembly of complexes containing SHC, GRB-2, mSOS1, and a 145-kDa tyrosine-phosphorylated protein.

Saxton, T. M., van Oostveen, I., Bowtell, D., Aebersold, R., & Gold, M. R. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.153.2.623 · Cited by 164 · see citing works

Evidence for an IgD homologue on chicken lymphocytes.

Chen, C.-L. H., Lehmeyer, J. E., & Cooper, M. D. (1982) · The Journal of Immunology · doi:10.4049/jimmunol.129.6.2580 · Cited by 160 · see citing works

A Second Type of Rat Phosphoinositide-specific Phospholipase C Containing a src-related Sequence Not Essential for Phosphoinositide-hydrolyzing Activity

Emori, Y., Homma, Y., Sorimachi, H., Kawasaki, H., Nakanishi, O., Suzuki, K., & Takenawa, T. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)88267-2 · Cited by 158 · see citing works

Molecular Cloning of the cDNA Encoding pp36, a Tyrosine-phosphorylated Adaptor Protein Selectively Expressed by T Cells and Natural Killer Cells

Weber, J. R., Ørstavik, S., Torgersen, K. M., Danbolt, N. C., Berg, S. F., Ryan, J. C., Taskén, K., Imboden, J. B., & Vaage, J. T. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.7.1157 · Cited by 145 · see citing works

Predominant expression and activation-induced tyrosine phosphorylation of phospholipase C-gamma 2 in B lymphocytes.

Coggeshall, K. M., McHugh, J. C., & Altman, A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5660 · Cited by 126 · see citing works

Association with B‐cell‐antigen receptor with protein‐tyrosine kinase p72syk and activation by engagement of membrane IgM

Yamada, T., Taniguchi, T., Yang, C., YASUE, S., Saitô, H., & Yamamura, H. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17781.x · Cited by 107 · see citing works

Shc Contains Two Grb2 Binding Sites Needed for Efficient Formation of Complexes with SOS in B Lymphocytes

Harmer, S. L., & DeFranco, A. L. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.7.4087 · Cited by 92 · see citing works

B cell antigen receptor stimulation induces formation of a Shc-Grb2 complex containing multiple tyrosine-phosphorylated proteins.

Smit, L., de Vries-Smits, A. M. M., Bos, J. L., & Borst, J. G. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31975-0 · Cited by 88 · see citing works

Reconstitution of B Cell Antigen Receptor-induced Signaling Events in a Nonlymphoid Cell Line by Expressing the Syk Protein-tyrosine Kinase

Richards, J. D., Gold, M. R., Hourihane, S. L., DeFranco, A. L., & Matsuuchi, L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.11.6458 · Cited by 54 · see citing works

Identification of Two Tyrosine Phosphoproteins, pp70 and pp68, Which Interact with Phospholipase Cγ, Grb2, and Vav after B Cell Antigen Receptor Activation

Fu, C., & Chan, A. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.43.27362 · Cited by 50 · see citing works

Expression of phospholipase C isozymes by murine B lymphocytes

Hempel, W. M., & DeFranco, A. L. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.146.11.3713 · Cited by 43 · see citing works

Phospholipase Cγ2 Is Essential in the Functions of B Cell and Several Fc Receptors

Wang, D., Feng, J., Wen, R., Marine, J.-C., Sangster, M. Y., Parganas, E., Hoffmeyer, A., Jackson, C. W., Cleveland, J. L., Murray, P. J., et al. (2000) · Immunity · doi:10.1016/s1074-7613(00)00005-4 · Cited by 475 · see citing works

BLNK

Kurosaki, T., & Tsukada, S. (2000) · Immunity · doi:10.1016/s1074-7613(00)80153-3 · Cited by 223 · see citing works

Signal Transduction by the High-Affinity Immunoglobulin E Receptor FcεRI: Coupling Form to Function

Nadler, M. J. S., Matthews, S. A., Turner, H., & Kinet, J.-P. (2001) · Advances in Immunology · doi:10.1016/s0065-2776(01)76022-1 · Cited by 203 · see citing works

Phospholipase C-γ2 and Vav cooperate within signaling microclusters to propagate B cell spreading in response to membrane-bound antigen

Weber, M., Treanor, B., Depoil, D., Shinohara, H., Harwood, N. E., Hikida, M., Kurosaki, T., & Batista, F. D. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20072619 · Cited by 170 · see citing works

Cutting Edge: Essential Role of Phospholipase C-γ2 in B Cell Development and Function

Hashimoto, A., Takeda, K., Inaba, M., Sekimata, M., Kaisho, T., Ikehara, S., Homma, Y., Akira, S., & Kurosaki, T. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.4.1738 · Cited by 155 · see citing works

Regulation of phospholipase C γ isoforms in haematopoietic cells

Wilde, J. I., & Watson, S. P. (2001) · Cellular Signalling · doi:10.1016/s0898-6568(01)00191-7 · Cited by 149 · see citing works

Four Tyrosine Residues in Phospholipase C-γ2, Identified as Btk-dependent Phosphorylation Sites, Are Required for B Cell Antigen Receptor-coupled Calcium Signaling

Watanabe, D., Hashimoto, S., Ishiai, M., Matsushita, M., Baba, Y., Kishimoto, T., Kurosaki, T., & Tsukada, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103675200 · Cited by 136 · see citing works

Requirement for Ras Guanine Nucleotide Releasing Protein 3 in Coupling Phospholipase C-γ2 to Ras in B Cell Receptor Signaling

Oh-hora, M., Johmura, S., Hashimoto, A., Hikida, M., & Kurosaki, T. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20031547 · Cited by 113 · see citing works

Rac regulates its effector phospholipase Cγ2 through interaction with a split pleckstrin homology domain

Walliser, C., Retlich, M., Harris, R., Everett, K. L., Josephs, M. B., Vatter, P., Esposito, D., Driscoll, P. C., Katan, M., Gierschik, P., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803316200 · Cited by 56 · see citing works

STAC2 negatively regulates osteoclast formation by targeting the RANK signaling complex

Jeong, E., Choi, H. K., Park, J. H., & Lee, S. Y. (2018) · Cell Death &amp; Differentiation · doi:10.1038/s41418-017-0048-5 · Cited by 35 · see citing works

Src Homology Region 2 Domain-Containing Phosphatase 1 Positively Regulates B Cell Receptor-Induced Apoptosis by Modulating Association of B Cell Linker Protein with Nck and Activation of c-Jun NH2-Terminal Kinase

Mizuno, K., Tagawa, Y., Mitomo, K., Watanabe, N., Katagiri, T., Ogimoto, M., & Yakura, H. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.2.778 · Cited by 34 · see citing works

B Cell Receptor-Mediated Syk-Independent Activation of Phosphatidylinositol 3-Kinase, Ras, and Mitogen-Activated Protein Kinase Pathways

Yokozeki, T., Adler, K., Lankar, D., & Bonnerot, C. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.3.1328 · Cited by 31 · see citing works

Autoinhibition and adapter function of Syk

Kulathu, Y., Grothe, G., & Reth, M. G. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2009.00837.x · Cited by 87 · see citing works

SYK-dependent tonic B-cell receptor signaling is a rational treatment target in diffuse large B-cell lymphoma

Chen, L., Monti, S., Juszczyński, P., Daley, J. F., Chen, W., Witzig, T. E., Habermann, T. M., Kutok, J. L., & Shipp, M. A. (2007) · Blood · doi:10.1182/blood-2007-07-100115 · Cited by 317 · see citing works

[Not Available].

慈, 岩., 真吾, 中., 宏昭, 新., et al. (2015) · Japanese Journal of Clinical Immunology · doi:10.2177/jsci.38.313b

Interdomain A is crucial for ITAM-dependent and -independent regulation of Syk

Adachi, T., Wienands, J., Tsubata, T., & Kurosaki, T. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.09.100 · Cited by 11 · see citing works

Abstract B131: Quantitative modeling of Syk regulation in B cell chronic lymphocytic leukemia

Frushicheva, M. P. (2016) · Cancer Immunology Research · doi:10.1158/2326-6066.imm2016-b131