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Artykuły w czasopismach na temat „CSK”

Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 25 lipca 2025

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1

Nagy, Zoltan, Jun Mori, Vanesa-Sindi Ivanova, Alexandra Mazharian, and Yotis A. Senis. "Interplay between the tyrosine kinases Chk and Csk and phosphatase PTPRJ is critical for regulating platelets in mice." Blood 135, no. 18 (2020): 1574–87. http://dx.doi.org/10.1182/blood.2019002848.

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Abstract The Src family kinases (SFKs) Src, Lyn, and Fyn are essential for platelet activation and also involved in megakaryocyte (MK) development and platelet production. Platelet SFKs are inhibited by C-terminal Src kinase (Csk), which phosphorylates a conserved tyrosine in their C-terminal tail, and are activated by the receptor-type tyrosine phosphatase PTPRJ (CD148, DEP-1), which dephosphorylates the same residue. Deletion of Csk and PTPRJ in the MK lineage in mice results in increased SFK activity, but paradoxically hypoactive platelets resulting from negative feedback mechanisms, includ

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2

Sabe, H., M. Okada, H. Nakagawa, and H. Hanafusa. "Activation of c-Src in cells bearing v-Crk and its suppression by Csk." Molecular and Cellular Biology 12, no. 10 (1992): 4706–13. http://dx.doi.org/10.1128/mcb.12.10.4706-4713.1992.

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The protein product of the CT10 virus, p47gag-crk (v-Crk), which contains Src homology region 2 (SH2) and 3 (SH3) domains but lacks a kinase domain, is believed to cause an increase in cellular protein tyrosine phosphorylation. A candidate tyrosine kinase, Csk (C-terminal Src kinase), has been implicated in c-Src Tyr-527 phosphorylation, which negatively regulates the protein tyrosine kinase of pp60c-src (c-Src). To investigate how c-Src kinase activity is regulated in vivo, we first looked at whether v-Crk can activate c-Src kinase. We found that cooverexpression of v-Crk and c-Src caused ele

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3

Sabe, H., M. Okada, H. Nakagawa, and H. Hanafusa. "Activation of c-Src in cells bearing v-Crk and its suppression by Csk." Molecular and Cellular Biology 12, no. 10 (1992): 4706–13. http://dx.doi.org/10.1128/mcb.12.10.4706.

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The protein product of the CT10 virus, p47gag-crk (v-Crk), which contains Src homology region 2 (SH2) and 3 (SH3) domains but lacks a kinase domain, is believed to cause an increase in cellular protein tyrosine phosphorylation. A candidate tyrosine kinase, Csk (C-terminal Src kinase), has been implicated in c-Src Tyr-527 phosphorylation, which negatively regulates the protein tyrosine kinase of pp60c-src (c-Src). To investigate how c-Src kinase activity is regulated in vivo, we first looked at whether v-Crk can activate c-Src kinase. We found that cooverexpression of v-Crk and c-Src caused ele

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4

Karyati, Nur Etika, Latief Mahir Rachman, and Dwi Putro Tejo Baskoro. "Penetapan Alokasi Sawah Penerima Air Irigasi Berdasarkan Kondisi Hidroklimatologi di Daerah Irigasi Cihea." Jurnal Ilmu Pertanian Indonesia 27, no. 2 (2022): 216–25. http://dx.doi.org/10.18343/jipi.27.2.216.

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One of the main supporting factors for the agricultural sector in the Cihea Irrigation Area is the availability of sufficient water resources. However, uncertain climatic conditions due to climate change lead the changes in the rain distribution and affect the availability of water resources. The study aims to (1) assess the land water balance and drought index in Cihea Irrigation Area and (2) develop alternatives related to irrigation priority locations based on hydro climatological conditions. The water balance was analyzed using the Thornthwaite-Mather method (1957), while the irrigation pr

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5

Li, Leiming, Masaya Okura, and Akira Imamoto. "Focal Adhesions Require Catalytic Activity of Src Family Kinases To Mediate Integrin-Matrix Adhesion." Molecular and Cellular Biology 22, no. 4 (2002): 1203–17. http://dx.doi.org/10.1128/mcb.22.4.1203-1217.2002.

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ABSTRACT Members of the Src family of tyrosine kinases function to phosphorylate focal adhesion (FA) proteins. To explore the overlapping functions of Src kinases, we have targeted Csk, a negative regulator of the Src family, to FA structures. Expression of FA-targeted Csk (FA-Csk) effectively reduced the active form (nonphosphorylated at the C-terminal regulatory tyrosine) of Src members in the cell. We found that fibroblasts expressing FA-Csk lost integrin-mediated adhesion. Activated Src (SrcY529F) as well as activation of putative Src signaling mediators (Fak, Cas, Crk/CrkL, C3G, and Rap1)

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6

Yamaguchi, N., Y. Nakayama, T. Urakami, et al. "Overexpression of the Csk homologous kinase (Chk tyrosine kinase) induces multinucleation: a possible role for chromosome-associated Chk in chromosome dynamics." Journal of Cell Science 114, no. 9 (2001): 1631–41. http://dx.doi.org/10.1242/jcs.114.9.1631.

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The Csk family of non-receptor-type tyrosine kinases consists of Csk and the Csk homologous kinase Chk. Each enzyme suppresses the catalytic activity of Src family kinases by phosphorylating their C-terminal negative regulatory tyrosine residues. Ectopic and transient expression of Chk in COS-1 cells showed nuclear localization of Chk and growth inhibition. To further explore the role of Chk in cell growth, we overexpressed Chk in human immature myeloid KMT-2 cells. Chk overexpression brought about growth retardation and aberrant chromosome movement leading to multinucleation, and these events

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7

Howell, 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 (1994): 5402–11. http://dx.doi.org/10.1128/mcb.14.8.5402-5411.1994.

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Csk phosphorylates Src family members at a key regulatory tyrosine in the C-terminal tail and suppresses their activities. It is not known whether Csk activity is regulated. To examine the features of Csk required for Src suppression, we expressed Csk mutants in a cell line with a disrupted csk gene. Expression of wild-type Csk suppressed Src, but Csk with mutations in the SH2, SH3, and catalytic domains did not suppress Src. An SH3 deletion mutant of Csk was fully active against in vitro substrates, but two SH2 domain mutants were essentially inactive. Whereas Src repressed by Csk was predomi

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8

Howell, 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 (1994): 5402–11. http://dx.doi.org/10.1128/mcb.14.8.5402.

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Csk phosphorylates Src family members at a key regulatory tyrosine in the C-terminal tail and suppresses their activities. It is not known whether Csk activity is regulated. To examine the features of Csk required for Src suppression, we expressed Csk mutants in a cell line with a disrupted csk gene. Expression of wild-type Csk suppressed Src, but Csk with mutations in the SH2, SH3, and catalytic domains did not suppress Src. An SH3 deletion mutant of Csk was fully active against in vitro substrates, but two SH2 domain mutants were essentially inactive. Whereas Src repressed by Csk was predomi

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9

Chong, Yuh-Ping, Terrence D. Mulhern, and Heung-Chin Cheng. "C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK)—endogenous negative regulators of Src-family protein kinases." Growth Factors 23, no. 3 (2005): 233–44. http://dx.doi.org/10.1080/08977190500178877.

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10

Zagozdzon, Radoslaw, Rafal Kaminski, Yigong Fu, Wei Fu, Cecile Bougeret, and Hava Karsenty Avraham. "Csk homologous kinase (CHK), unlike Csk, enhances MAPK activation via Ras-mediated signaling in a Src-independent manner." Cellular Signalling 18, no. 6 (2006): 871–81. http://dx.doi.org/10.1016/j.cellsig.2005.07.016.

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11

Lee, Byeong-Chel, Shalom Avraham, Akira Imamoto, and Hava Karsenty Avraham. "Identification of the nonreceptor tyrosine kinase MATK/CHK as an essential regulator of immune cells using Matk/CHK-deficient mice." Blood 108, no. 3 (2006): 904–7. http://dx.doi.org/10.1182/blood-2005-12-4885.

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Abstract Matk/CHK knockout mice were reported to show no apparent phenotypic abnormalities. This was thought to be due to the homologous kinase Csk that compensates for Matk/CHK. Here, we present the first evidence that the nonreceptor tyrosine kinase, Matk/CHK, is an important modulator of immune cell signaling. We found that the frequency of primitive hematopoietic cells, the side population c-kit+ Lin– Sca-1+ (SPKLS) cells, in Matk/CHK–/– mice was increased 2.2-fold compared with the control mice. Moreover, Matk/CHK deficiency led to significantly higher pre–B cell colony formation followin

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12

Ouyang, Mingxing, Yujie Xing, Shumin Zhang, Liting Li, Yan Pan, and Linhong Deng. "Development of FRET Biosensor to Characterize CSK Subcellular Regulation." Biosensors 14, no. 4 (2024): 206. http://dx.doi.org/10.3390/bios14040206.

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C-terminal Src kinase (CSK) is the major inhibitory kinase for Src family kinases (SFKs) through the phosphorylation of their C-tail tyrosine sites, and it regulates various types of cellular activity in association with SFK function. As a cytoplasmic protein, CSK needs be recruited to the plasma membrane to regulate SFKs’ activity. The regulatory mechanism behind CSK activity and its subcellular localization remains largely unclear. In this work, we developed a genetically encoded biosensor based on fluorescence resonance energy transfer (FRET) to visualize the CSK activity in live cells. The

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13

Puthiyaveetil, Sujith, Iskander M. Ibrahim, and John F. Allen. "Evolutionary rewiring: a modified prokaryotic gene-regulatory pathway in chloroplasts." Philosophical Transactions of the Royal Society B: Biological Sciences 368, no. 1622 (2013): 20120260. http://dx.doi.org/10.1098/rstb.2012.0260.

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Photosynthetic electron transport regulates chloroplast gene transcription through the action of a bacterial-type sensor kinase known as chloroplast sensor kinase (CSK). CSK represses photosystem I (PS I) gene transcription in PS I light and thus initiates photosystem stoichiometry adjustment. In cyanobacteria and in non-green algae, CSK homologues co-exist with their response regulator partners in canonical bacterial two-component systems. In green algae and plants, however, no response regulator partner of CSK is found. Yeast two-hybrid analysis has revealed interaction of CSK with sigma fac

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14

Neet, K., and T. Hunter. "The nonreceptor protein-tyrosine kinase CSK complexes directly with the GTPase-activating protein-associated p62 protein in cells expressing v-Src or activated c-Src." Molecular and Cellular Biology 15, no. 9 (1995): 4908–20. http://dx.doi.org/10.1128/mcb.15.9.4908.

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CSK is a predominantly cytosolic protein-tyrosine kinase (PTK) that negatively regulates Src family PTKs by phosphorylation of a conserved tyrosine near their C termini. Little is known about how CSK itself is regulated. On the basis of immunofluorescence studies, a model has been proposed that when c-Src is activated, it is redistributed to podosomes, in which substrates become phosphorylated, creating binding sites for CSK. CSK is recruited to these sites of c-Src activation via its SH2 and SH3 domains and is then in a position to downregulate c-Src activity (B. W. Howell and J. A. Cooper, M

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15

Wang, 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 (2001): 1077–88. http://dx.doi.org/10.1128/mcb.21.4.1077-1088.2001.

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ABSTRACT The protein tyrosine kinase (PTK) Csk is a potent negative regulator of several signal transduction processes, as a consequence of its exquisite ability to inactivate Src-related PTKs. This function requires not only the kinase domain of Csk, but also its Src homology 3 (SH3) and SH2 regions. We showed previously that the Csk SH3 domain mediates highly specific associations with two members of the PEP family of nonreceptor protein tyrosine phosphatases (PTPs), PEP and PTP-PEST. In comparison, the Csk SH2 domain interacts with several tyrosine phosphorylated molecules, presumed to allo

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16

Drahovska, Z., I. Balicki, A. Trbolova, M. Mihalova, and M. Holickova. "A retrospective study of the occurrence of Chronic Superficial Keratitis in 308 German Shepherd dogs: 1999-2010." Polish Journal of Veterinary Sciences 17, no. 3 (2014): 543–46. http://dx.doi.org/10.2478/pjvs-2014-0082.

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Abstract Chronic Superficial Keratitis (CSK) is an autoimmune mediated inflammation of the cornea, that is usually bilateral but often with nonsymmetrical manifestation. The aim of this study was to determine the occurrence and appearance of clinical symptoms of CSK in German Shepherd dogs in Poland and Slovakia. CSK was diagnosed in 308 German Shepherds for a period of 11 years (from 1999 to 2010). The highest incidence of the CSK (p < 0.001) in Slovakia and in Poland was in dogs between the ages of 5-8 years. This study found similarity in gender ratio of affected patients with CSK in two

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17

I. Hussein, Raghad, Zahir M. Hussain, and Salah A. Albermany. "Performance of Differential CSK under Color Noise: A Comparison with CSK." Journal of Engineering and Applied Sciences 15, no. 1 (2019): 48–59. http://dx.doi.org/10.36478/jeasci.2020.48.59.

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Berman-Booty, Lisa D., Rukiye Eraslan, Umesh Hanumegowda, et al. "Systemic Loss of C-terminal Src Kinase Expression Elicits Spontaneous Suppurative Inflammation in Conditional Knockout Mice." Veterinary Pathology 55, no. 2 (2018): 331–40. http://dx.doi.org/10.1177/0300985817747330.

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C-terminal Src kinase (Csk) is one of the critical negative regulators of the Src family of kinases. The Src family of kinases are nonreceptor tyrosine kinases that regulate inflammation, cell proliferation, motility, and adhesion. To investigate potential histologic lesions associated with systemic loss of Csk gene activity in adult mice, conditional Csk-knockout mice were examined. Cre-mediated systemic excision of Csk induced by tamoxifen treatment resulted in multiorgan inflammation. Specifically, induction of Csk gene excision with three days of tamoxifen treatment resulted in greater tha

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Hampshire, Daniel, Aurore Saudemont, Alexander Tarakhovsky, and Francesco Colucci. "Conditional targeting of C-terminal Src kinase (Csk) in NK cells (135.2)." Journal of Immunology 182, no. 1_Supplement (2009): 135.2. http://dx.doi.org/10.4049/jimmunol.182.supp.135.2.

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Abstract Csk is a key negative regulator of Src-family kinases and has been shown to be a strong inhibitor of immunoreceptor signalling in T cells and granulocytes. Our hypothesis is that an increase in Src kinase activity might take place in NK cells following the elimination of Csk, resulting in an enhanced cellular response even at low levels of stimulation. We aim to establish the role of Csk in NK cells using conditional knockout mice. A transgenic mouse has been developed where the Csk gene is flanked by LoxP (floxed) sites. Crossing Csk floxed transgenic mice with transgenic mice expres

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JOUKOV, Vladimir, Mauno VIHINEN, Satu VAINIKKA, Janusz M. SOWADSKI, Kari ALITALO, and Mathias BERGMAN. "Identification of Csk tyrosine phosphorylation sites and a tyrosine residue important for kinase domain structure." Biochemical Journal 322, no. 3 (1997): 927–35. http://dx.doi.org/10.1042/bj3220927.

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The lack of a conserved tyrosine autophosphorylation site is a unique feature of the C-terminal Src-kinase, Csk, although this protein tyrosine kinase can be autophosphorylated on tyrosine residues in vitro and in bacteria. Here we show that human Csk is tyrosine phosphorylated in HeLa cells treated with sodium pervanadate. Phosphorylation in vivo occurs mainly at Tyr-184 and in vitro mainly at Tyr-304. A Y304F mutation strongly decreased Csk phosphorylation in vitro, and a Y184F mutation abolished tyrosine phosphorylation in vivo. A catalytically inactive form of Csk was also phosphorylated o

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21

Schmedt, Christian, та Alexander Tarakhovsky. "Autonomous Maturation of α/β T Lineage Cells in the Absence of Cooh-Terminal Src Kinase (Csk)". Journal of Experimental Medicine 193, № 7 (2001): 815–26. http://dx.doi.org/10.1084/jem.193.7.815.

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The deletion of COOH-terminal Src kinase (Csk), a negative regulator of Src family protein tyrosine kinases (PTKs), in immature thymocytes results in the development of α/β T lineage cells in T cell receptor (TCR) β-deficient or recombination activating gene (rag)-1–deficient mice. The function of Csk as a repressor of Lck and Fyn activity suggests activation of these PTKs is solely responsible for the phenotype observed in csk-deficient T lineage cells. We provide genetic evidence for this notion as α/β T cell development is blocked in lck−/−fyn−/− csk-deficient mice. It remains unclear wheth

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Radel, C., and V. Rizzo. "Integrin mechanotransduction stimulates caveolin-1 phosphorylation and recruitment of Csk to mediate actin reorganization." American Journal of Physiology-Heart and Circulatory Physiology 288, no. 2 (2005): H936—H945. http://dx.doi.org/10.1152/ajpheart.00519.2004.

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To identify the role of caveolin-1 in integrin mechanotransduction, we exposed bovine aortic endothelial cells to 10 dyn/cm2 of laminar shear stress. Caveolin-1 was acutely and transiently phosphorylated with shear, occurring downstream of β1-integrin activation as the β1-integrin blocking antibody JB1A was inhibitory. In manipulating Src family kinase (SFK) activity with knockdown of Csk or type 1 protein phosphatase (PP1) treatment, we observed coordinate increase and decrease in shear-induced caveolin-1 phosphorylation, respectively. Hence, shear-stimulated caveolin-1 phosphorylation is reg

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23

Duan, Li-Juan, Akira Imamoto, and Guo-Hua Fong. "Dual roles of the C-terminal Src kinase (Csk) during developmental vascularization." Blood 103, no. 4 (2004): 1370–72. http://dx.doi.org/10.1182/blood-2003-05-1701.

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Abstract Here we report that C-terminal Src kinase (Csk), a tyrosine kinase that negatively regulates the activity of Src and related kinases, is important for vascular development. In Csk–/– embryos, although vascular tubules were formed and organized into capillary-like networks during the initial genesis of blood vessels, the vessels failed to engage in normal sprout formation. In chimeric embryos containing both wild-type and Csk–/– cells, the presence of wild-type cells enabled Csk–/– endothelial cells to participate in branching morphogenesis. We suggest that wild-type cells may have sup

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24

Dobenecker, Marc-Werner, Christian Schmedt, Masato Okada, and Alexander Tarakhovsky. "The Ubiquitously Expressed Csk Adaptor Protein Cbp Is Dispensable for Embryogenesis and T-Cell Development and Function." Molecular and Cellular Biology 25, no. 23 (2005): 10533–42. http://dx.doi.org/10.1128/mcb.25.23.10533-10542.2005.

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ABSTRACT Regulation of Src family kinase (SFK) activity is indispensable for a functional immune system and embryogenesis. The activity of SFKs is inhibited by the presence of the carboxy-terminal Src kinase (Csk) at the cell membrane. Thus, recruitment of cytosolic Csk to the membrane-associated SFKs is crucial for its regulatory function. Previous studies utilizing in vitro and transgenic models suggested that the Csk-binding protein (Cbp), also known as phosphoprotein associated with glycosphingolipid microdomains (PAG), is the membrane adaptor for Csk. However, loss-of-function genetic evi

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25

Rahmouni, Souad, Torkel Vang, Andres Alonso, et al. "Removal of C-Terminal Src Kinase from the Immune Synapse by a New Binding Protein." Molecular and Cellular Biology 25, no. 6 (2005): 2227–41. http://dx.doi.org/10.1128/mcb.25.6.2227-2241.2005.

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ABSTRACT The Csk tyrosine kinase negatively regulates the Src family kinases Lck and Fyn in T cells. Engagement of the T-cell antigen receptor results in a removal of Csk from the lipid raft-associated transmembrane protein PAG/Cbp. Instead, Csk becomes associated with an ∼72-kDa tyrosine-phosphorylated protein, which we identify here as G3BP, a phosphoprotein reported to bind the SH3 domain of Ras GTPase-activating protein. G3BP reduced the ability of Csk to phosphorylate Lck at Y505 by decreasing the amount of Csk in lipid rafts. As a consequence, G3BP augmented T-cell activation as measured

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Pourati, Jacob, Andrew Maniotis, David Spiegel, et al. "Is cytoskeletal tension a major determinant of cell deformability in adherent endothelial cells?" American Journal of Physiology-Cell Physiology 274, no. 5 (1998): C1283—C1289. http://dx.doi.org/10.1152/ajpcell.1998.274.5.c1283.

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We tested the hypothesis that mechanical tension in the cytoskeleton (CSK) is a major determinant of cell deformability. To confirm that tension was present in adherent endothelial cells, we either cut or detached them from their basal surface by a microneedle. After cutting or detachment, the cells rapidly retracted. This retraction was prevented, however, if the CSK actin lattice was disrupted by cytochalasin D (Cyto D). These results confirmed that there was preexisting CSK tension in these cells and that the actin lattice was a primary stress-bearing component of the CSK. Second, to determ

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Mulyadi, Hanung Agus, Augy Syahailatua, and Zainal Arifin. "THE CO-OPERATIVE STUDY OF KUROSHIO (CSK): IS IT BENEFICIAL FOR INDONESIA?" Marine Research in Indonesia 44, no. 2 (2019): 63–71. http://dx.doi.org/10.14203/mri.v44i2.562.

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The Cooperative Study of Kuroshio and its marginal seas (CSK) is one of the international joint research project conducted in the Western Pacific region. Many Asian countries had been involved in this project from 1965 to1979. Data and information from the CSK are enormous and cover wide-ranging aspects of marine science from the Kuroshio and adjacent regions (e.g. physical aspects, biological aspects and biogeochemical aspects). Indonesia had committed to participate actively in several marine research programs in the area linked to the CSK program by conducting marine research in its interna

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YAQUB, Sheraz, Hilde ABRAHAMSEN, Bastian ZIMMERMAN, et al. "Activation of C-terminal Src kinase (Csk) by phosphorylation at serine-364 depends on the Csk-Src homology 3 domain." Biochemical Journal 372, no. 1 (2003): 271–78. http://dx.doi.org/10.1042/bj20030021.

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In the present study, we investigate the mechanism for the protein kinase A (PKA)-mediated activation of C-terminal Src kinase (Csk). Although isolated Csk kinase domain was phosphorylated at Ser364 by PKA to the same stoichiometry as wild-type Csk, significant activation of the isolated Csk kinase domain by PKA was observed only in the presence of the purified Src homology 3 domain (SH3 domain). Furthermore, the interaction between the SH3 and kinase domains was facilitated by PKA-mediated phosphorylation of the kinase domain, as evaluated by surface plasmon resonance. This suggests that an o

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Chen, Yuxin, Jie Cheng, Xiaodong Li, Xue Bai, and Zhixi Nie. "Research on Tracking Technique Based on BPSK-CSK Signals." Electronics 13, no. 8 (2024): 1517. http://dx.doi.org/10.3390/electronics13081517.

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The code-shift keying (CSK) modulation method can achieve higher information transmission rates without changing the spread spectrum signal bandwidth. In order to optimise the spread spectrum modulation and demodulation of GNSS signals, in addition to the signal structure, binary phase-shift keying (BPSK) and CSK signals using time-division multiplexing are proposed. A tracking method based on the BPSK-CSK signals is also proposed, which generates the P-branch local codes by fast Fourier transform to obtain the code-slice spacings for the E-branch and the L-branch local codes. Then, the tracke

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Honey, Karen. "Csk quenches the fire." Nature Reviews Immunology 4, no. 4 (2004): 246. http://dx.doi.org/10.1038/nri1336.

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Deng, Linhong, Nigel J. Fairbank, Ben Fabry, Paul G. Smith, and Geoffrey N. Maksym. "Localized mechanical stress induces time-dependent actin cytoskeletal remodeling and stiffening in cultured airway smooth muscle cells." American Journal of Physiology-Cell Physiology 287, no. 2 (2004): C440—C448. http://dx.doi.org/10.1152/ajpcell.00374.2003.

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Mechanical stress (MS) causes cytoskeletal (CSK) and phenotypic changes in cells. Such changes in airway smooth muscle (ASM) cells might contribute to the pathophysiology of asthma. We have shown that periodic mechanical strain applied to cultured ASM cells alters the structure and expression of CSK proteins and increases cell stiffness and contractility (Smith PG, Moreno R, and Ikebe M. Am J Physiol Lung Cell Mol Physiol 272: L20–L27, 1997; and Smith PG, Deng L, Fredberg JJ, and Maksym GN. Am J Physiol Lung Cell Mol Physiol 285: L456–L463, 2003). However, the mechanically induced CSK changes,

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Rathore, Vipul B., Peter J. Newman, and Debra K. Newman. "Paxillin Becomes Tyrosine-Phosphorylated and Binds Csk in a GpIIb-IIIa-Dependent Manner Following GPVI-Induced Activation of Murine Platelets." Blood 104, no. 11 (2004): 3889. http://dx.doi.org/10.1182/blood.v104.11.3889.3889.

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Though Src family kinases (SFKs) play a critical role in collagen-induced platelet activation, little is known about how SFK activity is regulated following exposure of platelets to collagen. In resting cells, SFKs are maintained in an inactive conformation, in part, via intramolecular interactions between their SH2 domain and a C-terminal tyrosine residue whose phosphorylation state is controlled by the C-terminal Src kinase, Csk. Access of Csk to SFKs, in turn, is regulated by recruitment of Csk, via its SH2 domain, to one or more tyrosine-phosphorylated Csk-binding proteins, which include C

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Hata, A., H. Sabe, T. Kurosaki, M. Takata, and H. Hanafusa. "Functional analysis of Csk in signal transduction through the B-cell antigen receptor." Molecular and Cellular Biology 14, no. 11 (1994): 7306–13. http://dx.doi.org/10.1128/mcb.14.11.7306-7313.1994.

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In B cells, two classes of protein tyrosine kinases (PTKs), the Src family of PTKs (Lyn, Fyn, Lck, and Blk) and non-Src family of PTKs (Syk), are known to be involved in signal transduction induced by the stimulation of the B-cell antigen receptor (BCR). Previous studies using Lyn-negative chicken B-cell clones revealed that Lyn is necessary for transduction of signals through the BCR. The kinase activity of the Src family of PTKs is negatively regulated by phosphorylation at the C-terminal tyrosine residue, and the PTK Csk has been demonstrated to phosphorylate this C-terminal residue of the

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Hata, A., H. Sabe, T. Kurosaki, M. Takata, and H. Hanafusa. "Functional analysis of Csk in signal transduction through the B-cell antigen receptor." Molecular and Cellular Biology 14, no. 11 (1994): 7306–13. http://dx.doi.org/10.1128/mcb.14.11.7306.

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In B cells, two classes of protein tyrosine kinases (PTKs), the Src family of PTKs (Lyn, Fyn, Lck, and Blk) and non-Src family of PTKs (Syk), are known to be involved in signal transduction induced by the stimulation of the B-cell antigen receptor (BCR). Previous studies using Lyn-negative chicken B-cell clones revealed that Lyn is necessary for transduction of signals through the BCR. The kinase activity of the Src family of PTKs is negatively regulated by phosphorylation at the C-terminal tyrosine residue, and the PTK Csk has been demonstrated to phosphorylate this C-terminal residue of the

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Bergman, M., V. Joukov, I. Virtanen, and K. Alitalo. "Overexpressed Csk tyrosine kinase is localized in focal adhesions, causes reorganization of alpha v beta 5 integrin, and interferes with HeLa cell spreading." Molecular and Cellular Biology 15, no. 2 (1995): 711–22. http://dx.doi.org/10.1128/mcb.15.2.711.

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The C-terminal Src kinase p50csk phosphorylates Src family tyrosine kinases and down-regulates their activity in vitro. To gain insight into the cellular functions of this potentially antioncogenic enzyme, we have overexpressed the csk cDNA by using an inducible promoter in HeLa cells. Despite some differences in basal Src activity in the clones analyzed, Src activity was not significantly suppressed, while the amount of p50csk and Csk activity increased at least 10-fold during 3 days of induction. Immunofluorescence for the induced p50csk was localized in the cytoplasm and distinctly in focal

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Rathore, Vipul B., Masato Okada, Peter J. Newman, and Debra K. Newman. "Paxillin family members function as Csk-binding proteins that regulate Lyn activity in human and murine platelets." Biochemical Journal 403, no. 2 (2007): 275–81. http://dx.doi.org/10.1042/bj20061618.

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SFKs (Src family kinases) contribute importantly to platelet function in haemostasis. SFK activity is controlled by Csk (C-terminal Src kinase), which phosphorylates a C-terminal tyrosine residue on SFKs, resulting in inhibition of SFK activity. Csk is recruited to sites of SFK activity by tyrosine-phosphorylated Csk-binding proteins. Paxillin, a multidomain adaptor protein, has been shown to act as a Csk-binding protein and to inhibit Src activity during growth factor signalling. Human platelets express Hic-5, a member of the paxillin family; however, its ability to act as a Csk-binding prote

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Yu, Chi-Hsin, and Hsin-Hsi Chen. "Commonsense Knowledge Mining from the Web." Proceedings of the AAAI Conference on Artificial Intelligence 24, no. 1 (2010): 1480–85. http://dx.doi.org/10.1609/aaai.v24i1.7505.

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Good and generous knowledge sources, reliable and efficient induction patterns, and automatic and controllable quality assertion approaches are three critical issues to commonsense knowledge (CSK) acquisition. This paper employs Open Mind Common Sense (OMCS), a volunteers-contributed CSK database, to study the first and the third issues. For those stylized CSK, our result shows that over 40% of CSK for four predicate types in OMCS can be found in the web, which contradicts to the assumption that CSK is not communicated in texts. Moreover, we propose a commonsense knowledge classifier trained f

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Vang, Torkel, Knut Martin Torgersen, Vibeke Sundvold, et al. "Activation of the Cooh-Terminal Src Kinase (Csk) by Camp-Dependent Protein Kinase Inhibits Signaling through the T Cell Receptor." Journal of Experimental Medicine 193, no. 4 (2001): 497–508. http://dx.doi.org/10.1084/jem.193.4.497.

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In T cells, cAMP-dependent protein kinase (PKA) type I colocalizes with the T cell receptor–CD3 complex (TCR/CD3) and inhibits T cell function via a previously unknown proximal target. Here we examine the mechanism for this PKA-mediated immunomodulation. cAMP treatment of Jurkat and normal T cells reduces Lck-mediated tyrosine phosphorylation of the TCR/CD3 ζ chain after T cell activation, and decreases Lck activity. Phosphorylation of residue Y505 in Lck by COOH-terminal Src kinase (Csk), which negatively regulates Lck, is essential for the inhibitory effect of cAMP on ζ chain phosphorylation

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Bougeret, Cécile, Shuxian Jiang, Iafa Keydar, and Hava Avraham. "Functional Analysis of Csk and CHK Kinases in Breast Cancer Cells." Journal of Biological Chemistry 276, no. 36 (2001): 33711–20. http://dx.doi.org/10.1074/jbc.m104209200.

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ALANZI, Ayed R. A., Raouf FAKHFAKH, and Fatimah ALSHAHRANI. "A characteristic property of the Semicircle law." Proceedings of the Romanian Academy, Series A: Mathematics, Physics, Technical Sciences, Information Science 25, no. 4 (2024): 273–76. https://doi.org/10.59277/pra-ser.a.25.4.02.

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Let ${\mathcal{F}_{+}}(\sigma)=\{\textbf{Q}_m^{\sigma}(dy); \ \ m\in (m_1^{\sigma},m_+^{\sigma})\}$ be the \CSK family induced by a (non-degenerate ) probability measure $\sigma$ possessing a one sided support boundary from above. For $\tau\geq0$, denote by $\widetilde{U}^{\tau}$ the $\tau$-deformation of measures introduced in \cite[Section 5]{Krystek-Yoshida-04}. In this article, a property is presented for the \CSK families based on the stability under $\tau$-deformation of measures. A \CSK family satisfying such stability property is nothing but the \CSK family generated by the Semicircle

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Martínez-Ciro, Roger Alexander, Francisco Eugenio López-Giraldo, Andrés Felipe Betancur-Perez, and Jose Martín Luna-Rivera. "Design and Implementation of a Multi-Colour Visible Light Communication System Based on a Light-to-Frequency Receiver." Photonics 6, no. 2 (2019): 42. http://dx.doi.org/10.3390/photonics6020042.

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Colour-shift keying (CSK) is a visible light communication (VLC) modulation scheme used in the existing IEEE 802.15.7 standard. In CSK, information is transmitted by changing the light intensities of the RGB LEDs. In this work, a low-complexity VLC system is proposed using CSK modulation and a novel receiver based on a light-to-frequency (LTF) converter. At the receiver, CSK symbols are interpreted and decoded in terms of frequencies, which are processed by a counter module of a generic microcontroller, thus avoiding the use of analog-to-digital converters (ADCs), which results in a low-cost V

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Davidson, Dominique, Lionel M. L. Chow, and André Veillette. "Chk, a Csk Family Tyrosine Protein Kinase, Exhibits Csk-like Activity in Fibroblasts, but Not in an Antigen-specific T-cell Line." Journal of Biological Chemistry 272, no. 2 (1997): 1355–62. http://dx.doi.org/10.1074/jbc.272.2.1355.

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Lee, Yeon-Ji, Joo-Hee Choi, Kyung-Ku Kang, et al. "Antioxidant and Antimelanogenic Activities of Lactobacillus kunkeei NCHBL-003 Isolated from Honeybees." Microorganisms 12, no. 1 (2024): 188. http://dx.doi.org/10.3390/microorganisms12010188.

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Excessive reactive oxygen species production can detrimentally impact skin cell physiology, resulting in cell growth arrest, melanogenesis, and aging. Recent clinical studies have found that lactic acid bacteria have a special effect directly or indirectly on skin organs, but the exact mechanism has not been elucidated. In this study, we investigated the mechanisms underlying the antioxidant protective effect and the inhibitory effect on melanin synthesis of Lactobacillus kunkeei culture supernatant (CSK), isolated from Apis mellifera Linnaeus (the Western honeybee). CSK exhibited notable effi

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Fakhfakh, Raouf. "Some results in Cauchy-Stieltjes kernel families." Filomat 36, no. 3 (2022): 869–80. http://dx.doi.org/10.2298/fil2203869f.

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In this paper we present two different results in the theory of Cauchy-Stieltjes Kernel (CSK) families. We firstly provide the construction of free Sheffer systems with the theory of CSK families. We associate a free additive convolution semigroup of probability measures to any free Sheffer systems and we prove that this is the only one that leads to an orthogonal free Sheffer systems. We also show that the orthogonality of free Sheffer systems occurs if and only if the associated free additive convolution semigroup of probability measures generates CSK families with quadratic variance functio

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Vuica, Milena, Stephen Desiderio та Jonathan P. Schneck. "Differential Effects of B Cell Receptor and B Cell Receptor–FcγRIIB1 Engagement on Docking of Csk to GTPase-activating Protein (GAP)-associated p62". Journal of Experimental Medicine 186, № 2 (1997): 259–67. http://dx.doi.org/10.1084/jem.186.2.259.

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The stimulatory and inhibitory pathways initiated by engagement of stimulatory receptors such as the B cell receptor for antigen (BCR) and inhibitory receptors such as Fcγ receptors of the IIB1 type (FcγRIIB1) intersect in ways that are poorly understood at the molecular level. Because the tyrosine kinase Csk is a potential negative regulator of lymphocyte activation, we examined the effects of BCR and FcγRIIB1 engagement on the binding of Csk to phosphotyrosine-containing proteins. Stimulation of a B lymphoma cell line, A20, with intact anti-IgG antibody induced a direct, SH2-mediated associa

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Wallis, Alicia, Zuoan Yi, and Gail Bishop. "TRAF3 regulates CSK and PTPN22 to enhance T cell receptor signaling (IRM7P.705)." Journal of Immunology 194, no. 1_Supplement (2015): 61.6. http://dx.doi.org/10.4049/jimmunol.194.supp.61.6.

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Abstract TCR signaling is critical for T cell activation, so further elucidation of this process is necessary to understanding T cell biology, and to manipulate T cell activation in clinical settings. Extensive research on TCR signaling has revealed many details, but additional information on the molecular mechanisms continues to be revealed. Our group previously produced a T cell-conditional (CD4-Cre) TRAF3-/- mouse, which demonstrated that TRAF3 plays an important positive role in TCR signaling and T cell functions. After TCR engagement, TRAF3 associates with the TCR complex, and TRAF3-/- ce

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Murphy, S. M., M. Bergman, and D. O. Morgan. "Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae." Molecular and Cellular Biology 13, no. 9 (1993): 5290–300. http://dx.doi.org/10.1128/mcb.13.9.5290-5300.1993.

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The kinase activity of c-Src is normally repressed in vertebrate cells by extensive phosphorylation of Y-527. C-terminal Src kinase (CSK) is a candidate for the enzyme that catalyzes this phosphorylation. We have used budding yeast to study the regulation of c-Src activity by CSK in intact cells. Expression of c-Src in Saccharomyces cerevisiae, which lacks endogenous c-Src and Y-527 kinases, induces a kinase-dependent growth inhibition. Coexpression of CSK in these cells results in phosphorylation of c-Src on Y-527 and suppression of the c-Src phenotype. CSK does not fully suppress the activit

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Murphy, S. M., M. Bergman, and D. O. Morgan. "Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae." Molecular and Cellular Biology 13, no. 9 (1993): 5290–300. http://dx.doi.org/10.1128/mcb.13.9.5290.

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The kinase activity of c-Src is normally repressed in vertebrate cells by extensive phosphorylation of Y-527. C-terminal Src kinase (CSK) is a candidate for the enzyme that catalyzes this phosphorylation. We have used budding yeast to study the regulation of c-Src activity by CSK in intact cells. Expression of c-Src in Saccharomyces cerevisiae, which lacks endogenous c-Src and Y-527 kinases, induces a kinase-dependent growth inhibition. Coexpression of CSK in these cells results in phosphorylation of c-Src on Y-527 and suppression of the c-Src phenotype. CSK does not fully suppress the activit

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Musso, T., L. Varesio, X. Zhang, et al. "IL-4 and IL-13 induce Lsk, a Csk-like tyrosine kinase, in human monocytes." Journal of Experimental Medicine 180, no. 6 (1994): 2383–88. http://dx.doi.org/10.1084/jem.180.6.2383.

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Lsk is a protein tyrosine kinase with homology to the COOH-terminal Src kinase (Csk). Unlike Csk that is ubiquitously expressed, Lsk has limited tissue distribution. Here we have examined the expression and regulation of Lsk and Csk in peripheral human monocytes. We have found that Lsk mRNA and protein were not expressed in resting monocytes but were induced by treatment with interleukin 4 (IL-4) or IL-13 but not by interferon gamma (IFN-gamma) or IL-2. In fact, IFN-gamma, but not IL-2, efficiently blocked Lsk induction by IL-4 or IL-13. In contrast, Csk was constitutively present in human mon

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Xu, Shengli, Jianxin Huo, Joy En-Lin Tan, and Kong-Peng Lam. "Cbp Deficiency Alters Csk Localization in Lipid Rafts but Does Not Affect T-Cell Development." Molecular and Cellular Biology 25, no. 19 (2005): 8486–95. http://dx.doi.org/10.1128/mcb.25.19.8486-8495.2005.

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ABSTRACT The ubiquitously expressed transmembrane adaptor Csk-binding protein (Cbp) recruits Csk to lipid rafts, where the latter exerts its negative regulatory effect on the Src family of protein tyrosine kinases. We have inactivated Cbp in the mouse germ line. In contrast to Csk gene inactivation, which leads to embryonic lethality and impaired T-cell development, Cbp-deficient mice were viable and exhibited normal T-cell development but with an increased thymocyte population. In the absence of Cbp, the amount of Csk that localizes to the lipid rafts was greatly reduced. Interestingly, this

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