Relevant bibliographies by topics / SRC kinases

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  2. Dissertations / Theses
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Academic literature on the topic 'SRC kinases'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "SRC kinases"

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Blake, Robert A., Martin A. Broome, Xiangdong Liu, Jianming Wu, Mikhail Gishizky, Li Sun, and Sara A. Courtneidge. "SU6656, a Selective Src Family Kinase Inhibitor, Used To Probe Growth Factor Signaling." Molecular and Cellular Biology 20, no. 23 (December 1, 2000): 9018–27. http://dx.doi.org/10.1128/mcb.20.23.9018-9027.2000.

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ABSTRACT The use of small-molecule inhibitors to study molecular components of cellular signal transduction pathways provides a means of analysis complementary to currently used techniques, such as antisense, dominant-negative (interfering) mutants and constitutively activated mutants. We have identified and characterized a small-molecule inhibitor, SU6656, which exhibits selectivity for Src and other members of the Src family. A related inhibitor, SU6657, inhibits many kinases, including Src and the platelet-derived growth factor (PDGF) receptor. The use of SU6656 confirmed our previous findings that Src family kinases are required for both Myc induction and DNA synthesis in response to PDGF stimulation of NIH 3T3 fibroblasts. By comparing PDGF-stimulated tyrosine phosphorylation events in untreated and SU6656-treated cells, we found that some substrates (for example, c-Cbl, and protein kinase C δ) were Src family substrates whereas others (for example, phospholipase C-γ) were not. One protein, the adaptor Shc, was a substrate for both Src family kinases (on tyrosines 239 and 240) and a distinct tyrosine kinase (on tyrosine 317, which is perhaps phosphorylated by the PDGF receptor itself). Microinjection experiments demonstrated that a Shc molecule carrying mutations of tyrosines 239 and 240, in conjunction with an SH2 domain mutation, interfered with PDGF-stimulated DNA synthesis. Deletion of the phosphotyrosine-binding domain also inhibited synthesis. These inhibitions were overcome by heterologous expression of Myc, supporting the hypothesis that Shc functions in the Src pathway. SU6656 should prove a useful additional tool for further dissecting the role of Src kinases in this and other signal transduction pathways.
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Yamboliev, Ilia A., Jennifer Chen, and William T. Gerthoffer. "PI 3-kinases and Src kinases regulate spreading and migration of cultured VSMCs." American Journal of Physiology-Cell Physiology 281, no. 2 (August 1, 2001): C709—C718. http://dx.doi.org/10.1152/ajpcell.2001.281.2.c709.

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Pulmonary artery smooth muscle cell (PASMC) adhesion, spreading, and migration depend on matrix-stimulated reorganization of focal adhesions. Platelet-derived growth factor (PDGF) activates intracellular signal transduction cascades that also regulate adhesion, spreading, and migration, but the signaling molecules involved in these events are poorly defined. We hypothesized that phosphatidylinositol (PI) 3-kinases and Src tyrosine kinases translate matrix and PDGF-initiated signals into cell motility. In experiments with cultured canine PASMCs, inhibition of PI 3-kinases with wortmannin (0.3 μM) and LY-294002 (50 μM) and of Src kinase with PP1 (30 μM) did not decrease spontaneous (nonstimulated) or PDGF-stimulated (10 ng/ml) adhesion onto collagen. PI 3-kinase and Src kinase activities, however, were necessary for cell spreading: PP1 inhibited cell spreading and Src Tyr-418 phosphorylation in a concentration-dependent manner. Inhibition of PI 3-kinase and Src partially reduced cell migration, while at 10 and 30 μM, PP1 eliminated migration, likely due to inhibition of PDGF receptors. In conclusion, both PI 3-kinases and Src tyrosine kinases are components of pathways that mediate spreading and migration of cultured PASMCs on collagen.
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Roche, S., M. Koegl, M. V. Barone, M. F. Roussel, and S. A. Courtneidge. "DNA synthesis induced by some but not all growth factors requires Src family protein tyrosine kinases." Molecular and Cellular Biology 15, no. 2 (February 1995): 1102–9. http://dx.doi.org/10.1128/mcb.15.2.1102.

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The Src family of protein tyrosine kinases have been implicated in the response of cells to several ligands. These include platelet-derived growth factor (PDGF), epidermal growth factor (EGF), and colony stimulating factor type 1 (CSF-1, in macrophages and in fibroblasts engineered to express the receptor). We recently described a microinjection approach which we used to demonstrate that Src family kinases are required for PDGF-induced S phase entry of fibroblasts. We now use this approach to ask whether other ligands also require Src kinases to stimulate cells to replicate DNA. An antibody specific for the carboxy terminus of Src, Fyn, and Yes (anti-cst.1) inhibited Src kinase activity in vitro and caused morphological reversion of Src transformed cells in vivo. Microinjection of this antibody was used to demonstrate that Src kinases were required for both CSF-1 and EGF to drive cells into the S phase. Expression of a kinase-inactive form of Src family kinases also prevented EGF- and CSF-1-stimulated DNA synthesis. However, even though the Src family kinases were necessary for both PDGF- and EGF-induced DNA synthesis in Swiss 3T3 cells, the responses to two other potent growth factors for these cells, lysophosphatidic acid and bombesin, were unaffected by the neutralizing antibodies. Therefore, some but not all growth factors required functional Src family kinases to transmit mitogenic responses.
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Mahajan, S., J. Fargnoli, A. L. Burkhardt, S. A. Kut, S. J. Saouaf, and J. B. Bolen. "Src family protein tyrosine kinases induce autoactivation of Bruton's tyrosine kinase." Molecular and Cellular Biology 15, no. 10 (October 1995): 5304–11. http://dx.doi.org/10.1128/mcb.15.10.5304.

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Bruton's tyrosine kinase (Btk) is tyrosine phosphorylated and enzymatically activated following ligation of the B-cell antigen receptor. These events are temporally regulated, and Btk activation follows that of various members of the Src family of protein tyrosine kinases, thus raising the possibility that Src kinases participate in the Btk activation process. We have evaluated the mechanism underlying Btk enzyme activation and have explored the potential regulatory relationship between Btk and Src protein kinases. We demonstrate in COS transient-expression assays that Btk can be activated through intramolecular autophosphorylation at tyrosine 551 and that Btk autophosphorylation is required for Btk catalytic functions. Coexpression of Btk with members of the Src family of protein tyrosine kinases, but not Syk, led to Btk tyrosine phosphorylation and activation. Using a series of point mutations in Blk (a representative Src protein kinase) and Btk, we show that Src kinases activate Btk through an indirect mechanism that requires membrane association of the Src enzymes as well as functional Btk SH3 and SH2 domains. Our results are compatible with the idea that Src protein tyrosine kinases contribute to Btk activation by indirectly stimulating Btk intramolecular autophosphorylation.
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Shibasaki, F., Y. Fukui, and T. Takenawa. "Different properties of monomer and heterodimer forms of phosphatidylinositol 3-kinases." Biochemical Journal 289, no. 1 (January 1, 1993): 227–31. http://dx.doi.org/10.1042/bj2890227.

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Phosphatidylinositol (PI) 3-kinase plays an important role in the signalling of cell growth. We previously purified two types of PI 3-kinase from bovine thymus, a monomer from (PI 3-kinase I) and a heterodimer form (PI 3-kinase II) [Shibasaki, Homma and Takenawa (1991) J. Biol. Chem. 266, 8108-8114]. Here we examine the properties of these purified PI 3-kinases. Both PI 3-kinases were inhibited strongly by quercetin and isoquercetin. The inhibition of PI 3-kinase I and PI 3-kinase II by quercetin appears to be non-competitive, with apparent Ki values of 4 microM and 2.5 microM respectively. PI 3-kinase II, but not PI 3-kinase I, co-immunoprecipitates with pp60v-src and polyoma middle T (mT)/pp60c-src, even under conditions where the PI 3-kinases are not phosphorylated, suggesting that non-phosphorylated PI 3-kinase recognizes autophosphorylated pp60v-src. PI 3-kinase II is phosphorylated by pp60v-src and binds to it. Anti-p85 (85 kDa subunit of PI 3-kinase II) antibody precipitates not only PI 3-kinase II but also co-immunoprecipitates pp60v-src in src-transformed cells, suggesting that PI 3-kinase II binds to pp60v-src in vivo. These data suggest that the two PI 3-kinases may be regulated independently.
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Nyga, Remy, Fabrice Gouilleux, Flora Cartier, Christian Pecquet, Aline Regnier, Jean-Pierre Marolleau, Jacques Rochette, Richard Moriggl, Hicham Bouhlal, and Kaiss Lassoued. "The Src Kinases Play a Crucial Role in the Growth of Hematopoietic Cells Transformed with Constitutively Activated Stat5 Mutants." Blood 114, no. 22 (November 20, 2009): 5041. http://dx.doi.org/10.1182/blood.v114.22.5041.5041.

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Abstract Abstract 5041 Stat5A and Stat5B transcription factors (TF) play an important role in the control of hematopoietic cell proliferation and survival and are constitutively activated in number of hematological malignancies and solid tumours. Studies conducted with constitutively active (ca) Stat5 mutants (Stat51*6 and cS5F) have shown that deregulated Stat5 activity promotes leukemogenesis. In order to evaluate the role of Src kinases in the transforming properties of Stat5 TF, caStat5 expressing Ba/F3 cells and primary murine bone marrow cells were treated with the PP1 Src kinase inhibitor and with its inactive analogue PP3 as a control. We found that PP1 but not PP3 strongly inhibited Stat5A1*6- and Stat5B1*6- expressing Ba/F3 cell growth and survival while no changes were observed in IL-3 stimulated-parental Ba/F3 cells when treated with PP1. Similarly, we were able to demonstrate specific requirement of Src kinases in cS5F-induced primary bone marrow cell growth. We then examined the contribution of Src kinases to the phosphorylation of various signaling molecules involved in cell growth and survival like Stat5, PI3-K/Akt, Ras/Mapk and NF-kB. The treatment of caStat5 (Stat51*6 or cS5F)-expressing Ba/F3 cells with PP1 resulted in a strong decrease of Erk1/2 phosphorylation, but not of Stat5, Akt and IKK species. In addition, caStat5-expressing Ba/F3 cells were found to express a constitutive molecular complex comprising Stat5, Shc, Grb2, Sos, Erk, Gab2, p85, Lyn and Hck. Finally we found that the Lyn Src kinase was overexpressed in the caStat5-expressing cells. Our data suggest a direct implication of Src kinases in the proliferation of caStat5- Ba/F3 transformed cells through the Shc/Erk1/2 signaling pathway and that Src family members are required for caStat5 (Stat51*6 and cS5F)-induced hematopoietic cell growth. Disclosures No relevant conflicts of interest to declare.
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Klomp, Jennifer E., Vincent Huyot, Anne-Marie Ray, Kerrie B. Collins, Asrar B. Malik, and Andrei V. Karginov. "Mimicking transient activation of protein kinases in living cells." Proceedings of the National Academy of Sciences 113, no. 52 (December 12, 2016): 14976–81. http://dx.doi.org/10.1073/pnas.1609675114.

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Physiological stimuli activate protein kinases for finite periods of time, which is critical for specific biological outcomes. Mimicking this transient biological activity of kinases is challenging due to the limitations of existing methods. Here, we report a strategy enabling transient kinase activation in living cells. Using two protein-engineering approaches, we achieve independent control of kinase activation and inactivation. We show successful regulation of tyrosine kinase c-Src (Src) and Ser/Thr kinase p38α (p38), demonstrating broad applicability of the method. By activating Src for finite periods of time, we reveal how the duration of kinase activation affects secondary morphological changes that follow transient Src activation. This approach highlights distinct roles for sequential Src-Rac1– and Src-PI3K–signaling pathways at different stages during transient Src activation. Finally, we demonstrate that this method enables transient activation of Src and p38 in a specific signaling complex, providing a tool for targeted regulation of individual signaling pathways.
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Brott, B. K., S. Decker, M. C. O'Brien, and R. Jove. "Molecular features of the viral and cellular Src kinases involved in interactions with the GTPase-activating protein." Molecular and Cellular Biology 11, no. 10 (October 1991): 5059–67. http://dx.doi.org/10.1128/mcb.11.10.5059.

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GTPase-activating protein (GAP) enhances the rate of GTP hydrolysis by cellular Ras proteins and is implicated in mitogenic signal transduction. GAP is phosphorylated on tyrosine in cells transformed by Rous sarcoma virus and serves as an in vitro substrate of the viral Src (v-Src) kinase. Our previous studies showed that GAP complexes stably with normal cellular Src (c-Src), although its association with v-Src is less stable. To further investigate the molecular basis for interactions between GAP and the Src kinases, we examined GAP association with and phosphorylation by a series of c-Src and v-Src mutants. Analysis of GAP association with c-Src/v-Src chimeric proteins demonstrates that GAP associates stably with Src proteins possessing low kinase activity and poorly with activated Src kinases, especially those that lack the carboxy-terminal segment of c-Src containing the regulatory amino acid Tyr-527. Phosphorylated Tyr-527 is a major determinant of c-Src association with GAP, as demonstrated by c-Src point mutants in which Tyr-527 is changed to Phe. While the isolated amino-terminal half of the c-Src protein is insufficient for stable GAP association, analysis of point substitutions of highly conserved amino acid residues in the c-Src SH2 region indicate that this region also influences Src-GAP complex formation. Therefore, our results suggest that both Tyr-527 phosphorylation and the SH2 region contribute to stable association of c-Src with GAP. Analysis of in vivo phosphorylation of GAP by v-Src mutants containing deletions encompassing the SH2, SH3, and unique regions suggests that the kinase domain of v-Src contains sufficient substrate specificity for GAP phosphorylation. Even though tyrosine phosphorylation of GAP correlates to certain extent with the transforming ability of various c-Src and v-Src mutants, our data suggest that other GAP-associated proteins may also have roles in Src-mediated oncogenic transformation. These findings provide additional evidence for the specificity of Src interactions with GAP and support the hypothesis that these interactions contribute to the biological functions of the Scr kinases.
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Brott, B. K., S. Decker, M. C. O'Brien, and R. Jove. "Molecular features of the viral and cellular Src kinases involved in interactions with the GTPase-activating protein." Molecular and Cellular Biology 11, no. 10 (October 1991): 5059–67. http://dx.doi.org/10.1128/mcb.11.10.5059-5067.1991.

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GTPase-activating protein (GAP) enhances the rate of GTP hydrolysis by cellular Ras proteins and is implicated in mitogenic signal transduction. GAP is phosphorylated on tyrosine in cells transformed by Rous sarcoma virus and serves as an in vitro substrate of the viral Src (v-Src) kinase. Our previous studies showed that GAP complexes stably with normal cellular Src (c-Src), although its association with v-Src is less stable. To further investigate the molecular basis for interactions between GAP and the Src kinases, we examined GAP association with and phosphorylation by a series of c-Src and v-Src mutants. Analysis of GAP association with c-Src/v-Src chimeric proteins demonstrates that GAP associates stably with Src proteins possessing low kinase activity and poorly with activated Src kinases, especially those that lack the carboxy-terminal segment of c-Src containing the regulatory amino acid Tyr-527. Phosphorylated Tyr-527 is a major determinant of c-Src association with GAP, as demonstrated by c-Src point mutants in which Tyr-527 is changed to Phe. While the isolated amino-terminal half of the c-Src protein is insufficient for stable GAP association, analysis of point substitutions of highly conserved amino acid residues in the c-Src SH2 region indicate that this region also influences Src-GAP complex formation. Therefore, our results suggest that both Tyr-527 phosphorylation and the SH2 region contribute to stable association of c-Src with GAP. Analysis of in vivo phosphorylation of GAP by v-Src mutants containing deletions encompassing the SH2, SH3, and unique regions suggests that the kinase domain of v-Src contains sufficient substrate specificity for GAP phosphorylation. Even though tyrosine phosphorylation of GAP correlates to certain extent with the transforming ability of various c-Src and v-Src mutants, our data suggest that other GAP-associated proteins may also have roles in Src-mediated oncogenic transformation. These findings provide additional evidence for the specificity of Src interactions with GAP and support the hypothesis that these interactions contribute to the biological functions of the Scr kinases.
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Bauer, Markus, Petra Maschberger, Lynn Quek, Stephen Briddon, Debabrata Dash, Michael Weiss, Steve Watson, and Wolfgang Siess. "Genetic and Pharmacological Analyses of Involvement of Src-family, Syk and Btk Tyrosine Kinases in Platelet Shape Change." Thrombosis and Haemostasis 85, no. 02 (2001): 331–40. http://dx.doi.org/10.1055/s-0037-1615689.

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SummaryPlatelet shape change was found to be associated with an increase in protein tyrosine phosphorylation upon stimulation of thrombin-, ADPand thromboxane A2-G-protein coupled receptors in human platelets and thromboxane A2 receptors in mouse platelets. By using PP1 and PD173956, two structurally unrelated specific inhibitors of Src-family tyrosine kinases, and mouse platelets deficient in the Src-kinase Fyn or Lyn, we show that Src-family kinases cause the increase in protein tyrosine phosphorylation. We further detected that the non-Src tyrosine kinase Syk was activated during shape change in a manner dependent on Src-family kinaseactivation. The pharmacological experiments and the studies on Fyn-, Lyn- and Syk-deficient mouse platelets showed that neither Src-family kinases nor Syk are functionally involved in shape change. Also human platelets deficient of the tyrosine kinase Btk showed a normal shape change. Binding of PAC-1 that recognizes activated integrin αIIb β3 complexes on the platelet surface was enhanced during shape change and blocked by inhibition of Src-kinases. We conclude that the activation of Src-kinases and the subsequent Syk stimulation upon activation of G-protein coupled receptors are not involved in the cytoskeletal changes underlying shape change of human and mouse platelets, but that the stimulation of this evolutionary conserved pathway leads to integrin αIIb β3 exposure during shape change.
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Dissertations / Theses on the topic "SRC kinases"

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Rupniewska, Ewa. "Targeting SRC family kinases in lung cancer." Thesis, Imperial College London, 2012. http://hdl.handle.net/10044/1/9234.

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Lung cancer is the commonest cancer killer worldwide. This is mainly due to the rapid development of drug resistance and early metastatic dissemination of the disease. SRC family kinases (SFKs) are frequently over-expressed in various cancers and have been implicated in tumorigenesis through their ability to promote cancer cell proliferation, survival and invasiveness. Therefore, we sought to evaluate the involvement of SFKs in lung cancer biology and assess the possible therapeutic benefits of their inhibition, either alone or in combination with additional treatments. We demonstrate that SRC family kinases are over-expressed and activated in-vitro in a panel of lung cancer cell lines as compared to immortalised normal lung epithelial cells. SRC, FYN and LYN are expressed in a high proportion of lung cancer but not normal lung tissue sections. Furthermore, enhanced expression of LYN correlates with poor patients’ survival. Dasatinib is a novel SRC/ABL inhibitor which effectively blocks SFKs activity at nanomolar concentrations. Dasatinib reduces cell numbers in 10 out of 11 NSCLC cell lines tested, which correlates with a strong inhibition of DNA synthesis and cell proliferation, while apoptosis is moderately enhanced only in a few cell lines. Interestingly, dasatinib potently induces autophagy in all NSCLC cell lines tested. This appears to be a pro-survival mechanism as autophagy inhibition using chemical compounds or siRNA-mediated depletion of ATG5 sensitises NSCLC cells to dasatinib through enhanced apoptosis. Lastly, our results indicate that SFKs have both overlapping and isoform-specific functions in NSCLC cell biology, as demonstrated by the effects of siRNA-mediated knockdown of SRC, YES, FYN or LYN. Our results suggest that inhibition of SRC family kinases alone or in combination with autophagy inhibitors may be a beneficial therapeutic strategy in the management of lung cancer patients.
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Keenan, Sarah. "Structure-function studies of the neuronal Src kinases." Thesis, University of York, 2012. http://etheses.whiterose.ac.uk/3294/.

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N1- and N2-Src are neuronal specific splice variants of the ubiquitously expressed tyrosine kinase C-Src. They differ only by short amino acid inserts within their SH3 domains, a region known to confer substrate specificity. Due to their highly identical sequence it has been difficult to attribute specific neuronal functions to each Src enzyme, however, many C-Src SH3 domain substrates do not bind to the N-Src SH3 domains. The limited functional N1-Src data indicate that it is involved in neuronal differentiation. Furthermore, high expression levels of the N-Srcs in childhood neuroblastoma correlate with cases in which the tumour spontaneously differentiates to a harmless neuronal phenotype. In this study, I sought to explain how the amino acid inserts in the N-Src SH3 domains affect substrate specificity and kinase activity and how they might act to drive neuronal differentiation. I employed a multi-disciplinary approach to investigate the functions of the N Srcs. Studies in heterologous cells revealed a specific role for the N-Srcs in cytoskeletal rearrangement. A sensitive in vitro kinase assay was developed and this showed that the N-Src SH3 domain ligand preferences differ from those of C-Src. A subsequent phage display screen was able to identify a novel consensus sequence for the N1-Src SH3 domain and peptides containing this consensus motif were shown to be highly specific N1-Src inhibitors both in vitro and in cells. Bioinformatic analyses revealed the consensus sequence to be present in many neuronal proteins and identified a number of putative N1-Src substrates. In cultured neurons I identified a specific role for N1-Src acting in the L1-CAM pathway to modulate neurite outgrowth. The data presented here provide evidence that the inserts in the SH3 domains of the N-Srcs confer significant differences in their substrate preferences and that the functions mediated by the N-Srcs are different to those of C-Src. A role for N1-Src has been identified in the modulation of axon outgrowth in cultured neurons and the putative substrates identified now provide promising targets for the further study of N1-Src function. Future investigations will be able to utilise the data presented here to elucidate how N1-Src regulates the neuronal cytoskeleton, while tools I have developed; including a highly specific N1-Src inhibitor will greatly aid these investigations.
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Scales, Timothy M. E. "Tyrosine phosphorylation of tau protein by Src-family kinases." Thesis, King's College London (University of London), 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.406870.

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Lewis, Philip Alexander. "The role of N-Src kinases in neuronal differentiation." Thesis, University of York, 2014. http://etheses.whiterose.ac.uk/8000/.

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The ubiquitous proto-oncogene C-Src has two neuronal splice variants, N1- and N2-Src, which contain 6 and 17 amino acid inserts in their SH3 domains respectively. These inserts are thought to modify SH3 domain binding in a manner that decreases auto-inhibition and changes substrate specificity. Although high levels of neuronal Src expression are associated with neuronal differentiation, both during development and in the developmental cancer neuroblastoma, the functions, molecular mechanisms and specific substrate proteins of neuronal Srcs remain largely uncharacterised. Employing a highly multidisciplinary approach, this project aimed to characterise the role of N-Src expression in neuronal differentiation. Neuronal Srcs were demonstrated to be highly active in neuroblastoma cell lines, and overexpression can drive significant neuritogenesis in the retinoic acid-resistant cell lines KELLY and SK-N-AS. N2-Src expression was also shown to decrease the expression of Ki67 in SK-N-AS cells, indicating that N2-Src can drive neuroblastoma cells into quiescence. Using the Xenopus embryo as a model system for neuronal development, the expression pattern of xN1-Src during neurulation was characterised and a novel neuronal splice variant was identified in this species. It was demonstrated that xN1-Src is essential for healthy primary neurogenesis, and that xN1-Src knockdown caused a dramatic locomotive and patterning phenotype in X.tropicalis. Using stable, inducible HeLa cell lines, a phosphoproteomic screen demonstrated significant changes in the phosphotyrosine profile between C- and N2-Src over-expressing cells. Several candidate N2-Src substrates were identified, including paxillin, plakophilin and BCAR1. Bioinformatic analyses of the proteomic data revealed the enrichment of signalling pathways and protein complexes involved in membrane traffic and cell adhesion. Through these multidisciplinary approaches, the cellular effects of N1- and N2-Src signalling during both neuronal precursor and neuroblastoma differentiation have been characterised. Furthermore, a library of potential N-Src substrates has been generated that provides a framework for future studies.
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Gatesman, Ammer Amanda. "PKCalpha direct cSrc activation and podosome formation through the adaptor protein AFAP-110." Morgantown, W. Va. : [West Virginia University Libraries], 2004. https://etd.wvu.edu/etd/controller.jsp?moduleName=documentdata&jsp%5FetdId=3762.

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Thesis (Ph. D.)--West Virginia University, 2004
Title from document title page. Document formatted into pages; contains vii, 350 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references (p. 322-346).
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Hooker, Erika. "Negative regulators of the Src family kinases in renal epithelial cells." Thesis, McGill University, 2013. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=116932.

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The Src kinases are non-receptor tyrosine kinases involved in many epithelial processes in both normal and injured cells. Src was originally identified as a viral oncogene and has since been characterized as an important regulator of cellular proliferation, differentiation, and motility. Our lab has previously demonstrated that the Src kinases are important modifiers of gene expression in tubule cells of the kidney during ischemia-reperfusion injury. The signalling events that control and mediate the Src kinase transcriptional response in renal epithelial cells are not well understood. In this thesis, I have identified two novel negative regulators of the Src transcriptional response in renal epithelial cells. In Manuscript I and II, I demonstrate that the adapter protein Dok-4 can act as an inhibitor of Src-mediated transcription. Unlike most other adapter proteins, several members of the Dok family are primarily characterized by their inhibitory actions downstream of active tyrosine kinases. Despite being the most ubiquitously expressed Dok family member, Dok-4 function has remained elusive as few interacting proteins have been identified. In Manuscript I, we found that the previously defined boundaries of the Dok-4 PTB domain needed to be extended for proper function. We demonstrate that the PTB domain of Dok-4 contains an extended C-terminal alpha helix critical for canonical PTB-mediated interaction and identified the lipid phosphatase Ship1 as a novel partner of this redefined Dok-4 PTB domain. This interaction is greatly increased in the presence of active Src kinases and occurs through a canonical NPXpY motif present in the C-terminal region of Ship1. In contrast to the Dok-4-Ship1 interaction, in Manuscript II we present a non-canonical PTB-mediated interaction between Dok-4 and the nuclear transcription factor, Elk4. This interaction leads to relocalization of Elk4 from the nucleus to the cytoplasm and degradation of full-length Elk4. In renal cells, Dok-4 inhibits Src-mediated activation of Elk4 and represses expression of the immediate early genes, such as egr-1 and fos1, as well as some of their transcriptional targets. In agreement with this data, knock-down of Dok-4 was associated with increased proliferation of renal epithelial cells. During renal ischemia-reperfusion injury, where upregulation of immediate early genes is known to occur, we have for the first time detected a strong activation of the Src kinases and a delayed upregulation of Elk4, suggesting that Elk4 may be not only highly expressed, but also highly active. Dok-4, which is expressed in the kidney, may be essential for limiting damage to the kidney caused by Elk4-induced expression of the immediate early genes. In addition to activating transcription of the immediate early genes, we have previously shown that the Src kinases are responsible for transcriptionally upregulating the receptor tyrosine kinase, EphA2, during renal ischemia-reperfusion injury. In the preliminary manuscript presented here, we observed that while the Src kinases are highly active, the Stat proteins, downstream effectors of the Jak kinases, are dephosphorylated and inactive. As a corollary of this observation, overexpression of all three ubiquitous Jak family members, Jak1, Jak2 and Tyk2 could attenuate Src-mediated activation of the EphA2 promoter. Inhibition of endogenous Jak kinase by siRNA-mediated knock-down or incubation with the pharmacological inhibitor, Jak inhibitor I also activated EphA2 transcription. Surprisingly, Jak-mediated inhibition of EphA2 expression occurs independently of the Stat family and the cytokine receptors. Collectively, this thesis identifies two novel regulators of the Src kinase family in renal epithelial cells, the Dok-4 adapter protein and the family of Jak kinases.
Les kinases Src sont des tyrosine-kinases cytosoliques qui sont impliquées dans multiples processus dans les cellules épithéliales et autres. Originalement identifiée comme un oncogène viral, la kinase Src est maintenant caractérisée comme une régulatrice de la prolifération, la différenciation et la motilité cellulaire. Nous avons précédemment montré que les kinases Src sont capables de modifier l'expression génique dans les tubules des reins durant le domage rénal par ischémie et réperfusion. Cependant, les mécanismes de signalisation qui contrôle la réponse transcriptionelle des kinases Src ne sont pas bien compris. La présente thèse décrit deux nouveaux inhibiteurs endogènes de la famille de kinases Src dans les cellules rénale épithéliales.Les deux premiers manuscrits établissent que la protéine adaptatrice Dok-4 fonctionne comme un inhibiteur des kinases Src. Contrairement à la plus part de protéines adaptatrices, la famille Dok est caractérisée par des actions inhibitrices durant la signalisation par les tyrosines kinases. Malgré que Dok-4 soit le membre de la famille Dok exprimé de manière la plus ubiquitaire, sa fonction est encore mal connue. Le premier manuscrit que je présente (Manuscrit I) décrit le domaine PTB de Dok-4. On y a démontré que le domaine PTB contient une extension C-terminal consistant probablement en une hélice alpha et que celle-ci est essentielle pour les interactions canoniques du domaine PTB de Dok-4. De plus, nous avons identifié la phosphatase lipidique Ship1 comme un nouveau partenaire de ce domaine PTB redéfini. Cette interaction est augmentée quand les kinases Src sont actives et elle implique un motif NPXpY dans la région C-terminale de Ship1. Contrairement à l'interaction entre Dok-4 et Ship1, l'interaction décrite dans le deuxième manuscrit (Manuscrit II) entre Dok-4 et le facteur de transcription, Elk4, implique le domaine PTB, mais se fait dans une manière atypique. L'interaction entre Dok-4 et Elk4 induit la relocalisation d'Elk4 du noyau au cytoplasme et cause la dégradation de la protéine Elk4. Dans les cellules rénales, Dok-4 inhibe l'activation d'Elk4 par les kinases Src et réprime l'expression des gènes de réponse précoce ("immediate early genes"), comme egr-1 et fos, et quelques cibles transcriptionelles de ces gènes. En accord avec ces données, suppression de Dok-4 est associée avec une augmentation de prolifération. En utilisant un modèle in vivo d'ischémie-reperfusion rénale, où la surexpression de gène de réponse précoce a déjà été démontrée, nous avons détecté une forte activation des kinases Src suivie d'une augmentation retardée de l'expression d'Elk4 dans les lysates de reins. Ces données suggèrent que dans ce modèle Dok-4 pourrait être critique pour limiter les dommages aux reins causé par l'induction des gènes de réponse précoce par Elk4. En plus d'activer l'expression des gènes de réponse précoce, nous avons précédemment montré que les kinases Src sont impliquées dans l'induction transcriptionnelle du récepteur tyrosine-kinase, EphA2, durant l'ischémie-reperfusion rénale. Dans le manuscrit préliminaire que je présente, nous avons noté que dans un modèle de déplétion et réplétion d'ATP, les kinases Src sont activées et les protéines Stat, des effecteurs des kinases Jak, sont déphsophorylés et inactives. Comme corollaire de cette observation, la surexpression de trois membres de de la famille Jak inhibent l'activation du promoteur d'EphA2 par les Src kinases. En plus, l'inhibition des kinases Jak endogènes par traitement aux siRNA ou par un inhibiteur pharmacologique, Jak Inhibitor I, active le promoteur d'EphA2. Étonnement, l'inhibition de l'expression d'EphA2 par les kinases Jak se fait indépendamment des protéines Stat et les récepteurs à cytokines. Mises ensemble, les données de cette thèse démontrent deux nouveaux inhibiteurs de la famille Src dans les cellules rénales épithéliales, la protéine adaptatrice, Dok-4 et les kinases, Jak1 et Jak2.
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Allard, Pierre. "Caractérisation des tyrosine kinases Src, Lyn et Fer dans la prostate." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0028/NQ52134.pdf.

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Brignatz, Constance. "Importance du repliement intramoléculaire dans la fonction biologique et l'évolution des Src-kinases." Aix-Marseille 2, 2008. http://www.theses.fr/2008AIX22081.

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Shor, Audrey Cathryn. "Src kinase inhibitors for the treatment of sarcomas : cellular and molecular mechanisms of action." [Tampa, Fla] : University of South Florida, 2007. http://purl.fcla.edu/usf/dc/et/SFE0001906.

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Tatton, Emma Louise. "The role of Src kinases in cytokine induced signalling in haemopoietic cells." Thesis, University College London (University of London), 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.406642.

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Books on the topic "SRC kinases"

1

Mustelin, Tomas. Src family tyrosine kinases in leukocytes. Austin: R.G. Landes, 1994.

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Wei, Alice C. The role of Src family kinases in the pathogenesis of fulminant viral hepatitis due to murine hepatitis virus strain-3. Ottawa: National Library of Canada, 2000.

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Abl family kinases in development and disease. New York, NY: Landes bioscience/Springer Science+Business Media, 2007.

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Koleske, Anthony. Abl Family Kinases in Development and Disease. Springer, 2007.

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Khadaroo, Rachel G. The cellular and molecular mechanisms regulating oxidative stress-induced priming of the macrophage: The role of the Src family of tyrosine kinases. 2004.

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Xu, Jindong. The role of C-terminial SRC kinase (Csk) in the regulation of N-methyl-D-aspartate receptors. 2006.

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Stavar, Laura. Evidence for a role of Src tyrosine kinase in high glucose-induced collagen accumulation in mesangial cells. 2005.

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Book chapters on the topic "SRC kinases"

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Šuša, Mira, Martin Missbach, Rainer Gamse, Michaela Kneissel, Thomas Buhl, Jürg A. Gasser, Markus Glatt, Terence O’Reilly, Anna Teti, and Jonathan Green. "Src as a Target for Pharmaceutical Intervention." In Protein Tyrosine Kinases, 71–92. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:071.

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Veillette, André, and Joseph B. Bolen. "src-related protein tyrosine kinases." In Cancer Treatment and Research, 121–42. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4613-1599-5_5.

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Burck, Kathy B., Edison T. Liu, and James W. Larrick. "src and Related Protein Kinases." In Oncogenes, 133–55. New York, NY: Springer New York, 1988. http://dx.doi.org/10.1007/978-1-4612-3718-1_7.

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van Roy, Frans, Volker Nimmrich, Anton Bespalov, Achim Möller, Hiromitsu Hara, Jacob P. Turowec, Nicole A. St. Denis, et al. "c-Src Family of Tyrosine Kinases." In Encyclopedia of Signaling Molecules, 473–80. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_54.

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Sen, Banibrata, and Faye M. Johnson. "c-Src Family of Tyrosine Kinases." In Encyclopedia of Signaling Molecules, 1231–39. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_54.

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Couture, C., and T. Mustelin. "The Src Family of Protein Tyrosine Kinases." In Signal Transduction in Testicular Cells, 219–46. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-662-03230-5_11.

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Silva, Corinne M., Julie L. Boerner, and Sarah J. Parsons. "Interactions of STATs with Src Family Kinases." In Signal Transducers and Activators of Transcription (STATs), 223–36. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-017-3000-6_15.

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Courtneidge, Sara A. "Src Family Kinases and the Cell Cycle." In Cancer Genes, 45–56. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5895-8_3.

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Mukhund, Vidya, Afroz Alam, and Ganji Purnachandra Nagaraju. "EGFR and Cytoplasmic Kinase Src Targeting in Pancreatic Cancer." In Role of Tyrosine Kinases in Gastrointestinal Malignancies, 97–105. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-1486-5_8.

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Martín-Pérez, Jorge, José Manuel García-Martínez, María Pilar Sánchez-Bailón, Víctor Mayoral-Varo, and Annarica Calcabrini. "Role of Src Family Kinases in Prolactin Signaling." In Advances in Experimental Medicine and Biology, 163–88. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-12114-7_7.

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Conference papers on the topic "SRC kinases"

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Bußmann, L., A. Münscher, K. Rothkamm, and K. Hoffer. "Kinom profiling of tyrosine kinases identifies Src-family kinases to be highly activated in HNSCC." In Abstract- und Posterband – 89. Jahresversammlung der Deutschen Gesellschaft für HNO-Heilkunde, Kopf- und Hals-Chirurgie e.V., Bonn – Forschung heute – Zukunft morgen. Georg Thieme Verlag KG, 2018. http://dx.doi.org/10.1055/s-0038-1639995.

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Vojtěchová, Martina, Zdena Tuháčková, Jan Hlaváček, and Vlasta Sovová. "Transformation of hamster fibroblasts by v-Src resulted in increased activity of both Src and Csk protein kinases." In VIIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2001. http://dx.doi.org/10.1135/css200104072.

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Rust, Heather L., Jamie A. Moroco, John J. Alvarado, John J. Engen, and Thomas E. Smithgall. "Abstract B190: Allosteric modulation of Src family kinases via SH3 domain displacement." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics; November 5-9, 2015; Boston, MA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1535-7163.targ-15-b190.

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Zhang, Siyuan, Chenyu Zhang, Wen-Chien Huang, Frank J. Lowery, Suyun Huang, Kenneth D. Aldape, Patricia S. Steeg, and Dihua Yu. "Abstract 2974: Combating breast cancer brain metastasis by targeting Src family kinases." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-2974.

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Nelson, Michael P., Benjamin S. Christmann, Allison E. Metz, and Chad Steele. "Src-family Tyrosine Kinases Regulate Alveolar Macrophage Alternative Activation During Pneumocystis Murina Lung Infection." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a5222.

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Veith, C., N. Kahn, M. Hristova, C. M. Dustin, M. Kreuter, M. A. Schneider, F. Van Schooten, A. Van Der Vliet, and A. Boots. "SRC family kinases modulate molecular pathways associated with mitochondrial dysfunction in idiopathic pulmonary fibrosis." In ERS Lung Science Conference 2021 abstracts. European Respiratory Society, 2021. http://dx.doi.org/10.1183/23120541.lsc-2021.90.

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Patel, Ravi K., Mark Weir, Sabine Hellwig, Heather Dorman, and Thomas E. Smithgall. "Abstract 2363: Targeting Src-family kinases to combat acquired inhibitor resistance in FLT3-ITD+AML." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-2363.

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Urazov, Mark, Maria Vedunova, and Elena Mitroshina. "NEUROPROTECTIVE EFFECT OF BLOCKADE OF SRC AND RIPK1 KINASES IN MODELING CEREBRAL ISCHEMIA IN VIVO." In XVII INTERNATIONAL INTERDISCIPLINARY CONGRESS NEUROSCIENCE FOR MEDICINE AND PSYCHOLOGY. LCC MAKS Press, 2021. http://dx.doi.org/10.29003/m2359.sudak.ns2021-17/379-380.

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Acquafreda Lakind, Thais, Kenneth Soprano, and Dianne Soprano. "Abstract 1854: Evidence that RARs interact with Src family kinases and that inhibition of Src family kinase activity can affect the growth response of SKOV3 ovarian cancer cell to atRA." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1854.

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Vojtěchová, Martina, Zdena Tuháčková, Jan Hlaváček, Jiří Velek, and Vlasta Sovová. "The v-Src and c-Src tyrosine kinases immunoprecipitated from Rous sarcoma virus-transformed cells display different specificities to three commonly used peptide substrates." In VIIIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2003. http://dx.doi.org/10.1135/css200306119.

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Reports on the topic "SRC kinases"

1

Smith, Gary. Dependency on Src-Family Kinases for Recurrence of Androgen-Independent Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2012. http://dx.doi.org/10.21236/ada566557.

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Gelman, Irwin H. Dependency on Src-Family Kinases for Recurrence of Androgen-Independent Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2012. http://dx.doi.org/10.21236/ada566985.

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Smith, Gary. Dependency on SRC-Family Kinases for Recurrence of Androgen-Independent Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2010. http://dx.doi.org/10.21236/ada546171.

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Gelman, Irwin H. Dependency on SRC-Family Kinases for Recurrence of Androgen-Independent Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2010. http://dx.doi.org/10.21236/ada544923.

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Mohler, James L. Dependency on Src-Family Kinases (SFK) for Recurrence of Androgen-Independent Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2012. http://dx.doi.org/10.21236/ada566915.

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