Relevant bibliographies by topics / Protein Kinase, c-Src

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  2. Dissertations / Theses
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Academic literature on the topic 'Protein Kinase, c-Src'

Author: Grafiati
Published: 14 March 2023
Last updated: 31 July 2025

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Journal articles on the topic "Protein Kinase, c-Src"

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Brábek, J., D. Mojžita, L. Hamplová, and Petr Folk. "The Regulatory Region of Prague C v-Src Inhibits the Activity of the Schmidt-Ruppin A v-Src Kinase Domain." Folia Biologica 48, no. 1 (2002): 28–33. https://doi.org/10.14712/fb2002048010028.

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Existing variants of the oncogene v-src differ in their transforming potential as well as in the range of their hosts. We compared the protein kinase activities of two Prague C v-Src variants (PRC and H19), reported to be of low oncogenic potential (Plachý et al., 1995), with the highly oncogenic Schmidt-Ruppin A v-Src (SRA). We employed in vitro kinase assays of affinity-purified proteins expressed in rabbit reticulocyte lysate and in S. cerevisiae. In both systems used, the specific kinase activity of the Prague C v-Sre kinases amounted to only ca 20% of the activity of SRA. This positions t
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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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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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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 (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 an
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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 (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 an
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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 (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 fi
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Zhang, Jiayi, Ching-hang Wong, Weiliang Xia та ін. "Regulation of Sertoli-Germ Cell Adherens Junction Dynamics via Changes in Protein-Protein Interactions of the N-Cadherin-β-Catenin Protein Complex which Are Possibly Mediated by c-Src and Myotubularin-Related Protein 2: An in Vivo Study Using an Androgen Suppression Model". Endocrinology 146, № 3 (2005): 1268–84. http://dx.doi.org/10.1210/en.2004-1194.

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Using a well characterized model of cell-cell actin-based adherens junction (AJ) disruption by suppressing the intratesticular testosterone level in adult rats with testosterone-estradiol implants, we have confirmed earlier findings that Sertoli-germ cell AJ dynamics are regulated by the activation of kinases via putative signaling pathways but with some unexpected findings as follows. First, the loss of germ cells from the seminiferous epithelium during androgen suppression was associated with a surge in myotubularin-related protein 2 (MTMR2, a lipid phosphatase, in which adult MTMR2−/− mice
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Richard, S., D. Yu, K. J. Blumer, et al. "Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1." Molecular and Cellular Biology 15, no. 1 (1995): 186–97. http://dx.doi.org/10.1128/mcb.15.1.186.

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src family tyrosine kinases contain two noncatalytic domains termed src homology 3 (SH3) and SH2 domains. Although several other signal transduction molecules also contain tandemly occurring SH3 and SH2 domains, the function of these closely spaced domains is not well understood. To identify the role of the SH3 domains of src family tyrosine kinases, we sought to identify proteins that interacted with this domain. By using the yeast two-hybrid system, we identified p62, a tyrosine-phosphorylated protein that associates with p21ras GTPase-activating protein, as a src family kinase SH3-domain-bi
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Ahn, Bong-Hyun, Shi Yeon Kim, Eun Hee Kim, et al. "Transmodulation between Phospholipase D and c-Src Enhances Cell Proliferation." Molecular and Cellular Biology 23, no. 9 (2003): 3103–15. http://dx.doi.org/10.1128/mcb.23.9.3103-3115.2003.

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ABSTRACT Phospholipase D (PLD) has been implicated in the signal transduction pathways initiated by several mitogenic protein tyrosine kinases. We demonstrate for the first time that most notably PLD2 and to a lesser extent the PLD1 isoform are tyrosine phosphorylated by c-Src tyrosine kinase via direct association. Moreover, epidermal growth factor induced tyrosine phosphorylation of PLD2 and its interaction with c-Src in A431 cells. Interaction between these proteins is via the pleckstrin homology domain of PLD2 and the catalytic domain of c-Src. Coexpression of PLD1 or PLD2 with c-Src syner
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Levy, J. B., and J. S. Brugge. "Biological and biochemical properties of the c-src+ gene product overexpressed in chicken embryo fibroblasts." Molecular and Cellular Biology 9, no. 8 (1989): 3332–41. http://dx.doi.org/10.1128/mcb.9.8.3332-3341.1989.

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The c-src protein isolated from neuronal cells (pp60c-src+) displays a higher level of protein kinase activity than does pp60c-src from nonneural tissues. There are two structural alterations present in the amino-terminal half of pp60c-src+ expressed in neurons which could contribute to the enhanced activity of this form of pp60c-src: (i) a hexapeptide insert located at amino acid 114 of avian pp60c-src+ and (ii) a novel site(s) of serine phosphorylation. We characterized pp60c-src+ expressed in a nonneuronal cell type to identify factors that regulate the activity of the c-src+ protein and th
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Dissertations / Theses on the topic "Protein Kinase, c-Src"

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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<br>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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Molinari, Alessio. "Design, synthesis and biological evaluation of novel small molecules inhibitors of c-Src, Hck and TAK1 Protein Kinases for treatment of cancer disease." Doctoral thesis, Università di Siena, 2018. http://hdl.handle.net/11365/1048703.

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The interest in protein kinase had been improved in recent years since the entry into the market of the first protein Kinase inhibitor. In this thesis have been designed, and synthesized new small molecules able to inhibit separately three different kinases, c-Src, Hck and TAK1, widely implicated in cancer disease. Protein kinases catalyse the transfer of phosphate groups from nucleoside triphosphates, usually adenosine triphosphate (ATP), to specific serine, threonine, or tyrosine residues in substrate proteins as a way of regulating their activities1,2. Deregulation of their activities can l
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Summy, Justin Matthew. "Functional domain contributions to signaling specificity between the non-receptor tyrosine kinases c-src and c-yes." Morgantown, W. Va. : [West Virginia University Libraries], 2001. http://etd.wvu.edu/templates/showETD.cfm?recnum=2239.

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Thesis (Ph. D.)--West Virginia University, 2001.<br>Title from document title page. Document formatted into pages; contains vi, 195 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references (p. 182-190).
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Lin, Xiaofeng. "Probing the regulatory mechanisms of protein tyrosine kinases, using C-terminal SRC kinase (CSK) as a model system /." View online ; access limited to URI, 2005. http://0-wwwlib.umi.com.helin.uri.edu/dissertations/dlnow/3188064.

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Baisden, Joseph M. "AFAP-110 is a cSrc activator." Morgantown, W. Va. : [West Virginia University Libraries], 2003. http://etd.wvu.edu/templates/showETD.cfm?recnum=2766.

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Thesis (Ph. D.)--West Virginia University, 2003.<br>Title from document title page. Document formatted into pages; contains v, 149 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references.
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Lou, Qiang 1962. "Identification of peptide substrates and development of pseudosubstrate-based peptide inhibitors for p60(C-SRC) protein tyrosine kinase." Diss., The University of Arizona, 1996. http://hdl.handle.net/10150/282230.

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Protein tyrosine kinases (PTKs) mediate important signaling events associated with cellular growth, differentiation, and mitogenesis. The p60c-src protein is the first described cellular protein tyrosine kinase. Human p60c-src PTK has been implicated in the development of colon and breast cancer, and leukemia. However, the exact physiological role of p60c-src PTK or its physiological target proteins are not well known, and the mechanism by which the p60c-src PTK activity is regulated is not completely understood. Peptide substrates can be used to determine the substrate specificity and kinetic
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Song, Jaekyung Cecilia. "Protein Kinase C-δ and Protein Kinase C-ε Cooperatively Enhance Epithelial Cell Spreading via Transactivation of Epidermal Growth Factor Receptor and Actin-Dependent Phosphorylation of Focal Adhesion-Associated Proteins". Cincinnati, Ohio : University of Cincinnati, 2005. http://www.ohiolink.edu/etd/view.cgi?acc%5Fnum=ucin1132198567.

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Thesis (Ph. D.)--University of Cincinnati, 2005.<br>Title from electronic thesis title page (viewed Sept. 13, 2007). Includes abstract. Keywords: Protein Kinase C; Cell spreading; Cell migration; Epithelial Cells; Epidermal Growth Factor Receptor; Transactivation; Focal Adhesion; Actin; Focal Adhesion Kinase; Src; Paxillin Includes bibliographical references.
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Koh, Wonshill. "Molecular control of endothelial lumen formation by Rho GTPases in three dimensional collagen matrices." Diss., Columbia, Mo. : University of Missouri-Columbia, 2008. http://hdl.handle.net/10355/6045.

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Thesis (Ph. D.)--University of Missouri-Columbia, 2008.<br>The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Vita. "May 2008" Includes bibliographical references.
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Lennartsson, Johan. "Stem Cell Factor Induced Signal Transduction." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Univ.-bibl. [distributör], 2002. http://publications.uu.se/theses/91-554-5291-4/.

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Wortmann, Andreas. "In vitro and in vivo examination of the cell surface glycoprotein CDCP1." Thesis, Queensland University of Technology, 2010. https://eprints.qut.edu.au/40975/1/Andreas_Wortmann_Thesis.pdf.

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A number of reports have demonstrated the importance of the CUB domaincontaining protein 1 (CDCP1) in facilitating cancer progression in animal models and the potential of this protein as a prognostic marker in several malignancies. CDCP1 facilitates metastasis formation in animal models by negatively regulating anoikis, a type of apoptosis triggered by the loss of attachment signalling from cell-cell contacts or cell-extra cellular matrix (ECM) contacts. Due to the important role CDCP1 plays in cancer progression in model systems, it is considered a potential drug target to prevent the metast
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Book chapters on the topic "Protein Kinase, c-Src"

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Barnekow, Angelika. "Phosphorylation of Synaptophysin by the c-src Encoded Protein Tyrosin Kinase pp60 c-src." In Cellular Regulation by Protein Phosphorylation. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-75142-4_38.

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Schoeberl, Christian, Edith Ossendorf, Joachim Kremerskothen, Charlotte Brewster, Steve Dilworth, and Angelika Barnekow. "Binding studies on the neuronal isoform of the non-receptor protein tyrosine kinase pp60 c-src , pp60 c-srcN and potential target proteins." In Interacting Protein Domains. Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-60848-3_19.

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Xiao, Xiang, Dolores D. Mruk, Pranitha Jenardhanan, et al. "Nonreceptor Protein Kinases c-Src, c-Yes, and FAK Are Biomarkers for Male Contraceptive Research." In New Advances on Disease Biomarkers and Molecular Targets in Biomedicine. Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-456-2_1.

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Peruzzi, Barbara, Nadia Rucci, and Anna Teti. "The Crucial Role of c-Src Tyrosine Kinase in Bone Metabolism." In Protein Kinases. InTech, 2012. http://dx.doi.org/10.5772/37995.

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Stewart, Alexander a. "Purification of protein (tyrosine) kinases." In Protein Phosphorylation. Oxford University PressOxford, 1993. http://dx.doi.org/10.1093/oso/9780199633067.003.0007.

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Abstract This chapter describes the general principles involved in the purification of protein (tyrosine) kinases (PTKs). The importance of PTKs, and reasons for purifying them are briefly described. The best sources for protein (tyrosine) kinase purification, and methods for their assay are discussed. Purification techniques which are either unique or particularly appropriate for PTKs as a group of enzymes are described, with examples from the purification of three of these enzymes: c-src,epidermal growth factor (EGF) receptor, and platelet-derived growth factor (PDGF) receptor kinases.
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Jung Yoon, Hyun, Sungmin Lee, Suhyun Park, and Sangwook Wu. "Time Series Analysis on the Conformational Change of c-Src Tyrosine Kinase." In Protein Kinase - New Opportunities, Challenges and Future Perspectives [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97726.

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c-Src tyrosine kinase plays an important role in signal transduction pathways, where its activity is regulated by phosphorylation of the two tyrosine residues. We performed targeted molecular dynamics simulation to obtain trajectory of conformational change from inactive to active form. To investigate the conformational change of c-Src tyrosine kinase, we applied network analysis to time series of correlation among residues. The time series of correlation between residues during the conformational change generated by targeted molecular dynamic simulation. With centrality measures such as betwe
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Paterson, Andrew. "Application of the baculoviral expression system to signal transduction." In Signal Transduction. Oxford University PressOxford, 1999. http://dx.doi.org/10.1093/oso/9780199637218.003.0007.

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Abstract The Baculovirus Expression Vector System (BEYS) is an extremely versatile and powerful laboratory tool (1). In simplest terms, the BEYS allows the forced heterologous expression of recombinant protein in susceptible host strains of insect cells. Gene products from the simplest prokaryotes through to the higher eukaryotes have been expressed successfully in this system. Recombinant proteins are recovered in a folded and active form, and posttranslation modifications, such as phosphorylation, lipid acylation, and simple glycosylation are often preserved. Oligomerization is preserved als
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R., Ronald, Elaine L., Janica C., and Mary G. "Nitric Oxide/Protein Kinase G-Iα Promotes c-Src Activation, Proliferation and Chemoresistance in Ovarian Cancer." In Ovarian Cancer - Basic Science Perspective. InTech, 2012. http://dx.doi.org/10.5772/28437.

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Gorski, Jerome L. "FGD1 and Faciogenital Dysplasia (Aarskog–Scott Syndrome)." In Inborn Errors Of Development. Oxford University PressNew York, NY, 2008. http://dx.doi.org/10.1093/oso/9780195306910.003.0145.

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Abstract FGD1 mutations result in faciogenital dysplasia (FGDY; Aarskog–Scott syndrome), an X-linked recessive multiple congenital anomaly syndrome. Skeletal anomalies dominate the FGDY phenotype. Cardinal clinical features include a characteristic set of craniofacial and skeletal anomalies, disproportionate acromelic short stature, delayed skeletal maturation, and urogenital malformations. FGD1 encodes a guanine nucleotide exchange factor (GEF) that speci’cally activates Cdc42, a Rho guanosine triphosphatase (GTPase) that is involved in cell signaling and the regulation of the actin cytoskele
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Chatila, Talal A., and Markku Heikinheimo. "Severe Combined Immunodeficiency Due to Mutations in the CD45 Gene." In Primary Immunodeficiency Diseases. Oxford University PressNew York, NY, 2006. http://dx.doi.org/10.1093/oso/9780195147742.003.0013.

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Abstract The protein tyrosine phosphatase CD45, also known as protein-tyrosine phosphatase, receptor type, C (PTPRC), and leukocyte common antigen (LCA), is a high–molecular weight type I transmembrane protein that is exclusively expressed on all nucleated hematopoietic cells (Tonks et al., 1988; Thomas, 1989; Trowbridge and Thomas, 1994). It is an abundant protein estimated to comprise up to 10% of the cell surface areas of B and T lymphocytes. Despite its abundance and potentially high catalytic capacity, CD45 activity is directed at a limited number of physiologically relevant substrates th
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Conference papers on the topic "Protein Kinase, c-Src"

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Lin, Li-Fang, Ming-Hsi Wu, Tsann-Long Su, and Te-Chang Lee. "Abstract 3594: P-glycoprotein attenuates Src activation and DNA repair activity via increased C-terminal Src kinase-binding protein, a negative regulator of Src, in multidrug-resistant cells." 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.am2015-3594.

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Gomes, Evan, Sarah F. Connelly, and Justin M. Summy. "Abstract 2859: Dual targeting of protein tyrosine kinase c-Src and protein tyrosine phosphatase SHP-2 is a novel therapeutic strategy that induces potent inhibition of pancreatic cancer cell viabilityin vitroand tumor progressionin vivo." 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.am2012-2859.

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