Relevant bibliographies by topics / Tyrosine‐protein kinase (tyrosine kinase)

Academic literature on the topic 'Tyrosine‐protein kinase (tyrosine kinase)'

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Published: 10 December 2022
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Journal articles on the topic "Tyrosine‐protein kinase (tyrosine kinase)"

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King, P. D., A. Sadra, J. M. Teng, L. Xiao-Rong, A. Han, A. Selvakumar, A. August, and B. Dupont. "Analysis of CD28 cytoplasmic tail tyrosine residues as regulators and substrates for the protein tyrosine kinases, EMT and LCK." Journal of Immunology 158, no. 2 (January 15, 1997): 580–90. http://dx.doi.org/10.4049/jimmunol.158.2.580.

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Abstract The CD28 cell surface receptor provides an important costimulatory signal for T cells necessary for their response to Ag. Early events in CD28 signaling include recruitment and activation of phosphatidylinositol 3-kinase (PI3-kinase) and activation of the protein tyrosine kinases (PTKs), LCK and EMT. Recruitment and activation of PI3-kinase is known to be dependent upon phosphorylation of tyrosine 173 of the CD28 cytoplasmic tail contained within a YMNM motif. By contrast, little is known of which residues of the CD28 tail, including tyrosines, are required for the activation of PTKs. To address this we studied the ability of truncation mutants and tyrosine to phenylalanine substitution mutants of the CD28 cytoplasmic tail to activate LCK and EMT in Jurkat T leukemia cells. Our results indicate that 1) activation of EMT is partially dependent upon tyrosine 173 of the CD28 tail, although it does not require PI3-kinase activation; 2) activation of LCK is independent of CD28 cytoplasmic tail tyrosine residues; and 3) elements sufficient for the activation of both kinases are contained within the first half of the tail. In addition we studied the CD28 tail as a substrate for both PTKs in in vitro kinase assays. We demonstrate that EMT can phosphorylate all four tyrosines of the CD28 tail, in contrast to LCK, which phosphorylates only tyrosine 173. Together with evidence that in vivo, tyrosines other than tyrosine 173 become phosphorylated following CD28 stimulation, this finding suggests that, like LCK, one function of EMT during CD28 signaling is phosphorylation of the receptor.
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Dailey, D., G. L. Schieven, M. Y. Lim, H. Marquardt, T. Gilmore, J. Thorner, and G. S. Martin. "Novel yeast protein kinase (YPK1 gene product) is a 40-kilodalton phosphotyrosyl protein associated with protein-tyrosine kinase activity." Molecular and Cellular Biology 10, no. 12 (December 1990): 6244–56. http://dx.doi.org/10.1128/mcb.10.12.6244-6256.1990.

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Extracts of bakers' yeast (Saccharomyces cerevisiae) contain protein-tyrosine kinase activity that can be detected with a synthetic Glu-Tyr copolymer as substrate (G. Schieven, J. Thorner, and G.S. Martin, Science 231:390-393, 1986). By using this assay in conjunction with ion-exchange and affinity chromatography, a soluble tyrosine kinase activity was purified over 8,000-fold from yeast extracts. The purified activity did not utilize typical substrates for mammalian protein-tyrosine kinases (enolase, casein, and histones). The level of tyrosine kinase activity at all steps of each preparation correlated with the content of a 40-kDa protein (p40). Upon incubation of the most highly purified fractions with Mn-ATP or Mg-ATP, p40 was the only protein phosphorylated on tyrosine. Immunoblotting of purified p40 or total yeast extracts with antiphosphotyrosine antibodies and phosphoamino acid analysis of 32P-labeled yeast proteins fractionated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that the 40-kDa protein is normally phosphorylated at tyrosine in vivo. 32P-labeled p40 immunoprecipitated from extracts of metabolically labeled cells by affinity-purified anti-p40 antibodies contained both phosphoserine and phosphotyrosine. The gene encoding p40 (YPK1) was cloned from a yeast genomic library by using oligonucleotide probes designed on the basis of the sequence of purified peptides. As deduced from the nucleotide sequence of YPK1, p40 is homologous to known protein kinases, with features that resemble known protein-serine kinases more than known protein-tyrosine kinases. Thus, p40 is a protein kinase which is phosphorylated in vivo and in vitro at both tyrosine and serine residues; it may be a novel type of autophosphorylating tyrosine kinase, a bifunctional (serine/tyrosine-specific) protein kinase, or a serine kinase that is a substrate for an associated tyrosine kinase.
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Dailey, D., G. L. Schieven, M. Y. Lim, H. Marquardt, T. Gilmore, J. Thorner, and G. S. Martin. "Novel yeast protein kinase (YPK1 gene product) is a 40-kilodalton phosphotyrosyl protein associated with protein-tyrosine kinase activity." Molecular and Cellular Biology 10, no. 12 (December 1990): 6244–56. http://dx.doi.org/10.1128/mcb.10.12.6244.

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Extracts of bakers' yeast (Saccharomyces cerevisiae) contain protein-tyrosine kinase activity that can be detected with a synthetic Glu-Tyr copolymer as substrate (G. Schieven, J. Thorner, and G.S. Martin, Science 231:390-393, 1986). By using this assay in conjunction with ion-exchange and affinity chromatography, a soluble tyrosine kinase activity was purified over 8,000-fold from yeast extracts. The purified activity did not utilize typical substrates for mammalian protein-tyrosine kinases (enolase, casein, and histones). The level of tyrosine kinase activity at all steps of each preparation correlated with the content of a 40-kDa protein (p40). Upon incubation of the most highly purified fractions with Mn-ATP or Mg-ATP, p40 was the only protein phosphorylated on tyrosine. Immunoblotting of purified p40 or total yeast extracts with antiphosphotyrosine antibodies and phosphoamino acid analysis of 32P-labeled yeast proteins fractionated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that the 40-kDa protein is normally phosphorylated at tyrosine in vivo. 32P-labeled p40 immunoprecipitated from extracts of metabolically labeled cells by affinity-purified anti-p40 antibodies contained both phosphoserine and phosphotyrosine. The gene encoding p40 (YPK1) was cloned from a yeast genomic library by using oligonucleotide probes designed on the basis of the sequence of purified peptides. As deduced from the nucleotide sequence of YPK1, p40 is homologous to known protein kinases, with features that resemble known protein-serine kinases more than known protein-tyrosine kinases. Thus, p40 is a protein kinase which is phosphorylated in vivo and in vitro at both tyrosine and serine residues; it may be a novel type of autophosphorylating tyrosine kinase, a bifunctional (serine/tyrosine-specific) protein kinase, or a serine kinase that is a substrate for an associated tyrosine kinase.
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Hoekstra, M. F., N. Dhillon, G. Carmel, A. J. DeMaggio, R. A. Lindberg, T. Hunter, and J. Kuret. "Budding and fission yeast casein kinase I isoforms have dual-specificity protein kinase activity." Molecular Biology of the Cell 5, no. 8 (August 1994): 877–86. http://dx.doi.org/10.1091/mbc.5.8.877.

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We have examined the activity and substrate specificity of the Saccharomyces cerevisiae Hrr25p and the Schizosaccharomyces pombe Hhp1, Hhp2, and Cki1 protein kinase isoforms. These four gene products are isotypes of casein kinase I (CKI), and the sequence of these protein kinases predicts that they are protein serine/threonine kinases. However, each of these four protein kinases, when expressed in Escherichia coli in an active form, was recognized by anti-phosphotyrosine antibodies. Phosphoamino acid analysis of 32P-labeled proteins showed phosphorylation on serine, threonine, and tyrosine residues. The E. coli produced forms of Hhp1, Hhp2, and Cki1 were autophosphorylated on tyrosine, and both Hhp1 and Hhp2 were capable of phosphorylating the tyrosine-protein kinase synthetic peptide substrate polymer poly-E4Y1. Immune complex protein kinases assays from S. pombe cells showed that Hhp1-containing precipitates were associated with a protein-tyrosine kinase activity, and the Hhp1 present in these immunoprecipitates was phosphorylated on tyrosine residues. Although dephosphorylation of Hhp1 and Hhp2 by Ser/Thr phosphatase had little effect on the specific activity, tyrosine dephosphorylation of Hhp1 and Hhp2 caused a 1.8-to 3.1-fold increase in the Km for poly-E4Y1 and casein. These data demonstrate that four different CKI isoforms from two different yeasts are capable of protein-tyrosine kinase activity and encode dual-specificity protein kinases.
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Lawrence, David S., and Jinkui Niu. "Protein Kinase InhibitorsThe Tyrosine-Specific Protein Kinases." Pharmacology & Therapeutics 77, no. 2 (February 1998): 81–114. http://dx.doi.org/10.1016/s0163-7258(97)00052-1.

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Trojanek, Joanna B., Maria M. Klimecka, Anna Fraser, Grazyna Dobrowolska, and Grazyna Muszyńska. "Characterization of dual specificity protein kinase from maize seedlings." Acta Biochimica Polonica 51, no. 3 (September 30, 2004): 635–47. http://dx.doi.org/10.18388/abp.2004_3549.

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A protein kinase of 57 kDa, able to phosphorylate tyrosine in synthetic substrates pol(Glu4,Tyr1) and a fragment of Src tyrosine kinase, was isolated and partly purified from maize seedlings (Zea mays). The protein kinase was able to phosphorylate exogenous proteins: enolase, caseins, histones and myelin basic protein. Amino acid analysis of phosphorylated casein and enolase, as well as of phosphorylated endogenous proteins, showed that both Tyr and Ser residues were phosphorylated. Phosphotyrosine was also immunodetected in the 57 kDa protein fraction. In the protein fraction there are present 57 kDa protein kinase and enolase. This co-purification suggests that enolase can be an endogenous substrate of the kinase. The two proteins could be resolved by two-dimensional electrophoresis. Specific inhibitors of typical protein-tyrosine kinases had essentially no effect on the activity of the maize enzyme. Staurosporine, a nonspecific inhibitor of protein kinases, effectively inhibited the 57 kDa protein kinase. Also, poly L-lysine and heparin inhibited tyrosine phosphorylation by 57 kDa maize protein kinase. The substrate and inhibitor specificities of the 57 kDa maize protein kinase phosphorylating tyrosine indicate that it is a novel plant dual-specificity protein kinase.
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Stern, D. F., P. Zheng, D. R. Beidler, and C. Zerillo. "Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine." Molecular and Cellular Biology 11, no. 2 (February 1991): 987–1001. http://dx.doi.org/10.1128/mcb.11.2.987-1001.1991.

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A Saccharomyces cerevisiae lambda gt11 library was screened with antiphosphotyrosine antibodies in an attempt to identify a gene encoding a tyrosine kinase. A subclone derived from one positive phage was sequenced and found to contain an 821-amino-acid open reading frame that encodes a protein with homology to protein kinases. We tested the activity of the putative kinase by constructing a vector encoding a glutathione-S-transferase fusion protein containing most of the predicted polypeptide. The fusion protein phosphorylated endogenous substrates and enolase primarily on serine and threonine. The gene was designated SPK1 for serine-protein kinase. Expression of the Spk1 fusion protein in bacteria stimulated serine, threonine, and tyrosine phosphorylation of bacterial proteins. These results, combined with the antiphosphotyrosine immunoreactivity induced by the kinase, indicate that Spk1 is capable of phosphorylating tyrosine as well as phosphorylating serine and threonine. In in vitro assays, the fusion protein kinase phosphorylated the synthetic substrate poly(Glu/Tyr) on tyrosine, but the activity was weak compared with serine and threonine phosphorylation of other substrates. To determine if other serine/threonine kinases would phosphorylate poly(Glu/Tyr), we tested calcium/calmodulin-dependent protein kinase II and the catalytic subunit of cyclic AMP-dependent protein kinase. The two kinases had similar tyrosine-phosphorylating activities. These results establish that the functional difference between serine/threonine- and tyrosine-protein kinases is not absolute and suggest that there may be physiological circumstances in which tyrosine phosphorylation is mediated by serine/threonine kinases.
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Stern, D. F., P. Zheng, D. R. Beidler, and C. Zerillo. "Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine." Molecular and Cellular Biology 11, no. 2 (February 1991): 987–1001. http://dx.doi.org/10.1128/mcb.11.2.987.

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A Saccharomyces cerevisiae lambda gt11 library was screened with antiphosphotyrosine antibodies in an attempt to identify a gene encoding a tyrosine kinase. A subclone derived from one positive phage was sequenced and found to contain an 821-amino-acid open reading frame that encodes a protein with homology to protein kinases. We tested the activity of the putative kinase by constructing a vector encoding a glutathione-S-transferase fusion protein containing most of the predicted polypeptide. The fusion protein phosphorylated endogenous substrates and enolase primarily on serine and threonine. The gene was designated SPK1 for serine-protein kinase. Expression of the Spk1 fusion protein in bacteria stimulated serine, threonine, and tyrosine phosphorylation of bacterial proteins. These results, combined with the antiphosphotyrosine immunoreactivity induced by the kinase, indicate that Spk1 is capable of phosphorylating tyrosine as well as phosphorylating serine and threonine. In in vitro assays, the fusion protein kinase phosphorylated the synthetic substrate poly(Glu/Tyr) on tyrosine, but the activity was weak compared with serine and threonine phosphorylation of other substrates. To determine if other serine/threonine kinases would phosphorylate poly(Glu/Tyr), we tested calcium/calmodulin-dependent protein kinase II and the catalytic subunit of cyclic AMP-dependent protein kinase. The two kinases had similar tyrosine-phosphorylating activities. These results establish that the functional difference between serine/threonine- and tyrosine-protein kinases is not absolute and suggest that there may be physiological circumstances in which tyrosine phosphorylation is mediated by serine/threonine kinases.
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Creeden, Justin F., Khaled Alganem, Ali S. Imami, F. Charles Brunicardi, Shi-He Liu, Rammohan Shukla, Tushar Tomar, Faris Naji, and Robert E. McCullumsmith. "Kinome Array Profiling of Patient-Derived Pancreatic Ductal Adenocarcinoma Identifies Differentially Active Protein Tyrosine Kinases." International Journal of Molecular Sciences 21, no. 22 (November 17, 2020): 8679. http://dx.doi.org/10.3390/ijms21228679.

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Pancreatic cancer remains one of the most difficult malignancies to treat. Minimal improvements in patient outcomes and persistently abysmal patient survival rates underscore the great need for new treatment strategies. Currently, there is intense interest in therapeutic strategies that target tyrosine protein kinases. Here, we employed kinome arrays and bioinformatic pipelines capable of identifying differentially active protein tyrosine kinases in different patient-derived pancreatic ductal adenocarcinoma (PDAC) cell lines and wild-type pancreatic tissue to investigate the unique kinomic networks of PDAC samples and posit novel target kinases for pancreatic cancer therapy. Consistent with previously described reports, the resultant peptide-based kinome array profiles identified increased protein tyrosine kinase activity in pancreatic cancer for the following kinases: epidermal growth factor receptor (EGFR), fms related receptor tyrosine kinase 4/vascular endothelial growth factor receptor 3 (FLT4/VEGFR-3), insulin receptor (INSR), ephrin receptor A2 (EPHA2), platelet derived growth factor receptor alpha (PDGFRA), SRC proto-oncogene kinase (SRC), and tyrosine kinase non receptor 2 (TNK2). Furthermore, this study identified increased activity for protein tyrosine kinases with limited prior evidence of differential activity in pancreatic cancer. These protein tyrosine kinases include B lymphoid kinase (BLK), Fyn-related kinase (FRK), Lck/Yes-related novel kinase (LYN), FYN proto-oncogene kinase (FYN), lymphocyte cell-specific kinase (LCK), tec protein kinase (TEC), hemopoietic cell kinase (HCK), ABL proto-oncogene 2 kinase (ABL2), discoidin domain receptor 1 kinase (DDR1), and ephrin receptor A8 kinase (EPHA8). Together, these results support the utility of peptide array kinomic analyses in the generation of potential candidate kinases for future pancreatic cancer therapeutic development.
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Tan, J. L., and J. A. Spudich. "Developmentally regulated protein-tyrosine kinase genes in Dictyostelium discoideum." Molecular and Cellular Biology 10, no. 7 (July 1990): 3578–83. http://dx.doi.org/10.1128/mcb.10.7.3578-3583.1990.

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Dictyostelium discoideum, an organism that undergoes development and that is amenable to biochemical and molecular genetic approaches, is an attractive model organism with which to study the role of tyrosine phosphorylation in cell-cell communication. We report the presence of protein-tyrosine kinase genes in D. discoideum. Screening of a Dictyostelium cDNA expression library with an anti-phosphotyrosine antibody identifies fusion proteins that exhibit protein-tyrosine kinase activity. Two distinct cDNAs were identified and isolated. Though highly homologous to protein kinases in general, these kinases do not exhibit many of the hallmarks of protein-tyrosine kinases of higher eucaryotes. In addition, these genes are developmentally regulated, which suggests a role for tyrosine phosphorylation in controlling Dictyostelium development.
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Dissertations / Theses on the topic "Tyrosine‐protein kinase (tyrosine kinase)"

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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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Holland, Pamela M. "Identification, interactions, and specificity of a novel MAP kinase kinase, MKK7 /." Thesis, Connect to this title online; UW restricted, 1999. http://hdl.handle.net/1773/9262.

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Bäckesjö, Carl-Magnus. "Molecular biology of Bruton's tyrosine kinase /." Stockholm, 2003. http://diss.kib.ki.se/2003/91-7349-693-6.

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Dikic, Inga. "Signal Transduction by Proline-Rich Tyrosine Kinase Pyk2." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Univ.-bibl. [distributör], 2002. http://publications.uu.se/theses/91-554-5316-3/.

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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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Hardwick, James S. "Regulation of the Lck tyrosine protein kinase by oxidant-induced tyrosine phosphorylation /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 1997. http://wwwlib.umi.com/cr/ucsd/fullcit?p9814544.

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Benjamin, Audra Ruth. "Lung liquid homeostasis : The involvement of protein kinase A and protein tyrosine kinase." Thesis, St George's, University of London, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.511892.

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Pursglove, Sharon Elizabeth. "Biophysical analysis of Tec Kinase regulatory regions : implications for the control of Kinase activity." Title page, contents and summary only, 2001. http://web4.library.adelaide.edu.au/theses/09PH/09php9863.pdf.

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Collins-De, Peyer Laurence. "Screening of a rat thymus and a human hippocampus cDNA library for a novel fyn-related oncogene." Thesis, Hong Kong : University of Hong Kong, 1999. http://sunzi.lib.hku.hk/hkuto/record.jsp?B21253870.

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Griaud, François. "Proteomic analysis of leukaemogenic protein tyrosine kinase action." Thesis, University of Manchester, 2012. https://www.research.manchester.ac.uk/portal/en/theses/proteomic-analysis-of-leukaemogenic-protein-tyrosine-kinase-action(ff9d490b-5a94-45fc-a857-4f0826e4a11a).html.

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Introduction: Chronic myeloid leukaemia is a blood cancer which progresses from a chronic phase to an acute blast crisis if untreated. Disease progression and treatment resistance may be precipitated by the mutator action of BCR/ABL protein tyrosine kinase (PTK), but only few protein phosphosites involved in the DNA damage response have been investigated with respect to BCR/ABL action. Aim: The aim of this PhD project was to demonstrate that BCR/ABL PTK expression can affect the response to genotoxic stress signalling at the protein phosphorylation level. Methodology: Etoposide-induced DNA damage response has been studied in control and BCR/ABL PTK-expressing Ba/F3 cells using apoptosis and γH2AX assays. Quantitative phosphoproteomics was performed with iTRAQ peptide labelling to discover putative modulated phosphorylation sites. Absolute quantification (AQUA ) performed with selected reaction monitoring was used to validate discovery phosphoproteomics. The effect of genotoxic stress on the THO complex protein Thoc5/Fmip was studied using western blots. Results: The expression of BCR/ABL PTK induced γH2AX phosphorylation after etoposide exposure. This was associated with the modulation of H2AX tyrosine 142 phosphorylation, MDC1 (serines 595 and 1053) and Hemogen serine 380 phosphorylation among proteins regulated by both BCR/ABL PTK and etoposide. We identified that leukaemogenic PTKs mediate Thoc5/Fmip phosphorylation on tyrosine 225 via Src proto-oncogene and oxidative stress, while ATM and MEK1/2 may control its phosphorylation. Human CD34+ CD38- leukaemic stem cells showed pronounced level of THOC5/FMIP tyrosine phosphorylation. Expression of phosphomutant Thoc5/Fmip Y225F might reduce apoptosis mediated by etoposide and H2O2. Conclusion: BCR/ABL PTK can sustain, create, block and change the intensity of protein phosphorylation related to genotoxic stress. Modulation of H2AX, MDC1, Hemogen and Thoc5/Fmip post-translational modifications by BCR/ABL PTK might promote unfaithful DNA repair, genomic instability, anti-apoptotic signalling or abnormal cell differentiation, resulting in leukaemia progression.
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Books on the topic "Tyrosine‐protein kinase (tyrosine kinase)"

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

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Kellie, Stuart. Tyrosine kinases and neoplastic transformation. Austin: R.G. Landes, 1994.

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Germano, Serena. Receptor tyrosine kinases: Methods and protocols. New York: Humana Press, 2015.

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Easterfield, Howard James. Analogues of phosphotyrosine: New components of ligands for protein tyrosine kinase enzymes. Birmingham: University of Birmingham, 1999.

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Danielian, Sylvia. Protéines tyrosine kinases et signalisation cellulaire: Le modèle des lymphocytes T. Paris: Editions INSERM, 1993.

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Schmidt, Holger. NMR-Lösungsstruktur der humanen Hck SH3-Domäne im Komplex mit einem artifiziellen, hochoffinen Peptid-Liganden. Jülich: Forschungszentrum Jülich, Zentralbibliothek, 2006.

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Phosphoinositide 3-kinase in health and disease. Heidelberg: Springer Verlag, 2010.

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Tran, Thi Tuyen. Analyse der Bindungsspezifität der humanen Lck-SH3-Domäne anhand artifizieller und physiologischer Peptid-Liganden und strukturelle Charakterisierung dieser Peptide im Komplex mit SH3-Domänen. Jülich: Forschungszentrum Jülich, Zentralbibliothek, 2005.

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Rommel, Christian. Phosphoinositide 3-kinase in Health and Disease: Volume 2. Berlin, Heidelberg: Springer-Verlag Berlin Heidelberg, 2011.

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Matthews, David J. Targeting protein kinases for cancer therapy. Hoboken, N.J: John Wiley & Sons, 2009.

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Book chapters on the topic "Tyrosine‐protein kinase (tyrosine kinase)"

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Finan, Peter M., and Stephen G. Ward. "PI3-Kinase Inhibition." In Protein Tyrosine Kinases, 53–69. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:053.

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Schomburg, Dietmar, and Dörte Stephan. "Protein-tyrosine kinase." In Enzyme Handbook, 39–46. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59025-2_7.

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Scheijen, Blanca, and James D. Griffin. "Activated FLT3 Receptor Tyrosine Kinase as a Therapeutic Target In Leukemia." In Protein Tyrosine Kinases, 93–113. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:093.

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Harvey, Amanda. "Protein Tyrosine Kinase-6 (PTK6)." In Encyclopedia of Signaling Molecules, 4238–44. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_305.

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Harvey, Amanda. "Protein Tyrosine Kinase-6 (PTK6)." In Encyclopedia of Signaling Molecules, 1–7. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_305-1.

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Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "Protein Tyrosine Kinase-6 (PTK6)." In Encyclopedia of Signaling Molecules, 1483–88. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_305.

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Nelson, Robert P. "Lymphocyte-Specific Protein Tyrosine Kinase: LCK." In Encyclopedia of Medical Immunology, 438–41. New York, NY: Springer New York, 2020. http://dx.doi.org/10.1007/978-1-4614-8678-7_103.

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Nelson, R. P. "Lymphocyte-Specific Protein Tyrosine Kinase: LCK." In Encyclopedia of Medical Immunology, 1–3. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4614-9209-2_103-1.

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Lawan, Ahmed, and Anton M. Bennett. "Mitogen-Activated Protein Kinase Phosphatases in Metabolism." In Protein Tyrosine Phosphatase Control of Metabolism, 221–38. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-7855-3_12.

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Brossier, Nicole M., Stephanie J. Byer, Lafe T. Peavler, and Steven L. Carroll. "ErbB Membrane Tyrosine Kinase Receptors: Analyzing Migration in a Highly Complex Signaling System." In Protein Kinase Technologies, 105–31. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-824-5_7.

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Conference papers on the topic "Tyrosine‐protein kinase (tyrosine kinase)"

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Chen, Yu. "Progress in research on protein tyrosine kinase inhibitors." In INTERNATIONAL CONFERENCE ON FRONTIERS OF BIOLOGICAL SCIENCES AND ENGINEERING (FBSE 2018). Author(s), 2019. http://dx.doi.org/10.1063/1.5085519.

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Shoni, Melina, Jinyan Du, Junzheng Yang, Shu-Kay Ng, Michael George Muto, William Welch, Christopher Crum, Ross Berkowitz, Todd Golub, and Shu-Wing Ng. "Abstract 1271: Aberrant activation of Spleen Tyrosine Kinase in ovarian cancer identified through a global phosphorylation profiling of protein tyrosine 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.am2012-1271.

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Grotterød, Ida, Kjetil Boye, and Gunhild Mari Mælandsmo. "Abstract 5321: Tyrosine kinase activation by the metastasis promoting protein S100A4." 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.am2012-5321.

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Ahn, Joseph, Peter Truesdell, Alexander H. Boag, and Andrew W. B. Craig. "Abstract 462: Fer protein-tyrosine kinase promotes lung tumor progression and metastases." 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.am2012-462.

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Alotaibi, Faizah Mesfer, Connie Zhang, Sam Basta, and Peter A. Greer. "Abstract B05: An immune modulatory role for the Fes protein tyrosine kinase." In Abstracts: AACR Special Conference: Tumor Angiogenesis and Vascular Normalization: Bench to Bedside to Biomarkers; March 5-8, 2015; Orlando, FL. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-8514.tumang15-b05.

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French, Pim, Ya Gao, Maurice de Wit, Darlene Mercieca, Iris de Heer, Bart Valkenburg, Martin van Royen, Joachim Aerts, and Peter Sillevis Smitt. "Abstract 2071: Protein aggregate formation predicts clinical responses to EGFR tyrosine kinase inhibitors." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-2071.

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Aubele, M., AK Walch, H. Braselmann, N. Ludyga, MJ Atkinson, B. Luber, G. Auer, and JM Bartlett. "Protein tyrosine kinase 6 (PTK6): a new/potential therapy target in breast cancer?." In CTRC-AACR San Antonio Breast Cancer Symposium: 2008 Abstracts. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-3073.

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French, Pim, Ya Gao, Maurice de Wit, Darlene Mercieca, Iris de Heer, Bart Valkenburg, Martin van Royen, Joachim Aerts, and Peter Sillevis Smitt. "Abstract 2071: Protein aggregate formation predicts clinical responses to EGFR tyrosine kinase inhibitors." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-2071.

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Bijli, Kaiser M., Fabeha Fazal, Mohammad Minhajuddin, and Arshad Rahman. "Protein Tyrosine Kinase Syk Regulates ICAM-1 Expression And PMN Sequestration In Mouse Lungs." 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.a2671.

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Mathur, Priya S., Jessica J. Gierut, Rosa M. Xicola, Xavier Llor, and Angela L. Tyner. "Abstract LB-059: Opposing roles for protein tyrosine kinase 6 (PTK6) in colon cancer." 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-lb-059.

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Reports on the topic "Tyrosine‐protein kinase (tyrosine kinase)"

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Perrimon, Norbert. Regulation of ErbB Receptor Tyrosine Kinase Activities in Breast Cancer by the Kek Proteins. Fort Belvoir, VA: Defense Technical Information Center, October 2001. http://dx.doi.org/10.21236/ada398163.

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Perrimon, Norbert M. Regulation of ErbB Receptor Tyrosine Kinase Activities in Breast Cancer by the Kek Proteins. Fort Belvoir, VA: Defense Technical Information Center, October 2000. http://dx.doi.org/10.21236/ada392883.

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Weier, Heinz-Ulrich. Expression Profiling of Tyrosine Kinase Genes. Fort Belvoir, VA: Defense Technical Information Center, August 2003. http://dx.doi.org/10.21236/ada423672.

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Weier, Heinz U. Expression Profiling of Tyrosine Kinase Genes. Fort Belvoir, VA: Defense Technical Information Center, August 2000. http://dx.doi.org/10.21236/ada391061.

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Miller, Tod. Peptide-Bassed Inhibitors of Neu Tyrosine Kinase. Fort Belvoir, VA: Defense Technical Information Center, June 1999. http://dx.doi.org/10.21236/ada375133.

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Miller, W. T. Peptide-Based Inhibitors of Neu Tyrosine Kinase. Fort Belvoir, VA: Defense Technical Information Center, December 2000. http://dx.doi.org/10.21236/ada392289.

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Riese, David J. Functional Analysis of the ErbB4 Receptor Tyrosine Kinase. Fort Belvoir, VA: Defense Technical Information Center, July 2001. http://dx.doi.org/10.21236/ada396642.

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Riese, David J. Functional Analysis of the ErbB4 Receptor Tyrosine Kinase. Fort Belvoir, VA: Defense Technical Information Center, July 2001. http://dx.doi.org/10.21236/ada396717.

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Riese II, David J. Functional Analysis of the ErbB4 Receptor Tyrosine Kinase. Fort Belvoir, VA: Defense Technical Information Center, July 2002. http://dx.doi.org/10.21236/ada410069.

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Tyner, Angela. A Novel Tyrosine Kinase Expressed in Breast Tumors. Fort Belvoir, VA: Defense Technical Information Center, September 1997. http://dx.doi.org/10.21236/ada334915.

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