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Dailey, D., G. L. Schieven, M. Y. Lim, H. Marquardt, T. Gilmore, J. Thorner et 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 (décembre 1990) : 6244–56. http://dx.doi.org/10.1128/mcb.10.12.6244-6256.1990.
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 et 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 (décembre 1990) : 6244–56. http://dx.doi.org/10.1128/mcb.10.12.6244.
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 et J. Kuret. « Budding and fission yeast casein kinase I isoforms have dual-specificity protein kinase activity. » Molecular Biology of the Cell 5, no 8 (août 1994) : 877–86. http://dx.doi.org/10.1091/mbc.5.8.877.
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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Creeden, Justin F., Khaled Alganem, Ali S. Imami, F. Charles Brunicardi, Shi-He Liu, Rammohan Shukla, Tushar Tomar, Faris Naji et 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 (17 novembre 2020) : 8679. http://dx.doi.org/10.3390/ijms21228679.
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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Boutin, Jean A. « Tyrosine protein kinase assays ». Journal of Chromatography B : Biomedical Sciences and Applications 684, no 1-2 (septembre 1996) : 179–99. http://dx.doi.org/10.1016/0378-4347(95)00563-3.
Stern, D. F., P. Zheng, D. R. Beidler et C. Zerillo. « Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine ». Molecular and Cellular Biology 11, no 2 (février 1991) : 987–1001. http://dx.doi.org/10.1128/mcb.11.2.987-1001.1991.
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 et C. Zerillo. « Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine. » Molecular and Cellular Biology 11, no 2 (février 1991) : 987–1001. http://dx.doi.org/10.1128/mcb.11.2.987.
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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Trojanek, Joanna B., Maria M. Klimecka, Anna Fraser, Grazyna Dobrowolska et Grazyna Muszyńska. « Characterization of dual specificity protein kinase from maize seedlings. » Acta Biochimica Polonica 51, no 3 (30 septembre 2004) : 635–47. http://dx.doi.org/10.18388/abp.2004_3549.
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.
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.
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.
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.
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.
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.
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.
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.
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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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.
O'Brien, Richard Mark. « Studies on the insulin receptor tyrosine-specific protein kinase ». Thesis, University of Cambridge, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.252645.
Che, Azmi Norhaida. « Functional proteomic analysis of leukaemogenic protein tyrosine kinase targets ». Thesis, University of Manchester, 2015. https://www.research.manchester.ac.uk/portal/en/theses/functional-proteomic-analysis-of-leukaemogenic-protein-tyrosine-kinase-targets(a6dc9816-886b-495f-a6e1-f00aec05382f).html.
Myeloproliferative neoplasms (MPNs) are clonal proliferative disorders associated with JAK2 mutation (e.g JAK2 K539L, JAK2 V617F), MPL mutation (e.g MPL W515L) or product from reciprocal chromosomal translocations in many cases (e.g BCR/ABL). The mutated thrombopoietin receptor MPL W515L found in thrombocytosis and myelofibrosis is constitutively activated leading to a downstream signal transduction cascade activation including the JAK-STAT signalling pathway. MPL W515L induced JAK2 mutation is associated with polycythaemia vera. Using quantitative proteomics I have investigated the effects of the MPL W515L oncogene on the proteome. This was performed to delineate specific features of MPL W515L action with a view to identifying new therapeutic targets for MPN patients. Within the proteins identified as being differentially expressed as a consequence of MPL W515L expression I observed an enrichment of proteins involved in motility. This was associated with a MPL W515L induced increase in chemokinesis. Further investigation into this altered chemokinesis elucidated a pathway from CXCL12/CXCR4/CD45 mediated Src activation through to THOC5 Y225 phosphorylation that had been compromised by MPL W515L. The MPL W515L induced THOC5 phosphorylation was linked to elevated MYC expression. Either chemical inhibition of MYC or gene silencing reduced both the level of THOC5 Y225 phosphorylation and also the increased chemokinesis. Of interest, because of its reported role in both myelofibrosis and motility, the MPL W515L expressing cells were found to demonstrate increased release of transforming growth factor beta (TGFβ). I demonstrated that TGFβ stimulates the phosphorylation of THOC5. Via the expression of Y225F mutants of THOC5 and the chemical inhibition of TGFβ I show a role for this elevated TGFβ in the increased chemokinesis of MPL W515L expressing cells. TGFβ has been reported to upregulate sphingosine-1-phosphate (S1P) which contributes to fibrosis. Having previously published on the differential effects of S1P on the motility of HSC populations I investigated the potential role of S1P in the MPL W515L induced chemokinesis. Inhibition of sphingosine kinase reduced the increase in chemokinesis and THOC5 Y225 phosphorylation in MPL W515L expressing cells. Furthermore I demonstrated that MPL W515L expression led to an increase in the intracellular levels of S1P suggesting a role for S1P in MPN. To further understand the role of THOC5 phosphorylation in the increased chemokinesis I undertook a discovery proteomics screen of MPL W515L cells co-expressing either wild type or Y225F mutant THOC5. Enhancer zester homolog 2 (EZH2) was shown to increase in MPL W515L as compared to MPL W515L mutant THOC5 Y225F expressing and control cells and as such may be linked to the increases in chemokinesis observed. Present work is aimed at clarifying the role of EZH2 in chemokinesis. In conclusion I have identified a novel pathway disrupted in MPN and allow me to start to understand the mechanisms by which the phosphorylation of THOC5 may contribute to leukaemogenic transformation through links to TGFβ, MYC, and S1P biology.
Schmidt, Holger. NMR-Lösungsstruktur der humanen Hck SH3-Domäne im Komplex mit einem artifiziellen, hochoffinen Peptid-Liganden. Jülich : Forschungszentrum Jülich, Zentralbibliothek, 2006.
Easterfield, Howard James. Analogues of phosphotyrosine : New components of ligands for protein tyrosine kinase enzymes. Birmingham : University of Birmingham, 1999.
Heilmeyer, L. M. G. 1937- et NATO Advanced Study Institute on Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling (1992 : Acquafredda di Maratea, Italy), dir. Tyrosine phosphorylation/dephosphorylation and downstream signalling. Berlin : Springer-Verlag, 1993.
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.
Chapitres de livres sur le sujet "Protein-tyrosine kinase":
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Finan, Peter M., et Stephen G. Ward. « PI3-Kinase Inhibition ». Dans Protein Tyrosine Kinases, 53–69. Totowa, NJ : Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:053.
Scheijen, Blanca, et James D. Griffin. « Activated FLT3 Receptor Tyrosine Kinase as a Therapeutic Target In Leukemia ». Dans Protein Tyrosine Kinases, 93–113. Totowa, NJ : Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:093.
Harvey, Amanda. « Protein Tyrosine Kinase-6 (PTK6) ». Dans 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.
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) ». Dans 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.
Nelson, Robert P. « Lymphocyte-Specific Protein Tyrosine Kinase : LCK ». Dans 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.
Nelson, R. P. « Lymphocyte-Specific Protein Tyrosine Kinase : LCK ». Dans 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.
Lawan, Ahmed, et Anton M. Bennett. « Mitogen-Activated Protein Kinase Phosphatases in Metabolism ». Dans 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.
Kidger, Andrew M., et Stephen M. Keyse. « Dual-Specificity Map Kinase (MAPK) Phosphatases (MKPs) and Their Involvement in Cancer ». Dans Protein Tyrosine Phosphatases in Cancer, 201–31. New York, NY : Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3649-6_7.
Actes de conférences sur le sujet "Protein-tyrosine kinase":
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Chen, Yu. « Progress in research on protein tyrosine kinase inhibitors ». Dans INTERNATIONAL CONFERENCE ON FRONTIERS OF BIOLOGICAL SCIENCES AND ENGINEERING (FBSE 2018). Author(s), 2019. http://dx.doi.org/10.1063/1.5085519.
Grotterød, Ida, Kjetil Boye et Gunhild Mari Mælandsmo. « Abstract 5321 : Tyrosine kinase activation by the metastasis promoting protein S100A4 ». Dans 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.
Shoni, Melina, Jinyan Du, Junzheng Yang, Shu-Kay Ng, Michael George Muto, William Welch, Christopher Crum, Ross Berkowitz, Todd Golub et Shu-Wing Ng. « Abstract 1271 : Aberrant activation of Spleen Tyrosine Kinase in ovarian cancer identified through a global phosphorylation profiling of protein tyrosine kinases ». Dans 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.
Ahn, Joseph, Peter Truesdell, Alexander H. Boag et Andrew W. B. Craig. « Abstract 462 : Fer protein-tyrosine kinase promotes lung tumor progression and metastases ». Dans 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.
Alotaibi, Faizah Mesfer, Connie Zhang, Sam Basta et Peter A. Greer. « Abstract B05 : An immune modulatory role for the Fes protein tyrosine kinase ». Dans 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.
French, Pim, Ya Gao, Maurice de Wit, Darlene Mercieca, Iris de Heer, Bart Valkenburg, Martin van Royen, Joachim Aerts et Peter Sillevis Smitt. « Abstract 2071 : Protein aggregate formation predicts clinical responses to EGFR tyrosine kinase inhibitors ». Dans 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.
Aubele, M., AK Walch, H. Braselmann, N. Ludyga, MJ Atkinson, B. Luber, G. Auer et JM Bartlett. « Protein tyrosine kinase 6 (PTK6) : a new/potential therapy target in breast cancer?. » Dans 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.
French, Pim, Ya Gao, Maurice de Wit, Darlene Mercieca, Iris de Heer, Bart Valkenburg, Martin van Royen, Joachim Aerts et Peter Sillevis Smitt. « Abstract 2071 : Protein aggregate formation predicts clinical responses to EGFR tyrosine kinase inhibitors ». Dans 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.
Bijli, Kaiser M., Fabeha Fazal, Mohammad Minhajuddin et Arshad Rahman. « Protein Tyrosine Kinase Syk Regulates ICAM-1 Expression And PMN Sequestration In Mouse Lungs ». Dans 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.
Mathur, Priya S., Jessica J. Gierut, Rosa M. Xicola, Xavier Llor et Angela L. Tyner. « Abstract LB-059 : Opposing roles for protein tyrosine kinase 6 (PTK6) in colon cancer ». Dans 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.
Rapports d'organisations sur le sujet "Protein-tyrosine kinase":
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Edelman, Arthur. Study of Inhibitors of Neu and Related Tyrosine-Specific Protein Kinases : Implications for the Treatment of Breast Cancer. Fort Belvoir, VA : Defense Technical Information Center, septembre 1998. http://dx.doi.org/10.21236/ada360940.
Edelman, Arthur. Study of Inhibitors of Neu and Related Tyrosine-Specific Protein Kinases : Implications for the Treatment of Breast Cancer. Fort Belvoir, VA : Defense Technical Information Center, septembre 1997. http://dx.doi.org/10.21236/ada338938.
Roy, Madhumita. Black Tea Extract prevents 4-nitroquinoline 1-oxide induced oral tumorigenesis in mice by targeting Protein Tyrosine Kinases and associated biological response. Science Repository OÜ, mars 2019. http://dx.doi.org/10.31487/j.cor.2019.01.102.
