Bibliographies thématiques / Protein-tyrosine kinase

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Littérature scientifique sur le sujet « Protein-tyrosine kinase »

Auteur : Grafiati
Publié le 4 juin 2021
Mis à jour le 3 mars 2023

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Articles de revues sur le sujet "Protein-tyrosine kinase"

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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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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
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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
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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 res
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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 net
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Boutin, Jean A. "Tyrosine protein kinase assays." Journal of Chromatography B: Biomedical Sciences and Applications 684, no. 1-2 (September 1996): 179–99. http://dx.doi.org/10.1016/0378-4347(95)00563-3.

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Laneuville, P. "Abl tyrosine protein kinase." Seminars in Immunology 7, no. 4 (August 1995): 255–66. http://dx.doi.org/10.1006/smim.1995.0030.

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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.
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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.
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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 presen
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Thèses sur le sujet "Protein-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<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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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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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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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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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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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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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 dam
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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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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.

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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.

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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
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Livres sur le sujet "Protein-tyrosine kinase"

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

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D, Fabbro, and McCormick Frank 1950-, eds. Protein tyrosine kinases: From inhibitors to useful drugs. Totowa, N.J: Humana Press, 2006.

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

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

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

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Heilmeyer, L. M. G. 1937- and NATO Advanced Study Institute on Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling (1992 : Acquafredda di Maratea, Italy), eds. Tyrosine phosphorylation/dephosphorylation and downstream signalling. Berlin: Springer-Verlag, 1993.

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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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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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Chapitres de livres sur le sujet "Protein-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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Kidger, Andrew M., and Stephen M. Keyse. "Dual-Specificity Map Kinase (MAPK) Phosphatases (MKPs) and Their Involvement in Cancer." In 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.

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Actes de conférences sur le sujet "Protein-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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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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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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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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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, September 1998. http://dx.doi.org/10.21236/ada360940.

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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, September 1997. http://dx.doi.org/10.21236/ada338938.

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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, March 2019. http://dx.doi.org/10.31487/j.cor.2019.01.102.

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