Relevant bibliographies by topics / Protein-tyrosine kinases

Academic literature on the topic 'Protein-tyrosine kinases'

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Published: 4 June 2021
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Journal articles on the topic "Protein-tyrosine 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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Hunter, T., and J. A. Cooper. "Protein-Tyrosine Kinases." Annual Review of Biochemistry 54, no. 1 (June 1985): 897–930. http://dx.doi.org/10.1146/annurev.bi.54.070185.004341.

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Mahajan, S., J. Fargnoli, A. L. Burkhardt, S. A. Kut, S. J. Saouaf, and J. B. Bolen. "Src family protein tyrosine kinases induce autoactivation of Bruton's tyrosine kinase." Molecular and Cellular Biology 15, no. 10 (October 1995): 5304–11. http://dx.doi.org/10.1128/mcb.15.10.5304.

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Bruton's tyrosine kinase (Btk) is tyrosine phosphorylated and enzymatically activated following ligation of the B-cell antigen receptor. These events are temporally regulated, and Btk activation follows that of various members of the Src family of protein tyrosine kinases, thus raising the possibility that Src kinases participate in the Btk activation process. We have evaluated the mechanism underlying Btk enzyme activation and have explored the potential regulatory relationship between Btk and Src protein kinases. We demonstrate in COS transient-expression assays that Btk can be activated through intramolecular autophosphorylation at tyrosine 551 and that Btk autophosphorylation is required for Btk catalytic functions. Coexpression of Btk with members of the Src family of protein tyrosine kinases, but not Syk, led to Btk tyrosine phosphorylation and activation. Using a series of point mutations in Blk (a representative Src protein kinase) and Btk, we show that Src kinases activate Btk through an indirect mechanism that requires membrane association of the Src enzymes as well as functional Btk SH3 and SH2 domains. Our results are compatible with the idea that Src protein tyrosine kinases contribute to Btk activation by indirectly stimulating Btk intramolecular autophosphorylation.
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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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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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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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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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Shi, Lei, Ahasanul Kobir, Carsten Jers, and Ivan Mijakovic. "Bacterial Protein-Tyrosine Kinases." Current Proteomics 7, no. 3 (October 1, 2010): 188–94. http://dx.doi.org/10.2174/157016410792928198.

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Dissertations / Theses on the topic "Protein-tyrosine kinases"

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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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Wan, Yong. "Role of tyrosine kinases in G-protein signaling /." Access full-text from WCMC, 1997. http://proquest.umi.com/pqdweb?did=733008261&sid=12&Fmt=2&clientId=8424&RQT=309&VName=PQD.

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Gruszczyk, Jakub. "Structural analysis of bacterial protein tyrosine kinases (by-kinases) and their substrates." Paris 11, 2010. http://www.theses.fr/2010PA112135.

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Des tyrosine-kinases bactériennes atypiques (appelées BY-kinases) ont été identifiées comme constituant d'un complexe multiprotéique transmembranaire responsable de la synthèse et l'export des polysaccharides de la capsule bactérienne. Les BY-kinases s'autophosphorylent sur un cluster de tyrosine C-terminal et phosphorylent des protéines endogènes de la bactérie comme des UDP-sucres déshydrogénases impliquées dans la synthèse des précurseurs des exopolysaccharides. Les données structurales et fonctionnelles disponibles posaient la question de la conservation du degré d'oligomérisation et du mécanisme d'autophosphorylation entre BY-kinases de firmicutes et de protéobactéries. J'ai donc résolu la structure cristalline du domaine cytoplasmique de la BY-kinase Wzc de la protéobactérie E. Coli. Cette nouvelle structure montre que, comme la BY-kinase CapAB du firmicute S. Aureus, Wzc forme un anneau octamérique expliquant le mécanisme d'autophosphorylation intermoléculaire. Des mesures d'affinité par fluorimétrie m'ont également permis de montrer qu'une tyrosine interne Y569, initialement supposée réguler la trans-autophosphorylation du tyrosine-cluster, est directement impliquée dans la fixation du nucléotide. Nous montrons également qu'une boucle flexible riche en résidus basiques joue un rôle essentiel dans la synthèse de la capsule, probablement en interagissant avec d'autres protéines impliquées dans ce processus. De plus, j'ai résolu la structure cristalline de l'UDP-N-acétylmannosamine déshydrogenase CapO, substrat de la BY-kinase CapAB de S. Aureus. Cette structure révèle la formation d'un pont disulfure entre la cystéine catalytique C258 et le résidu C92 et la présence de potentiels sites de phosphorylation, Y89 et Y264, à proximité de ces deux cystéines. L'analyse de mutants est en cours afin d'élucider le mécanisme de régulation de cette enzyme. La comparaison avec les structures d'autres membres de cette famille de déshydrogénases permet également de mieux comprendre leur spécificité de substrat
Atypical bacterial tyrosine kinases (BY-kinases) have been identified as part of a multiprotein transmembrane complex responsible of the biosynthesis and export of capsular polysaccharides. BY-kinases autophosphorylate on a C-terminal tyrosine cluster and phosphorylate endogenous bacterial proteins like UDP-sugar dehydrogenases involved in the synthesis of exopolysaccharide precursors. Available structural and functional data raised the question of the conservation of the oligomerization state and of the autophosphorylation mechanism between BY-kinases from proteobacteria and firmicutes. I thus solved the crystal structure of the cytoplasmic domain of the BY-kinase Wzc from E. Coli. This new structure shows that, like the BY-kinase CapAB from the firmicute S. Aureus, Wzc forms an octameric ring explaining the intermolecular autophosphorylation mechanism. Fluorimetric affinity measurements further allowed me to show that the internal tyrosine Y569, initially supposed to regulate tyrosine-cluster trans-autophosphorylation, is directly involved in nucleotide binding. We also show that a flexible loop rich in basic residues plays an essential role in capsule synthesis, most probably through interaction with other proteins involved in this process. Moreover, I solved the crystal structure of UDP-N-acetylmannosamine dehydrogenase CapO, the substrate of the BY-kinases CapAB from S. Aureus. The structure reveals the formation of a disulfide bridge between the catalytic cysteine C258 and residue C92 and the presence of potential phosphorylation sites, Y89 and Y264, close to these two cysteines. Mutational analysis is underway in order to elucidate the regulatory mechanism of this enzyme. Comparison with the structures of other members of this family of dehydrogenases also allows us to shed light on their specific substrate recognition
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Vearing, Christopher John, and chris vearing@med monash edu au. "Structure, function & control of the EphA3 receptor tyrosine kinase." Swinburne University of Technology, 2005. http://adt.lib.swin.edu.au./public/adt-VSWT20051017.094940.

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The implication of the transmembrane signalling Receptor Tyrosine Kinases (RTKs) in cancer has accelerated the pursuit for drugs to target these molecules. In the process our understanding of how these membrane bound molecules are entangled in cell signalling has significantly expanded. There is now evidence that RTKs can facilitate the formation of a lattice-type network of signalling molecules to elicit whole cell responses to external ligand stimuli. Although beginning to be unravelled, knowledge pertaining to the mechanisms of molecular control that initiate these signalling pathways is still in its infancy. In this thesis, a random mutagenesis approach allowed the identification of the crucial interaction surfaces between membrane-bound EphA3 and its preferential binding partner ephrinA5, that are required to induce the formation of higher-order Eph signalling complexes. Modelling and experimental dissection of this co-ordinated receptor aggregation has provided detailed insights into the molecular mechanisms of Eph receptor activation, which in some aspects may also apply to other members of the RTK family. In particular, the importance of certain molecular interfaces in determining preferential and non-preferential Eph/ephrin interactions, suggests their role in the selection of biologically important binding partners. In addition to the assignment of the ephrin-interaction surfaces, the random mutagenesis strategy also identified a continuous conformational epitope as binding site for an anti-EphA3 monoclonal antibody. Fortuitously, antibody binding to this site functionally mimics ephrin stimulation of EphA3 positive cells, and in particular together with divalent ephrinA5, yields synergistically enhanced EphA3 activation. Elucidation of the underlying mechanism has provided opportunities to develop an efficient EphA3 targeting mechanism that is based on increased affinity and accelerated ephrinA5 uptake as consequence of this unique activation mechanism. On a genetic level, novel oligonucleotide analogues known as Peptide Nucleic Acids (PNAs) were analysed for their ability to sterically inhibit EphA3 DNA transcription and suggest a dosedependent downregulation of EphA3 expression, in malignant melanoma cells. Combined, ephrinA5, the anti-EphA3 MAb (IIIA4) and PNA, offer the possibility to investigate the specific machinery involved in Eph receptor expression and signalling for the specific targeting of EphA3 expressing tumour cells.
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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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Persson, Camilla. "Protein Tyrosine Phosphatases as Regulators of Receptor Ryrosine Kinases." Doctoral thesis, Uppsala University, Ludwig Institute for Cancer Research, 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3345.

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Tyrosine phosphorylation is a crucial mechanism in cellular signaling and regulates proliferation, differentiation, migration and adhesion. The phosphorylation reaction is reversible and is governed by two families of enzymes: protein tyrosine kinases and protein tyrosine phosphatases (PTPs). This thesis investigates the role of PTPs in regulating receptor protein tyrosine kinases (RTKs), and explores a mechanism for regulation of phosphatase activity.

Most receptor tyrosine kinases are activated by ligand induced dimerization, which results in an increase in receptor phosphorylation. Preparations of ligand-stimulated dimeric PDGF β-receptors were shown to be less susceptible to dephosphorylation compared with unstimulated receptors. This revealed that reduced receptor dephosphorylation contributes to ligand-induced increase in RTK phosphorylation.

The receptor-like phosphatase DEP-1 site-selectively dephosphorylates the PDGF β-receptor. One of the most preferred sites is the PLC-γ binding phosphotyrosine pY1021, and the autoregulatory pY857 is one of the least preferred sites. By using chimeric phospho-peptides derived from these two sites as substrate for DEP-1, it was shown that a lysine residue at position +3 acts as a negative determinant for DEP-1 and that an aspartic acid residue at position –1 is a positive determinant.

The modulatory effect of TC-PTP on PDGF β-receptor signaling was explored by using mouse embryonic fibroblasts derived from TC-PTP knockout mice. PDGF β-receptors derived from knockout cells exhibited a higher level of ligand-induced phosphorylation compared to receptors from wildtype cells. The increase was unevenly distributed between different autophosphorylation sites. The PLC-γ binding site, previously implicated in chemotactic response, displayed the largest increase. Consistently, a cell migration assay revealed hyper-responsiveness to PDGF of TC-PTP knockout cells as compared to wildtype cells.

Reversible oxidation of the active site cysteine in PTPs is a mechanism, which have been postulated to regulate phosphatase specific activity. An antibody-based generic method for detection of oxidized PTPs was developed. Using this method it was revealed for the first time that UV-induced inactivation of PTPs involves oxidation of the active site cysteine.

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Kee, Nohjin. "Receptor protein tyrosine kinases in perinatal developing rat kidney." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape11/PQDD_0007/MQ44193.pdf.

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Kee, Nohjin. "Receptor protein tyrosine kinases in perinatal developing rat kidney." Thesis, McGill University, 1996. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=20260.

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We have identified receptor protein tyrosine kinases (PTKs) that are expressed and/or activated during kidney development. mRNA from fetal rat kidneys in late gestation (embryonic day 21), was used to prepare cDNA template for polymerase chain reaction amplification with primers based on conserved regions of PTKs, and products were subcloned and sequenced. Among 346 clones, we identified epidermal growth factor receptor (EGFr), Tie 2, platelet derived growth factor receptor (PDGFr)-alpha, PDGFr-beta, Flk-1, Flt-4, fibroblast growth factor receptor (FGFr)-1, FGFr-3, FGFr-4, Met, and RYK//Nbtk-1. PTK expression was studied by immunoprecipitation and immunoblotting of kidney membrane proteins with specific antibodies. EGFr, PDGFr-alpha, FGFr-1, FGFr-3, Met, and in some cases Tie-2 protein expression was greater in fetal kidneys, as compared with kidneys from 12 week adult rats, (controls). Flk-1, PDGFr-beta, and FGFr-4 proteins were expressed comparably; Flt-4 was not detected. As a reflection of receptor PTK activity, we assessed endogenous tyrosine phosphorylation, and in vitro autophosphorylation. EGFr and PDGFr-alpha displayed activity in fetal, but not adult kidneys. FGFr-3 and Flk-1 were active in some fetal kidneys; the other PTKs were not active. Thus, in late gestational rat kidney, there are distinct patterns of receptor PTK expression and activity. EGFr, PDGFr-alpha, FGFr-3 and Flk-1 are among PTKs that are activated, and they may mediate perinatal development of renal epithelial, interstitial, or vascular structures.
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Munawar, Munawar Ali. "The synthesis of novel inhibitors of protein tyrosine kinases." Thesis, Cardiff University, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.364476.

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Books on the topic "Protein-tyrosine kinases"

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Fabbro, Doriano, and Frank McCormick, eds. Protein Tyrosine Kinases. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1592599621.

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Mustelin, Tomas. Src family tyrosine kinases in leukocytes. 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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Kellie, Stuart. Tyrosine kinases and neoplastic transformation. 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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Bence, Kendra K. Protein tyrosine phosphatase control of metabolism. New York: Springer, 2013.

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Cunningham, Bernadette Deirdre Mary. Flavones and related compounds as inhibitors of protein tyrosine kinases. Birmingham: Aston University. Department of Pharmaceutical Sciences, 1987.

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

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

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Book chapters on the topic "Protein-tyrosine kinases"

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Pearson, Mark, Carlos García-Echeverría, and Doriano Fabbro. "Protein Tyrosine Kinases as Targets for Cancer and Other Indications." In Protein Tyrosine Kinases, 1–29. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:001.

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García-Echeverría, Carlos. "Inhibitors of Signaling Interfaces." In Protein Tyrosine Kinases, 31–52. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:031.

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

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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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Burger, Renate, and Martin Gramatzki. "JAK Kinases in Leukemias, Lymphomas, and Multiple Myeloma." In Protein Tyrosine Kinases, 115–44. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:115.

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Buchdunger, Elisabeth, and Renaud Capdeville. "Glivec® (Gleevec®, Imatinib, STI571)." In Protein Tyrosine Kinases, 145–60. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:145.

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Sjöblom, Tobias, Kristian Pietras, Arne östman, and Carl-Henrik Heldin. "Platelet-Derived Growth Factor." In Protein Tyrosine Kinases, 161–86. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:161.

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Cowan-Jacob, Sandra W., Paul Ramage, Wilhelm Stark, Gabriele Fendrich, and Wolfgang Jahnke. "Structural Biology of Protein Tyrosine Kinases." In Protein Tyrosine Kinases, 187–230. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:187.

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O’Reilly, Terence, and Robert Cozens. "Testing of Signal Transduction Inhibitors in Animal Models of Cancer." In Protein Tyrosine Kinases, 231–64. Totowa, NJ: Humana Press, 2006. http://dx.doi.org/10.1385/1-59259-962-1:231.

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Conference papers on the topic "Protein-tyrosine kinases"

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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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LeDuc, Philip R. "Dynamic Formation for the Mechanical Connection of Focal Adhesion Complexes to Study Localized Mechanisms of Angiogenesis Through Modeling With Cellular Automata." In ASME 2001 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2001. http://dx.doi.org/10.1115/imece2001/bed-23159.

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Abstract The mechanical connection through the formation of focal adhesion complexes (FACs) is critical in cell growth and apoptosis. The FACs act between the cells and the extracellular matrix (ECM), which in turn influences angiogenesis, the growth of new capillary blood vessels [1]. These complexes form direct connections from ECM into the cell cytoskeleton through a series of protein binding events. This linkage is critical for mechanical force sensing and mechanotransduction signaling [2]. Here, the probabilistic modeling of this complex formation is undertaken to begin to uncover the effect of the spatial distribution and temporal effects on this dynamic process. In this, the rich dynamic process of the FACs formation through the binding events of integrin, paxillin, talin, and vinculin are examined. The FACs are mediated through the clustering of transmembrane integrins, which initiate the binding cascade. This interaction has been shown to be a critical event in the activation of the mechanochemical cascade and further mediates downstream signaling of protein tyrosine kinases including focal adhesion kinase [3].
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Gu, Mingxin, Yifan Lu, and Yuxin Jin. "The profile of receptor protein tyrosine kinases (RPTKs): taking AXL and DDR as examples." In International Conference on Modern Medicine and Global Health (ICMMGH 2023), edited by Sheiladevi Sukumaran. SPIE, 2023. http://dx.doi.org/10.1117/12.2692473.

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Ferguson, Peter J., Mark D. Vincent, and James Koropatnick. "Abstract 2019: Synergistic anticancer activity of the RAD51 inhibitor IBR2 with inhibitors of receptor tyrosine kinases and microtubule protein." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-2019.

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Ye, Jianfeng, Baoguo Chen, and Lisa X. Xu. "Shear Stress Effect on the Production of Nitric Oxide in Cultured Rat Aorta Endothelial Cells." In ASME 2002 International Mechanical Engineering Congress and Exposition. ASMEDC, 2002. http://dx.doi.org/10.1115/imece2002-33074.

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Atherosclerotic lesions tend to develop in regions where there are separations from unidirectional laminar blood flow, typically near branches, bifurcations, regions of arterial narrowing, and curvatures in the arteries (1, 2). Obviously, homodynamic forces play a key role in atherosclerosis. Studies also indicate that vascular endothelium function disturbance, especially impairment of endothelium dependent vasodilation, is involved (3). Shear stress affects endothelial cells in many ways, such as cytoskeletal rearrangement, decrease of intracellular pH, release of PGI2 and some growth factors (PDGF, FGF, ECGF, TGF-b, etc), activation of IP3 and mitogen-activated protein kinases, and the significant increase in the production of nitric oxide (1,2,4,5). As an important function factor of vascular endothelial cells, nitric oxide (NO) is closely related to the endothelial dysfunction and atherosclerosis (6). Endothelial derived nitric oxide involves in many events in the vasculature, including vasodilation, inhibition of platelet aggregation, adhesion molecule expression, and vascular smooth muscle proliferation, which are directly or indirectly related to atherosclerosis. Endothelial cells release NO more potently in response to increased shear stress than to agonists that raise intracellular free calcium concentration [Ca2+]i. Studies have indicated that NO production increases with a calcium/CaM dependent manner in the first few minutes after exposed to shear stress, followed by a sustained NO production that occurs more than 30min which is Ca2+ independent (7). The activation of eNOS by shear stress, which modulated by Ca/CaM, G protein, tyrosine kinase phosphorylation and eNOS gene expression, is responsible for the increase of NO production (8). However, the contribution of extracellular calcium to the production of NO is somewhat contradictory.
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Arora, Sumit, Sharanjot Saini, Shahana Majid, Varahram Shahryari, Soichiro Yamamura, Takeshi Chiyomaru, Shinichiro Fukuhara, et al. "Abstract 3068: MicroRNA 4723-5p is novel tumor suppressor microRNA in prostate cancer that directly regulates Abelson family of nonreceptor protein tyrosine kinases." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-3068.

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Stewart, Teneale A., Iman Azimi, Felicity M. Davis, Erik W. Thompson, Andrew J. Brooks, Sarah J. Roberts-Thomson, and Gregory R. Monteith. "Abstract P2-07-05: A potential role for Janus protein tyrosine kinases in the regulation of epithelial-mesenchymal transition in a model of epidermal growth factor induced breast cancer epithelial-mesenchymal transition." In Thirty-Seventh Annual CTRC-AACR San Antonio Breast Cancer Symposium; December 9-13, 2014; San Antonio, TX. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.sabcs14-p2-07-05.

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McKie, Arthur B., Sebastian Vaughan, Imoh Okon, Joshua L. C. Wong, Elisa Zanini, Eric W.-F. Lam, Naomi E. Chayen, and Hani Gabra. "Abstract 1616: The OPCML tumor suppressor negatively regulates a specific repertoire of 5 receptor tyrosine kinases via a novel proteasomal mechanism, and its recombinant derivative is a potent in-vivo anticancer protein therapy." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-1616.

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Pereira, Washington A., Érica C. M. Nascimento, and João B. L. Martins. "Estudo QM/MM da proteína tirosina Bcr-Abl mutada T315I." In VIII Simpósio de Estrutura Eletrônica e Dinâmica Molecular. Universidade de Brasília, 2020. http://dx.doi.org/10.21826/viiiseedmol2020148.

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Bcr-Abl tyrosine kinase protein activates the substrate starting kinase signaling cascade that results in cell division. When in excess this activation can lead to chronic myeloid leukemia. Currently, the treatment of this disease is achieved through drugs developed by rational drug design, e.g., imatinib. In this work we study descriptors of the following molecules: imatinib, nilotinib and ponatinib, together with a mutated protein. To characterize interactions between the residues of the active site against those inhibitors, a QM/MM study was carried out, using the hybrid method ONIOM, through the AMBER Force field (low layer) and the semi-empirical method PM6 (high layer).
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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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Reports on the topic "Protein-tyrosine kinases"

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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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