Relevant bibliographies by topics / Receptor tyrosine kinase family

Academic literature on the topic 'Receptor tyrosine kinase family'

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Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "Receptor tyrosine kinase family"

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GIBSON, Spencer, Ken TRUITT, Yiling LU, Ruth LAPUSHIN, Humera KHAN, B. John IMBODEN, and B. Gordon MILLS. "Efficient CD28 signalling leads to increases in the kinase activities of the TEC family tyrosine kinase EMT/ITK/TSK and the SRC family tyrosine kinase LCK." Biochemical Journal 330, no. 3 (March 15, 1998): 1123–28. http://dx.doi.org/10.1042/bj3301123.

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Optimal T cell activation requires crosslinking of the T cell receptor (TCR) concurrently with an accessory receptor, most efficiently CD28. Crosslinking of CD28 leads to increased interleukin 2 (IL2) production, inhibition of anergy and prevention of programmed cell death. Crosslinking of CD28 leads to rapid increases in tyrosine phosphorylation of specific intracellular substrates including CD28 itself. Since CD28 does not encode an intrinsic tyrosine kinase domain, CD28 must activate an intracellular tyrosine kinase(s). Indeed, crosslinking of CD28 increases the activity of the intracellular tyrosine kinases EMT/ITK and LCK. The phosphatidylinositol 3-kinase (PI3K) and GRB2 binding site in CD28 is dispensable for optimal IL2 production in Jurkat T cells. We demonstrate herein that murine Y170 (equivalent to human Y173) in CD28 is also dispensable for activation of the SRC family tyrosine kinase LCK and the TEC family tyrosine kinase EMT/ITK. In contrast, the distal three tyrosines in CD28 are required for optimal IL2 production as well as for optimal activation of the LCK and EMT/ITK tyrosine kinases. The distal three tyrosines of CD28, however, are not required for recruitment of PI3K to CD28. Furthermore, PI3K is recruited to CD28 in JCaM1 cells which lack LCK and in which EMT/ITK is not activated by ligation of CD28. Thus optimal activation of LCK or EMT/ITK is not obligatory for recruitment of PI3K to CD28 and thus is also not required for tyrosine phosphorylation of the YMNM motif in CD28. Taken together the data indicate that the distal three tyrosines in CD28 are integral to the activation of LCK and EMT/ITK and for subsequent IL2 production.
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BISOTTO, Sandra, and Elizabeth D. FIXMAN. "Src-family tyrosine kinases, phosphoinositide 3-kinase and Gab1 regulate extracellular signal-regulated kinase 1 activation induced by the type A endothelin-1 G-protein-coupled receptor." Biochemical Journal 360, no. 1 (November 8, 2001): 77–85. http://dx.doi.org/10.1042/bj3600077.

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The multisubstrate docking protein, growth-factor-receptor-bound protein 2-associated binder 1 (Gab1), which is phosphorylated on tyrosine residues following activation of receptor tyrosine kinases and cytokine receptors, regulates cell proliferation, survival and epithelial morphogenesis. Gab1 is also tyrosine phosphorylated following activation of G-protein-coupled receptors (GPCRs) where its function is poorly understood. To elucidate the role of Gab1 in GPCR signalling, we investigated the mechanism by which the type A endothelin-1 (ET-1) GPCR induced tyrosine phosphorylation of Gab1. Tyrosine phosphorylation of Gab1 induced by endothelin-1 was inhibited by PP1, a pharmacological inhibitor of Src-family tyrosine kinases. ET-1-induced Gab1 tyrosine phosphorylation was also inhibited by LY294002, which inhibits phosphoinositide 3-kinase (PI 3-kinase) enzymes. Inhibition of Src-family tyrosine kinases or PI 3-kinase also inhibited ET-1-induced activation of the mitogen activated protein kinase family member, extracellular signal-regulated kinase (ERK) 1. Thus we determined whether Gab1 regulated ET-1-induced ERK1 activation. Overexpression of wild-type Gab1 potentiated ET-1-induced activation of ERK1. Structure–function analyses of Gab1 indicated that mutant forms of Gab1 that do not bind the Src homology (SH) 2 domains of the p85 adapter subunit of PI 3-kinase or the SH2-domain-containing protein tyrosine phosphatase 2 (SHP-2) were impaired in their ability to potentiate ET-1-induced ERK1 activation. Taken together, our data indicate that PI 3-kinase and Src-family tyrosine kinases regulate ET-1-induced Gab1 tyrosine phosphorylation, which, in turn, induces ERK1 activation via PI 3-kinase- and SHP-2-dependent pathways.
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Forrester, W. C. "The Ror receptor tyrosine kinase family." Cellular and Molecular Life Sciences (CMLS) 59, no. 1 (January 1, 2002): 83–96. http://dx.doi.org/10.1007/s00018-002-8407-9.

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Sharfe, N., HK Dadi, and CM Roifman. "JAK3 protein tyrosine kinase mediates interleukin-7-induced activation of phosphatidylinositol-3' kinase." Blood 86, no. 6 (September 15, 1995): 2077–85. http://dx.doi.org/10.1182/blood.v86.6.2077.bloodjournal8662077.

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The interleukin-7 (IL-7) receptor is expressed throughout T-cell differentiation and, although lacking a tyrosine kinase domain, mediates tyrosine phosphorylation in T cells. We have identified IL-7- induced activation of three cyoplasmic tyrosine kinases in T cells, Jak1, Jak3, and the src-like kinase p56lck. Many members of the cytokine receptor superfamily activate the Jak protein tyrosine kinase family, with resultant phosphorylation of the Stat transcriptional activator factors. We describe here a novel function of the Jak kinases, because Jak kinase activity is not only required for Stat activation but also for P13 kinase response to IL-7 in human T cells. We show that IL-7 receptor-mediated Jak activation can occur independently of p56lck activity. IL-7-induced P13 kinase activation, mediated by tyrosine phosphorylation of the P13 kinase p85 subunit, is essential to the IL-7 proliferative signal and also occurs in the absence of src family kinase activity. Jak3 is found associated with the p85 subunit of P13 kinase in an IL-7-responsive manner in T cells and appears to regulate IL-7-induced P13 kinase activation by mediating tyrosine phosphorylation of the p85 subunit. Specific inhibition of IL- 7-induced Jak kinase activity ablates p85 tyrosine phosphorylation, subsequent P13 kinase activation, and, ultimately, proliferation. The ability to regulate P13 kinase activity indicates a more generalized role for the Jak family than activation of gene transcription via the Stat family in cytokine receptor signal transduction.
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Pyne, N. J., C. Waters, N. A. Moughal, B. S. Sambi, and S. Pyne. "Receptor tyrosine kinase–GPCR signal complexes." Biochemical Society Transactions 31, no. 6 (December 1, 2003): 1220–25. http://dx.doi.org/10.1042/bst0311220.

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The formation of complexes between growth factor receptors and members of a family of G-protein-coupled receptors whose natural ligands are S1P (sphingosine 1-phosphate) and LPA (lysophosphatidic acid) represents a new signalling entity. This receptor complex allows for integrated signalling in response to growth factor and/or S1P/LPA and provides a mechanism for more efficient activation (due to integrated close-proximity signalling from both receptor classes) of the p42/p44 MAPK (mitogen-activated protein kinase) pathway. This article provides information on the molecular events at the interface between receptor tyrosine kinases and S1P/LPA receptors. Examples include the PDGF (platelet-derived growth factor)-induced tyrosine phosphorylation of Giα, released upon S1P1 receptor activation, which is required for initiation of the p42/p44 MAPK pathway. Critical to this event is the formation of endocytic vesicles containing functionally active PDGFβ receptor–S1P1 receptor complexes, which are internalized and relocated with components of the p42/p44 MAPK pathway. We also report examples of cross-talk signal integration between the Trk A (tropomyosin receptor kinase A) receptor and the LPA1 receptor in terms of the NGF (nerve growth factor)-dependent regulation of the p42/p44 MAPK pathway. NGF induces recruitment of the LPA1 receptor to the nucleus (delivery might be Trk A-dependent), whereupon the LPA1 receptor may govern gene expression via novel nuclear signalling processes.
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Artim, Stephen C., Jeannine M. Mendrola, and Mark A. Lemmon. "Assessing the range of kinase autoinhibition mechanisms in the insulin receptor family." Biochemical Journal 448, no. 2 (November 7, 2012): 213–20. http://dx.doi.org/10.1042/bj20121365.

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To investigate the range of autoinhibitory mechanisms used by TKDs (tyrosine kinase domains) from the insulin receptor family of RTKs (receptor tyrosine kinases), we determined crystal structures of TKDs from TrkA (tropomyosin receptor kinase A, a nerve growth factor receptor) and Ror2 (receptor tyrosine kinase-like orphan receptor 2, an unconventional Wnt receptor). TrkA autoinhibition closely resembles that seen for the insulin receptor, relying on projection of an activation loop tyrosine residue into the substrate-binding site and occlusion of the ATP-binding site by the activation loop. Ror2 employs similar mechanisms, but the unusual replacement of the phenylalanine residue in its Asp-Phe-Gly motif with leucine necessitates occlusion of the ATP-binding site by other means. The unusual Asp-Leu-Gly motif in Ror2 is displaced compared with other inactive kinases, allowing the activation loop to interact directly with the TKD's αC helix, in another mode of autoinhibition that is characteristic of the other extreme of this receptor family: ALK (anaplastic lymphoma kinase) and Met. These findings provide insight into the expected range of activating mutations in these TKDs in cancer. We also describe symmetrical dimers of the inactive TrkA TKD resembling those found in other RTKs, possibly reflecting an arrangement of kinase domains in a pre-formed TrkA dimer.
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Truitt, Luke, and Andrew Freywald. "Dancing with the dead: Eph receptors and their kinase-null partnersThis paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health and Disease, and has undergone the Journal’s usual peer review process." Biochemistry and Cell Biology 89, no. 2 (April 2011): 115–29. http://dx.doi.org/10.1139/o10-145.

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Eph receptor tyrosine kinases and their ligands, ephrins, are membrane proteins coordinating a wide range of biological functions both in developing embryos and in adult multicellular organisms. Numerous studies have implicated Eph receptors in the induction of opposing responses, including cell adhesion or repulsion, support or inhibition of cell proliferation and cell migration, and progression or suppression of multiple malignancies. Similar to other receptor tyrosine kinases, Eph receptors rely on their ability to catalyze tyrosine phosphorylation for signal transduction. Interestingly, however, Eph receptors also actively utilize three kinase-deficient receptor tyrosine kinases, EphB6, EphA10, and Ryk, in their signaling network. The accumulating evidence suggests that the unusual flexibility of the Eph family, allowing it to initiate antagonistic responses, might be partially explained by the influence of the kinase-dead participants and that the exact outcome of an Eph-mediated action is likely to be defined by the balance between the signaling of catalytically potent and catalytically null receptors. We discuss in this minireview the emerging functions of the kinase-dead EphB6, EphA10, and Ryk receptors both in normal biological responses and in malignancy, and analyze currently available information related to the molecular mechanisms of their action in the context of the Eph family.
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Pertel, Thomas, Defen Zhu, Reynold A. Panettieri, Naoto Yamaguchi, Charles W. Emala, and Carol A. Hirshman. "Expression and muscarinic receptor coupling of Lyn kinase in cultured human airway smooth muscle cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 290, no. 3 (March 2006): L492—L500. http://dx.doi.org/10.1152/ajplung.00344.2005.

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Src family tyrosine kinases are signaling intermediates in a diverse array of cellular events including cell differentiation, motility, proliferation, and survival. In nonairway smooth muscle cells, muscarinic receptors directly interact with Src family tyrosine kinases. As little is known about the expression and signaling of these Src family tyrosine kinases in human airway smooth muscle cells, we determined the expression of Src family members and characterized the muscarinic receptor-mediated activation of Lyn kinase in these cells. RT-PCR revealed mRNA transcripts for FYN, c- SRC, YES, FRK, and LYN. Fyn, c-Src, Yes, and Lyn were identified in cultured airway smooth muscle cells by immunoblot analysis. In both nontransformed human cultured airway smooth muscle cells and cells transduced with wild-type human Lyn kinase, carbachol increased Lyn kinase activity. Pertussis toxin pretreatment failed to block carbachol activation of Lyn kinase but did attenuate the carbachol-induced increase in ERK/MAPK phosphorylation. Moreover, carbachol inhibited adenylyl cyclase but failed to increase total inositol phosphate synthesis in these cells. The present study shows that Lyn kinase is expressed in human cultured airway smooth muscle cells at both the mRNA and protein levels and that carbachol, an M2 muscarinic receptor agonist in these cells, activates Lyn kinase by a pertussis toxin-insensitive signaling pathway.
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Vignais, M. L., H. B. Sadowski, D. Watling, N. C. Rogers, and M. Gilman. "Platelet-derived growth factor induces phosphorylation of multiple JAK family kinases and STAT proteins." Molecular and Cellular Biology 16, no. 4 (April 1996): 1759–69. http://dx.doi.org/10.1128/mcb.16.4.1759.

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Receptors for interferons and other cytokines signal through the action of associated protein tyrosine kinases of the JAK family and latent cytoplasmic transcription factors of the STAT family. Genetic and biochemical analysis of interferon signaling indicates that activation of STATs by interferons requires two distinct JAK family kinases. Loss of either of the required JAKs prevents activation of the other JAK and extinguishes STAT activation. These observations suggest that JAKs provide interferon receptors with a critical catalytic signaling function and that at least two JAKs must be incorporated into an active receptor complex. JAK and STAT proteins are also activated by ligands such as platelet-derived growth factor (PDGF), which act through receptors that possess intrinsic protein tyrosine kinase activity, raising questions about the role of JAKs in signal transduction by this class of receptors. Here, we show that all three of the ubiquitously expressed JAKs--JAK1, JAK2, and Tyk2--become phosphorylated on tyrosine in both mouse BALB/c 3T3 cells and human fibroblasts engineered to express the PDGF-beta receptor. All three proteins are also associated with the activated receptor. Through the use of cell lines each lacking an individual JAK, we find that in contrast to interferon signaling, PDGF-induced JAK phosphorylation and activation of STAT1 and STAT3 is independent of the presence of any other single JAK but does require receptor tyrosine kinase activity. These results suggests that the mechanism of JAK activation and JAK function in signaling differs between receptor tyrosine kinases and interferon receptors.
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Mendrola, Jeannine M., Fumin Shi, Jin H. Park, and Mark A. Lemmon. "Receptor tyrosine kinases with intracellular pseudokinase domains." Biochemical Society Transactions 41, no. 4 (July 18, 2013): 1029–36. http://dx.doi.org/10.1042/bst20130104.

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As with other groups of protein kinases, approximately 10% of the RTKs (receptor tyrosine kinases) in the human proteome contain intracellular pseudokinases that lack one or more conserved catalytically important residues. These include ErbB3, a member of the EGFR (epidermal growth factor receptor) family, and a series of unconventional Wnt receptors. We showed previously that, despite its reputation as a pseudokinase, the ErbB3 TKD (tyrosine kinase domain) does retain significant, albeit weak, kinase activity. This led us to suggest that a subgroup of RTKs may be able to signal even with very inefficient kinases. Recent work suggests that this is not the case, however. Other pseudokinase RTKs have not revealed significant kinase activity, and mutations that impair ErbB3′s weak kinase activity have not so far been found to exhibit signalling defects. These findings therefore point to models in which the TKDs of pseudokinase RTKs participate in receptor signalling by allosterically regulating associated kinases (such as ErbB3 regulation of ErbB2) and/or function as regulated ‘scaffolds’ for other intermolecular interactions central to signal propagation. Further structural and functional studies, particularly of the pseudokinase RTKs involved in Wnt signalling, are required to shed new light on these intriguing signalling mechanisms.
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Dissertations / Theses on the topic "Receptor tyrosine kinase family"

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Lorén, Christina. "Investigating the function of the Receptor Tyrosine Kinase ALK during Drosophila melanogaster development /." Umeå : Univ, 2004. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-411.

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Guiton, Michelle. "Molecular basis of signal transduction by the Trk family of receptor tyrosine kinases." Thesis, University of Bristol, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.296366.

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KIM, SOYEON. "INVESTIGATING THE MOLECULAR INTERACTION OF ERBB RECEPTOR TYROSINE KINASES USING FLUORESCENCE CROSS CORRELATION SPECTROSCOPY." University of Akron / OhioLINK, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=akron1632756640189756.

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Reschke, Markus Oliver. "Mitogen-inducible gene-6 is a negative regulator of the HER-family of receptor tyrosine kinases." kostenfrei, 2008. http://mediatum2.ub.tum.de/doc/654949/654949.pdf.

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Qi, Wenqing, Larry Cooke, Amy Stejskal, Christopher Riley, Kimiko Croce, Jose Saldanha, David Bearss, and Daruka Mahadevan. "MP470, a novel receptor tyrosine kinase inhibitor, in combination with Erlotinib inhibits the HER family/PI3K/Akt pathway and tumor growth in prostate cancer." BioMed Central, 2009. http://hdl.handle.net/10150/610342.

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BACKGROUND:Prostate cancer is a common disease in men and at present there is no effective therapy available due to its recurrence despite androgen deprivation therapy. The epidermal growth factor receptor family (EGFR/HER1, HER2/neu and HER3)/PI3K/Akt signaling axis has been implicated in prostate cancer development and progression. However, Erlotinib, an EGFR tyrosine kinase inhibitor, has less effect on proliferation and apoptosis in prostate cancer cell lines. In this study, we evaluate whether MP470, a novel receptor tyrosine kinase inhibitor alone or in combination with Erlotinib has inhibitory effect on prostate cancer in vitro and in vivo.METHODS:The efficacy of MP470 or MP470 plus Erlotinib was evaluated in vitro using three prostate cancer cell lines by MTS and apoptosis assays. The molecular mechanism study was carried out by phosphorylation antibody array, immunoblotting and immunohistochemistry. A LNCaP mouse xenograft model was also used to determine the tumor growth inhibition by MP470, Erlotinib or the combination treatments.RESULTS:MP470 exhibits low muM IC50 in prostate cancer cell lines. Additive effects on both cytotoxicity and induction of apoptosis were observed when LNCaP were treated with MP470 in combination with Erlotinib. This combination treatment completely inhibited phosphorylation of the HER family members (HER1, 2, 3), binding of PI3K regulatory unit p85 to HER3 and downstream Akt activity even after androgen depletion. Furthermore, in a LNCaP mouse xenograft model, the MP470-Erlotinib combination produced 30-65% dose-dependent tumor growth inhibition (TGI).CONCLUSION:We propose that MP470-Erlotinib targets the HER family/PI3K/Akt pathway and may represent a novel therapeutic strategy for prostate cancer.
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Beji, Abdelhamid [Verfasser], Kay Akademischer Betreuer] Schneitz, and Axel [Akademischer Betreuer] [Ullrich. "Significance of the Negative Regulator of HER Receptor Tyrosine Kinase Family, mig-6 Protein, in Colon Cancer and Glioblastoma / Abdelhamid Beji. Gutachter: Axel Ullrich. Betreuer: Kay Schneitz." München : Universitätsbibliothek der TU München, 2012. http://d-nb.info/1019590297/34.

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Goebel, Susan Michelle. "Phospho-regulation of hippocampal NMDA receptor localization and function /." Connect to full text via ProQuest. Limited to UCD Anschutz Medical Campus, 2007.

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Thesis (Ph.D. in Neuroscience) -- University of Colorado Denver, 2007.
Typescript. Includes bibliographical references (leaves 200-233). Free to UCD affiliates. Online version available via ProQuest Digital Dissertations;
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Zhao, Haotian. "Exploring the role of fibroblast growth factor (FGF) signaling in mouse lens fiber differentiation through tissue-specific disruption of FGF receptor gene family." Connect to this title online, 2004. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1072722841.

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Thesis (Ph. D.)--Ohio State University, 2004.
Title from first page of PDF file. Document formatted into pages; contains xii, 203 p.; also includes graphics (some col.) Includes bibliographical references (p. 179-203). Available online via OhioLINK's ETD Center
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Lennmyr, Fredrik. "Signal Transduction in Focal Cerebral Ischemia : Experimental Studies on VEGF, MAPK and Src family kinases." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Univ.-bibl. [distributör], 2002. http://publications.uu.se/theses/91-554-5267-1/.

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Ljuslinder, Ingrid. "Studies of LRIG1 and the ERBB receptor family in breast and colorectal cancer." Doctoral thesis, Umeå : Umeå university, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-25678.

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Books on the topic "Receptor tyrosine kinase family"

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Wheeler, Deric L., and Yosef Yarden, eds. Receptor Tyrosine Kinases: Family and Subfamilies. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-11888-8.

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

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Shulman, Johanna. Biochemical analysis of activating mutations of the Kit receptor tyrosine kinase. Ottawa: National Library of Canada, 1998.

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

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Ho, Jacqueline. A requirement for the receptor tyrosine kinase, Flk1, in hematopoiesis and vasculogenesis. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1999.

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Keane, Noeleen Emily. Nuclear magnetic resonance studies of the human insulin receptor tyrosine kinase autophosphorylation and activity. Birmingham: University of Birmingham, 1994.

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Gibson, Spencer Bruce. Role of the TEC family tyrosine kinase EMT in T cell activation. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1997.

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Viegas, Muriel. The intrinsic tyrosine kinase activity of the epidermal growth factor receptor is necessary for phospholipase A2 activation. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1993.

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Alaimo, Darrick James. Hepatic insulin receptor tyrosine kinase activity in diabetes: Modulation by assorted adenosine triphosphatases/phosphatases which copurify in partially purified preparations of the insulin receptor. [s.l: s.n.], 1992.

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1949-, Lichtner R. B., and Harkins R. N. 1947-, eds. EGF receptor in tumor growth and progression. Berlin: Springer, 1997.

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Book chapters on the topic "Receptor tyrosine kinase family"

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Palmer, Ruth H., and Bengt Hallberg. "The ALK Receptor Family." In Receptor Tyrosine Kinases: Family and Subfamilies, 1–51. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-11888-8_1.

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Chitu, Violeta, Cristina I. Caescu, E. Richard Stanley, Johan Lennartsson, Lars Rönnstrand, and Carl-Henrik Heldin. "The PDGFR Receptor Family." In Receptor Tyrosine Kinases: Family and Subfamilies, 373–538. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-11888-8_10.

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Lhoumeau, Anne-Catherine, Sébastien Martinez, Thomas Prébet, and Jean-Paul Borg. "The PTK7 Receptor Family." In Receptor Tyrosine Kinases: Family and Subfamilies, 539–58. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-11888-8_11.

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Melillo, Rosa Marina, and Massimo Santoro. "The RET Receptor Family." In Receptor Tyrosine Kinases: Family and Subfamilies, 559–91. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-11888-8_12.

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Endo, Mitsuharu, Michiru Nishita, Ryosuke Doi, Makoto Hayashi, and Yasuhiro Minami. "The ROR Receptor Family." In Receptor Tyrosine Kinases: Family and Subfamilies, 593–640. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-11888-8_13.

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Charest, Alain. "The ROS1 Receptor Family." In Receptor Tyrosine Kinases: Family and Subfamilies, 641–84. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-11888-8_14.

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Halford, Michael M., Maria L. Macheda, and Steven A. Stacker. "The RYK Receptor Family." In Receptor Tyrosine Kinases: Family and Subfamilies, 685–741. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-11888-8_15.

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Saharinen, Pipsa, Michael Jeltsch, Mayte M. Santoyo, Veli-Matti Leppänen, and Kari Alitalo. "The TIE Receptor Family." In Receptor Tyrosine Kinases: Family and Subfamilies, 743–75. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-11888-8_16.

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Hondermarck, Hubert, Yohann Demont, and Ralph A. Bradshaw. "The TrK Receptor Family." In Receptor Tyrosine Kinases: Family and Subfamilies, 777–820. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-11888-8_17.

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Zhuang, Guanglei, and Napoleone Ferrara. "The VEGF Receptor Family." In Receptor Tyrosine Kinases: Family and Subfamilies, 821–41. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-11888-8_18.

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Conference papers on the topic "Receptor tyrosine kinase family"

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Alvarado, Diego, Laura Vitale, Mike Murphy, Thomas O'Neill, Andrew Proffitt, Jay Lillquist, Gwenda Ligon, et al. "Abstract 1555: Monoclonal antibodies targeting the TAM family of receptor tyrosine kinases." 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.sabcs18-1555.

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Alvarado, Diego, Laura Vitale, Mike Murphy, Thomas O'Neill, Andrew Proffitt, Jay Lillquist, Gwenda Ligon, et al. "Abstract 1555: Monoclonal antibodies targeting the TAM family of receptor tyrosine kinases." 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.am2019-1555.

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Brand, Toni M., Mari Iida, Matthew J. Wleklinski, Neha Luthar, Megan M. Starr, and Deric L. Wheeler. "Abstract 4276: Mapping C-terminal transactivation domains of nuclear HER family receptor 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.am2013-4276.

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Iwanaga, Kentaro, Naoko Sueoka-Aragane, Akemi Sato, Tomomi Nakamura, Naomi Kobayashi, Eisaburo Sueoka, and Shinya Kimura. "Abstract 1906: Mechanisms of resistance to EGFR tyrosine kinase inhibitors involving HER-family ligands and receptors." 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.am2012-1906.

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Brand, Toni Michel, Mari Iida, Kelsey L. Corrigan, Neha Luthar, Megan Hornung, Mahmoud Toulany, Parkash Gill, Ravi Salgia, and Deric L. Wheeler. "Abstract LB-215: The TAM family of receptor tyrosine kinases play a role in acquired resistance to cetuximab." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-lb-215.

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Alvarado, Diego, Laura Vitale, Michael Murphy, Thomas O'Neill, Andrew Proffitt, Jay Lillquist, Gwenda Ligon, et al. "Abstract B194: Identification and characterization of monoclonal antibodies targeting the Tyro3, Axl and MerTK (TAM) family of receptor tyrosine kinases." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics; October 26-30, 2017; Philadelphia, PA. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1535-7163.targ-17-b194.

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Wang, Gary T., Robert A. Mantei, Robert D. Hubbard, Julie L. Wilsbacher, Qian Zhang, Lora Tucker, Xiaoming Hu, et al. "Abstract A248: Substituted 4‐amino‐1H‐pyrazolo[3,4‐d]pyrimidines as multitargeted inhibitors targeting insulin‐like growth factor‐1 receptor (IGF1R) and members of ErbB‐family receptor tyrosine kinases." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-a248.

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Jathak, Maitreyee K., Thomas M. Steele, Salma Siddiqui, Benjamin A. Mooso, Leandro S. D'Abronzo, Christiana M. Drake, and Paramita M. Ghosh. "Abstract 868: The pan-ErbB inhibitor dacomitinib but not the dual EGFR/ErbB2 inhibitor labatinib disrupts membrane localization of the EGFR family of receptor tyrosine kinases." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-868.

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Oudin, Madeleine J., Shannon K. Hughes-Alford, Miles Miller, Sreeja B. Asokan, James E. Bear, Doug A. Lauffenburger, and Frank B. Gertler. "Abstract C41: MenaINVdysregulation of receptor tyrosine kinase signaling." In Abstracts: AACR Special Conference on Tumor Invasion and Metastasis - January 20-23, 2013; San Diego, CA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.tim2013-c41.

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Lai, Andrea, and Morag Park. "Abstract 4688: Met receptor tyrosine kinase cross-talk in tumorigenesis." 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.am2011-4688.

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Reports on the topic "Receptor tyrosine kinase family"

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King, Megan, and Mark Lemmon. The Role of Dynamin in the Regulation of Signaling by the erbB Family of Receptor Tyrosine Kinases. Fort Belvoir, VA: Defense Technical Information Center, April 2003. http://dx.doi.org/10.21236/ada416747.

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Kockel, Lutz. Isolation and Analysis of Human Kekkon-Like Molecules, a Family of Potential Inhibitors of ErbB Receptor Tyrosine Kinases. Fort Belvoir, VA: Defense Technical Information Center, April 2005. http://dx.doi.org/10.21236/ada443751.

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

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

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

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Riese, David J. Functional Analysis of the ErbB4 Receptor Tyrosine Kinase. Fort Belvoir, VA: Defense Technical Information Center, July 2003. http://dx.doi.org/10.21236/ada418035.

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Riese, David J., and II. Functional Analysis of the ErbB4 Receptor Tyrosine Kinase. Fort Belvoir, VA: Defense Technical Information Center, July 2003. http://dx.doi.org/10.21236/ada418740.

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Stearns, Carrie. Role of the Non-Receptor Tyrosine Kinase ACK2 in EGF Receptor Degradation. Fort Belvoir, VA: Defense Technical Information Center, April 2004. http://dx.doi.org/10.21236/ada427754.

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Stearns, Carrie. Role of the Non-Receptor Tyrosine Kinase ACK2 in EGF Receptor Degradation. Fort Belvoir, VA: Defense Technical Information Center, April 2005. http://dx.doi.org/10.21236/ada435047.

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Calero, Guillermo A., Rick Cerione, and Jon Clardy. Structural Studies of a New Nuclear Target for EGF Receptor Tyrosine Kinase. Fort Belvoir, VA: Defense Technical Information Center, August 2002. http://dx.doi.org/10.21236/ada415658.

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