Relevant bibliographies by topics / Tyrosine

Academic literature on the topic 'Tyrosine'

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Published: 4 June 2021
Last updated: 5 March 2023

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Journal articles on the topic "Tyrosine"

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Hunter, Tony. "THE CROONIAN LECTURE 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and disease." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 353, no. 1368 (April 29, 1998): 583–605. http://dx.doi.org/10.1098/rstb.1998.0228.

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The reversible phosphorylation of tyrosines in proteins plays a key role in regulating many different processes in eukaryotic organisms, such as growth control, cell cycle control, differentiation, cell shape and movement, gene transcription, synaptic transmission, and insulin action. Phosphorylation of proteins is brought about by enzymes called protein–tyrosine kinases that add phosphate to specific tyrosines in target proteins; phosphate is removed from phosphorylated tyrosines by enzymes called protein–tyrosine phosphatases. Phosphorylated tyrosines are recognized by specialized binding domains on other proteins, and such interactions are used to initiate intracellular signalling pathways. Currently, more than 95 protein–tyrosine kinases and more than 55 protein–tyrosine phosphatase genes are known in Homo sapiens . Aberrant tyrosine phosphorylation is a hallmark of many types of cancer and other human diseases. Drugs are being developed that antagonize the responsible protein–tyrosine kinases and phosphatases in order to combat these diseases.
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Longmore, Gregory D., Yun You, Jaime Molden, Kathleen D. Liu, Aki Mikami, Stephen Y. Lai, Pamela Pharr, and Mark A. Goldsmith. "Redundant and Selective Roles for Erythropoietin Receptor Tyrosines in Erythropoiesis In Vivo." Blood 91, no. 3 (February 1, 1998): 870–78. http://dx.doi.org/10.1182/blood.v91.3.870.

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Abstract Cytokine receptors have been shown in cell culture systems to use phosphotyrosine residues as docking sites for certain signal transduction intermediates. Studies using various cellular backgrounds have yielded conflicting information about the importance of such residues. The present studies were undertaken to determine whether or not tyrosine residues within the erythropoietin receptor (EPOR) are essential for biologic activity during hematopoiesis in vivo. A variant of the EPOR was constructed that contains both a substitution (R129C) causing constitutive receptor activation as well as replacement of all eight cytoplasmic tyrosines by phenylalanines (cEPORYF). A comparison between animals exposed to recombinant retroviruses expressing cEPOR and cEPORYF showed that efficient red blood cell (RBC) development in vivo is dependent on the presence of tyrosine residues in the cytoplasmic domain of the EPOR. In addition, an inefficient EPOR tyrosine independent pathway supporting RBC development was detected. Tyrosine add-back mutants showed that multiple individual tyrosines have the capacity to restore full erythropoietic potential to the EPOR as determined in whole animals. The analysis of primary erythroid progenitors transduced with the various cEPOR tyrosine mutants and tyrosine add-backs showed that only tyrosine 343 (Y1) and tyrosine 479 (Y8) were capable of supporting immature burst-forming unit–erythroid progenitor development. Thus, this receptor is characterized by striking functional redundancy of tyrosines in a biologically relevant context. However, selective tyrosine residues may be uniquely important for early signals supporting erythroid development.
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Longmore, Gregory D., Yun You, Jaime Molden, Kathleen D. Liu, Aki Mikami, Stephen Y. Lai, Pamela Pharr, and Mark A. Goldsmith. "Redundant and Selective Roles for Erythropoietin Receptor Tyrosines in Erythropoiesis In Vivo." Blood 91, no. 3 (February 1, 1998): 870–78. http://dx.doi.org/10.1182/blood.v91.3.870.870_870_878.

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Cytokine receptors have been shown in cell culture systems to use phosphotyrosine residues as docking sites for certain signal transduction intermediates. Studies using various cellular backgrounds have yielded conflicting information about the importance of such residues. The present studies were undertaken to determine whether or not tyrosine residues within the erythropoietin receptor (EPOR) are essential for biologic activity during hematopoiesis in vivo. A variant of the EPOR was constructed that contains both a substitution (R129C) causing constitutive receptor activation as well as replacement of all eight cytoplasmic tyrosines by phenylalanines (cEPORYF). A comparison between animals exposed to recombinant retroviruses expressing cEPOR and cEPORYF showed that efficient red blood cell (RBC) development in vivo is dependent on the presence of tyrosine residues in the cytoplasmic domain of the EPOR. In addition, an inefficient EPOR tyrosine independent pathway supporting RBC development was detected. Tyrosine add-back mutants showed that multiple individual tyrosines have the capacity to restore full erythropoietic potential to the EPOR as determined in whole animals. The analysis of primary erythroid progenitors transduced with the various cEPOR tyrosine mutants and tyrosine add-backs showed that only tyrosine 343 (Y1) and tyrosine 479 (Y8) were capable of supporting immature burst-forming unit–erythroid progenitor development. Thus, this receptor is characterized by striking functional redundancy of tyrosines in a biologically relevant context. However, selective tyrosine residues may be uniquely important for early signals supporting erythroid development.
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Marumo, K., and J. H. Waite. "Optimization of hydroxylation of tyrosine and tyrosine-containing peptides by mushroom tyrosinase." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 872, no. 1-2 (July 1986): 98–103. http://dx.doi.org/10.1016/0167-4838(86)90152-4.

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Hansen, J. A., L. H. Hansen, X. Wang, J. J. Kopchick, F. Gouilleux, B. Groner, J. H. Nielsen, A. Møldrup, E. D. Galsgaard, and N. Billestrup. "The role of GH receptor tyrosine phosphorylation in Stat5 activation." Journal of Molecular Endocrinology 18, no. 3 (June 1997): 213–21. http://dx.doi.org/10.1677/jme.0.0180213.

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ABSTRACT Stimulation of GH receptors leads to rapid activation of Jak2 kinase and subsequent tyrosine phosphorylation of the GH receptor. Three specific tyrosines located in the C-terminal domain of the GH receptor have been identified as being involved in GH-stimulated transcription of the Spi 2·1 promoter. Mutated GH receptors lacking all but one of these three tyrosines are able to mediate a transcriptional response when transiently transfected into CHO cells together with a Spi 2·1 promoter/luciferase construct. Similarly, these GH receptors were found to be able to mediate activation of Stat5 DNA-binding activity, whereas the GH receptor mutant lacking all intracellular tyrosines was not. Synthetic tyrosine phosphorylated peptides corresponding to the GH receptor sequence around the three tyrosines inhibited Stat5 DNA-binding activity while their non-phosphorylated counterparts were ineffective. Tyrosine phosphorylated GST-GH receptor fusion proteins specifically bound to Stat5 in extracts from COS 7 cells transfected with Stat5 cDNA. This binding could be inhibited by tyrosine phosphorylated peptides derived from the GH receptor. This study thus demonstrated that specific GH receptor tyrosine residues, in their phosphorylated state, are involved in transcriptional signaling by directly interacting with Stat5.
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King, M. J., and G. J. Sale. "Dephosphorylation of insulin-receptor autophosphorylation sites by particulate and soluble phosphotyrosyl-protein phosphatases." Biochemical Journal 266, no. 1 (February 15, 1990): 251–59. http://dx.doi.org/10.1042/bj2660251.

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Insulin stimulates autophosphorylation of the insulin receptor on multiple tyrosines in three domains: tyrosines 1316 and 1322 in the C-terminal tail, 1146, 1150 and 1151 in the tyrosine-1150 domain, and possibly 953, 960 or 972 in the juxtamembrane domain. In the present work the sequence of dephosphorylation of the various autophosphorylation sites by particulate and cytosolic preparations of phosphotyrosyl-protein phosphatase from rat liver was studied with autophosphorylated human placental insulin receptor as substrate. Both phosphatase preparations elicited a broadly similar pattern of dephosphorylation. The tyrosine-1150 domain in triphosphorylated form was found to be exquisitely sensitive to dephosphorylation, and was dephosphorylated 3-10-fold faster than the di- and monophosphorylated forms of the tyrosine-1150 domain or phosphorylation sites in other domains. The major route for dephosphorylation of the triphosphorylated tyrosine-1150 domain involved dephosphorylation of one of the phosphotyrosyl pair, 1150/1151, followed by phosphotyrosyl 1146 to generate a species monophosphorylated mainly (greater than 80%) at tyrosine 1150 or 1151. Insulin receptors monophosphorylated in the tyrosine-1150 domain disappeared slowly, and overall the other domains were completely dephosphorylated faster than the tyrosine-1150 domain. Dephosphorylation of the diphosphorylated C-terminal domain yielded insulin receptor in which the domain was singly phosphorylated at tyrosine 1322. Triphosphorylation of the insulin receptor in the tyrosine-1150 domain appears important in activating the receptor tyrosine kinase to phosphorylate other proteins. The extreme sensitivity of the triphosphorylated form of the tyrosine-1150 domain to dephosphorylation may thus be important in terminating or regulating insulin-receptor tyrosine kinase action and insulin signalling.
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Pao, Lily I., Sara J. Famiglietti, and John C. Cambier. "Asymmetrical Phosphorylation and Function of Immunoreceptor Tyrosine-Based Activation Motif Tyrosines in B Cell Antigen Receptor Signal Transduction." Journal of Immunology 160, no. 7 (April 1, 1998): 3305–14. http://dx.doi.org/10.4049/jimmunol.160.7.3305.

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Abstract CD79a and CD79b function as transducers of B cell antigen receptor signals via a cytoplasmic sequence, termed the immunoreceptor tyrosine-based activation motif (ITAM). ITAMs contain two conserved tyrosines that may become phosphorylated upon receptor aggregation and bind distinct effectors by virtue of the distinct preference of phosphotyrosyl-containing sequences for SH2 domains. To explore the function of CD79a and CD79b ITAM tyrosines, we created membrane molecules composed of MHC class II I-Ak extracellular and transmembrane domains, and CD79a or CD79b cytoplasmic domains in which one or both of the ITAM tyrosines were mutated to phenylalanine. Functional analysis revealed that both ITAM tyrosines are required for ligand-induced Syk phosphorylation. However CD79a-ITAM and CD79b-ITAM tyrosine phosphorylations were asymmetrical, with >80% of phosphorylation occurring on the N-terminal tyrosine (Y-E-G-L). Thus, these findings suggest that following receptor ligation, only a minor proportion of phosphorylated ITAMs are doubly phosphorylated and thus can engage Syk. Only the N-terminal ITAM tyrosine of CD79a was required for ligand-mediated phosphorylation of the receptor and a subset of downstream substrates, including p62, p110, and Shc, and for Ca2+ mobilization. However, responses mediated through CD79b exhibited a greater dependence on the presence of both tyrosines. Neither tyrosine in CD79a or CD79b appeared absolutely essential for Src family kinase phosphorylation. These results indicate that phosphorylations of the tyrosines in CD79a and CD79b occur with very different stoichiometry, and the respective tyrosyl residues have distinct functions.
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Argetsinger, Lawrence S., Jean-Louis K. Kouadio, Hanno Steen, Allan Stensballe, Ole N. Jensen, and Christin Carter-Su. "Autophosphorylation of JAK2 on Tyrosines 221 and 570 Regulates Its Activity." Molecular and Cellular Biology 24, no. 11 (June 1, 2004): 4955–67. http://dx.doi.org/10.1128/mcb.24.11.4955-4967.2004.

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ABSTRACT The tyrosine kinase JAK2 is a key signaling protein for at least 20 receptors in the cytokine/hematopoietin receptor superfamily and is a component of signaling by insulin receptor and several G-protein-coupled receptors. However, there is only limited knowledge of the physical structure of JAK2 or which of the 49 tyrosines in JAK2 are autophosphorylated. In this study, mass spectrometry and two-dimensional peptide mapping were used to determine that tyrosines 221, 570, and 1007 in JAK2 are autophosphorylated. Phosphorylation of tyrosine 570 is particularly robust. In response to growth hormone, JAK2 was rapidly and transiently phosphorylated at tyrosines 221 and 570, returning to basal levels by 60 min. Analysis of the sequences surrounding tyrosines 221 and 570 in JAK2 and tyrosines in other proteins that are phosphorylated in response to ligands that activate JAK2 suggests that the YXX[L/I/V] motif is one of the motifs recognized by JAK2. Experiments using JAK2 with tyrosines 221 and 570 mutated to phenylalanine suggest that tyrosines 221 and 570 in JAK2 may serve as regulatory sites in JAK2, with phosphorylation of tyrosine 221 increasing kinase activity and phosphorylation of tyrosine 570 decreasing kinase activity and thereby contributing to rapid termination of ligand activation of JAK2.
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Deng, Kaiping, Jason R. Mock, Steven Greenberg, Nicolai S. C. van Oers, and Eric J. Hansen. "Haemophilus ducreyi LspA Proteins Are Tyrosine Phosphorylated by Macrophage-Encoded Protein Tyrosine Kinases." Infection and Immunity 76, no. 10 (August 4, 2008): 4692–702. http://dx.doi.org/10.1128/iai.00513-08.

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ABSTRACTThe LspA proteins (LspA1 and LspA2) ofHaemophilus ducreyiare necessary for this pathogen to inhibit the phagocytic activity of macrophage cell lines, an event that can be correlated with a reduction in the level of active Src family protein tyrosine kinases (PTKs) in these eukaryotic cells. During studies investigating this inhibitory mechanism, it was discovered that the LspA proteins themselves were tyrosine phosphorylated after wild-typeH. ducreyicells were incubated with macrophages. LspA proteins in cell-free concentratedH. ducreyiculture supernatant fluid could also be tyrosine phosphorylated by macrophages. This ability to tyrosine phosphorylate the LspA proteins was not limited to immune cell lineages but could be accomplished by both HeLa and COS-7 cells. Kinase inhibitor studies with macrophages demonstrated that the Src family PTKs were required for this tyrosine phosphorylation activity. In silico methods and site-directed mutagenesis were used to identify EPIYG and EPVYA motifs in LspA1 that contained tyrosines that were targets for phosphorylation. A total of four tyrosines could be phosphorylated in LspA1, with LspA2 containing eight predicted tyrosine phosphorylation motifs. Purified LspA1 fusion proteins containing either the EPIYG or EPVYA motifs were shown to be phosphorylated by purified Src PTK in vitro. Macrophage lysates could also tyrosine phosphorylate the LspA proteins and an LspA1 fusion protein via a mechanism that was dependent on the presence of both divalent cations and ATP. Several motifs known to interact with or otherwise affect eukaryotic kinases were identified in the LspA proteins.
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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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Dissertations / Theses on the topic "Tyrosine"

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Iron, Albert. "L'acide DL-amino-1-(parahydroxyphényl)-2-éthylphosphonique, analogue phosphonique de la tyrosine : quelques propriétés physicochimiques et métaboliques." Bordeaux 2, 1989. http://www.theses.fr/1989BOR2E001.

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Nadeau, Robert J. "Sprouty Regulation of Tyrosine Kinase Signal Transduction is Governed by Tyrosine Phosphorylation: A Functional Role for Sprouty2 N- and C- Terminal Tyrosines." Fogler Library, University of Maine, 2006. http://www.library.umaine.edu/theses/pdf/NadeauRJ2006.pdf.

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Lee, Joseph Moon-Hee 1967. "Characterization of tyrosine phosphorylation in the protein tyrosine phosphatase CD45." Thesis, McGill University, 2001. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=37758.

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The enzymatic activity of the protein tyrosine phosphatase, CD45 has been demonstrated to play an absolutely required role in the regulation of Src family protein tyrosine kinases in T lymphocytes. CD45 function during early events of antigen receptor signaling has been well established, however, the role of CD45 during later stages of T cell activation is only beginning to emerge. Transient tyrosine phosphorylation of CD45 has previously been demonstrated. We show this phosphorylation can be sustained through treatment of a T cell hybridoma cell line with the PTPase inhibitor, pervanadate. Tyrosine phosphorylation of CD45 is significantly increased in the presence of an activated form of Lck. Tyrosine phosphorylated CD45 is correlated with the association of a subset of signaling molecules containing SH2 domains. These molecules include p56Lck, p59Fyn, rasGAP, Grb2 and Csk. Although CD45 becomes abundantly tyrosine phosphorylated upon pervanadate treatment, no other SH2-containing molecules that we had tested demonstrated association with CD45. The interaction between CD45 and Grb2 in particular was found to be dependent upon CD45 tyrosine phosphorylation and mediated through the SH2 domain of Grb2. Interestingly, both Grb2 and a close homolog, Grap are able to bind CD45 in in vitro binding assays. Grap does not, however, associate with CD45 in vivo as was observed for Grb2.
CD45 contains two Grb2 consensus binding sequences. Deletion of both results in a greatly diminished capacity for CD45- Grb2 association. However, interaction between the two is not completely abolished and appears to result from an unconventional peptide sequence as observed by 2-dimensional phosphopeptide mapping studies. In the process of mapping the phosphotyrosine sequences required for CD45-Grb2 interaction, many tyrosine-phosphorylated peptides have been identified and assigned to tyrosine residues in CD45.
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Lu, Wei. "Regulation of protein tyrosine phosphatase SHP-2 by tyrosine phosphorylation." Available to US Hopkins community, 2002. http://wwwlib.umi.com/dissertations/dlnow/3080719.

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Chen, Shirley Chun-Jyue. "The regulation and function of protein tyrosine phosphatase alpha (PTPα) tyrosine phosphorylation." Thesis, University of British Columbia, 2007. http://hdl.handle.net/2429/31583.

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Protein tyrosine phosphatase alpha (PTPα) is a ubiquitously expressed receptor protein tyrosine phosphatase that functions as an early upstream regulator in the integrin signaling pathway. The integrins, by interacting with extracellular matrix components, regulate cell growth, migration, and survival, and are functionally linked to multiple aspects of cancer biology such as invasion and metastasis. PTPα plays a major role in the integrin signaling cascade by activating Src family kinases (SFKs), which are required for the full activation of the central signaling molecule focal adhesion kinase (FAK). The importance of PTPα in integrin signaling is demonstrated by defects observed in integrin-mediated cytoskeletal rearrangement and focal adhesion formation in PTPα-deficient fibroblasts. PTPα contains a tyrosine phosphorylation site, Tyr-789, located in the intracellular C-terminal tail. Tyr-789 phosphorylation is shown to not affect PTPα catalytic activity, but allows binding of Src and the adaptor protein Grb2. Little is known about the regulation and function of PTPα Tyr-789 phosphorylation. Recent work from our laboratory has discovered that PTPα Tyr-789 phosphorylation is positively regulated upon integrin engagement and is functionally required for integrin-induced cytoskeletal reorganization events, suggesting the importance of the phospho-Tyr-789 motif in PTPα-mediated signaling events. In a search for other regulators of PTPα Tyr-789 phosphorylation, IGF-1, and potentially aFGF, LPA, and PMA, were found to positively regulate PTPα Tyr-789 phosphorylation. These inductions occurred in a Src/Fyn/Yes-independent manner, indicating an involvement of likely non-SFK cellular kinases distinct from those involved in integrin-induced PTPα phosphorylation. Although PTPα Tyr-789 phosphorylation mediates integrin-induced cytoskeletal remodeling, this phosphorylation event did not appear to act upstream of the Rho family of small GTPases that are key regulators of cellular actin structures. To further understand the precise action of PTPα Tyr-789 phosphorylation in integrin (and other) signaling pathway, the interaction between the PTPα phospho-Tyr-789 motif and other cellular proteins was investigated. Integrin-induced PTPα Tyr-789 phosphorylation was accompanied by increased Grb2 recruitment to phospho-PTPα which provides for a mechanism by which Grb2-interacting signaling proteins are recruited to PTPα to mediate downstream integrin signaling events. In addition, several proteins representing potential PTPα phospho-Y789 interacting proteins were isolated by (phospho)peptide affinity purification. The identification of these proteins and validation of their interactions with PTPα may reveal the precise signaling role of PTPα Tyr-789 phosphorylation.
Medicine, Faculty of
Pathology and Laboratory Medicine, Department of
Graduate
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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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Fustier, Caroline. "Tyrosinase nanocapsules for the lowering of systemic tyrosine for the treatment of melanoma." Thesis, McGill University, 2007. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=18429.

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This study describes the preparation and characterization of biodegradable nano-artificial cells containing the enzyme tyrosinase. The rationale for doing this is that this may have potential implication for the treatment of melanoma, a fatal skin tumour that is tyrosine-dependent. A poly (ethylene glycol)- poly (lactic acid) block-copolymer has been prepared and characterized. A method for the preparation of the tyrosinase nanocapsules has been designed. The physical properties and the membrane properties of the nanocapsules have been characterized. The electron microscopy images show round and unaggregated nanocapsules. The average size of these nanocapsules can be controlled by modifying the stirring speed. Studies on the enzymatic properties show that tyrosinase can be nanoencapsulated without being inactivated. Nanoencapsulated tyrosinase is stable for several weeks when stored at 4ºC. Nanoencapsulation greatly increases the stability of tyrosinase at 37ºC. In vivo studies show that one intravenous injection of tyrosinase nanocapsules can effectively and quickly decrease the systemic tyrosine level to very low levels.
Cette thèse décrit la préparation et la caractérisation de nano-cellules artificielles biodégradables contenant l'enzyme tyrosinase. La raison de cette étude est la possibilité d'application au traitement du mélanome, un cancer de la peau mortel. Un copolymère de polyethylène glycol et d'acide polylactique a été préparé et caractérisé. Une méthode pour la préparation des nanocapsules de tyrosinase a été mise au point. Les propriétés physiques des nanocapsules ainsi que les propriétés de leur membrane ont été étudiées. Les images prises à l'aide de microscopes à électrons montrent des nanocapsules rondes et qui ne s'agrègent pas. La taille moyenne des nanocapsules peut être contrôlée en modifiant la vitesse de l'agitateur magnétique lors de leur préparation. L'étude de l'activité enzymatique montre que la tyrosinase peut être nano-encapsulée sans être inactivée. La tyrosinase dans les nanocapsules est stable pendant plusieurs semaines à 4ºC. La nano-encapsulation augmente fortement la stabilité de la tyrosinase à 37ºC. Les expériences in vivo montrent que les niveaux de tyrosine circulant peuvent être réduits efficacement et rapidement avec une injection intraveineuse de ces nanocapsules contenant de l'enzyme tyrosinase. fr
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Sun, Guobin. "The role of protein tyrosine phosphatase alpha tyrosine 789 phosphorylation in integrin signaling." Thesis, University of British Columbia, 2013. http://hdl.handle.net/2429/43924.

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Focal adhesions (FA) form interfaces between the extracellular matrix and the cytoskeleton to regulate cell responses such as cell proliferation, survival, and migration. The functions and dynamic interactions of many of the ~180 molecules in this integrin-initiated FA complex network are far from fully understood. Among these is the receptor-like protein tyrosine phosphatase PTPα. In addition to the integrin-proximal action of PTPα to catalyze activation of Src family kinases, subsequent phosphorylation of PTPα at its C-terminal Tyr789 site is essential and acts in an unknown manner to promote cell spreading and migration. We used reconstitution assays in PTPα-null cells to identify and distinguish integrin signaling events that were PTPα-dependent and PTPα-Tyr789-dependent. Results show that PTPα-Tyr789 mediates the localization of PTPα and the scaffolding protein Cas to FAs where Cas interacts with and gets phosphorylated by Src to initiate Cas/Crk-Rac/Cdc42-PAK signaling. Linking these events, this study identifies the Cas-binding protein BCAR3 as a molecular connector of PTPα and Cas, with phosphoTyr789-PTPα interacting with the BCAR3 SH2 domain to recruit BCAR3-Cas to newly forming adhesion sites. These findings identify phospho-Tyr789-PTPα as the first cellular ligand for the SH2 domain of BCAR3, and reveal a role of PTPα in integrin-induced adhesion complex assembly that enables Src-mediated activation of the pivotal function of Cas in cell migration. Furthermore I extended this study into a cancer cell model by showing that the disruption of this PTPα-BCAR3-Cas-Src signaling module inhibits the invasive motility in a rhabdomyosarcoma cell line. In summary, my results in this thesis elucidate the molecular mechanism underlying the PTPα-Tyr789-dependent cell spreading and migration, and support that the PTPα-BCAR3-Cas complex is a critical regulator of cell migration as well as cancer cell invasion and metastasis.
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Mehere, Prajwalini V. "Towards the Characterization of Enzymes Involved in the Metabolism of Tyrosine and Tyrosine Derivatives." Diss., Virginia Tech, 2010. http://hdl.handle.net/10919/77289.

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Tyrosine is involved in many biological processes including protein synthesis. This dissertation is focused on two different aspects: tyrosine catabolism and tyrosine derivative metabolism. Tyrosine undergoes degradation via tyrosine aminotransferase (TAT). Deficiency of TAT leads to some disease conditions or tyrosinemia type II. TAT has been characterized in several species, including humans. Mouse tyrosine aminotransferase was used as a model protein for the tyrosine catabolism portion of this study. Characterization of TAT included its expression in a bacterial expression system, purification using various chromatographic techniques, crystallization under different conditions, and its kinetic analysis, and molecular dynamics simulations. Based on sequence, structure, and kinetic data we have shown that mouse TAT behaves like human TAT. Our crystallization studies added new insights into the mechanism of TAT by shedding light on involvement of a disulfide bond in the regulation of mTAT. Molecular dynamics analysis provided perspective on the differences (preferences) in the substrate specificities of mouse and Trypanosome cruzi TAT. Tyrosine is a precursor of several key neurotransmitters. These neurotransmitters must be regulated in order to function properly. The hypothetical N-acetyltransferases from Aedes aegypti were used as model proteins for investigation of tyrosine derivative metabolism. We found nine potential arylalkylamine N-acetyltransferase (AANAT) genes in Ae. aegypti. Phylogenetic analysis suggests that these Ae. aegypti AANATs (AeAANATs) can be further divided into three clusters. Phylogenetic analysis suggests that insect AANATs may have different functions as compared with the mammalian AANATs, for which function is specific to circadian rhythm regulation. PCR amplification indicates that eight of the nine putative AeAANATs are expressed in the mosquito. Expression of the eight putative AeAANATs and substrate screening of their recombinant proteins against dopamine, octopamine, tyramine, epinephrine, tryptamine, 5-hydroxytryptamine, and methoxytryptamine established that five of the eight putative AeAANATs are true AANATs. The discontinuous expression profiles of AeAANAT genes were studied in detail. Six of the AeAANATs were expressed in the head before and after blood feeding, suggesting their potential role in neurotransmission inactivation. Down-regulation of these genes after blood feeding suggests that blood feeding or factors related to blood feeding impact on the regulation of these genes. Kinetic studies determined that two AeAANAT proteins are highly efficient in mediating the acetylation of dopamine and 5-hydroxytryptamine. Substrate analysis of AeAANATs supports the notion that acetylation of arylalkylamines is vital to the biology of mosquito species, and that these genes emerged in response to specific pressures related to necessities for biogenic amine acetylation.
Ph. D.
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Veenstra, Cynthia. "The receptor tyrosine kinase Met and the protein tyrosine phosphatase PTPN2 in breast cancer." Doctoral thesis, Linköpings universitet, Avdelningen för kliniska vetenskaper, 2017. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-135047.

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Breast cancer is the most common form of cancer in women worldwide and the second leading cause of cancer death. It is a heterogeneous disease and is subdivided into different subtypes, all with different treatment responses and survival outcomes. Luminal breast cancers are characterised by the expression of oestrogen receptor and generally have a good prognosis. More aggressive tumours are marked by the presence of growth stimulating receptor tyrosine kinase HER2 (HER2-like breast cancer) or the absence of oestrogen receptor, progesterone receptor, and HER2 (triple-negative breast cancer,TNBC). The latter is the most aggressive form and is difficult to treat due to lack of treatment targets. This thesis aimed to explore possible prognostic and predictive biomarkers in different subtypes and study their role in breast cancer. To this aid, breast cancer tumours of pre- and post-menopausal patients enrolled in two cohorts were analysed for gene copy numbers and expression of proteins involved in cell proliferation. Gene copy numbers of receptor tyrosine kinases MET and EGFR, Met’s ligand HGF, and protein tyrosine phosphatase PTPN2 were determined by droplet digital PCR or quantitative PCR in both cohorts. Met, phosphorylated Met (pMet), HGF, and PTPN2 protein expression levels were analysed with immunohistochemical staining in the pre-menopausal cohort. Moreover,the role of the aforementioned proteins was investigated in breast cancer cell lines. Amplification of MET, HGF, and EGFR in breast tissues was found to be low (5-8%). These three genes, all located on chromosome 7, were found to be strongly correlated with eachother and to be associated with shortened distant recurrence-free survival. High protein expression of Met, pMet, and HGF was found in 33%, 53%, and 49% of the breast tumours. MET and EGFR were found to be more often amplified in TNBC disease, correlating with worse survival. Moreover, stromal expression of HGF was associated with shorter survival in TNBC. EGF stimulation in TNBC cell line MDA-MB-468 led to inhibited cell proliferation and migration. Partial knockdown of EGFR caused TNBC cells to proliferate and migrate more upon EGF treatment, mirroring EGFR inhibitor resistance. Knockdown of Met had in part the opposite effects, indicating that Met inhibitors might be useful in the treatment of TNBC. The increase in proliferation and migration upon EGFR depletion could be counteracted with simultaneous knockdown of EGFR and Met, indicating that dual inhibition of these proteins might be a future treatment option in TNBC. Copy loss of PTPN2 was reported in 15% of the cases in both pre- and post-menopausal cohorts. Low cytoplasmic PTPN2 protein expression was found in half of the cases. Loss of PTPN2 gene or protein was associated with a shorter distant recurrence-free survival in Luminal A and HER2-positive tumours, not in TNBC, suggesting a subtype-related prognostic value of PTPN2. Subtype relevance of PTPN2 was further implied by in vitro analyses. Whereas PTPN2 knockdown had no observed effect on TNBC cell lines, knockdown in the Luminal A cell line MCF7 inhibited Met phosphorylation and promoted phosphorylation of Akt, a key regulator of cellular proliferation and survival. The cell growth and survival regulating RAS/MAPK pathway remained unaffected. Knockdown in the HER2-positive cell line SKBR3 led to increased Met phosphorylation and decreased RAS/MAPK-related Erk phosphorylation as well as EGF-mediated transcription factor STAT3 phosphorylation. These results indicate that the role of PTPN2 in breast cancer is subtype-related and needs to be further investigated for future treatment options.
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Books on the topic "Tyrosine"

1

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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Goldstein, Barry J. Tyrosine phosphoprotein phosphatases. 2nd ed. Oxford: Oxford University Press, 1998.

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Germano, Serena, ed. Receptor Tyrosine Kinases. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-1789-1.

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Pulido, Rafael, ed. Protein Tyrosine Phosphatases. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3746-2.

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Barker, Iain F. Studies on tyrosine metabolism. [s.l.]: typescript, 1987.

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

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Daëron, Marc, and Eric Vivier, eds. Immunoreceptor Tyrosine-based Inhibition Motifs. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-58537-1.

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Neel, Benjamin G., and Nicholas K. Tonks, eds. Protein Tyrosine Phosphatases in Cancer. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3649-6.

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Focosi, Daniele, ed. Resistance to Tyrosine Kinase Inhibitors. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-46091-8.

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Goldstein, Barry J. Phosphoprotein phosphatases 1: tyrosine phosphatases. London: Academic Press, 1995.

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Book chapters on the topic "Tyrosine"

1

Bährle-Rapp, Marina. "Tyrosine." In Springer Lexikon Kosmetik und Körperpflege, 569. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_10824.

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Kobayashi, Kensei. "Tyrosine." In Encyclopedia of Astrobiology, 1715. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-11274-4_1624.

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Kobayashi, Kensei. "Tyrosine." In Encyclopedia of Astrobiology, 2560. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_1624.

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Colzato, Lorenza S. "Tyrosine." In Theory-Driven Approaches to Cognitive Enhancement, 5–15. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-57505-6_1.

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Kvittingen, E. A., P. T. Clayton, and J. V. Leonard. "Tyrosine." In Inborn Metabolic Diseases, 161–66. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-662-03147-6_13.

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Kobayashi, Kensei. "Tyrosine." In Encyclopedia of Astrobiology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27833-4_1624-5.

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Penney, Christopher. "Stearyl Tyrosine." In Vaccine Design, 611–24. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1823-5_26.

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Holme, Elisabeth, and Grant A. Mitchell. "Tyrosine Metabolism." In Physician's Guide to the Diagnosis, Treatment, and Follow-Up of Inherited Metabolic Diseases, 23–31. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-40337-8_2.

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Bährle-Rapp, Marina. "Oleoyl Tyrosine." In Springer Lexikon Kosmetik und Körperpflege, 387. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_7144.

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Schomburg, Dietmar, and Margit Salzmann. "Tyrosine decarboxylase." In Enzyme Handbook 1, 99–102. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_23.

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Conference papers on the topic "Tyrosine"

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Pakhomov, V. I., D. V. Rudoy, T. A. Maltseva, N. A. Kulikova, and N. T. Ugrekhelidze. "ANALYSIS OF THE INFLUENCE OF MICROWAVE PROCESSING ON THE CONTENT OF NON-REPLACEABLE AMINO ACIDS IN COMBINE FEEDS." In INNOVATIVE TECHNOLOGIES IN SCIENCE AND EDUCATION. DSTU-Print, 2020. http://dx.doi.org/10.23947/itno.2020.34-37.

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The article presents the results of a study of the effect of micronization of feed samples on proteinogenic amino acids, such as: arginine, lysine, tyrosine, phenylalanine, histidine, leucine-isoleucine, methionine, valine, proline, tyrosine, serine, alanine. The optimal parameters of the micronization of compound feeds are substantiated in order to increase the digestibility of compound feeds and disinfection.
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Ludwig, M., and S. A. Asher. "UV Resonance Raman Studies of Aromatic Amino Acids and Proteins." In Laser Applications to Chemical Analysis. Washington, D.C.: Optica Publishing Group, 1987. http://dx.doi.org/10.1364/laca.1987.pdp3.

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The ultraviolet resonance Raman (UVRR) excitation profiles have been measured for the aromatic amino acids phenylalanine, tryptophan, tyrosine and tyrosinate. Resonance excitation enhances Raman scattering from vibrational modes that distort the ground state configuration towards the configuration of the excited state. The excitation profile maxima are red-shifted with respect to the absorption spectral maxima for each aromatic amino acid. These excitation profiles indicate the excitation required to maximally enhance a particular aromatic amino acid residue in a protein. Individual aromatic amino acids in environmentally distinguishable positions in a protein may have slightly different transition energies, and could therefore be identified and distinguished by proper tuning of the excitation frequency. For example, surface tyrosyl residues in hydrophilic environments will have lower lying excited states due to extensive hydrogen bonding. These residues will be maximally enhanced with longer wavelength excitation than residues buried in hydrophobic pockets within a protein. The frequency of certain vibrational bands, particularly those known to be influenced by substituents on the aromatic ring may also be indicative of the local environment. The relative intensities of other enhanced bands may also contain information concerning specific local environment. For example, the relative intensity of the peaks of the 830/850 cm-1 Fermi resonance doublet of tyrosine are known from normal Raman studies to be sensitive to hydgrogen bonding. Vibrational substructure is not observed in absorption spectral measurements due to the breadth of the absorption spectral features. The vibrational substructure is amplified in the resonance Raman excitation profiles.
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Tichý, Tomáš, Karel Pomeisl, Marcela Krečmerová, and Charles E. McKenna. "Tyrosine-based prodrugs of acyclic nucleoside phosphonates." In XVIth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2014. http://dx.doi.org/10.1135/css201414126.

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Abid, H., N. Siddiqui, and V. Thirukonda. "Tyrosine Kinase Inhibitor Induced Interstitial Lung Disease." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a3137.

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Wang, Binghua, Minghui Wang, Yujie Jiang, Dongdong Sun, and Xiaoyi Xu. "Predicting tyrosine phosphorylation from site-modification network." In 2015 34th Chinese Control Conference (CCC). IEEE, 2015. http://dx.doi.org/10.1109/chicc.2015.7260996.

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Nasir, M. N., E. Bergmann, E. Benichou, I. Russier-Antoine, N. Lascoux, Ch Jonin, F. Besson, and P. F. Brevet. "Second harmonic generation from tyrosine containing peptides." In SPIE NanoScience + Engineering, edited by Norihisa Kobayashi, Fahima Ouchen, and Ileana Rau. SPIE, 2013. http://dx.doi.org/10.1117/12.2026866.

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Gueron, Geraldine, Nicolás Anselmino, Paula Chiarella, Emiliano Ortiz, Alejandra Paez, Jimena Giudice, Federico Schuster, et al. "Abstract 4717: Clinical implications for m-tyrosine, an isomer of p-tyrosine, for the treatment of aggressive prostate tumors." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-4717.

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Yang, Hui, Xue Xiao, Xuesong Zhao, and Yan Wu. "Intrinsic Fluorescence Spectra of Tryptophan, Tyrosine and Phenyloalanine." In 5th International Conference on Advanced Design and Manufacturing Engineering. Paris, France: Atlantis Press, 2015. http://dx.doi.org/10.2991/icadme-15.2015.46.

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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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Yang, Hui, Xue Xiao, Xuesong Zhao, and Yan Wu. "Intrinsic fluorescence spectra of tryptophan, tyrosine and phenyloalanine." In Selected Papers of the Chinese Society for Optical Engineering Conferences held October and November 2016, edited by Yueguang Lv, Jialing Le, Hesheng Chen, Jianyu Wang, and Jianda Shao. SPIE, 2017. http://dx.doi.org/10.1117/12.2268397.

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Reports on the topic "Tyrosine"

1

Wirtman, Richard J. Tyrosine, Tryptophan and Performance. Fort Belvoir, VA: Defense Technical Information Center, December 1992. http://dx.doi.org/10.21236/ada266278.

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

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

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

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

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

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

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

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

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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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