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Relevant bibliographies by topics / Tyrosine

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Academic literature on the topic 'Tyrosine'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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Journal articles on the topic "Tyrosine"

1

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 (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 do

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Longmore, Gregory D., Yun You, Jaime Molden, et al. "Redundant and Selective Roles for Erythropoietin Receptor Tyrosines in Erythropoiesis In Vivo." Blood 91, no. 3 (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 wel

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Longmore, Gregory D., Yun You, Jaime Molden, et al. "Redundant and Selective Roles for Erythropoietin Receptor Tyrosines in Erythropoiesis In Vivo." Blood 91, no. 3 (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 repl

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Hansen, J. A., L. H. Hansen, X. Wang, et al. "The role of GH receptor tyrosine phosphorylation in Stat5 activation." Journal of Molecular Endocrinology 18, no. 3 (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 S

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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 (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 d

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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 (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 whic

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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 (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 grow

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GIBSON, Spencer, Ken TRUITT, Yiling LU, et al. "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 (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 intracellula

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Zhang, Juan, Teruaki Kimura, and Reuben P. Siraganian. "Mutations in the Activation Loop Tyrosines of Protein Tyrosine Kinase Syk Abrogate Intracellular Signaling But Not Kinase Activity." Journal of Immunology 161, no. 8 (1998): 4366–74. http://dx.doi.org/10.4049/jimmunol.161.8.4366.

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Abstract The protein tyrosine kinase Syk plays a pivotal role in mediating the high-affinity IgE receptor (FcεRI)-induced degranulation of mast cells. To examine the mechanism of Syk regulation, the two tyrosine residues at 519 and 520 in the putative activation loop of rat Syk were mutated to phenylalanine either singly or in combination. The various mutants were expressed in a Syk-negative variant of the RBL-2H3 (rat basophilic leukemia 2H3) mast cell line. In these transfected cell lines, mutant Syk did show increased tyrosine phosphorylation in vivo and increased enzymatic activity in vitr

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King, P. D., A. Sadra, J. M. Teng, et al. "Analysis of CD28 cytoplasmic tail tyrosine residues as regulators and substrates for the protein tyrosine kinases, EMT and LCK." Journal of Immunology 158, no. 2 (1997): 580–90. http://dx.doi.org/10.4049/jimmunol.158.2.580.

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Abstract The CD28 cell surface receptor provides an important costimulatory signal for T cells necessary for their response to Ag. Early events in CD28 signaling include recruitment and activation of phosphatidylinositol 3-kinase (PI3-kinase) and activation of the protein tyrosine kinases (PTKs), LCK and EMT. Recruitment and activation of PI3-kinase is known to be dependent upon phosphorylation of tyrosine 173 of the CD28 cytoplasmic tail contained within a YMNM motif. By contrast, little is known of which residues of the CD28 tail, including tyrosines, are required for the activation of PTKs.

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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. Ty

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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

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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 a

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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 promot

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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, purificat

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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

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Books on the topic "Tyrosine"

1

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

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

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Germano, Serena, ed. Receptor Tyrosine Kinases. 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. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3746-2.

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Thévenin, Damien, and Jörg P. Müller, eds. Protein Tyrosine Phosphatases. Springer US, 2024. http://dx.doi.org/10.1007/978-1-0716-3569-8.

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

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Barker, Iain F. Studies on tyrosine metabolism. typescript, 1987.

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Daëron, Marc, and Eric Vivier, eds. Immunoreceptor Tyrosine-based Inhibition Motifs. 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. 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. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-46091-8.

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Book chapters on the topic "Tyrosine"

1

Bährle-Rapp, Marina. "Tyrosine." In Springer Lexikon Kosmetik und Körperpflege. 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. 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. Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_1624.

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Kobayashi, Kensei. "Tyrosine." In Encyclopedia of Astrobiology. Springer Berlin Heidelberg, 2023. http://dx.doi.org/10.1007/978-3-662-65093-6_1624.

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Colzato, Lorenza S. "Tyrosine." In Theory-Driven Approaches to Cognitive Enhancement. 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. 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. 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. 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. 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. Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_7144.

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Conference papers on the topic "Tyrosine"

1

Devarakonda, Shanmukha Sreeya, Shaik Basha, Anjana Pithakumar, et al. "Probing the Peroxynitrite-Induced Nitration of Proteins by Autofluorescence and FTIR Spectroscopy." In Frontiers in Optics. Optica Publishing Group, 2024. https://doi.org/10.1364/fio.2024.jd4a.67.

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Protein tyrosine nitration can cause alterations in protein structure and function, which can impact cell homeostasis. The current study investigates the structural alterations of proteins induced by Peroxynitrite in vitro using autofluorescence and FTIR spectroscopy.

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Unsal, Tuba, Di Wang, Tingyue Gu, Sith Kumseranee, and Suchada Punpruk. "Enhanced Biocide Treatment Using D-tyrosine against Desulfovibrio Vulgaris Corrosion of Carbon Steel." In CORROSION 2020. NACE International, 2020. https://doi.org/10.5006/c2020-14527.

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Abstract Biocides are used to control problematic microorganisms in the oil and gas industry. High doses of biocides cause environmental and operational problems. Therefore, using biocide enhancers to make biocides more effective is highly desirable. 2,2-dibromo-3-nitrilopropionamide (DBNPA) is a popular biocide because it is broad-spectrum, effective, kills microorganisms immediately upon addition, and it degrades rapidly. D-amino acids are natural chemicals that have been used in lab tests to enhance biocides to treat biofilms. In this work, D-tyrosine was used to enhance DBNPA against Desul

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Ivanović-Šašić, Ana, Stevan Maćešić, Jelena Maksimović, Željko Čupić, and Ljiljana Kolar-Anić. "Numerical simulations of the oscillatory dynamics in the Bray-Liebhafsky reaction perturbed by L-tyrosine." In 2nd International Conference on Chemo and Bioinformatics. Institute for Information Technologies, University of Kragujevac, 2023. http://dx.doi.org/10.46793/iccbi23.609is.

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It is well known that almost all living or biological systems are naturally in the oscillatory dynamic states and can be considered as biochemical reaction systems. These oscillatory dynamic states can be caused by internal self-organized phenomena, but also by external periodic variations of temperature, light, food, or seasonal changes. The hypothalamic-pituitary-thyroid (HPT) axis is one such nonlinear system with feedback that is always in an oscillatory dynamic state and L-tyrosine is its main representative. The biological importance of L-tyrosine interactions with iodine species was the

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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. 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 a

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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. 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, et al. "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, 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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Reports on the topic "Tyrosine"

1

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

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

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

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

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

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

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

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

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

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

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