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Relevant bibliographies by topics / TYROSINE KINASE ASSAY

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Journal articles

Academic literature on the topic 'TYROSINE KINASE ASSAY'

Author: Grafiati

Published: 11 March 2023

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Journal articles on the topic "TYROSINE KINASE ASSAY"

1

Tyner, Jeffrey W., Stephanie Willis, Michael W. N. Deininger, and Brian J. Druker. "RNAi Functional Screening of the Tyrosine Kinome Identifies Therapeutic Targets in Acute Myeloid Leukemia Patients." Blood 110, no. 11 (2007): 208. http://dx.doi.org/10.1182/blood.v110.11.208.208.

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Abstract A large percentage of cancer cases present without knowledge of the causative genetic events. Tyrosine kinases are frequently implicated in the pathogenesis of cancer, but identification of specific tyrosine kinases as cancer targets has been a slow process. Tyrosine kinases are thought to play a causative role in acute myeloid leukemia (AML), based in part on the high percentage of cases with phosphorylation of STAT5—a marker for activity of tyrosine kinase signaling. However, known abnormalities in tyrosine kinases in AML are restricted to internal tandem duplications of FLT3 or gen

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2

Pritz, Stephan, Gabriele Meder, Klaus Doering, et al. "A Fluorescence Lifetime-Based Assay for Abelson Kinase." Journal of Biomolecular Screening 16, no. 1 (2010): 65–72. http://dx.doi.org/10.1177/1087057110385817.

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We present a novel homogeneous in vitro assay format and apply it to the quantitative determination of the enzymatic activity of a tyrosine kinase. The assay employs a short peptidic substrate containing a single tyrosine and a single probe attached via a cysteine side chain. The structural flexibility of the peptide allows for the dynamic quenching of the probe by the nonphosphorylated tyrosine side chain. The probe responds with changes in its fluorescence lifetime depending on the phosphorylation state of the tyrosine. We use this effect to directly follow the enzymatic phosphorylation of t

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3

Lebakken, Connie S., Hee Chol Kang, and Kurt W. Vogel. "A Fluorescence Lifetime–Based Binding Assay to Characterize Kinase Inhibitors." Journal of Biomolecular Screening 12, no. 6 (2007): 828–41. http://dx.doi.org/10.1177/1087057107304480.

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The authors present a fluorescence lifetime—based kinase binding assay that identifies and characterizes compounds that bind to the adenosine triphosphate (ATP)—binding pocket of a range of tyrosine and serine/threonine kinases. The assay is based on displacement of an Alexa Fluor® 647 conjugate of staurosporine from the ATP-binding site of a kinase, which is detected by a change in the fluorescence lifetime of the probe between the free (displaced) and kinase-bound states. The authors screened 257 kinases for specific binding and displacement of the Alexa Fluor® 647-staurosporine probe and fo

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4

Kobayashi, Tomoko, Shun-Ichi Nakamura, and Hirohei Yamamura. "Cytosolic Protein-Tyrosine Kinase Activities in Various Rat Tissues." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 26, no. 2 (1989): 164–68. http://dx.doi.org/10.1177/000456328902600213.

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Suitable assay conditions for the detection of cytosolic protein-tyrosine kinase activities in crude extracts of various rat tissues have been determined. Cytosolic protein-tyrosine kinases showed common characteristics including substrate specificity and divalent cation requirement. Using (Val5) angiotensin II and Mn2+ rather than a src-related synthetic peptide, E11G1, and Mg2+, we obtained higher activities of cytosolic protein-tyrosine kinases. Among various rat tissues tested, spleen, bone marrow, thymus, small intestine, appendix and lung, in decreasing order of total activity, contained

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5

Tyner, Jeffrey W., Denise K. Walters, Stephanie G. Willis, et al. "RNAi screening of the tyrosine kinome identifies therapeutic targets in acute myeloid leukemia." Blood 111, no. 4 (2008): 2238–45. http://dx.doi.org/10.1182/blood-2007-06-097253.

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Despite vast improvements in our understanding of cancer genetics, a large percentage of cancer cases present without knowledge of the causative genetic events. Tyrosine kinases are frequently implicated in the pathogenesis of numerous types of cancer, but identification and validation of tyrosine kinase targets in cancer can be a time-consuming process. We report the establishment of an efficient, functional screening assay using RNAi technology to directly assess and compare the effect of individually targeting each member of the tyrosine kinase family. We demonstrate that siRNA screening ca

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6

Wu, Jinzi J., Donna R. Yarwood, Quynhchi Pham, and Matthew A. Sills. "Identification of a High-Affinity Anti-Phosphoserine Antibody for the Development of a Homogeneous Fluorescence Polarization Assay of Protein Kinase C." Journal of Biomolecular Screening 5, no. 1 (2000): 23–30. http://dx.doi.org/10.1177/108705710000500106.

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In the last few years, fluorescence polarization (FP) has been applied to the development of robust, homogeneous, high throughput assays in molecular recognition research, such as ligand-protein interactions. Recently, this technology has been applied to the development of homogeneous tyrosine kinase assays, since there are high-affinity anti-phosphotyrosine antibodies available. Unlike tyrosine kinases, application of FP to assay development for serine/threonine kinases has been impeded because of lack of high-affinity anti-phosphoserine/threonine antibodies. In the present study, we report t

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7

Tyner, Jeffrey W., Luke Fletcher, Wayne Yang, et al. "Development of a Small-Molecule Inhibitor Screen to Rapidly Identify Key Signaling Pathways in Leukemogenesis." Blood 114, no. 22 (2009): 708. http://dx.doi.org/10.1182/blood.v114.22.708.708.

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Abstract Abstract 708 Aberrantly activated tyrosine kinases and their associated signaling pathways are critical to leukemogenesis and primary acute myeloid leukemia (AML) cell viability. While aberrant kinase activation has been confirmed in a significant percentage of AML, constitutive phosphorylation of STAT5, a marker of tyrosine kinase activation, is present in the majority of AML samples indicating that as yet unidentified tyrosine kinases can be aberrantly activated and contribute to leukemogenesis. Efforts to identify activating tyrosine kinase mutations using high-throughput sequencin

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8

Nakayama, Grace R., Michael P. Nova, and Zahra Parandoosh. "A Scintillating Microplate Assay for the Assessment of Protein Kinase Activity." Journal of Biomolecular Screening 3, no. 1 (1998): 43–48. http://dx.doi.org/10.1177/108705719800300106.

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Protein kinases, a class of enzymes that phosphorylate certain tyrosine, serine, and threonine residues, play an important role in cellular functions and are important targets in drug discovery research. Thus, it is of interest to develop a simple assay that can be used to measure protein kinase activity toward specific substrates and is suitable for the high throughput screening (HTS) of potential kinase inhibitors. The scintillation proximity concept has been successfully applied for measuring specific kinase activity using surfaces passively coated with a peptide substrate. In this study, w

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9

Binns, Kathleen L., Paul P. Taylor, Frank Sicheri, Tony Pawson, and Sacha J. Holland. "Phosphorylation of Tyrosine Residues in the Kinase Domain and Juxtamembrane Region Regulates the Biological and Catalytic Activities of Eph Receptors." Molecular and Cellular Biology 20, no. 13 (2000): 4791–805. http://dx.doi.org/10.1128/mcb.20.13.4791-4805.2000.

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ABSTRACT Members of the Eph family of receptor tyrosine kinases exhibit a striking degree of amino acid homology, particularly notable in the kinase and membrane-proximal regions. A mutagenesis approach was taken to address the functions of specific conserved tyrosine residues within these catalytic and juxtamembrane domains. Ligand stimulation of wild-type EphB2 in neuronal NG108-15 cells resulted in an upregulation of catalytic activity and an increase in cellular tyrosine phosphorylation, accompanied by a retraction of neuritic processes. Tyrosine-to-phenylalanine substitutions within the c

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10

Rivard, N., G. Rydzewska, J. S. Lods, and J. Morisset. "Novel model of integration of signaling pathways in rat pancreatic acinar cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 269, no. 3 (1995): G352—G362. http://dx.doi.org/10.1152/ajpgi.1995.269.3.g352.

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Cholecystokinin (CCK) is the major pancreatic secretagogue and acinar cell mitogen. This study was performed to determine by which effector systems CCK regulates tyrosine kinases, phosphatidylinositol (PtdIns) 3-kinase, and phospholipase D (PLD) activities. Pancreatic acini loaded with [3H]myristic acid or [3H]inositol were used to assay PLD and PtdIns 3-kinase. G protein activation with NaF increased particulate and crude cytosolic tyrosine kinase and PLD activities. PLD activation was pertussis toxin sensitive. Inhibition of phospholipase C (PLC) slightly reduced caerulein-stimulated particu

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