• Archives of Pharmacal Research
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• v.29 no.11
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• pp.1006-1017
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• 2006

A series of 3-(substituted-benylidene)-1, 3-dihydro- indolin-2-one, 3-(substituted-benylidene)-1, 3-dihydro- indolin-2-thione and 2, 2'-dithiobis 3-(substituted-benylidene)-1, 3-dihydro-indole derivatives was investigated as inhibitor of $p60^{c-Src}$tyrosine kinase by performing receptor docking studies and inhibitory activity toward tyrosine phosphorylation. Some compounds were shown to be docked at the site, where the selective inhibitor PP1 [1-tert-Butyl-3-p-tolyl-1H-pyrazolo[3,4-d]pyrimidine-4-yl-amine] was embedded at the enzyme active site. Evaluation of all compounds for the interactions with the parameters of lowest binding energy levels, capability of hydrogen bond formations and superimposibility on enzyme active site by docking studies, it can be assumed that 3-(substituted-benzylidene)-1, 3-dihydro-indolin-2-one and thione derivatives have better interaction with enzyme active site then 2, 2'-dithiobis 3-(substituted-benzylidene)-1, 3-dihydro indole derivatives. The test results for the inhibitory activity against tyrosine kinase by Elisa method revealed that 3-(substituted-benylidene)-1, 3-dihydro- indolin-2-thione derivatives have more activity then 3-(substituted-benylidene)-1, 3-dihydro- indolin-2-one derivatives.

• Molecules and Cells
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• v.26 no.4
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• pp.329-337
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• 2008

Src-family kinases are critically involved in the control of cytoskeleton organization and in the generation of integrin-dependent signaling responses, inducing tyrosine phosphorylation of many signaling and cytoskeletal proteins. Activity of the Src family of tyrosine kinases is tightly controlled by inhibitory phosphorylation of a carboxy-terminal tyrosine residue, inducing an inactive conformation through binding with its SH2 domain. Dephosphorylation of C-ter tyrosine, as well as its deletion of substitution with phenylalanine in oncogenic Src kinases, leads to autophosphorylation at a tyrosine in the activation loop, thereby leading to enhanced Src activity. Beside this phophorylation/dephosphorylation circuitry, cysteine oxidation has been recently reported as a further mechanism of enzyme activation. Mounting evidence describes Src activation via its redox regulation as a key outcome in several circumstances, including growth factor and cytokines signaling, integrin-mediated cell adhesion and motility, membrane receptor cross-talk as well in cell transformation and tumor progression. Among the plethora of data involving Src kinase in physiological and pathophysiological processes, this review will give emphasis to the redox component of the regulation of this master kinase.

• The Korean Journal of Zoology
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• v.7 no.1
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• pp.19-22
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• 1964

The free amino acid content of Indian meal moth (Plodia interpunctella HUBNER) was analysed at various developmental stages by means of paper chromatography. 1) The free amino acids : present are alanine , arginine, aspartic acid, glutamic acid, glycine, histidine, leucine, methionine, proline, serine, threonine, tyrosine and valine. 2) Proline was detectable only in the acid-hydrolyzed Indian meal moth. 3) Arginine was clearly detected only in the larva stage. 4) Tyrosine methionine and valine were increased in the pupa stage. 5) Serine, glycine and tyrosine were present in high concentration in all stages.

• Proceedings of the KSAR Conference
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• 2002.06a
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• pp.85-85
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• 2002

As an effort to direct differentiation of human embryonic stem cells (hES, MB03) to dopamine-producing neuronal cells, we expressed Nurr-l in hES and examined the expression of tyrosine hydroxylase (TH) after bFGF induction. To introduce Nurr-l, hES cells were maintained in humidified chamber with 5% CO₂ and 95% air in DMEM/Fl2 supplemented with FBS (10%), penicillin (100U/㎖), and streptomycin (100㎍/㎖). (omitted)

• Archives of Pharmacal Research
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• v.21 no.3
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• pp.330-337
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• 1998

N-(tert-Butoxycarbonyl)-O-(dimethythiophosphono)-L-tyrosine (6) and N-(tert-butoxycarbonyl)-O-(dicyanoethylthiophosphono)-L-tyrosine (15) were prepared as intermediates for the synthesis of thiophosphotyrosine-containing peptides. The reactivity and suitability of two compounds for the solid phase or solution phase peptide synthesis utilizing t-Boc chemistry were examined.

• Annals of Clinical Neurophysiology
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• v.19 no.1
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• pp.74-76
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• 2017

Muscle specific tyrosine kinase (MuSK) myasthenia gravis (MG) is a rare subtype of MG, which is immunologically distinct and differential therapeutic response. Though MG is often associated with other autoimmune disorders or malignancy, concurrence of other disease and MuSK MG has been infrequently reported. We present a patient of MuSK MG associated with multicentric Castelman disease.

• BMB Reports
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• v.43 no.5
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• pp.311-318
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• 2010

This review explored the mechanism of breast carcinoma progression by focusing on integrins and receptor tyrosine kinases (or growth factor receptors). While the primary role of integrins was previously thought to be solely as mediators of adhesive interactions between cells and extracellular matrices, it is now believed that integrins also regulate signaling pathways that control cancer cell growth, survival, and invasion. A large body of evidence suggests that the cooperation between integrin and receptor tyrosine kinase signaling regulates certain signaling functions that are important for cancer progression. Recent developments on the crosstalk between integrins and receptor tyrosine kinases, and its implication in mammary tumor progression, are discussed.

• Tuberculosis and Respiratory Diseases
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• v.79 no.4
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• pp.248-256
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• 2016

Somatic mutations that lead to hyperactivation of epidermal growth factor receptor (EGFR) signaling are detected in approximately 50% of lung adenocarcinoma in people from the Far East population and tyrosine kinase inhibitors are now the standard first line treatment for advanced disease. They have led to a doubling of progression-free survival and an increase in overall survival by more than 2 years. However, emergence of resistant clones has become the primary cause for treatment failure, and has created a new challenge in the daily management of patients with EGFR mutations. Identification of mechanisms leading to inhibitor resistance has led to new therapeutic modalities, some of which have now been adapted for patients with unsuccessful tyrosine kinase inhibitor treatment. In this review, we describe mechanisms of tyrosine kinase inhibitor resistance and the available strategies to overcoming resistance.

• Toxicological Research
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• v.3 no.1
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• pp.9-14
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• 1987

The effects of monosodium glutamate (MSG) on the activities if tyrosine hydroxylase (TH), dopamine ${\beta}$-hydroxylase (DBH), tryptophan hydroxylase (TPH) and monoamine oxidase (MAO) in various regions (cerebral cortex, striatum, midbrain, pons and medulla of nat brain have been determined. It was observed that up to 1mM MSGhad no significant effects on the activities of brain tyrosine hydroxylase, dopamine ${\beta}$-hydroxylase, tryptophan hydroxylase and monoamine oxidase in all regions of rat brain. These results indicated that MSG itself exerted no direct effect on the important enzymes synthsizing and metabolizing the monoaminergic neuronal system.

• BMB Reports
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• v.45 no.12
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• pp.693-699
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• 2012

Together with protein tyrosine kinases (PTKs), protein tyrosine phosphatases (PTPs) serve as hallmarks in cellular signal transduction by controlling the reversible phosphorylation of their substrates. The human genome is estimated to encode more than 100 PTPs, which can be divided into eleven sub-groups according to their structural and functional characteristics. All the crystal structures of catalytic domains of sub-groups have been elucidated, enabling us to understand their precise catalytic mechanism and to compare their structures across all sub-groups. In this review, I describe the structure and mechanism of catalytic domains of PTPs in the structural context.