Search results for "Tyrosine"

showing 4 items of 644 documents

Safety of Tyrosine Kinase Inhibitors in Patients With Differentiated Thyroid Cancer: Real-World Use of Lenvatinib and Sorafenib in Korea

2019

Background: Thyroid cancer has become the most common cancer in Korea. Generally, thyroid cancer patients have a good prognosis; however, 15–20% of patients experience recurrence or distant metastasis or are refractory to standard treatment. We assessed the safety of sorafenib and lenvatinib in patients with advanced or metastatic radioactive iodine-refractory differentiated thyroid cancers (DTC) consecutively treated at a tertiary center in South Korea.Methods: We retrospectively reviewed the charts of all consecutive patients with DTC treated during ≥6 months with lenvatinib (February 2016–April 2018) and sorafenib (January 2014–April 2018) at Gangnam Severance Hospital. Patients were tre…

safety0301 basic medicineSorafenibmedicine.medical_specialtyEndocrinology Diabetes and Metabolismdifferentiated thyroid cancerrefractory thyroid cancer030209 endocrinology & metabolismlenvatiniblcsh:Diseases of the endocrine glands. Clinical endocrinologyGastroenterologyPapillary thyroid cancer03 medical and health scienceschemistry.chemical_compoundEndocrinology0302 clinical medicineInternal medicinetyrosine kinase inhibitorsmedicineAdverse effectFollicular thyroid cancerThyroid cancerOriginal Researchlcsh:RC648-665business.industryStandard treatmentCancermedicine.disease030104 developmental biologychemistryadverse effectschart reviewsorafenibbusinessLenvatinibmedicine.drugFrontiers in Endocrinology
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Protein tyrosine nitration and thiol oxidation by peroxynitrite-strategies to prevent these oxidative modifications.

2013

The reaction product of nitric oxide and superoxide, peroxynitrite, is a potent biological oxidant. The most important oxidative protein modifications described for peroxynitrite are cysteine-thiol oxidation and tyrosine nitration. We have previously demonstrated that intrinsic heme-thiolate (P450)-dependent enzymatic catalysis increases the nitration of tyrosine 430 in prostacyclin synthase and results in loss of activity which contributes to endothelial dysfunction. We here report the sensitive peroxynitrite-dependent nitration of an over-expressed and partially purified human prostacyclin synthase (3.3 μM) with an EC50 value of 5 μM. Microsomal thiols in these preparations effectively co…

thiol oxidationprotein tyrosine nitrationlcsh:Chemistrychemistry.chemical_compoundCytochrome P-450 Enzyme SystemSf9 CellsTyrosinelcsh:QH301-705.5Spectroscopychemistry.chemical_classification0303 health sciencesbiologySuperoxide030302 biochemistry & molecular biologyGeneral MedicineComputer Science ApplicationsIntramolecular OxidoreductasesBiochemistryThiolprostacyclin synthasesuperoxideOxidation-ReductionPeroxynitriteOxidative phosphorylationSpodopteraCatalysisArticleperoxynitriteNitric oxideProstacyclin synthaseInorganic Chemistry03 medical and health sciencesnitric oxideddc:570NitrationPeroxynitrous AcidAnimalsHumansSulfhydryl CompoundsPhysical and Theoretical ChemistryMolecular Biology030304 developmental biologyOrganic Chemistrynitric oxide; superoxide; peroxynitrite; protein tyrosine nitration; thiol oxidation; peroxynitrite scavengers; prostacyclin synthasechemistrylcsh:Biology (General)lcsh:QD1-999biology.proteinTyrosineCattleperoxynitrite scavengersProtein Processing Post-TranslationalInternational journal of molecular sciences
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Effect of ligand-binding on protein function

2014

tietokonesimulointifilamiinitliganditsitoutuminenionotrooppiset glutamaattireseptoritfilaminpeptidiliganditmolecular dynamicsionotropic glutamate receptorlääkesuunnitteluFLNaiGluRlaskennallinen tiedelaskennalliset menetelmätmolekyylidynamiikkaTCPTPsimulointiproteiinitbinding free energyT-cell protein tyrosine phosphatase
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Yeast vectors for the integration/expression of any sequence at the TYRI locus

2007

We have constructed new yeast vectors for targeted integration and conditional expression of any sequence at the Saccharomyces cerevisiae TYR1 locus which becomes disrupted. We show that vector integration is not neutral, causing prototrophy for tyrosine and auxotrophy for the vector's selectable marker (uracil or leucine, depending on the vector used). This feature allows a double screening of transformed yeast cells, improving the identification of colonies with the desired chromosomal structure. The GAL10 gene promoter has been added to drive conditional expression of cloned sequences. Using these vectors, chromosomal structure verification of recombinant clones is no longer necessary, s…

yeast molecular biology tyrosine
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