Relevant bibliographies by topics / Tyrosine oxidation

Academic literature on the topic 'Tyrosine oxidation'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Tyrosine oxidation"

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Naish-Byfield, S., and P. A. Riley. "Oxidation of monohydric phenol substrates by tyrosinase. An oximetric study." Biochemical Journal 288, no. 1 (November 15, 1992): 63–67. http://dx.doi.org/10.1042/bj2880063.

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The purity of commercially available mushroom tyrosinase was investigated by non-denaturing PAGE. Most of the protein in the preparation migrated as a single band under these conditions. This band contained both tyrosinase and dopa oxidase activity. No other activity of either classification was found in the preparation. Oxygen consumption by tyrosinase during oxidation of the monohydric phenol substrates tyrosine and 4-hydroxyanisole (4HA) was monitored by oximetry in order to determine the stoichiometry of the reactions. For complete oxidation, the molar ratio of oxygen: 4HA was 1:1. Under identical conditions, oxidation of tyrosine required 1.5 mol of oxygen/mol of tyrosine. The additional oxygen uptake during tyrosine oxidation is due to the internal cyclization of dopaquinone to form cyclodopa, which undergoes a redox reaction with dopaquinone to form dopachrome and dopa, which is then oxidized by the enzyme, leading to an additional 0.5 mol of oxygen/mol of original substrate. Oxygen consumption for complete oxidation of 200 nmol of 4HA was constant over a range of concentrations of tyrosinase of 33-330 units/ml of substrate. The maximum rate of reaction was directly proportional to the concentration of tyrosinase, whereas the length of the lag phase decreased non-linearly with increasing tyrosinase concentration. Activation of the enzyme by exposure to citrate was not seen, nor was the lag phase abolished by exposure of the enzyme to low pH. Michaelis-Menten analysis of tyrosinase in which the lag phase is abolished by pre-exposure of the enzyme to a low concentration of dithiothreitol gave Km values for tyrosine and 4HA of 153 and 20 microM respectively.
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Sun, Biyun, A. Daryl Ariawan, Holly Warren, Sophia C. Goodchild, Marc in het Panhuis, Lars M. Ittner, and Adam D. Martin. "Programmable enzymatic oxidation of tyrosine–lysine tetrapeptides." Journal of Materials Chemistry B 8, no. 15 (2020): 3104–12. http://dx.doi.org/10.1039/d0tb00250j.

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Fmoc-capped tetrapeptides bearing two lysines and two tyrosines show programmable enzymatic activity. Solvent accessible tyrosines determine the extent of reactivity with tyrosinase, and subsequent quinone formation drives polymerisation.
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Nirmala, N. Baby, and P. Vani P. Vani. "Oxidation of L-Tyrosine by Tetrachloroaurate(III) – a Kinetic Study." International Journal of Scientific Research 2, no. 4 (June 1, 2012): 25–27. http://dx.doi.org/10.15373/22778179/apr2013/11.

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Moller, Matias N., Duane M. Hatch, Hye-Young H. Kim, and Ned a. Porter. "Tyrosine Oxidation-Derived Electrophiles." Free Radical Biology and Medicine 51 (November 2011): S148. http://dx.doi.org/10.1016/j.freeradbiomed.2011.10.254.

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Mariano, Alessia, Irene Bigioni, Anna Scotto d’Abusco, Alessia Baseggio Conrado, Simonetta Maina, Antonio Francioso, Luciana Mosca, and Mario Fontana. "Pheomelanin Effect on UVB Radiation-Induced Oxidation/Nitration of l-Tyrosine." International Journal of Molecular Sciences 23, no. 1 (December 27, 2021): 267. http://dx.doi.org/10.3390/ijms23010267.

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Pheomelanin is a natural yellow-reddish sulfur-containing pigment derived from tyrosinase-catalyzed oxidation of tyrosine in presence of cysteine. Generally, the formation of melanin pigments is a protective response against the damaging effects of UV radiation in skin. However, pheomelanin, like other photosensitizing substances, can trigger, following exposure to UV radiation, photochemical reactions capable of modifying and damaging cellular components. The photoproperties of this natural pigment have been studied by analyzing pheomelanin effect on oxidation/nitration of tyrosine induced by UVB radiation at different pH values and in presence of iron ions. Photoproperties of pheomelanin can be modulated by various experimental conditions, ranging from the photoprotection to the triggering of potentially damaging photochemical reactions. The study of the photomodification of l-Tyrosine in the presence of the natural pigment pheomelanin has a special relevance, since this tyrosine oxidation/nitration pathway can potentially occur in vivo in tissues exposed to sunlight and play a role in the mechanisms of tissue damage induced by UV radiation.
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Tien, Ming. "Myeloperoxidase-Catalyzed Oxidation of Tyrosine." Archives of Biochemistry and Biophysics 367, no. 1 (July 1999): 61–66. http://dx.doi.org/10.1006/abbi.1999.1226.

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KRAPFENBAUER, K., R. BIRNBACHER, H. VIERHAPPER, K. HERKNER, D. KAMPEL, and G. LUBEC. "Glycoxidation, and protein and DNA oxidation in patients with diabetes mellitus." Clinical Science 95, no. 3 (September 1, 1998): 331–37. http://dx.doi.org/10.1042/cs0950331.

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1.The role of oxidative stress in the pathogenesis of the diabetic state is being investigated extensively. Although oxidative stress has been reported in terms of glycoxidation, protein oxidation and DNA oxidation in diabetes mellitus, oxidation parameters have not been determined in parallel on the same study population. 2.We studied 24 patients with diabetes mellitus (14 patients with Type I diabetes with a mean age of 62.3±6.3 years and 10 patients with Type II diabetes aged 67.3±5.9 years) and compared them with age-matched non-diabetic controls. Urinary o-tyrosine, 8-hydroxy-2′-deoxyguanosine and pentosidine measurements by HPLC were made on two occasions (t1 and t2). 3.A clear statistical difference was found between diabetic patients and controls at t1 or t2 for 8-hydroxy-2′-deoxyguanosine and pentosidine, but not for o-tyrosine. No significant correlations were found between clinical and other laboratory parameters except high-density lipoprotein and uric acid. We revealed significantly increased glycoxidation and DNA oxidation in patients with Type I and Type II diabetes, but protein oxidation was not different from controls. 4.The finding of increased glycoxidation reflects increased oxidation of the carbohydrate moiety, whereas the increased levels of oxidized DNA may also be interpreted as due to increased DNA repair. The increased 8-hydroxy-2′-deoxyguanosine does not indicate the generation of an individual active oxygen species, but DNA could have been oxidized simply by alkenals from lipid peroxidation, as e.g. malondialdehyde. As no difference in protein oxidation (i.e. o-tyrosine) between diabetics and controls could be revealed, the oxidation of DNA by hydroxyl radical attack is unlikely, as o-tyrosine was proposed as a marker for hydroxyl radical attack. Therefore, the message is that increased glycoxidation can be confirmed, protein oxidation does not appear to take place and increased DNA oxidation is still not proven, as increased 8-hydroxy-2′-deoxyguanosine may simply reflect repair.
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Saleh, Maysoon B., and Russell G. Kerr. "Oxidation of Tyrosine Diketopiperazine to DOPA Diketopiperazine with Tyrosine Hydroxylase†." Journal of Natural Products 67, no. 8 (August 2004): 1390–91. http://dx.doi.org/10.1021/np034083j.

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Palumbo, A., G. Misuraca, M. D'Ischia, and G. Prota. "Effect of metal ions on the kinetics of tyrosine oxidation catalysed by tyrosinase." Biochemical Journal 228, no. 3 (June 15, 1985): 647–51. http://dx.doi.org/10.1042/bj2280647.

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The conversion of tyrosine into dopa [3-(3,4-dihydroxyphenyl)alanine] is the rate limiting step in the biosynthesis of melanins catalysed by tyrosinase. This hydroxylation reaction is characterized by a lag period, the extent of which depends on various parameters, notably the presence of a suitable hydrogen donor such as dopa or tetrahydropterin. We have now found that catalytic amounts of Fe2+ ions have the same effect as dopa in stimulating the tyrosine hydroxylase activity of the enzyme. Kinetic experiments showed that the shortening of the induction time depends on the concentration of the added metal and the nature of the buffer system used and is not suppressed by superoxide dismutase, catalase, formate or mannitol. Notably, Fe3+ ions showed only a small delaying effect on tyrosinase activity. Among the other metals which were tested, Zn2+, Co2+, Cd2+ and Ni2+ had no detectable influence, whereas Cu2+ and Mn2+ exhibited a marked inhibitory effect on the kinetics of tyrosine oxidation. These findings are discussed in the light of the commonly accepted mechanism of action of tyrosinase.
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Adamiec, J., K. Cejpek, J. Rössner, and J. Velíšek. "Novel Strecker degradation products of tyrosine and dihydroxyphenylalanine." Czech Journal of Food Sciences 19, No. 1 (February 7, 2013): 13–18. http://dx.doi.org/10.17221/6568-cjfs.

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Tyrosine was oxidised with either potassium peroxodisulphate or glyoxal. Volatile reaction products were isolated and analysed by GC/FID and GC/MS, derivatised with diazomethane and analysed by the same methods. Eight reaction products were identified. The major products were the expected Strecker aldehyde (4-hydroxyphenylacetaldehyde) and its lower homologue 4-hydroxybenzaldehyde. They were followed by 1-(4-hydroxyphenyl)-3-propionaldehyde, phenylacetaldehyde, benzaldehyde, phenol, 4-hydroxybenzoic, and benzoic acid. Analogously, the oxidation of 3,4-dihydroxyphenylalanine yielded the corresponding Strecker aldehyde (3,4-dihydroxyphenylacetaldehyde), its lower homologue 3,4-dihydroxybenzaldehyde, 3,4-dihydroxybenzoic, 3,4-dihydroxyphenylacetic, and caffeic acid. An identification of these oxidation products of tyrosine and 3,4-dihydroxyphenylalanine assumes homolytic cleavage of the Strecker aldehydes and a recombination of free radicals formed by this cleavage. As minor products, six O- and N-heterocyclic compounds arose in systems containing glyoxal (pyrazine, methyl- and ethylpyrazine, 3-furancarbaldehyde, 5-methyl-2-furancarbaldehyde, 2-pyrrolcarbaldehyde).
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Dissertations / Theses on the topic "Tyrosine oxidation"

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Kadlčík, Vojtěch. "Oxidation of beta-amyloid and model peptides." Paris 11, 2006. http://www.theses.fr/2006PA112008.

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Le but de mon travail de thèse était de caractériser les produits de l'oxydation du peptide beta-amyloïde (Abeta) impliqué dans le développement de la maladie d'Alzheimer. Pour étudier l'effet de la structure de peptide sur les processus redox, les propriétés du peptide Abeta (1-40) ont été comparées au peptide de séquence inverse, Abeta (40-1). Les radicaux libres choisis ont été produits en radiolyse gamma. Les produits finaux ont été caractérisés par des techniques d'analyse diverses (HPLC, GC, MALDI-TOF MS, spectrométrie de fluorescence, spectrométrie raman). Pour établir l'effet de l'environnement sur le processus d'oxydation, peptides ont été oxydés dans trois systèmes différents: solution aqueuse homogène, milieu micellaire (SDS) et système des vésicules phospholipidiques (POPC). En solution aqueuse homogène, les produits d'oxydation sont différents pour les deux peptides. Les résidus facilement oxydables sont Met35 pour Abeta(1-40) et Tyr10 pour Abeta(40-1). La présence des micelles ainsi que des vésicules phospholipidiques change profondément le cours de l'oxydation. Une étude structurale en dichroïsme circulaire nous permet d'avancer des hypothèses pour interpréter ces résultats. Nous avons montré que des produits de dégradation des peptides Abeta peuvent induire d'une manière catalytique l'altération des phospholipides. Cette propriété est attribuée à l'action des atomes d'hydrogène sur le peptide. Nos résultats sont intéressants dans le contexte du développement de la maladie d'Alzheimer, car ils peuvent aider à éclairer le rôle de l'interaction de peptide Abeta(1-40) avec des membranes phospholipidique dans les propriétés redox du peptide
The goal of my thesis work was to characterize oxidation products of beta-amyloid peptide (Abeta), which is implied in the development of Alzheimer's disease. To study the effect of peptide structure on the redox processes, oxidation properties of Abeta(1-40) were compared to the peptide with reverse sequence, Abeta(40-1). Azide and hydroxyl radicals used for oxidation were produced by gamma radiolysis. Final products were characterized by a variety of analytical techniques (HPLC, GC, MALDI-TOF MS, fluorescence and raman spectrometry). To establish the role of peptide environment on its redox properties, oxidation was carried out in three different systems: homogeneous aqueous solution, micellar system (SDS) and in the presence of phospholipids vesicles (POPC). In homogeneous aqueous solution, oxidation products are different for both peptides. The main oxidation targets are Met35 for Abeta(1-40) and Tyr10 for Abeta(40-1). The presence of micelles and phospholipid vesicles has an important impact on the oxidation pathways. These changes could be related to changes in peptide conformations studied by circular dichroism. We have also shown that Abeta degradation products may catalytically induce alternation of phospholipids. This process is initiated by reaction of hydrogen radicals with the peptide. Our results are interesting in the context of the development of Alzheimer's disease as they may bring an insight into the role of Abeta(1-40) interaction with phospholipids membrane for the redox properties of the peptide
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Wells, Geoffrey. "Chemical diversity from the oxidation of bioactive phenols." Thesis, University of Nottingham, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.324523.

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Hingorani, Kastoori. "Photo-oxidation of tyrosine in a bio-engineered bacterioferritin 'reaction centre'." Phd thesis, Canberra, ACT : The Australian National University, 2012. http://hdl.handle.net/1885/11774.

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The photosynthetic reaction centre (RC) is central to conversion of solar energy into chemical energy. In this thesis, in order to introduce the redox-active cofactors similar to that of the Photosystem II RC, a non-photosynthetic protein scaffold was used as an in vitro model. The protein tasked for this purpose was the heme containing bacterioferritin (BFR) protein found in E. coli. The BFR protein naturally expresses as a homodimer based on a 4-helix bundle monomer. Desirable properties included: (i) a promiscuos di-nuclear metal binding site which provides ligands for class II metals such as Mn (ii) a hydrophobic pocket at the dimer interface which can bind a photosensitive porphyrin, in this case a chlorin (Ce6), and (iii) presence of tyrosine residues proximal to the bound cofactors, which can be utilised as efficient electron-tunnelling intermediates. The work in this thesis extends earlier work in the group by refining and improving the BFR system. Several mutants were made and an improved protein expression system was developed. For these samples experiments demonstrated ligation of weakly coupled equivalent Mn2II,II at the di-nuclear binding site of apo-BFR, and binding of the photo-active pigment ZnCe6 in hydrophobic pocket of the protein. Light-induced electron transfer from proximal tyrosine residue(s) to the photo-oxidised ZnCe6+, in the modified BFR reconsitituted with both ZnCe6 and MnII is presented. Three site-specific tyrosine mutants (Y25F, Y58F and Y45F) were made to localise the redox-active tyrosine in this engineered system. The results indicate that: (i) presence of bound MnII is necessary to observe tyrosine oxidation in all BFR variants, (ii) Y45 (within van Der Waals network of ZnCe6) is singly the most important tyrosine as the immediate electron donor to the oxidised ZnCe6+, and (iii) Y25 and Y58 are both redox-active in this system, but appear to be interchangebale. A high-resolution (~1.5 Ã…) crystal structure of the three tyrosine mutants was obtained and these structures showed there to be no mutation-induced effects on the overall 3-D structure of the protein. Minimal effects observed in the Y45F mutant are reported. The molecular design of a "second generation" of the BFR series is also presented where the symmetry of the BFR homodimer is broken to generate a BFR heterodimer to contain genetically distinct electron donor and acceptor subunits. The BFR heterodimer was made by introducing a small (20 aa) peptide linker between the two subunits. The ultimate goal will be to demonstrate light-induced directional electron flow in the BFR heterodimer.
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LaButti, Jason N. Gates Kent S. "Investigations into the chemistry of protein tyrosine phosphatase redox regulation." Diss., Columbia, Mo. : University of Missouri--Columbia, 2009. http://hdl.handle.net/10355/6158.

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Title from PDF of title page (University of Missouri--Columbia, viewed on Feb 15, 2010). The entire thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file; a non-technical public abstract appears in the public.pdf file. Dissertation advisor: Dr. Kent S. Gates. Vita. Includes bibliographical references.
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Song, Wei. "MASS SPECTROMETRY-BASED HIGH THROUGHPUT APPROACH FOR IDENTIFICATION OF MOLECULAR MODIFICATION OF OXIDATIVE PROCESS IN RESPIRATORY." Cleveland State University / OhioLINK, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=csu1226685494.

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Sjöholm, Johannes. "Trapping Tyrosine Z : Exploring the Relay between Photochemistry and Water Oxidation in Photosystem II." Doctoral thesis, Uppsala universitet, Molekylär biomimetik, 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-173575.

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Photosystem II is unique! It remains the only enzyme that can oxidize water using light as energy input. Water oxidation in photosystem II is catalyzed by the CaMn4 cluster. The electrons extracted from the CaMn4 cluster are transferred to P680+ via the tyrosine residue D1-Tyr161 (YZ). Favorable oxidation of YZ is coupled to a proton transfer along a hydrogen bond to the nearby D1-His190 residue, resulting in the neutral radical YZ•. By illuminating photosystem II at cryogenic temperatures, YZ• can be trapped in a stable state. Magnetic interaction between this radical and the CaMn4 cluster gives rise to a split electron paramagnetic resonance (EPR) signal with characteristics that depend on the oxidation state (S state) of the cluster. The mechanism by which the split EPR signals are formed is different depending on the S state. In the S0 and S1 states, split signal induction proceeds via a P680+-centered mechanism, whereas in the S2 and S3 states, our results show that split induction stems from a Mn-centered mechanism. This S state-dependent pattern of split EPR signal induction can be correlated to the charge of the CaMn4 cluster in the S state in question and has prompted us to propose a general model for the induction mechanism across the different S states. At the heart of this model is the stability or otherwise of the YZ•–(D1-His190)+ pair during cryogenic illumination. The model is closely related to the sequence of electron and proton transfers from the cluster during the S cycle. Furthermore, the important hydrogen bond between YZ and D1-His190 has been investigated by following the split EPR signal formation in the different S states as a function of pH. All split EPR signals investigated decrease in intensity with a pKa of ~4-5. This pKa can be correlated to a titration event that disrupts the essential hydrogen bond, possibly by a direct protonation of D1-His190.  This has important consequences for the function of the CaMn4 cluster as this critical YZ–D1-His190 hydrogen bond steers a multitude of reactions at the cluster.
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Jenson, David L. Jenson. "Proton-coupled electron transfer and tyrosine D of phototsystem II." Diss., Atlanta, Ga. : Georgia Institute of Technology, 2009. http://hdl.handle.net/1853/29667.

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Thesis (Ph. D.)--Chemistry and Biochemistry, Georgia Institute of Technology, 2010.
Committee Chair: Bridgette Barry; Committee Member: Ingeborg Schmidt-Krey; Committee Member: Jake Soper; Committee Member: Nils Kroger; Committee Member: Wendy Kelly. Part of the SMARTech Electronic Thesis and Dissertation Collection.
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Machado, Luciana E. S. F., Tun-Li Shen, Rebecca Page, and Wolfgang Peti. "The KIM-family protein-tyrosine phosphatases use distinct reversible oxidation intermediates: Intramolecular or intermolecular disulfide bond formation." AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2017. http://hdl.handle.net/10150/624478.

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The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes hematopoietic protein-tyrosine phosphatase (HePTP), striatal-enriched protein-tyrosine phosphatase (STEP), and protein-tyrosine phosphatase receptor type R (PTPRR). KIM-PTPs bind and dephosphorylate mitogen-activated protein kinases (MAPKs) and thereby critically modulate cell proliferation and differentiation. PTP activity can readily be diminished by reactive oxygen species (ROS), e.g. H2O2, which oxidize the catalytically indispensable active-site cysteine. This initial oxidation generates an unstable sulfenic acid intermediate that is quickly converted into either a sulfinic/sulfonic acid (catalytically dead and irreversible inactivation) or a stable sulfenamide or disulfide bond intermediate (reversible inactivation). Critically, our understanding of ROS-mediated PTP oxidation is not yet sufficient to predict the molecular responses of PTPs to oxidative stress. However, identifying distinct responses will enable novel routes for PTP-selective drug design, important for managing diseases such as cancer and Alzheimer's disease. Therefore, we performed a detailed biochemical and molecular study of all KIM-PTP family members to determine their H2O2 oxidation profiles and identify their reversible inactivation mechanism(s). We show that despite having nearly identical 3D structures and sequences, each KIM-PTP family member has a unique oxidation profile. Furthermore, we also show that whereas STEP and PTPRR stabilize their reversibly oxidized state by forming an intramolecular disulfide bond, HePTP uses an unexpected mechanism, namely, formation of a reversible intermolecular disulfide bond. In summary, despite being closely related, KIM-PTPs significantly differ in oxidation profiles. These findings highlight that oxidation protection is critical when analyzing PTPs, for example, in drug screening.
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Salsman, Scott J. "Redox regulation of protein tyrosine phosphatases in cell membrane receptor-mediated signal transduction." Oklahoma City : [s.n.], 2005.

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Cooper, Ian Blake. "Photosynthetic water oxidation and proton-coupled electron transfer." Diss., Atlanta, Ga. : Georgia Institute of Technology, 2008. http://hdl.handle.net/1853/26707.

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Thesis (Ph. D.)--Chemistry and Biochemistry, Georgia Institute of Technology, 2009.
Committee Chair: Bridgette Barry; Committee Member: El-Sayed, Mostafa; Committee Member: Fahrni, Christoph; Committee Member: Kröger, Nils; Committee Member: McCarty, Nael. Part of the SMARTech Electronic Thesis and Dissertation Collection.
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Books on the topic "Tyrosine oxidation"

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Khadaroo, Rachel G. The cellular and molecular mechanisms regulating oxidative stress-induced priming of the macrophage: The role of the Src family of tyrosine kinases. 2004.

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Book chapters on the topic "Tyrosine oxidation"

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Hutinec, A., G. Jung, A. Rieker, and A. Ziogas. "Oxidation of tyrosine derivatives." In Peptides 1994, 704–5. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-1468-4_324.

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Bruins, Jorick J., Criss van de Wouw, Jordi F. Keijzer, Bauke Albada, and Floris L. van Delft. "Inducible, Selective Labeling of Proteins via Enzymatic Oxidation of Tyrosine." In Methods in Molecular Biology, 357–68. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9546-2_18.

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Nakamura, Shin. "Proton Release Reaction of Tyrosine D in Photosystem II." In Molecular Mechanisms of Proton-coupled Electron Transfer and Water Oxidation in Photosystem II, 37–51. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-1584-2_3.

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Huang, Wen-zhang, Zhao-ming Xie, Shuang-kou Chen, and Dan Li. "Optimizing the Properties of Tyrosine and It’s Oxidation Derivatives Based on Quantum Computation." In Advances in Intelligent and Soft Computing, 945–51. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-03664-4_102.

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Magnuson, Ann, Maria Rova, Fikret Mamedov, Per-Olof Fredriksson, and Stenbjörn Styringl. "Changes in the Oxidation State of Cytochrome B-559 and Tyrosine-D During in Vivo Photoactivation of Photosystem II." In Photosynthesis: Mechanisms and Effects, 1097–100. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_261.

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Diner, B. A., and P. J. Nixon. "Evidence for D1-His190 as the Proton Acceptor Implicated in the Oxidation of Redox-Active Tyrosine YZ of PSII." In Photosynthesis: Mechanisms and Effects, 1177–80. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_281.

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Tsiropoulou, Sofia, and Rhian M. Touyz. "Assessment of Protein Carbonylation and Protein Tyrosine Phosphatase (PTP) Oxidation in Vascular Smooth Muscle Cells (VSMCs) Using Immunoblotting Approaches." In Methods in Molecular Biology, 31–46. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7030-8_3.

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Schieven, Gary L. "Tyrosine Phosphorylation in Oxidative Stress." In Oxidative Stress and Signal Transduction, 181–99. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5981-8_8.

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Mehdi, Syed Jafar, Steven W. Barger, Merle G. Paule, Syed F. Ali, and Syed Z. Imam. "Tyrosine Kinase Inhibitors and Neurodegenerative Disorders." In Inflammation, Aging, and Oxidative Stress, 81–91. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-33486-8_5.

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Srivastava, Jyoti, Joyabrata Mal, Manju Verma, and Rupika Sinha. "Mini-review on Inhibitors of Human Tyrosinase." In Proceedings of the Conference BioSangam 2022: Emerging Trends in Biotechnology (BIOSANGAM 2022), 96–105. Dordrecht: Atlantis Press International BV, 2022. http://dx.doi.org/10.2991/978-94-6463-020-6_10.

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AbstractMelanin is a major pigment of human skin that protects the skin from harmful ultraviolet radiation, DNA damage and oxidative stress. However, the excess accumulation of melanin may lead to various hyperpigmentation-related diseases. Tyrosinase is a copper containing enzyme that regulates the rate-limiting step of melanin synthesis. So, inhibiting tyrosinase is the crucial target for researchers for the treatment of hyperpigmentation. Unfortunately, almost all the literature is based on mushroom tyrosinase (mTYR) for their application on humans as pure human tyrosinase (hTYR) is difficult to isolate. Since presently used tyrosinase inhibitors are developed using mushroom tyrosinase, they are insufficient to match the affinity, selectivity and efficacy required to target the human tyrosinase. Therefore, there is an urgent need for identifying a selective tyrosinase inhibitor that matches the selectivity and safety standards of human tyrosinase. This mini-review is focused on the tyrosinase inhibitors developed and evaluated using human tyrosinase.
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Conference papers on the topic "Tyrosine oxidation"

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Šebestík, Jaroslav. "Raman Spectroscopy with Nanoparticles for Investigation of Protein Tyrosine Oxidation." In 36th European Peptide Symposium. The European Peptide Society, 2022. http://dx.doi.org/10.17952/36eps/36eps.2022.124.

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Kuban-Jankowska, Alicja, Magdalena Gorska-Ponikowska, and Pawel Niedzialkowski. "The oxidation-reduction reactions in regulation of protein tyrosine phosphatases activity." In RECENT ADVANCES ON ENVIRONMENT, CHEMICAL ENGINEERING AND MATERIALS. Author(s), 2018. http://dx.doi.org/10.1063/1.5060694.

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Kosmachevskaya, Olga, Elvira Nasybullina, Konstantin Shumaev, and Alexey Topunov. "HEMOGLOBIN-BOUND DYNITROSIL IRON COMPLEXES PROTECT IT FROM OXIDATIVE MODIFICATION." In NEW TECHNOLOGIES IN MEDICINE, BIOLOGY, PHARMACOLOGY AND ECOLOGY. Institute of information technology, 2021. http://dx.doi.org/10.47501/978-5-6044060-1-4.51.

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Under the action of peroxynitrite, DNICs associated with hemoglobin are dose-dependently destroyed, while inhibiting the oxidation of tryptophan and tyrosine residues, the formation of carbonyl derivatives, preventing the formation of covalent cross-links between subunits, and preventing the degradation of the heme group.
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McMullen, CJ, C. McCluskey, SJ Kim, S. Laovitthayanggoon, M. MacDonald, M. Safar, R. Wood, MR Cunningham, and S. Currie. "12 Anti-cancer tyrosine kinase inhibitors increase oxidative stress in primary cardiac fibroblasts." In The Scottish Cardiovascular Forum 2018, 3rd February 2018, Trinity Biomedical Science Institute, Trinity College Dublin Ireland. BMJ Publishing Group Ltd and British Cardiovascular Society, 2018. http://dx.doi.org/10.1136/heartjnl-2018-scf.22.

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Cvijetić, Ilija, Petar Ristivojević, Maja Krstić-Ristivojević, and Dušanka Milojković-Opsenica. "EXPLORING THE POTENTIAL OF Α-ARBUTIN AS THE INHIBITOR OF NEURODEGENERATIVE DISORDERS." In 1st INTERNATIONAL Conference on Chemo and BioInformatics. Institute for Information Technologies, University of Kragujevac, 2021. http://dx.doi.org/10.46793/iccbi21.292c.

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Tyrosinase is an enzyme involved in generation of dopamine-quinones, which has an important role in oxidative stress associated with the Parkinson’s disease. It is also a common molecular target for the design of novel anti-melanogenic agents. The inhibition of tyrosinase might be responsible for the experimentally observed intracellular antioxidant activity of α-arbutin. Moreover, intrinsic radical scavenging capacity of α-arbutin should also be considered. The binding mode of α-arbutin into the active site of Bacillus megaterium tyrosinase is predicted using AutoDock Vina 1.1. To map the thermodynamic feasibility of HAT and SET-PT mechanisms of the intrinsic antioxidant capacity α-arbutin, bond dissociation enthalpies (BDEs) and ionization potential (IP) are calculated using DFT with B3LYP functional and 6-31+g(d,p) basis set. α-Arbutin fitted well into the active site of tyrosinase, with the calculated binding affinity of -17.5 kcal/mol. The phenolic moiety is located deep into the binding pocket, interacting with His residues around Cu2+ ion. The binding mode of α-arbutin is stabilized via HBD interactions with His231, His42, His60, Arg209, Gly216, and Asn205, HBA interaction with Arg209 at the outer part of active site, and hydrophobic interactions with His208, Val218 and Ala221. The calculated IP of α-arbutin is 175.18 kcal/mol, and BDE of phenolic group is 79.85 kcal/mol. The spin densities of radical-cation and hydroxyl radical are delocalized on the aglycone moiety. The results of this study provide valuable structural insights into the molecular mechanisms of biological action of α-arbutin, and might be exploited for the design of more potent analogues.
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Li, Guanghui, Chaoying Qiu, Ning Liu, and Xuanxuan Lu. "Simultaneous loading of (–)-epigallocatechin gallate and ferulic acid in chitosan-based nanoparticles as effective antioxidant and skin-whitening agent." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/wuud7971.

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A chitosan (CS) based nanoparticles simultaneously loaded with (–)-epigallocatechin gallate (EGCG) and ferulic acid (FA) was synthesized via ionic gelation reaction between chitosan and sodium tripolyphosphate and subsequent modification by genipin. Average particle size, chemical structure, morphology, rheological properties, entrapment efficiency, in vitro anti-oxidative and tyrosinase inhibitory activity of CS nanoparticles were investigated. Results showed that the nanoparticles showed an ellipsoidal shape with an average diameter of 412.3 ± 3.5 nm, and zeta potential of 35.47 ± 0.90 mV with high DPPH and ABTS·+ scavenging ability. The entrapment efficiency of EGCG and FA were 46.0 ± 1.32% and 46.8 ± 1.64% in the nanoparticles, respectively. Cytotoxicity experiment on NIH 3T3 fibroblast cells reveals that CS based NPs show no toxic effects with concentration less than 200 mg/mL–1. Meanwhile, the nanoparticles improved cell viability from ~65% to 105% and ameliorated the morphological damage by H2O2. Moreover, it showed a higher tyrosinase inhibitory activity compar-ing with blank NPs without bioactives and a commonly used bioactive compound kojic acid (P < 0.05), suggesting the good skin repair and whitening effects of nanoparticles. This research would provide new insights and basis for the designation of novel particles which can be applied as Pickering stabilizers loaded with dual bioactive agents with beneficial activities.
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Cobbaut, Mathias, Rita Derua, Etienne Waelkens, Peter Störz, Veerle Janssens, and Johan Van Lint. "Abstract B08: Differential regulation of Protein Kinase D isoforms in oxidative stress conditions via tyrosine phosphorylation in the activation segment." In Abstracts: AACR International Conference: New Frontiers in Cancer Research; January 18-22, 2017; Cape Town, South Africa. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.newfront17-b08.

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Vahedi, Shahrooz, Fu-Yu Chueh, and Chao-Lan Yu. "Abstract 3041: Lymphocyte-specific protein tyrosine kinase (Lck) interacts with CR6-interacting factor 1 (CRIF1) in mitochondria to repress oxidative phosphorylation." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-3041.

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Bagheri-Yarmand, Rozita, Krishna M. Sinha, Ling Li, Yue Lu, and Robert F. Gagel. "Abstract 2426: Tyrosine kinase and ERAD inhibitors promote oxidative stress-induced apoptosis through activation of ATF4 / KLF9 axis in medullary thyroid cancer." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-2426.

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Reports on the topic "Tyrosine oxidation"

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Ohad, Itzhak, and Himadri Pakrasi. Role of Cytochrome B559 in Photoinhibition. United States Department of Agriculture, December 1995. http://dx.doi.org/10.32747/1995.7613031.bard.

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The aim of this research project was to obtain information on the role of the cytochrome b559 in the function of Photosystem-II (PSII) with special emphasis on the light induced photo inactivation of PSII and turnover of the photochemical reaction center II protein subunit RCII-D1. The major goals of this project were: 1) Isolation and sequencing of the Chlamydomonas chloroplast psbE and psbF genes encoding the cytochrome b559 a and b subunits respectively; 2) Generation of site directed mutants and testing the effect of such mutation on the function of PSII under various light conditions; 3) To obtain further information on the mechanism of the light induced degradation and replacement of the PSII core proteins. This information shall serve as a basis for the understanding of the role of the cytochrome b559 in the process of photoinhibition and recovery of photosynthetic activity as well as during low light induced turnover of the D1 protein. Unlike in other organisms in which the psbE and psbF genes encoding the a and b subunits of cytochrome b559, are part of an operon which also includes the psbL and psbJ genes, in Chlamydomonas these genes are transcribed from different regions of the chloroplast chromosome. The charge distribution of the derived amino-acid sequences of psbE and psbF gene products differs from that of the corresponding genes in other organisms as far as the rule of "positive charge in" is concerned relative to the process of the polypeptide insertion in the thylakoid membrane. However, the sum of the charges of both subunits corresponds to the above rule possibly indicating co-insertion of both subunits in the process of cytochrome b559 assembly. A plasmid designed for the introduction of site-specific mutations into the psbF gene of C. reinhardtii. was constructed. The vector consists of a DNA fragment from the chromosome of C. reinhardtii which spans the region of the psbF gene, upstream of which the spectinomycin-resistance-conferring aadA cassette was inserted. This vector was successfully used to transform wild type C. reinhardtii cells. The spectinomycin resistant strain thus obtained can grow autotrophically and does not show significant changes as compared to the wild-type strain in PSII activity. The following mutations have been introduced in the psbF gene: H23M; H23Y; W19L and W19. The replacement of H23 involved in the heme binding to M and Y was meant to permit heme binding but eventually alter some or all of the electron transport properties of the mutated cytochrome. Tryptophane W19, a strictly conserved residue, is proximal to the heme and may interact with the tetrapyrole ring. Therefore its replacement may effect the heme properties. A change to tyrosine may have a lesser affect on the potential or electron transfer rate while a replacement of W19 by leucine is meant to introduce a more prominent disturbance in these parameters. Two of the mutants, FW19L and FH23M have segregated already and are homoplasmic. The rest are still grown under selection conditions until complete segregation will be obtained. All mutants contain assembled and functional PSII exhibiting an increased sensitivity of PSII to the light. Work is still in progress for the detailed characterization of the mutants PSII properties. A tobacco mutant, S6, obtained by Maliga and coworkers harboring the F26S mutation in the b subunit was made available to us and was characterized. Measurements of PSII charge separation and recombination, polypeptide content and electron flow indicates that this mutation indeed results in light sensitivity. Presently further work is in progress in the detailed characterization of the properties of all the above mutants. Information was obtained demonstrating that photoinactivation of PSII in vivo initiates a series of progressive changes in the properties of RCII which result in an irreversible modification of the RCII-D1 protein leading to its degradation and replacement. The cleavage process of the modified RCII-D1 protein is regulated by the occupancy of the QB site of RCII by plastoquinone. Newly synthesized D1 protein is not accumulated in a stable form unless integrated in reassembled RCII. Thus the degradation of the irreversibly modified RCII-D1 protein is essential for the recovery process. The light induced degradation of the RCII-D1 protein is rapid in mutants lacking the pD1 processing protease such as in the LF-1 mutant of the unicellular alga Scenedesmus obliquus. In this case the Mn binding site of PSII is abolished, the water oxidation process is inhibited and harmful cation radicals are formed following light induced electron flow in PSII. In such mutants photo-inactivation of PSII is rapid, it is not protected by ligands binding at the QB site and the degradation of the inactivated RCII-D1 occurs rapidly also in the dark. Furthermore the degraded D1 protein can be replaced in the dark in absence of light driven redox controlled reactions. The replacement of the RCII-D1 protein involves the de novo synthesis of the precursor protein, pD1, and its processing at the C-terminus end by an unknown processing protease. In the frame of this work, a gene previously isolated and sequenced by Dr. Pakrasi's group has been identified as encoding the RCII-pD1 C-terminus processing protease in the cyanobacterium Synechocystis sp. PCC 6803. The deduced sequence of the ctpA protein shows significant similarity to the bovine, human and insect interphotoreceptor retinoid-binding proteins. Results obtained using C. reinhardtii cells exposes to low light or series of single turnover light flashes have been also obtained indicating that the process of RCII-D1 protein turnover under non-photoinactivating conditions (low light) may be related to charge recombination in RCII due to back electron flow from the semiquinone QB- to the oxidised S2,3 states of the Mn cluster involved in the water oxidation process.
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