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Showing 13 to 24 of 327 entries
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Immunoglobulins and Antibodies.

Russian journal of immunology : RJI : official journal of Russian Society of Immunology

Kulberg AY.
PMID: 12687133
Russ J Immunol. 1999 Oct;4(3):241-242.

In recent years it has become more and more clear that immunoglobulins are regulators of homeostasis, independent of their specificity as antibodies. The presence in immunoglobulins of biochemical characteristics, inherent to oxidoreductases with their capability of coordinating transition metals,...

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Kulberg AY. Immunoglobulins and Antibodies. Russ J Immunol. 1999;4(3):241-242
Kulberg, A. Y. (1999). Immunoglobulins and Antibodies. Russian journal of immunology : RJI : official journal of Russian Society of Immunology, 4(3), 241-242.
Kulberg, Alexander Ya.. "Immunoglobulins and Antibodies." Russian journal of immunology : RJI : official journal of Russian Society of Immunology vol. 4,3 (1999): 241-242.
Kulberg AY. Immunoglobulins and Antibodies. Russ J Immunol. 1999 Oct;4(3):241-242. PMID: 12687133.
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Overproduction in Escherichia coli and Characterization of a Soybean Ferric Leghemoglobin Reductase.

Plant physiology

Ji L, Becana M, Sarath G, Shearman L, Klucas RV.
PMID: 12232320
Plant Physiol. 1994 Sep;106(1):203-209. doi: 10.1104/pp.106.1.203.

We previously cloned and sequenced a cDNA encoding soybean ferric leghemoglobin reductase (FLbR), an enzyme postulated to play an important role in maintaining leghemoglobin in a functional ferrous state in nitrogen-fixing root nodules. This cDNA was sub-cloned into an...

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Ji L, Becana M, Sarath G, et al. Overproduction in Escherichia coli and Characterization of a Soybean Ferric Leghemoglobin Reductase. Plant Physiol. 1994;106(1):203-209doi: 10.1104/pp.106.1.203.
Ji, L., Becana, M., Sarath, G., Shearman, L., & Klucas, R. V. (1994). Overproduction in Escherichia coli and Characterization of a Soybean Ferric Leghemoglobin Reductase. Plant physiology, 106(1), 203-209. https://doi.org/10.1104/pp.106.1.203
Ji, L., et al. "Overproduction in Escherichia coli and Characterization of a Soybean Ferric Leghemoglobin Reductase." Plant physiology vol. 106,1 (1994): 203-209. doi: https://doi.org/10.1104/pp.106.1.203
Ji L, Becana M, Sarath G, Shearman L, Klucas RV. Overproduction in Escherichia coli and Characterization of a Soybean Ferric Leghemoglobin Reductase. Plant Physiol. 1994 Sep;106(1):203-209. doi: 10.1104/pp.106.1.203. PMID: 12232320; PMCID: PMC159517.
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Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases.

Plant physiology

Van Gestelen P, Asard H, Caubergs RJ.
PMID: 12223822
Plant Physiol. 1997 Oct;115(2):543-550. doi: 10.1104/pp.115.2.543.

Solubilization and ion-exchange chromatography of plasma membrane proteins obtained from bean (Phaseolus vulgaris L.) seedlings resulted in a single NAD(P)H-O2--synthase protein peak. This enzyme showed a high preference toward NADPH as a substrate (reaction rate, 27.4 nmol O2- produced...

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Van Gestelen P, Asard H, Caubergs RJ. Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases. Plant Physiol. 1997;115(2):543-550doi: 10.1104/pp.115.2.543.
Van Gestelen, P., Asard, H., & Caubergs, R. J. (1997). Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases. Plant physiology, 115(2), 543-550. https://doi.org/10.1104/pp.115.2.543
Van Gestelen, P., et al. "Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases." Plant physiology vol. 115,2 (1997): 543-550. doi: https://doi.org/10.1104/pp.115.2.543
Van Gestelen P, Asard H, Caubergs RJ. Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases. Plant Physiol. 1997 Oct;115(2):543-550. doi: 10.1104/pp.115.2.543. PMID: 12223822; PMCID: PMC158513.
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Structural Aspects of Plant Ferredoxin : NADP(+) Oxidoreductases.

Photosynthesis research

Karplus PA, Faber HR.
PMID: 16034534
Photosynth Res. 2004;81(3):303-15. doi: 10.1023/B:PRES.0000036884.57303.2e.

Ferredoxin reductase (FNR) is ubiquitous among photosynthetic organisms as the enzyme directly responsible for the generation of NADPH. Structural studies over the last 15 years have generated over 30 crystal structures of wild-type and mutant FNRs that have yielded...

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Karplus PA, Faber HR. Structural Aspects of Plant Ferredoxin : NADP(+) Oxidoreductases. Photosynth Res. 2004;81(3):303-15doi: 10.1023/B:PRES.0000036884.57303.2e.
Karplus, P. A., & Faber, H. R. (2004). Structural Aspects of Plant Ferredoxin : NADP(+) Oxidoreductases. Photosynthesis research, 81(3), 303-15. https://doi.org/10.1023/B:PRES.0000036884.57303.2e
Karplus, P Andrew, and Faber, H Richard. "Structural Aspects of Plant Ferredoxin : NADP(+) Oxidoreductases." Photosynthesis research vol. 81,3 (2004): 303-15. doi: https://doi.org/10.1023/B:PRES.0000036884.57303.2e
Karplus PA, Faber HR. Structural Aspects of Plant Ferredoxin : NADP(+) Oxidoreductases. Photosynth Res. 2004;81(3):303-15. doi: 10.1023/B:PRES.0000036884.57303.2e. PMID: 16034534.
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Multienzyme electrochemical array sensor for determination of phenols and pesticides.

Talanta

Solná R, Sapelnikova S, Skládal P, Winther-Nielsen M, Carlsson C, Emnéus J, Ruzgas T.
PMID: 18969806
Talanta. 2005 Jan 30;65(2):349-57. doi: 10.1016/j.talanta.2004.07.005.

The screen-printed four-electrode system was used as the amperometric transducer for determination of phenols and pesticides using immobilised tyrosinase, peroxidase, acetylcholinesterase and butyrylcholinesterase. Acetylthiocholine chloride was chosen as substrate for cholinesterases to measure inhibition by pesticides, hydrogen peroxide served...

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Solná R, Sapelnikova S, Skládal P, et al. Multienzyme electrochemical array sensor for determination of phenols and pesticides. Talanta. 2005;65(2):349-57doi: 10.1016/j.talanta.2004.07.005.
Solná, R., Sapelnikova, S., Skládal, P., Winther-Nielsen, M., Carlsson, C., Emnéus, J., & Ruzgas, T. (2005). Multienzyme electrochemical array sensor for determination of phenols and pesticides. Talanta, 65(2), 349-57. https://doi.org/10.1016/j.talanta.2004.07.005
Solná, R, et al. "Multienzyme electrochemical array sensor for determination of phenols and pesticides." Talanta vol. 65,2 (2005): 349-57. doi: https://doi.org/10.1016/j.talanta.2004.07.005
Solná R, Sapelnikova S, Skládal P, Winther-Nielsen M, Carlsson C, Emnéus J, Ruzgas T. Multienzyme electrochemical array sensor for determination of phenols and pesticides. Talanta. 2005 Jan 30;65(2):349-57. doi: 10.1016/j.talanta.2004.07.005. PMID: 18969806.
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Extracellular ABTS-oxidizing activity of autochthonous fungal strains from Argentina in solid medium.

Revista iberoamericana de micologia

Saparrat MC, Margarita-Bucsinszky AM, Alfio-Tournier H, Cabello MN, Arambarri AM.
PMID: 15813698
Rev Iberoam Micol. 2000 Jun;17(2):64-8.

The screening for extracellular oxidases and peroxidases from autochthonous filamentous fungi isolated from different substrates is an important step towards the detection of extracellular fungal oxidative systems. Thirty-one autochthonous fungal strains from Argentina, belonging to different ecophysiological and taxonomic...

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Saparrat MC, Margarita-Bucsinszky AM, Alfio-Tournier H, et al. Extracellular ABTS-oxidizing activity of autochthonous fungal strains from Argentina in solid medium. Rev Iberoam Micol. 2000;17(2):64-8
Saparrat, M. C., Margarita-Bucsinszky, A. M., Alfio-Tournier, H., Cabello, M. N., & Arambarri, A. M. (2000). Extracellular ABTS-oxidizing activity of autochthonous fungal strains from Argentina in solid medium. Revista iberoamericana de micologia, 17(2), 64-8.
Saparrat, M C, et al. "Extracellular ABTS-oxidizing activity of autochthonous fungal strains from Argentina in solid medium." Revista iberoamericana de micologia vol. 17,2 (2000): 64-8.
Saparrat MC, Margarita-Bucsinszky AM, Alfio-Tournier H, Cabello MN, Arambarri AM. Extracellular ABTS-oxidizing activity of autochthonous fungal strains from Argentina in solid medium. Rev Iberoam Micol. 2000 Jun;17(2):64-8. PMID: 15813698.
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An implantable multifunctional needle type biosensor with integrated RF capability.

Conference proceedings : ... Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual Conference

Chiu NF, Wang JM, Yang LJ, Liao CW, Chen CH, Chen HC, Lu SS, Lin CW.
PMID: 17282599
Conf Proc IEEE Eng Med Biol Soc. 2005;2005:1933-6. doi: 10.1109/IEMBS.2005.1616830.

We report the development of an implantable multifunctional (glucose and cholesterol) needle type biosensor with integrated RF wireless circuitry for continuous in vivo monitoring of metabolites during short term stays in emergency room or intensive care unit. Silicon-based MEMS...

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Chiu NF, Wang JM, Yang LJ, et al. An implantable multifunctional needle type biosensor with integrated RF capability. Conf Proc IEEE Eng Med Biol Soc. 2005;2005:1933-6doi: 10.1109/IEMBS.2005.1616830.
Chiu, N. F., Wang, J. M., Yang, L. J., Liao, C. W., Chen, C. H., Chen, H. C., Lu, S. S., & Lin, C. W. (2005). An implantable multifunctional needle type biosensor with integrated RF capability. Conference proceedings : ... Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual Conference, 20051933-6. https://doi.org/10.1109/IEMBS.2005.1616830
Chiu, Nan-Fu, et al. "An implantable multifunctional needle type biosensor with integrated RF capability." Conference proceedings : ... Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual Conference vol. 2005 (2005): 1933-6. doi: https://doi.org/10.1109/IEMBS.2005.1616830
Chiu NF, Wang JM, Yang LJ, Liao CW, Chen CH, Chen HC, Lu SS, Lin CW. An implantable multifunctional needle type biosensor with integrated RF capability. Conf Proc IEEE Eng Med Biol Soc. 2005;2005:1933-6. doi: 10.1109/IEMBS.2005.1616830. PMID: 17282599.
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Enzymatically synthesized polyaniline film deposition studied by simultaneous open circuit potential and electrochemical quartz crystal microbalance measurements.

Journal of colloid and interface science

Carrillo N, León-Silva U, Avalos T, Nicho ME, Serna S, Castillon F, Farias M, Cruz-Silva R.
PMID: 22209413
J Colloid Interface Sci. 2012 Mar 01;369(1):103-10. doi: 10.1016/j.jcis.2011.12.021. Epub 2011 Dec 16.

The chemical and enzymatic deposition of polyaniline (PANI) films by in situ polymerization was studied and the resulting films were characterized. The film formation and polymerization processes were simultaneously monitored by the evolution of the open circuit potential and...

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Carrillo N, León-Silva U, Avalos T, et al. Enzymatically synthesized polyaniline film deposition studied by simultaneous open circuit potential and electrochemical quartz crystal microbalance measurements. J Colloid Interface Sci. 2011;369(1):103-10doi: 10.1016/j.jcis.2011.12.021.
Carrillo, N., León-Silva, U., Avalos, T., Nicho, M. E., Serna, S., Castillon, F., Farias, M., & Cruz-Silva, R. (2012). Enzymatically synthesized polyaniline film deposition studied by simultaneous open circuit potential and electrochemical quartz crystal microbalance measurements. Journal of colloid and interface science, 369(1), 103-10. https://doi.org/10.1016/j.jcis.2011.12.021
Carrillo, Norma, et al. "Enzymatically synthesized polyaniline film deposition studied by simultaneous open circuit potential and electrochemical quartz crystal microbalance measurements." Journal of colloid and interface science vol. 369,1 (2012): 103-10. doi: https://doi.org/10.1016/j.jcis.2011.12.021
Carrillo N, León-Silva U, Avalos T, Nicho ME, Serna S, Castillon F, Farias M, Cruz-Silva R. Enzymatically synthesized polyaniline film deposition studied by simultaneous open circuit potential and electrochemical quartz crystal microbalance measurements. J Colloid Interface Sci. 2012 Mar 01;369(1):103-10. doi: 10.1016/j.jcis.2011.12.021. Epub 2011 Dec 16. PMID: 22209413.
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An oxidoreductase from 'Alphonso' mango catalyzing biosynthesis of furaneol and reduction of reactive carbonyls.

SpringerPlus

Kulkarni R, Chidley H, Deshpande A, Schmidt A, Pujari K, Giri A, Gershenzon J, Gupta V.
PMID: 24133645
Springerplus. 2013 Oct 01;2:494. doi: 10.1186/2193-1801-2-494. eCollection 2013.

Two furanones, furaneol (4-hydroxy-2,5-dimethyl-3(2H)-furanone) and mesifuran (2,5-dimethyl-4-methoxy-3(2H)-furanone), are important constituents of flavor of the Alphonso cultivar of mango (Mangifera indica). To get insights into the biosynthesis of these furanones, we isolated an enone oxidoreductase gene from the Alphonso mango....

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Kulkarni R, Chidley H, Deshpande A, et al. An oxidoreductase from 'Alphonso' mango catalyzing biosynthesis of furaneol and reduction of reactive carbonyls. Springerplus. 2013;2:494doi: 10.1186/2193-1801-2-494.
Kulkarni, R., Chidley, H., Deshpande, A., Schmidt, A., Pujari, K., Giri, A., Gershenzon, J., & Gupta, V. (2013). An oxidoreductase from 'Alphonso' mango catalyzing biosynthesis of furaneol and reduction of reactive carbonyls. SpringerPlus, 2494. https://doi.org/10.1186/2193-1801-2-494
Kulkarni, Ram, et al. "An oxidoreductase from 'Alphonso' mango catalyzing biosynthesis of furaneol and reduction of reactive carbonyls." SpringerPlus vol. 2 (2013): 494. doi: https://doi.org/10.1186/2193-1801-2-494
Kulkarni R, Chidley H, Deshpande A, Schmidt A, Pujari K, Giri A, Gershenzon J, Gupta V. An oxidoreductase from 'Alphonso' mango catalyzing biosynthesis of furaneol and reduction of reactive carbonyls. Springerplus. 2013 Oct 01;2:494. doi: 10.1186/2193-1801-2-494. eCollection 2013. PMID: 24133645; PMCID: PMC3797322.
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The Structure and Biological Function of CREG.

Frontiers in cell and developmental biology

Ghobrial G, Araujo L, Jinwala F, Li S, Lee LY.
PMID: 30416997
Front Cell Dev Biol. 2018 Oct 26;6:136. doi: 10.3389/fcell.2018.00136. eCollection 2018.

The cellular repressor of E1A-stimulated genes (CREG) is a 220 amino acid glycoprotein structurally similar to oxidoreductases. However, CREG does not have enzymatic activities because it cannot bind to the cofactor flavin mononucleotide. Although CREG can be secreted, it...

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Ghobrial G, Araujo L, Jinwala F, et al. The Structure and Biological Function of CREG. Front Cell Dev Biol. 2018;6:136doi: 10.3389/fcell.2018.00136.
Ghobrial, G., Araujo, L., Jinwala, F., Li, S., & Lee, L. Y. (2018). The Structure and Biological Function of CREG. Frontiers in cell and developmental biology, 6136. https://doi.org/10.3389/fcell.2018.00136
Ghobrial, Gaby, et al. "The Structure and Biological Function of CREG." Frontiers in cell and developmental biology vol. 6 (2018): 136. doi: https://doi.org/10.3389/fcell.2018.00136
Ghobrial G, Araujo L, Jinwala F, Li S, Lee LY. The Structure and Biological Function of CREG. Front Cell Dev Biol. 2018 Oct 26;6:136. doi: 10.3389/fcell.2018.00136. eCollection 2018. PMID: 30416997; PMCID: PMC6212480.
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Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides.

Chemical science

Ukuwela AA, Bush AI, Wedd AG, Xiao Z.
PMID: 29675162
Chem Sci. 2017 Dec 06;9(5):1173-1183. doi: 10.1039/c7sc04416j. eCollection 2018 Feb 07.

Glutaredoxins (Grxs) are a family of glutathione (GSH)-dependent thiol-disulfide oxidoreductases. They feature GSH-binding sites that directly connect the reversible redox chemistry of protein thiols to the abundant cellular nonprotein thiol pool GSSG/GSH. This work studied the pathways for oxidation...

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Ukuwela AA, Bush AI, Wedd AG, et al. Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides. Chem Sci. 2017;9(5):1173-1183doi: 10.1039/c7sc04416j.
Ukuwela, A. A., Bush, A. I., Wedd, A. G., & Xiao, Z. (2018). Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides. Chemical science, 9(5), 1173-1183. https://doi.org/10.1039/c7sc04416j
Ukuwela, Ashwinie A, et al. "Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides." Chemical science vol. 9,5 (2018): 1173-1183. doi: https://doi.org/10.1039/c7sc04416j
Ukuwela AA, Bush AI, Wedd AG, Xiao Z. Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides. Chem Sci. 2017 Dec 06;9(5):1173-1183. doi: 10.1039/c7sc04416j. eCollection 2018 Feb 07. PMID: 29675162; PMCID: PMC5885593.
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Ethanol Dehydrogenase I Contributes to Growth and Sporulation Under Low Oxygen Condition via Detoxification of Acetaldehyde in .

Frontiers in microbiology

Zhang E, Cao Y, Xia Y.
PMID: 30186258
Front Microbiol. 2018 Aug 21;9:1932. doi: 10.3389/fmicb.2018.01932. eCollection 2018.

The entomopathogenic fungi encounter hypoxic conditions in both nature and artificial culture. Alcohol dehydrogenases (ADHs) are a group of oxidoreductases that occur in many organisms. Here we demonstrate that an alcohol dehydrogenase I,

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Zhang E, Cao Y, Xia Y. Ethanol Dehydrogenase I Contributes to Growth and Sporulation Under Low Oxygen Condition via Detoxification of Acetaldehyde in . Front Microbiol. 2018;9:1932doi: 10.3389/fmicb.2018.01932.
Zhang, E., Cao, Y., & Xia, Y. (2018). Ethanol Dehydrogenase I Contributes to Growth and Sporulation Under Low Oxygen Condition via Detoxification of Acetaldehyde in . Frontiers in microbiology, 91932. https://doi.org/10.3389/fmicb.2018.01932
Zhang, Erhao, et al. "Ethanol Dehydrogenase I Contributes to Growth and Sporulation Under Low Oxygen Condition via Detoxification of Acetaldehyde in ." Frontiers in microbiology vol. 9 (2018): 1932. doi: https://doi.org/10.3389/fmicb.2018.01932
Zhang E, Cao Y, Xia Y. Ethanol Dehydrogenase I Contributes to Growth and Sporulation Under Low Oxygen Condition via Detoxification of Acetaldehyde in . Front Microbiol. 2018 Aug 21;9:1932. doi: 10.3389/fmicb.2018.01932. eCollection 2018. PMID: 30186258; PMCID: PMC6110892.
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Showing 13 to 24 of 327 entries