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The mechanism of the effect of U18666a on blocking the activity of 3β-hydroxysterol Δ-24-reductase (DHCR24): molecular dynamics simulation study and free energy analysis.

Journal of molecular modeling

Quan X, Chen X, Sun D, Xu B, Zhao L, Shi X, Liu H, Gao B, Lu X.
PMID: 26815033
J Mol Model. 2016 Feb;22(2):46. doi: 10.1007/s00894-016-2907-2. Epub 2016 Jan 27.

DHCR24 encodes 3β-hydroxysterol-Δ(24)-reductase (DHCR24) catalyzing the cholesterol synthesis from desmosterol using the flavin adenine dinucleotide (FAD) as a co-factor. It is generally accepted that U18666a inhibits the reductase activity of DHCR24, but the detailed mechanism remains elusive. To explore...

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Quan X, Chen X, Sun D, et al. The mechanism of the effect of U18666a on blocking the activity of 3β-hydroxysterol Δ-24-reductase (DHCR24): molecular dynamics simulation study and free energy analysis. J Mol Model. 2016;22(2):46doi: 10.1007/s00894-016-2907-2.
Quan, X., Chen, X., Sun, D., Xu, B., Zhao, L., Shi, X., Liu, H., Gao, B., & Lu, X. (2016). The mechanism of the effect of U18666a on blocking the activity of 3β-hydroxysterol Δ-24-reductase (DHCR24): molecular dynamics simulation study and free energy analysis. Journal of molecular modeling, 22(2), 46. https://doi.org/10.1007/s00894-016-2907-2
Quan, Xiaoping, et al. "The mechanism of the effect of U18666a on blocking the activity of 3β-hydroxysterol Δ-24-reductase (DHCR24): molecular dynamics simulation study and free energy analysis." Journal of molecular modeling vol. 22,2 (2016): 46. doi: https://doi.org/10.1007/s00894-016-2907-2
Quan X, Chen X, Sun D, Xu B, Zhao L, Shi X, Liu H, Gao B, Lu X. The mechanism of the effect of U18666a on blocking the activity of 3β-hydroxysterol Δ-24-reductase (DHCR24): molecular dynamics simulation study and free energy analysis. J Mol Model. 2016 Feb;22(2):46. doi: 10.1007/s00894-016-2907-2. Epub 2016 Jan 27. PMID: 26815033.
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Characterisation of the flavin adenine dinucleotide binding region of .

Biochemistry and biophysics reports

Boateng MO, Corrigall AV, Sturrock E, Meissner PN.
PMID: 29124218
Biochem Biophys Rep. 2015 Oct 29;4:306-311. doi: 10.1016/j.bbrep.2015.10.006. eCollection 2015 Dec.

Protoporphyrinogen oxidase (PPOX), the penultimate enzyme in the haem biosynthetic pathway catalysers the six electron oxidation of protoporphyrinogen-IX to protoporphyrin-IX, in the presence of flavin adenine dinucleotide (FAD) and oxygen. In humans, partial defects in PPOX result in variegate...

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Boateng MO, Corrigall AV, Sturrock E, et al. Characterisation of the flavin adenine dinucleotide binding region of . Biochem Biophys Rep. 2015;4:306-311doi: 10.1016/j.bbrep.2015.10.006.
Boateng, M. O., Corrigall, A. V., Sturrock, E., & Meissner, P. N. (2015). Characterisation of the flavin adenine dinucleotide binding region of . Biochemistry and biophysics reports, 4306-311. https://doi.org/10.1016/j.bbrep.2015.10.006
Boateng, Mavis O, et al. "Characterisation of the flavin adenine dinucleotide binding region of ." Biochemistry and biophysics reports vol. 4 (2015): 306-311. doi: https://doi.org/10.1016/j.bbrep.2015.10.006
Boateng MO, Corrigall AV, Sturrock E, Meissner PN. Characterisation of the flavin adenine dinucleotide binding region of . Biochem Biophys Rep. 2015 Oct 29;4:306-311. doi: 10.1016/j.bbrep.2015.10.006. eCollection 2015 Dec. PMID: 29124218; PMCID: PMC5669401.
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Application of Negative Curvature Hollow-Core Fiber in an Optical Fiber Sensor Setup for Multiphoton Spectroscopy.

Sensors (Basel, Switzerland)

Popenda MA, Stawska HI, Mazur LM, Jakubowski K, Kosolapov A, Kolyadin A, Bereś-Pawlik E.
PMID: 28984838
Sensors (Basel). 2017 Oct 06;17(10). doi: 10.3390/s17102278.

In this paper, an application of negative curvature hollow core fiber (NCHCF) in an all-fiber, multiphoton fluorescence sensor setup is presented. The dispersion parameter (D) of this fiber does not exceed the value of 5 ps/nm × km across...

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Popenda MA, Stawska HI, Mazur LM, et al. Application of Negative Curvature Hollow-Core Fiber in an Optical Fiber Sensor Setup for Multiphoton Spectroscopy. Sensors (Basel). 2017;17(10)doi: 10.3390/s17102278.
Popenda, M. A., Stawska, H. I., Mazur, L. M., Jakubowski, K., Kosolapov, A., Kolyadin, A., & Bereś-Pawlik, E. (2017). Application of Negative Curvature Hollow-Core Fiber in an Optical Fiber Sensor Setup for Multiphoton Spectroscopy. Sensors (Basel, Switzerland), 17(10), . https://doi.org/10.3390/s17102278
Popenda, Maciej Andrzej, et al. "Application of Negative Curvature Hollow-Core Fiber in an Optical Fiber Sensor Setup for Multiphoton Spectroscopy." Sensors (Basel, Switzerland) vol. 17,10 (2017). doi: https://doi.org/10.3390/s17102278
Popenda MA, Stawska HI, Mazur LM, Jakubowski K, Kosolapov A, Kolyadin A, Bereś-Pawlik E. Application of Negative Curvature Hollow-Core Fiber in an Optical Fiber Sensor Setup for Multiphoton Spectroscopy. Sensors (Basel). 2017 Oct 06;17(10). doi: 10.3390/s17102278. PMID: 28984838; PMCID: PMC5677438.
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Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis.

Chemical science

Harada H, Onoda A, Uchihashi T, Watanabe H, Sunagawa N, Samejima M, Igarashi K, Hayashi T.
PMID: 28989682
Chem Sci. 2017 Sep 01;8(9):6561-6565. doi: 10.1039/c7sc01672g. Epub 2017 Aug 03.

Cellobiose dehydrogenase (CDH) is a dual domain flavocytochrome, which consists of a dehydrogenase (DH) domain containing a flavin adenine dinucleotide and a cytochrome (CYT) domain containing

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Harada H, Onoda A, Uchihashi T, et al. Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis. Chem Sci. 2017;8(9):6561-6565doi: 10.1039/c7sc01672g.
Harada, H., Onoda, A., Uchihashi, T., Watanabe, H., Sunagawa, N., Samejima, M., Igarashi, K., & Hayashi, T. (2017). Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis. Chemical science, 8(9), 6561-6565. https://doi.org/10.1039/c7sc01672g
Harada, Hirofumi, et al. "Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis." Chemical science vol. 8,9 (2017): 6561-6565. doi: https://doi.org/10.1039/c7sc01672g
Harada H, Onoda A, Uchihashi T, Watanabe H, Sunagawa N, Samejima M, Igarashi K, Hayashi T. Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis. Chem Sci. 2017 Sep 01;8(9):6561-6565. doi: 10.1039/c7sc01672g. Epub 2017 Aug 03. PMID: 28989682; PMCID: PMC5627353.
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Energy and Potassium Ion Homeostasis during Gamma Oscillations.

Frontiers in molecular neuroscience

Kann O, Hollnagel JO, Elzoheiry S, Schneider J.
PMID: 27378847
Front Mol Neurosci. 2016 Jun 16;9:47. doi: 10.3389/fnmol.2016.00047. eCollection 2016.

Fast neuronal network oscillations in the gamma frequency band (30-100 Hz) occur in various cortex regions, require timed synaptic excitation and inhibition with glutamate and GABA, respectively, and are associated with higher brain functions such as sensory perception, attentional...

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Kann O, Hollnagel JO, Elzoheiry S, et al. Energy and Potassium Ion Homeostasis during Gamma Oscillations. Front Mol Neurosci. 2016;9:47doi: 10.3389/fnmol.2016.00047.
Kann, O., Hollnagel, J. O., Elzoheiry, S., & Schneider, J. (2016). Energy and Potassium Ion Homeostasis during Gamma Oscillations. Frontiers in molecular neuroscience, 947. https://doi.org/10.3389/fnmol.2016.00047
Kann, Oliver, et al. "Energy and Potassium Ion Homeostasis during Gamma Oscillations." Frontiers in molecular neuroscience vol. 9 (2016): 47. doi: https://doi.org/10.3389/fnmol.2016.00047
Kann O, Hollnagel JO, Elzoheiry S, Schneider J. Energy and Potassium Ion Homeostasis during Gamma Oscillations. Front Mol Neurosci. 2016 Jun 16;9:47. doi: 10.3389/fnmol.2016.00047. eCollection 2016. PMID: 27378847; PMCID: PMC4909733.
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Pathological changes in platelet histamine oxidases in atopic eczema.

Mediators of inflammation

Kiehl R, Ionescu G.
PMID: 18475554
Mediators Inflamm. 1993;2(6):403-6. doi: 10.1155/S0962935193000560.

Increased plasma histamine levels were associated with significantly lowered diamine and type B monoamine oxidase activities in platelet-rich plasma of atopic eczema (AE) patients. The diamine oxidase has almost normal cofactor levels (pyridoxal phosphate and Cu(2+)) but the cofactor...

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Kiehl R, Ionescu G. Pathological changes in platelet histamine oxidases in atopic eczema. Mediators Inflamm. 1993;2(6):403-6doi: 10.1155/S0962935193000560.
Kiehl, R., & Ionescu, G. (1993). Pathological changes in platelet histamine oxidases in atopic eczema. Mediators of inflammation, 2(6), 403-6. https://doi.org/10.1155/S0962935193000560
Kiehl, R, and Ionescu, G. "Pathological changes in platelet histamine oxidases in atopic eczema." Mediators of inflammation vol. 2,6 (1993): 403-6. doi: https://doi.org/10.1155/S0962935193000560
Kiehl R, Ionescu G. Pathological changes in platelet histamine oxidases in atopic eczema. Mediators Inflamm. 1993;2(6):403-6. doi: 10.1155/S0962935193000560. PMID: 18475554; PMCID: PMC2365432.
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Expression in Escherichia coli of Cytochrome c Reductase Activity from a Maize NADH:Nitrate Reductase Complementary DNA.

Plant physiology

Campbell WH.
PMID: 16668941
Plant Physiol. 1992 Jun;99(2):693-9. doi: 10.1104/pp.99.2.693.

A cDNA clone was isolated from a maize (Zea mays L. cv W64AxW183E) scutellum lambdagt11 library using maize leaf NADH:nitrate reductase Zmnr1 cDNA clone as a hybridization probe; it was designated Zmnr1S. Zmnr1S was shown to be an NADH:nitrate...

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Campbell WH. Expression in Escherichia coli of Cytochrome c Reductase Activity from a Maize NADH:Nitrate Reductase Complementary DNA. Plant Physiol. 1992;99(2):693-9doi: 10.1104/pp.99.2.693.
Campbell, W. H. (1992). Expression in Escherichia coli of Cytochrome c Reductase Activity from a Maize NADH:Nitrate Reductase Complementary DNA. Plant physiology, 99(2), 693-9. https://doi.org/10.1104/pp.99.2.693
Campbell, W H. "Expression in Escherichia coli of Cytochrome c Reductase Activity from a Maize NADH:Nitrate Reductase Complementary DNA." Plant physiology vol. 99,2 (1992): 693-9. doi: https://doi.org/10.1104/pp.99.2.693
Campbell WH. Expression in Escherichia coli of Cytochrome c Reductase Activity from a Maize NADH:Nitrate Reductase Complementary DNA. Plant Physiol. 1992 Jun;99(2):693-9. doi: 10.1104/pp.99.2.693. PMID: 16668941; PMCID: PMC1080520.
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The return of the Scarlet Pimpernel: cobalamin in inflammation II - cobalamins can both selectively promote all three nitric oxide synthases (NOS), particularly iNOS and eNOS, and, as needed, selectively inhibit iNOS and nNOS.

Journal of nutritional & environmental medicine

Wheatley C.
PMID: 18836533
J Nutr Environ Med. 2007 Sep;16(3):181-211. doi: 10.1080/10520290701791839.

The up-regulation of transcobalamins [hitherto posited as indicating a central need for cobalamin (Cbl) in inflammation], whose expression, like inducible nitric oxide synthase (iNOS), is Sp1- and interferondependent, together with increased intracellular formation of glutathionylcobalamin (GSCbl), adenosylcobalamin (AdoCbl), methylcobalamin...

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Wheatley C. The return of the Scarlet Pimpernel: cobalamin in inflammation II - cobalamins can both selectively promote all three nitric oxide synthases (NOS), particularly iNOS and eNOS, and, as needed, selectively inhibit iNOS and nNOS. J Nutr Environ Med. 2007;16(3):181-211doi: 10.1080/10520290701791839.
Wheatley, C. (2007). The return of the Scarlet Pimpernel: cobalamin in inflammation II - cobalamins can both selectively promote all three nitric oxide synthases (NOS), particularly iNOS and eNOS, and, as needed, selectively inhibit iNOS and nNOS. Journal of nutritional & environmental medicine, 16(3), 181-211. https://doi.org/10.1080/10520290701791839
Wheatley, Carmen. "The return of the Scarlet Pimpernel: cobalamin in inflammation II - cobalamins can both selectively promote all three nitric oxide synthases (NOS), particularly iNOS and eNOS, and, as needed, selectively inhibit iNOS and nNOS." Journal of nutritional & environmental medicine vol. 16,3 (2007): 181-211. doi: https://doi.org/10.1080/10520290701791839
Wheatley C. The return of the Scarlet Pimpernel: cobalamin in inflammation II - cobalamins can both selectively promote all three nitric oxide synthases (NOS), particularly iNOS and eNOS, and, as needed, selectively inhibit iNOS and nNOS. J Nutr Environ Med. 2007 Sep;16(3):181-211. doi: 10.1080/10520290701791839. PMID: 18836533; PMCID: PMC2556189.
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Biosynthesis of phenolic compounds in first internodes of sorghum: lignin and related products.

Plant physiology

Stafford HA.
PMID: 16656525
Plant Physiol. 1967 Mar;42(3):450-5. doi: 10.1104/pp.42.3.450.

Lignin biosynthesis in excised tissues of Sorghum vulgare variety Wheatland milo incubated in air with and without prior infiltration with H(2)O was presumably limited by H(2)O(2) production and was dependent upon an endogenous substrate, probably starch. In solution culture...

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Stafford HA. Biosynthesis of phenolic compounds in first internodes of sorghum: lignin and related products. Plant Physiol. 1967;42(3):450-5doi: 10.1104/pp.42.3.450.
Stafford, H. A. (1967). Biosynthesis of phenolic compounds in first internodes of sorghum: lignin and related products. Plant physiology, 42(3), 450-5. https://doi.org/10.1104/pp.42.3.450
Stafford, H A. "Biosynthesis of phenolic compounds in first internodes of sorghum: lignin and related products." Plant physiology vol. 42,3 (1967): 450-5. doi: https://doi.org/10.1104/pp.42.3.450
Stafford HA. Biosynthesis of phenolic compounds in first internodes of sorghum: lignin and related products. Plant Physiol. 1967 Mar;42(3):450-5. doi: 10.1104/pp.42.3.450. PMID: 16656525; PMCID: PMC1086557.
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The Flavin Content of Clovers Relative to Symbiosis with a Riboflavin-requiring Mutant of Rhizobium trifoli.

Plant physiology

Pankhurst CE.
PMID: 16658676
Plant Physiol. 1974 Feb;53(2):198-205. doi: 10.1104/pp.53.2.198.

A riboflavin-requiring auxotroph of Rhizobium trifolii (T1/D-his(r)-15) formed ineffective root nodules on red clover and on two cultivars of subterranean clover, but produced almost fully effective nodules on several other cultivars of subterranean clover. Fluorescence and bioassay measurements of...

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Pankhurst CE. The Flavin Content of Clovers Relative to Symbiosis with a Riboflavin-requiring Mutant of Rhizobium trifoli. Plant Physiol. 1974;53(2):198-205doi: 10.1104/pp.53.2.198.
Pankhurst, C. E. (1974). The Flavin Content of Clovers Relative to Symbiosis with a Riboflavin-requiring Mutant of Rhizobium trifoli. Plant physiology, 53(2), 198-205. https://doi.org/10.1104/pp.53.2.198
Pankhurst, C E. "The Flavin Content of Clovers Relative to Symbiosis with a Riboflavin-requiring Mutant of Rhizobium trifoli." Plant physiology vol. 53,2 (1974): 198-205. doi: https://doi.org/10.1104/pp.53.2.198
Pankhurst CE. The Flavin Content of Clovers Relative to Symbiosis with a Riboflavin-requiring Mutant of Rhizobium trifoli. Plant Physiol. 1974 Feb;53(2):198-205. doi: 10.1104/pp.53.2.198. PMID: 16658676; PMCID: PMC541364.
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A Poly(amphiphilic pyrrole)-Flavin Reductase Electrode for Amperometric Determination of Flavins.

Analytical chemistry

Cosnier S, Fontecave M, Limosin D, Nivière V.
PMID: 21639330
Anal Chem. 1997 Aug 01;69(15):3095-9. doi: 10.1021/ac961041+.

The electropolymerization of a flavin reductase-amphiphilic pyrrole ammonium mixture previously adsorbed on the electrode surface provides the efficient entrapment of the enzyme in a functionalized polypyrrole film. The enzyme film was characterized and applied to the detection of several...

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Cosnier S, Fontecave M, Limosin D, et al. A Poly(amphiphilic pyrrole)-Flavin Reductase Electrode for Amperometric Determination of Flavins. Anal Chem. 1997;69(15):3095-9doi: 10.1021/ac961041+.
Cosnier, S., Fontecave, M., Limosin, D., & Nivière, V. (1997). A Poly(amphiphilic pyrrole)-Flavin Reductase Electrode for Amperometric Determination of Flavins. Analytical chemistry, 69(15), 3095-9. https://doi.org/10.1021/ac961041+
Cosnier, S, et al. "A Poly(amphiphilic pyrrole)-Flavin Reductase Electrode for Amperometric Determination of Flavins." Analytical chemistry vol. 69,15 (1997): 3095-9. doi: https://doi.org/10.1021/ac961041+
Cosnier S, Fontecave M, Limosin D, Nivière V. A Poly(amphiphilic pyrrole)-Flavin Reductase Electrode for Amperometric Determination of Flavins. Anal Chem. 1997 Aug 01;69(15):3095-9. doi: 10.1021/ac961041+. PMID: 21639330.
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Effects of electrolyte and pH on the behavior of cross-linked films of ferrocene-modified poly(ethylenimine).

Langmuir : the ACS journal of surfaces and colloids

Merchant SA, Glatzhofer DT, Schmidtke DW.
PMID: 17902716
Langmuir. 2007 Oct 23;23(22):11295-302. doi: 10.1021/la701521s. Epub 2007 Sep 29.

Ferrocene redox polymers based on the coupling of ferrocenecarboxaldehyde to both linear and branched poly(ethylenimine) (PEI) have been prepared to investigate the effects of pH, electrolyte, and cross-linking on electron charge transport and film swelling. The redox behavior of...

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Merchant SA, Glatzhofer DT, Schmidtke DW. Effects of electrolyte and pH on the behavior of cross-linked films of ferrocene-modified poly(ethylenimine). Langmuir. 2007;23(22):11295-302doi: 10.1021/la701521s.
Merchant, S. A., Glatzhofer, D. T., & Schmidtke, D. W. (2007). Effects of electrolyte and pH on the behavior of cross-linked films of ferrocene-modified poly(ethylenimine). Langmuir : the ACS journal of surfaces and colloids, 23(22), 11295-302. https://doi.org/10.1021/la701521s
Merchant, Stephen A, et al. "Effects of electrolyte and pH on the behavior of cross-linked films of ferrocene-modified poly(ethylenimine)." Langmuir : the ACS journal of surfaces and colloids vol. 23,22 (2007): 11295-302. doi: https://doi.org/10.1021/la701521s
Merchant SA, Glatzhofer DT, Schmidtke DW. Effects of electrolyte and pH on the behavior of cross-linked films of ferrocene-modified poly(ethylenimine). Langmuir. 2007 Oct 23;23(22):11295-302. doi: 10.1021/la701521s. Epub 2007 Sep 29. PMID: 17902716.
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Showing 1 to 12 of 214 entries