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Showing 1 to 12 of 171 entries
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Heme as a Target for Therapeutic Interventions.

Frontiers in pharmacology

Immenschuh S, Vijayan V, Janciauskiene S, Gueler F.
PMID: 28420988
Front Pharmacol. 2017 Apr 04;8:146. doi: 10.3389/fphar.2017.00146. eCollection 2017.

Heme is a complex of iron and the tetrapyrrole protoporphyrin IX with essential functions in aerobic organisms. Heme is the prosthetic group of hemoproteins such as hemoglobin and myoglobin, which are crucial for reversible oxygen binding and transport. By...

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Immenschuh S, Vijayan V, Janciauskiene S, et al. Heme as a Target for Therapeutic Interventions. Front Pharmacol. 2017;8:146doi: 10.3389/fphar.2017.00146.
Immenschuh, S., Vijayan, V., Janciauskiene, S., & Gueler, F. (2017). Heme as a Target for Therapeutic Interventions. Frontiers in pharmacology, 8146. https://doi.org/10.3389/fphar.2017.00146
Immenschuh, Stephan, et al. "Heme as a Target for Therapeutic Interventions." Frontiers in pharmacology vol. 8 (2017): 146. doi: https://doi.org/10.3389/fphar.2017.00146
Immenschuh S, Vijayan V, Janciauskiene S, Gueler F. Heme as a Target for Therapeutic Interventions. Front Pharmacol. 2017 Apr 04;8:146. doi: 10.3389/fphar.2017.00146. eCollection 2017. PMID: 28420988; PMCID: PMC5378770.
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Osamu Hayaishi-from the discovery of oxygenases in soil microorganisms to unraveling the enigma of sleep in mammals.

Temperature (Austin, Tex.)

Lazarus M, Huang ZL, Urade Y.
PMID: 27227031
Temperature (Austin). 2015 Jul 25;2(3):303-7. doi: 10.1080/23328940.2015.1072658. eCollection 2015.

No abstract available.

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Lazarus M, Huang ZL, Urade Y. Osamu Hayaishi-from the discovery of oxygenases in soil microorganisms to unraveling the enigma of sleep in mammals. Temperature (Austin). 2015;2(3):303-7doi: 10.1080/23328940.2015.1072658.
Lazarus, M., Huang, Z. L., & Urade, Y. (2015). Osamu Hayaishi-from the discovery of oxygenases in soil microorganisms to unraveling the enigma of sleep in mammals. Temperature (Austin, Tex.), 2(3), 303-7. https://doi.org/10.1080/23328940.2015.1072658
Lazarus, Michael, et al. "Osamu Hayaishi-from the discovery of oxygenases in soil microorganisms to unraveling the enigma of sleep in mammals." Temperature (Austin, Tex.) vol. 2,3 (2015): 303-7. doi: https://doi.org/10.1080/23328940.2015.1072658
Lazarus M, Huang ZL, Urade Y. Osamu Hayaishi-from the discovery of oxygenases in soil microorganisms to unraveling the enigma of sleep in mammals. Temperature (Austin). 2015 Jul 25;2(3):303-7. doi: 10.1080/23328940.2015.1072658. eCollection 2015. PMID: 27227031; PMCID: PMC4843939.
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Activation of Dioxygen at a Lewis Acidic Nickel(II) Complex: Characterization of a Metastable Organoperoxide Complex.

Angewandte Chemie (International ed. in English)

Holze P, Corona T, Frank N, Braun-Cula B, Herwig C, Company A, Limberg C.
PMID: 28111896
Angew Chem Int Ed Engl. 2017 Feb 20;56(9):2307-2311. doi: 10.1002/anie.201609526. Epub 2017 Jan 23.

In metal-mediated O

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Holze P, Corona T, Frank N, et al. Activation of Dioxygen at a Lewis Acidic Nickel(II) Complex: Characterization of a Metastable Organoperoxide Complex. Angew Chem Int Ed Engl. 2017;56(9):2307-2311doi: 10.1002/anie.201609526.
Holze, P., Corona, T., Frank, N., Braun-Cula, B., Herwig, C., Company, A., & Limberg, C. (2017). Activation of Dioxygen at a Lewis Acidic Nickel(II) Complex: Characterization of a Metastable Organoperoxide Complex. Angewandte Chemie (International ed. in English), 56(9), 2307-2311. https://doi.org/10.1002/anie.201609526
Holze, Patrick, et al. "Activation of Dioxygen at a Lewis Acidic Nickel(II) Complex: Characterization of a Metastable Organoperoxide Complex." Angewandte Chemie (International ed. in English) vol. 56,9 (2017): 2307-2311. doi: https://doi.org/10.1002/anie.201609526
Holze P, Corona T, Frank N, Braun-Cula B, Herwig C, Company A, Limberg C. Activation of Dioxygen at a Lewis Acidic Nickel(II) Complex: Characterization of a Metastable Organoperoxide Complex. Angew Chem Int Ed Engl. 2017 Feb 20;56(9):2307-2311. doi: 10.1002/anie.201609526. Epub 2017 Jan 23. PMID: 28111896.
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Formation of 1-octen-3-ol from Aspergillus flavus conidia is accelerated after disruption of cells independently of Ppo oxygenases, and is not a main cause of inhibition of germination.

PeerJ

Miyamoto K, Murakami T, Kakumyan P, Keller NP, Matsui K.
PMID: 24883255
PeerJ. 2014 May 20;2:e395. doi: 10.7717/peerj.395. eCollection 2014.

Eight-carbon (C8) volatiles, such as 1-octen-3-ol, are ubiquitous among fungi. They are the volatiles critical for aroma and flavor of fungi, and assumed to be signals controlling germination of several fungi. In this study, we found that intact Aspergillus...

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Miyamoto K, Murakami T, Kakumyan P, et al. Formation of 1-octen-3-ol from Aspergillus flavus conidia is accelerated after disruption of cells independently of Ppo oxygenases, and is not a main cause of inhibition of germination. PeerJ. 2014;2:e395doi: 10.7717/peerj.395.
Miyamoto, K., Murakami, T., Kakumyan, P., Keller, N. P., & Matsui, K. (2014). Formation of 1-octen-3-ol from Aspergillus flavus conidia is accelerated after disruption of cells independently of Ppo oxygenases, and is not a main cause of inhibition of germination. PeerJ, 2e395. https://doi.org/10.7717/peerj.395
Miyamoto, Kana, et al. "Formation of 1-octen-3-ol from Aspergillus flavus conidia is accelerated after disruption of cells independently of Ppo oxygenases, and is not a main cause of inhibition of germination." PeerJ vol. 2 (2014): e395. doi: https://doi.org/10.7717/peerj.395
Miyamoto K, Murakami T, Kakumyan P, Keller NP, Matsui K. Formation of 1-octen-3-ol from Aspergillus flavus conidia is accelerated after disruption of cells independently of Ppo oxygenases, and is not a main cause of inhibition of germination. PeerJ. 2014 May 20;2:e395. doi: 10.7717/peerj.395. eCollection 2014. PMID: 24883255; PMCID: PMC4034645.
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Coordinated and Iterative Enzyme Catalysis in Fungal Polyketide Biosynthesis.

ACS catalysis

Hang L, Liu N, Tang Y.
PMID: 28529817
ACS Catal. 2016 Sep 02;6(9):5935-5945. doi: 10.1021/acscatal.6b01559. Epub 2016 Jul 27.

Fungal polyketides are natural products with great chemical diversity that exhibit a wide range of biological activity. This chemical diversity stems from specialized enzymes encoded in the biosynthetic gene cluster responsible for the natural product biosynthesis. Fungal polyketide synthases...

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Hang L, Liu N, Tang Y. Coordinated and Iterative Enzyme Catalysis in Fungal Polyketide Biosynthesis. ACS Catal. 2016;6(9):5935-5945doi: 10.1021/acscatal.6b01559.
Hang, L., Liu, N., & Tang, Y. (2016). Coordinated and Iterative Enzyme Catalysis in Fungal Polyketide Biosynthesis. ACS catalysis, 6(9), 5935-5945. https://doi.org/10.1021/acscatal.6b01559
Hang, Leibniz, et al. "Coordinated and Iterative Enzyme Catalysis in Fungal Polyketide Biosynthesis." ACS catalysis vol. 6,9 (2016): 5935-5945. doi: https://doi.org/10.1021/acscatal.6b01559
Hang L, Liu N, Tang Y. Coordinated and Iterative Enzyme Catalysis in Fungal Polyketide Biosynthesis. ACS Catal. 2016 Sep 02;6(9):5935-5945. doi: 10.1021/acscatal.6b01559. Epub 2016 Jul 27. PMID: 28529817; PMCID: PMC5436725.
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Purification and identification of trichloroethylene induced proteins from Stenotrophomonas maltophilia PM102 by immuno-affinity-chromatography and MALDI-TOF Mass spectrometry.

SpringerPlus

Mukherjee P, Roy P.
PMID: 23741645
Springerplus. 2013 May 07;2(1):207. doi: 10.1186/2193-1801-2-207. Print 2013 Dec.

A novel bacterial isolate capable of growth on trichloroethylene as the sole carbon source was identified as Stenotrophomonas maltophilia PM102 by 16S rDNA sequencing (GenBank Acc.no. JQ797560). Serum was obtained from a rabbit immunized with the total protein extracted...

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Mukherjee P, Roy P. Purification and identification of trichloroethylene induced proteins from Stenotrophomonas maltophilia PM102 by immuno-affinity-chromatography and MALDI-TOF Mass spectrometry. Springerplus. 2013;2(1):207doi: 10.1186/2193-1801-2-207.
Mukherjee, P., & Roy, P. (2013). Purification and identification of trichloroethylene induced proteins from Stenotrophomonas maltophilia PM102 by immuno-affinity-chromatography and MALDI-TOF Mass spectrometry. SpringerPlus, 2(1), 207. https://doi.org/10.1186/2193-1801-2-207
Mukherjee, Piyali, and Roy, Pranab. "Purification and identification of trichloroethylene induced proteins from Stenotrophomonas maltophilia PM102 by immuno-affinity-chromatography and MALDI-TOF Mass spectrometry." SpringerPlus vol. 2,1 (2013): 207. doi: https://doi.org/10.1186/2193-1801-2-207
Mukherjee P, Roy P. Purification and identification of trichloroethylene induced proteins from Stenotrophomonas maltophilia PM102 by immuno-affinity-chromatography and MALDI-TOF Mass spectrometry. Springerplus. 2013 May 07;2(1):207. doi: 10.1186/2193-1801-2-207. Print 2013 Dec. PMID: 23741645; PMCID: PMC3664754.
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Multicopper Oxidases and Oxygenases.

Chemical reviews

Solomon EI, Sundaram UM, Machonkin TE.
PMID: 11848837
Chem Rev. 1996 Nov 07;96(7):2563-2606. doi: 10.1021/cr950046o.

No abstract available.

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Solomon EI, Sundaram UM, Machonkin TE. Multicopper Oxidases and Oxygenases. Chem Rev. 1996;96(7):2563-2606doi: 10.1021/cr950046o.
Solomon, E. I., Sundaram, U. M., & Machonkin, T. E. (1996). Multicopper Oxidases and Oxygenases. Chemical reviews, 96(7), 2563-2606. https://doi.org/10.1021/cr950046o
Solomon, Edward I., et al. "Multicopper Oxidases and Oxygenases." Chemical reviews vol. 96,7 (1996): 2563-2606. doi: https://doi.org/10.1021/cr950046o
Solomon EI, Sundaram UM, Machonkin TE. Multicopper Oxidases and Oxygenases. Chem Rev. 1996 Nov 07;96(7):2563-2606. doi: 10.1021/cr950046o. PMID: 11848837.
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Mono- and binuclear complexes of iron(II) and iron(III) with an N4O ligand: synthesis, structures and catalytic properties in alkane oxidation.

Dalton transactions (Cambridge, England : 2003)

Li F, Wang M, Ma C, Gao A, Chen H, Sun L.
PMID: 16705341
Dalton Trans. 2006 May 28;(20):2427-34. doi: 10.1039/b516697g. Epub 2006 Mar 15.

Three mononuclear iron complexes and one binuclear iron complex, [Fe(tpoen)Cl].0.5(Fe2OCl6) (1), [Fe(tpoen)Cl]PF6 (2), Fe(tpoen)Cl3 (3) and [[Fe(tpoen)]2(mu-O)](ClO4)4 (4) (tpoen = N-(2-pyridylmethoxyethyl)-N,N-bis(2-pyridylmethyl)amine), were synthesized as functional models of non-heme iron oxygenases. Crystallographic studies revealed that the Fe(II) center of 1...

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Li F, Wang M, Ma C, et al. Mono- and binuclear complexes of iron(II) and iron(III) with an N4O ligand: synthesis, structures and catalytic properties in alkane oxidation. Dalton Trans. 2006;(20):2427-34doi: 10.1039/b516697g.
Li, F., Wang, M., Ma, C., Gao, A., Chen, H., & Sun, L. (2006). Mono- and binuclear complexes of iron(II) and iron(III) with an N4O ligand: synthesis, structures and catalytic properties in alkane oxidation. Dalton transactions (Cambridge, England : 2003), (20), 2427-34. https://doi.org/10.1039/b516697g
Li, Fei, et al. "Mono- and binuclear complexes of iron(II) and iron(III) with an N4O ligand: synthesis, structures and catalytic properties in alkane oxidation." Dalton transactions (Cambridge, England : 2003) vol. ,20 (2006): 2427-34. doi: https://doi.org/10.1039/b516697g
Li F, Wang M, Ma C, Gao A, Chen H, Sun L. Mono- and binuclear complexes of iron(II) and iron(III) with an N4O ligand: synthesis, structures and catalytic properties in alkane oxidation. Dalton Trans. 2006 May 28;(20):2427-34. doi: 10.1039/b516697g. Epub 2006 Mar 15. PMID: 16705341.
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Caenorhabditis Elegans Mutants Predict Regulation of Fatty Acids and Endocannabinoids by the CYP-35A Gene Family.

Frontiers in pharmacology

Aarnio V, Lehtonen M, Storvik M, Callaway JC, Lakso M, Wong G.
PMID: 21687507
Front Pharmacol. 2011 Mar 18;2:12. doi: 10.3389/fphar.2011.00012. eCollection 2011.

BACKGROUND: Cytochrome P450s (CYPs) are mono-oxygenases that metabolize endogenous compounds, such as fatty acids and lipid signaling molecules, and furthermore have a role in metabolism of xenobiotics. In order to investigate the role of CYP genes in fat metabolism...

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Aarnio V, Lehtonen M, Storvik M, et al. Caenorhabditis Elegans Mutants Predict Regulation of Fatty Acids and Endocannabinoids by the CYP-35A Gene Family. Front Pharmacol. 2011;2:12doi: 10.3389/fphar.2011.00012.
Aarnio, V., Lehtonen, M., Storvik, M., Callaway, J. C., Lakso, M., & Wong, G. (2011). Caenorhabditis Elegans Mutants Predict Regulation of Fatty Acids and Endocannabinoids by the CYP-35A Gene Family. Frontiers in pharmacology, 212. https://doi.org/10.3389/fphar.2011.00012
Aarnio, Vuokko, et al. "Caenorhabditis Elegans Mutants Predict Regulation of Fatty Acids and Endocannabinoids by the CYP-35A Gene Family." Frontiers in pharmacology vol. 2 (2011): 12. doi: https://doi.org/10.3389/fphar.2011.00012
Aarnio V, Lehtonen M, Storvik M, Callaway JC, Lakso M, Wong G. Caenorhabditis Elegans Mutants Predict Regulation of Fatty Acids and Endocannabinoids by the CYP-35A Gene Family. Front Pharmacol. 2011 Mar 18;2:12. doi: 10.3389/fphar.2011.00012. eCollection 2011. PMID: 21687507; PMCID: PMC3108558.
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Pharmacovigilance: effects of herbal components on human drugs interactions involving cytochrome P450.

Bioinformation

Saxena A, Tripathi KP, Roy S, Khan F, Sharma A.
PMID: 19255634
Bioinformation. 2008;3(5):198-204. doi: 10.6026/97320630003198. Epub 2008 Dec 31.

Cytochrome P450 (CYP P450) enzymes are a superfamily of mono-oxygenases that are found in all kingdoms of life. The CYP P450 enzymes constitute a large superfamily of haem-thiolate proteins involved in the metabolism of a wide variety of both...

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Saxena A, Tripathi KP, Roy S, et al. Pharmacovigilance: effects of herbal components on human drugs interactions involving cytochrome P450. Bioinformation. 2008;3(5):198-204doi: 10.6026/97320630003198.
Saxena, A., Tripathi, K. P., Roy, S., Khan, F., & Sharma, A. (2008). Pharmacovigilance: effects of herbal components on human drugs interactions involving cytochrome P450. Bioinformation, 3(5), 198-204. https://doi.org/10.6026/97320630003198
Saxena, Akansha, et al. "Pharmacovigilance: effects of herbal components on human drugs interactions involving cytochrome P450." Bioinformation vol. 3,5 (2008): 198-204. doi: https://doi.org/10.6026/97320630003198
Saxena A, Tripathi KP, Roy S, Khan F, Sharma A. Pharmacovigilance: effects of herbal components on human drugs interactions involving cytochrome P450. Bioinformation. 2008;3(5):198-204. doi: 10.6026/97320630003198. Epub 2008 Dec 31. PMID: 19255634; PMCID: PMC2646189.
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Alteration in the capacities of carcinogen metabolizing system of mouse-livers during pretreatment with various antineoplastic agents.

Oncology reports

Mostafa M, Chalvardjian K, Lami H, Badawi A, Hamzah R.
PMID: 21607420
Oncol Rep. 1994 May;1(3):651-6. doi: 10.3892/or.1.3.651.

The effect of treatment with antineoplastic drugs on the modification of the carcinog en-metabolizing capacity was studied in mice liver microsomes at different durations as a single and as a repeated dose treatment. It is generally demonstrated that there...

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Mostafa M, Chalvardjian K, Lami H, et al. Alteration in the capacities of carcinogen metabolizing system of mouse-livers during pretreatment with various antineoplastic agents. Oncol Rep. 1994;1(3):651-6doi: 10.3892/or.1.3.651.
Mostafa, M., Chalvardjian, K., Lami, H., Badawi, A., & Hamzah, R. (1994). Alteration in the capacities of carcinogen metabolizing system of mouse-livers during pretreatment with various antineoplastic agents. Oncology reports, 1(3), 651-6. https://doi.org/10.3892/or.1.3.651
Mostafa, M, et al. "Alteration in the capacities of carcinogen metabolizing system of mouse-livers during pretreatment with various antineoplastic agents." Oncology reports vol. 1,3 (1994): 651-6. doi: https://doi.org/10.3892/or.1.3.651
Mostafa M, Chalvardjian K, Lami H, Badawi A, Hamzah R. Alteration in the capacities of carcinogen metabolizing system of mouse-livers during pretreatment with various antineoplastic agents. Oncol Rep. 1994 May;1(3):651-6. doi: 10.3892/or.1.3.651. PMID: 21607420.
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In vitro neurotoxicity of methyl iodide.

Toxicology in vitro : an international journal published in association with BIBRA

Davenport CJ, Bonnefoi MS, Williams DA, Morgan KT.
PMID: 20732087
Toxicol In Vitro. 1992 Jan;6(1):11-20. doi: 10.1016/0887-2333(92)90080-b.

Methyl iodide (MeI) and two other commonly used monohalomethanes, methyl bromide and methyl chloride, are potent human neurotoxicants. In the present study neural cell cultures were used to investigate MeI neurotoxicity in vitro. In primary, dispersed mixed (neurons and...

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Davenport CJ, Bonnefoi MS, Williams DA, et al. In vitro neurotoxicity of methyl iodide. Toxicol In Vitro. 1992;6(1):11-20doi: 10.1016/0887-2333(92)90080-b.
Davenport, C. J., Bonnefoi, M. S., Williams, D. A., & Morgan, K. T. (1992). In vitro neurotoxicity of methyl iodide. Toxicology in vitro : an international journal published in association with BIBRA, 6(1), 11-20. https://doi.org/10.1016/0887-2333(92)90080-b
Davenport, C J, et al. "In vitro neurotoxicity of methyl iodide." Toxicology in vitro : an international journal published in association with BIBRA vol. 6,1 (1992): 11-20. doi: https://doi.org/10.1016/0887-2333(92)90080-b
Davenport CJ, Bonnefoi MS, Williams DA, Morgan KT. In vitro neurotoxicity of methyl iodide. Toxicol In Vitro. 1992 Jan;6(1):11-20. doi: 10.1016/0887-2333(92)90080-b. PMID: 20732087.
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Showing 1 to 12 of 171 entries