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The intrinsic fluorescence of FAD and its application in analytical chemistry: a review.

Methods and applications in fluorescence

Galbán J, Sanz-Vicente I, Navarro J, de Marcos S.
PMID: 28192293
Methods Appl Fluoresc. 2016 Dec 19;4(4):042005. doi: 10.1088/2050-6120/4/4/042005.

This review (with 106 references) mainly deals with the analytical applications of flavin-adenine dinucleotide (FAD) fluorescence. In the first section, the spectroscopic properties of this compound are reviewed at the light of his different acid-base, oxidation and structural forms;...

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Galbán J, Sanz-Vicente I, Navarro J, et al. The intrinsic fluorescence of FAD and its application in analytical chemistry: a review. Methods Appl Fluoresc. 2016;4(4):042005doi: 10.1088/2050-6120/4/4/042005.
Galbán, J., Sanz-Vicente, I., Navarro, J., & de Marcos, S. (2016). The intrinsic fluorescence of FAD and its application in analytical chemistry: a review. Methods and applications in fluorescence, 4(4), 042005. https://doi.org/10.1088/2050-6120/4/4/042005
Galbán, Javier, et al. "The intrinsic fluorescence of FAD and its application in analytical chemistry: a review." Methods and applications in fluorescence vol. 4,4 (2016): 042005. doi: https://doi.org/10.1088/2050-6120/4/4/042005
Galbán J, Sanz-Vicente I, Navarro J, de Marcos S. The intrinsic fluorescence of FAD and its application in analytical chemistry: a review. Methods Appl Fluoresc. 2016 Dec 19;4(4):042005. doi: 10.1088/2050-6120/4/4/042005. PMID: 28192293.
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Enzymatic oligomerization and polymerization of arylamines: state of the art and perspectives.

Chemicke zvesti

Ćirić-Marjanović G, Milojević-Rakić M, Janošević-Ležaić A, Luginbühl S, Walde P.
PMID: 28775395
Chem Zvesti. 2017;71(2):199-242. doi: 10.1007/s11696-016-0094-3. Epub 2016 Dec 19.

The literature concerning the oxidative oligomerization and polymerization of various arylamines, e.g., aniline, substituted anilines, aminonaphthalene and its derivatives, catalyzed by oxidoreductases, such as laccases and peroxidases, in aqueous, organic, and mixed aqueous organic monophasic or biphasic media, is...

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Ćirić-Marjanović G, Milojević-Rakić M, Janošević-Ležaić A, et al. Enzymatic oligomerization and polymerization of arylamines: state of the art and perspectives. Chem Zvesti. 2016;71(2):199-242doi: 10.1007/s11696-016-0094-3.
Ćirić-Marjanović, G., Milojević-Rakić, M., Janošević-Ležaić, A., Luginbühl, S., & Walde, P. (2017). Enzymatic oligomerization and polymerization of arylamines: state of the art and perspectives. Chemicke zvesti, 71(2), 199-242. https://doi.org/10.1007/s11696-016-0094-3
Ćirić-Marjanović, Gordana, et al. "Enzymatic oligomerization and polymerization of arylamines: state of the art and perspectives." Chemicke zvesti vol. 71,2 (2017): 199-242. doi: https://doi.org/10.1007/s11696-016-0094-3
Ćirić-Marjanović G, Milojević-Rakić M, Janošević-Ležaić A, Luginbühl S, Walde P. Enzymatic oligomerization and polymerization of arylamines: state of the art and perspectives. Chem Zvesti. 2017;71(2):199-242. doi: 10.1007/s11696-016-0094-3. Epub 2016 Dec 19. PMID: 28775395; PMCID: PMC5495875.
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Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases.

AMB Express

Chakraborty J, Suzuki-Minakuchi C, Okada K, Nojiri H.
PMID: 28050858
AMB Express. 2017 Dec;7(1):17. doi: 10.1186/s13568-016-0318-5. Epub 2017 Jan 04.

Rieske non-heme iron oxygenases, which have a Rieske-type [2Fe-2S] cluster and a non-heme catalytic iron center, are an important family of oxidoreductases involved mainly in regio- and stereoselective transformation of a wide array of aromatic hydrocarbons. Though present in...

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Chakraborty J, Suzuki-Minakuchi C, Okada K, et al. Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases. AMB Express. 2017;7(1):17doi: 10.1186/s13568-016-0318-5.
Chakraborty, J., Suzuki-Minakuchi, C., Okada, K., & Nojiri, H. (2017). Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases. AMB Express, 7(1), 17. https://doi.org/10.1186/s13568-016-0318-5
Chakraborty, Joydeep, et al. "Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases." AMB Express vol. 7,1 (2017): 17. doi: https://doi.org/10.1186/s13568-016-0318-5
Chakraborty J, Suzuki-Minakuchi C, Okada K, Nojiri H. Thermophilic bacteria are potential sources of novel Rieske non-heme iron oxygenases. AMB Express. 2017 Dec;7(1):17. doi: 10.1186/s13568-016-0318-5. Epub 2017 Jan 04. PMID: 28050858; PMCID: PMC5209329.
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Origin and Evolution of Flavin-Based Electron Bifurcating Enzymes.

Frontiers in microbiology

Poudel S, Dunham EC, Lindsay MR, Amenabar MJ, Fones EM, Colman DR, Boyd ES.
PMID: 30123204
Front Microbiol. 2018 Aug 03;9:1762. doi: 10.3389/fmicb.2018.01762. eCollection 2018.

Twelve evolutionarily unrelated oxidoreductases form enzyme complexes that catalyze the simultaneous coupling of exergonic and endergonic oxidation-reduction reactions to circumvent thermodynamic barriers and minimize free energy loss in a process known as flavin-based electron bifurcation. Common to these 12...

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Poudel S, Dunham EC, Lindsay MR, et al. Origin and Evolution of Flavin-Based Electron Bifurcating Enzymes. Front Microbiol. 2018;9:1762doi: 10.3389/fmicb.2018.01762.
Poudel, S., Dunham, E. C., Lindsay, M. R., Amenabar, M. J., Fones, E. M., Colman, D. R., & Boyd, E. S. (2018). Origin and Evolution of Flavin-Based Electron Bifurcating Enzymes. Frontiers in microbiology, 91762. https://doi.org/10.3389/fmicb.2018.01762
Poudel, Saroj, et al. "Origin and Evolution of Flavin-Based Electron Bifurcating Enzymes." Frontiers in microbiology vol. 9 (2018): 1762. doi: https://doi.org/10.3389/fmicb.2018.01762
Poudel S, Dunham EC, Lindsay MR, Amenabar MJ, Fones EM, Colman DR, Boyd ES. Origin and Evolution of Flavin-Based Electron Bifurcating Enzymes. Front Microbiol. 2018 Aug 03;9:1762. doi: 10.3389/fmicb.2018.01762. eCollection 2018. PMID: 30123204; PMCID: PMC6085437.
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Transcriptome sequencing revealed differences in the response of renal cancer cells to hypoxia and CoCl 2 treatment.

F1000Research

Zhigalova N, Artemov A, Mazur A, Prokhortchouk E.
PMID: 26925226
F1000Res. 2015 Dec 30;4:1518. doi: 10.12688/f1000research.7571.1. eCollection 2015.

Human cancer cells are subjected to hypoxic conditions in many tumours. Hypoxia causes alterations in the glycolytic pathway activation through stabilization of hypoxia-inducible factor 1. Currently, two approaches are commonly used to model hypoxia: an alternative to generating low-oxygen...

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Zhigalova N, Artemov A, Mazur A, et al. Transcriptome sequencing revealed differences in the response of renal cancer cells to hypoxia and CoCl 2 treatment. F1000Res. 2015;4:1518doi: 10.12688/f1000research.7571.1.
Zhigalova, N., Artemov, A., Mazur, A., & Prokhortchouk, E. (2015). Transcriptome sequencing revealed differences in the response of renal cancer cells to hypoxia and CoCl 2 treatment. F1000Research, 41518. https://doi.org/10.12688/f1000research.7571.1
Zhigalova, Nadezhda, et al. "Transcriptome sequencing revealed differences in the response of renal cancer cells to hypoxia and CoCl 2 treatment." F1000Research vol. 4 (2015): 1518. doi: https://doi.org/10.12688/f1000research.7571.1
Zhigalova N, Artemov A, Mazur A, Prokhortchouk E. Transcriptome sequencing revealed differences in the response of renal cancer cells to hypoxia and CoCl 2 treatment. F1000Res. 2015 Dec 30;4:1518. doi: 10.12688/f1000research.7571.1. eCollection 2015. PMID: 26925226; PMCID: PMC4712771.
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Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates.

Communications biology

Shenkman M, Ron E, Yehuda R, Benyair R, Khalaila I, Lederkremer GZ.
PMID: 30374462
Commun Biol. 2018 Oct 18;1:172. doi: 10.1038/s42003-018-0174-8. eCollection 2018.

Extensive mannose trimming of nascent glycoprotein N-glycans signals their targeting to endoplasmic reticulum-associated degradation (ERAD). ER mannosidase I (ERManI) and the EDEM protein family participate in this process. However, whether the EDEMs are truly mannosidases can be addressed only...

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Shenkman M, Ron E, Yehuda R, et al. Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates. Commun Biol. 2018;1:172doi: 10.1038/s42003-018-0174-8.
Shenkman, M., Ron, E., Yehuda, R., Benyair, R., Khalaila, I., & Lederkremer, G. Z. (2018). Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates. Communications biology, 1172. https://doi.org/10.1038/s42003-018-0174-8
Shenkman, Marina, et al. "Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates." Communications biology vol. 1 (2018): 172. doi: https://doi.org/10.1038/s42003-018-0174-8
Shenkman M, Ron E, Yehuda R, Benyair R, Khalaila I, Lederkremer GZ. Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates. Commun Biol. 2018 Oct 18;1:172. doi: 10.1038/s42003-018-0174-8. eCollection 2018. PMID: 30374462; PMCID: PMC6194124.
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Sequence-Based .

ChemCatChem

Velikogne S, Resch V, Dertnig C, Schrittwieser JH, Kroutil W.
PMID: 30197686
ChemCatChem. 2018 Aug 13;10(15):3236-3246. doi: 10.1002/cctc.201800607. Epub 2018 Jul 17.

Imine reductases (IREDs) have recently become a primary focus of research in biocatalysis, complementing other classes of amine-forming enzymes such as transaminases and amine dehydrogenases. Following in the footsteps of other research groups, we have established a set of...

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Velikogne S, Resch V, Dertnig C, et al. Sequence-Based . ChemCatChem. 2018;10(15):3236-3246doi: 10.1002/cctc.201800607.
Velikogne, S., Resch, V., Dertnig, C., Schrittwieser, J. H., & Kroutil, W. (2018). Sequence-Based . ChemCatChem, 10(15), 3236-3246. https://doi.org/10.1002/cctc.201800607
Velikogne, Stefan, et al. "Sequence-Based ." ChemCatChem vol. 10,15 (2018): 3236-3246. doi: https://doi.org/10.1002/cctc.201800607
Velikogne S, Resch V, Dertnig C, Schrittwieser JH, Kroutil W. Sequence-Based . ChemCatChem. 2018 Aug 13;10(15):3236-3246. doi: 10.1002/cctc.201800607. Epub 2018 Jul 17. PMID: 30197686; PMCID: PMC6120462.
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Effects of industrial heat treatments on the kinetics of inactivation of antimicrobial bovine milk xanthine oxidase.

NPJ science of food

Ozturk G, German JB, de Moura Bell JMLN.
PMID: 31396558
NPJ Sci Food. 2019 Aug 02;3:13. doi: 10.1038/s41538-019-0046-8. eCollection 2019.

Milk is a source of antimicrobial systems such as xanthine oxidoreductase, which has been proposed to modulate the oral and gut microbiota of infants. Heat treatments are applied to milk to ensure its microbial safety, however, the effects of...

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Ozturk G, German JB, de Moura Bell JMLN. Effects of industrial heat treatments on the kinetics of inactivation of antimicrobial bovine milk xanthine oxidase. NPJ Sci Food. 2019;3:13doi: 10.1038/s41538-019-0046-8.
Ozturk, G., German, J. B., & de Moura Bell, J. M. L. N. (2019). Effects of industrial heat treatments on the kinetics of inactivation of antimicrobial bovine milk xanthine oxidase. NPJ science of food, 313. https://doi.org/10.1038/s41538-019-0046-8
Ozturk, Gulustan, et al. "Effects of industrial heat treatments on the kinetics of inactivation of antimicrobial bovine milk xanthine oxidase." NPJ science of food vol. 3 (2019): 13. doi: https://doi.org/10.1038/s41538-019-0046-8
Ozturk G, German JB, de Moura Bell JMLN. Effects of industrial heat treatments on the kinetics of inactivation of antimicrobial bovine milk xanthine oxidase. NPJ Sci Food. 2019 Aug 02;3:13. doi: 10.1038/s41538-019-0046-8. eCollection 2019. PMID: 31396558; PMCID: PMC6677807.
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The Foliar Endophyte .

Microbiology resource announcements

Bhatnagar JM, Sabat G, Cullen D.
PMID: 30746512
Microbiol Resour Announc. 2019 Feb 07;8(6). doi: 10.1128/MRA.01280-18. eCollection 2019 Feb.

The conifer needle endophyte Phialocephala scopiformis DAOMC 229536 was cultivated in medium containing ground Pinus contorta wood as the sole carbon source. Mass spectrometry analyses identified 590 proteins. The expression of extracellular hydrolases and oxidoreductases indicates a capacity to...

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Bhatnagar JM, Sabat G, Cullen D. The Foliar Endophyte . Microbiol Resour Announc. 2019;8(6)doi: 10.1128/MRA.01280-18.
Bhatnagar, J. M., Sabat, G., & Cullen, D. (2019). The Foliar Endophyte . Microbiology resource announcements, 8(6), . https://doi.org/10.1128/MRA.01280-18
Bhatnagar, Jennifer M, et al. "The Foliar Endophyte ." Microbiology resource announcements vol. 8,6 (2019). doi: https://doi.org/10.1128/MRA.01280-18
Bhatnagar JM, Sabat G, Cullen D. The Foliar Endophyte . Microbiol Resour Announc. 2019 Feb 07;8(6). doi: 10.1128/MRA.01280-18. eCollection 2019 Feb. PMID: 30746512; PMCID: PMC6368647.
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Nanoinitiator for enzymatic anaerobic polymerization and graft enhancement of gelatin-PAAM hydrogel.

Journal of materials chemistry. B

Zhang Q, Lv Y, Liu M, Wang X, Mi Y, Wang Q.
PMID: 32254425
J Mater Chem B. 2018 Mar 07;6(9):1402-1409. doi: 10.1039/c7tb03244g. Epub 2018 Feb 19.

As an emerging method for mildly molding polymer hydrogel bioscaffolds, the enzymatically polymerized system is mainly based on the screening of various oxidoreductases to produce radicals, but the design of multifunctional nanoinitiators to facilitate hydrogel performance remains challenging. Here,...

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Zhang Q, Lv Y, Liu M, et al. Nanoinitiator for enzymatic anaerobic polymerization and graft enhancement of gelatin-PAAM hydrogel. J Mater Chem B. 2018;6(9):1402-1409doi: 10.1039/c7tb03244g.
Zhang, Q., Lv, Y., Liu, M., Wang, X., Mi, Y., & Wang, Q. (2018). Nanoinitiator for enzymatic anaerobic polymerization and graft enhancement of gelatin-PAAM hydrogel. Journal of materials chemistry. B, 6(9), 1402-1409. https://doi.org/10.1039/c7tb03244g
Zhang, Qi, et al. "Nanoinitiator for enzymatic anaerobic polymerization and graft enhancement of gelatin-PAAM hydrogel." Journal of materials chemistry. B vol. 6,9 (2018): 1402-1409. doi: https://doi.org/10.1039/c7tb03244g
Zhang Q, Lv Y, Liu M, Wang X, Mi Y, Wang Q. Nanoinitiator for enzymatic anaerobic polymerization and graft enhancement of gelatin-PAAM hydrogel. J Mater Chem B. 2018 Mar 07;6(9):1402-1409. doi: 10.1039/c7tb03244g. Epub 2018 Feb 19. PMID: 32254425.
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Potential impact of combined inhibition of 3α-oxidoreductases and 5α-reductases on prostate cancer.

Asian journal of urology

Fiandalo MV, Gewirth DT, Mohler JL.
PMID: 30775248
Asian J Urol. 2019 Jan;6(1):50-56. doi: 10.1016/j.ajur.2018.09.002. Epub 2018 Sep 26.

Prostate cancer (PCa) growth and progression rely on the interaction between the androgen receptor (AR) and the testicular ligands, testosterone and dihydrotestosterone (DHT). Almost all men with advanced PCa receive androgen deprivation therapy (ADT). ADT lowers circulating testosterone levels,...

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Fiandalo MV, Gewirth DT, Mohler JL. Potential impact of combined inhibition of 3α-oxidoreductases and 5α-reductases on prostate cancer. Asian J Urol. 2018;6(1):50-56doi: 10.1016/j.ajur.2018.09.002.
Fiandalo, M. V., Gewirth, D. T., & Mohler, J. L. (2019). Potential impact of combined inhibition of 3α-oxidoreductases and 5α-reductases on prostate cancer. Asian journal of urology, 6(1), 50-56. https://doi.org/10.1016/j.ajur.2018.09.002
Fiandalo, Michael V, et al. "Potential impact of combined inhibition of 3α-oxidoreductases and 5α-reductases on prostate cancer." Asian journal of urology vol. 6,1 (2019): 50-56. doi: https://doi.org/10.1016/j.ajur.2018.09.002
Fiandalo MV, Gewirth DT, Mohler JL. Potential impact of combined inhibition of 3α-oxidoreductases and 5α-reductases on prostate cancer. Asian J Urol. 2019 Jan;6(1):50-56. doi: 10.1016/j.ajur.2018.09.002. Epub 2018 Sep 26. PMID: 30775248; PMCID: PMC6363635.
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Transcriptome of the coral Mussismilia braziliensis symbiont Sargassococcus simulans.

Marine genomics

Varasteh T, Tschoeke D, Silva-Lima AW, Thompson C, Thompson F.
PMID: 34710723
Mar Genomics. 2021 Oct 26;61:100912. doi: 10.1016/j.margen.2021.100912. Epub 2021 Oct 26.

A transcriptomic profile of Sargassococcus simulans 103B3, isolated from the coral Mussismilia braziliensis in Abrolhos, Brazil, is presented. A total of 631.3 Mbp transcriptomic sequences were obtained. The transcriptomic analysis disclosed transcripts coding for enzymes relevant for holobiont health...

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Varasteh T, Tschoeke D, Silva-Lima AW, et al. Transcriptome of the coral Mussismilia braziliensis symbiont Sargassococcus simulans. Mar Genomics. 2021;61:100912doi: 10.1016/j.margen.2021.100912.
Varasteh, T., Tschoeke, D., Silva-Lima, A. W., Thompson, C., & Thompson, F. (2021). Transcriptome of the coral Mussismilia braziliensis symbiont Sargassococcus simulans. Marine genomics, 61100912. https://doi.org/10.1016/j.margen.2021.100912
Varasteh, Tooba, et al. "Transcriptome of the coral Mussismilia braziliensis symbiont Sargassococcus simulans." Marine genomics vol. 61 (2021): 100912. doi: https://doi.org/10.1016/j.margen.2021.100912
Varasteh T, Tschoeke D, Silva-Lima AW, Thompson C, Thompson F. Transcriptome of the coral Mussismilia braziliensis symbiont Sargassococcus simulans. Mar Genomics. 2021 Oct 26;61:100912. doi: 10.1016/j.margen.2021.100912. Epub 2021 Oct 26. PMID: 34710723.
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Showing 25 to 36 of 327 entries