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Ligninolytic enzymes and its mechanisms for degradation of lignocellulosic waste in environment.

Heliyon

Kumar A, Chandra R.
PMID: 32095645
Heliyon. 2020 Feb 19;6(2):e03170. doi: 10.1016/j.heliyon.2020.e03170. eCollection 2020 Feb.

Ligninolytic enzymes play a key role in degradation and detoxification of lignocellulosic waste in environment. The major ligninolytic enzymes are laccase, lignin peroxidase, manganese peroxidase, and versatile peroxidase. The activities of these enzymes are enhanced by various mediators as...

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Kumar A, Chandra R. Ligninolytic enzymes and its mechanisms for degradation of lignocellulosic waste in environment. Heliyon. 2020;6(2):e03170doi: 10.1016/j.heliyon.2020.e03170.
Kumar, A., & Chandra, R. (2020). Ligninolytic enzymes and its mechanisms for degradation of lignocellulosic waste in environment. Heliyon, 6(2), e03170. https://doi.org/10.1016/j.heliyon.2020.e03170
Kumar, Adarsh, and Chandra, Ram. "Ligninolytic enzymes and its mechanisms for degradation of lignocellulosic waste in environment." Heliyon vol. 6,2 (2020): e03170. doi: https://doi.org/10.1016/j.heliyon.2020.e03170
Kumar A, Chandra R. Ligninolytic enzymes and its mechanisms for degradation of lignocellulosic waste in environment. Heliyon. 2020 Feb 19;6(2):e03170. doi: 10.1016/j.heliyon.2020.e03170. eCollection 2020 Feb. PMID: 32095645; PMCID: PMC7033530.
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Molecular insights into a mechanism of resveratrol action using hybrid computational docking/CoMFA and machine learning approach.

Journal of biomolecular structure & dynamics

Pande A, Manchanda M, Bhat HR, Bairy PS, Kumar N, Gahtori P.
PMID: 33829956
J Biomol Struct Dyn. 2021 Apr 08;1-15. doi: 10.1080/07391102.2021.1910572. Epub 2021 Apr 08.

A phytoalexin, Resveratrol remains a legendary anticancer drug candidate in the archives of scientific literature. Although earlier wet-lab experiments rendering its multiple biological targets, for example, epidermal growth factors, Pro-apoptotic protein p53, sirtuins, and first apoptosis signal (Fas) receptor,...

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Pande A, Manchanda M, Bhat HR, et al. Molecular insights into a mechanism of resveratrol action using hybrid computational docking/CoMFA and machine learning approach. J Biomol Struct Dyn. 2021;1-15doi: 10.1080/07391102.2021.1910572.
Pande, A., Manchanda, M., Bhat, H. R., Bairy, P. S., Kumar, N., & Gahtori, P. (2021). Molecular insights into a mechanism of resveratrol action using hybrid computational docking/CoMFA and machine learning approach. Journal of biomolecular structure & dynamics, 1-15. https://doi.org/10.1080/07391102.2021.1910572
Pande, Akshara, et al. "Molecular insights into a mechanism of resveratrol action using hybrid computational docking/CoMFA and machine learning approach." Journal of biomolecular structure & dynamics vol. (2021): 1-15. doi: https://doi.org/10.1080/07391102.2021.1910572
Pande A, Manchanda M, Bhat HR, Bairy PS, Kumar N, Gahtori P. Molecular insights into a mechanism of resveratrol action using hybrid computational docking/CoMFA and machine learning approach. J Biomol Struct Dyn. 2021 Apr 08;1-15. doi: 10.1080/07391102.2021.1910572. Epub 2021 Apr 08. PMID: 33829956.
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Functions of NQO1 in Cellular Protection and CoQ.

Frontiers in physiology

Ross D, Siegel D.
PMID: 28883796
Front Physiol. 2017 Aug 24;8:595. doi: 10.3389/fphys.2017.00595. eCollection 2017.

NQO1 is one of the two major quinone reductases in mammalian systems. It is highly inducible and plays multiple roles in cellular adaptation to stress. A prevalent polymorphic form of NQO1 results in an absence of NQO1 protein and...

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Ross D, Siegel D. Functions of NQO1 in Cellular Protection and CoQ. Front Physiol. 2017;8:595doi: 10.3389/fphys.2017.00595.
Ross, D., & Siegel, D. (2017). Functions of NQO1 in Cellular Protection and CoQ. Frontiers in physiology, 8595. https://doi.org/10.3389/fphys.2017.00595
Ross, David, and Siegel, David. "Functions of NQO1 in Cellular Protection and CoQ." Frontiers in physiology vol. 8 (2017): 595. doi: https://doi.org/10.3389/fphys.2017.00595
Ross D, Siegel D. Functions of NQO1 in Cellular Protection and CoQ. Front Physiol. 2017 Aug 24;8:595. doi: 10.3389/fphys.2017.00595. eCollection 2017. PMID: 28883796; PMCID: PMC5573868.
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Genomic Analyses of the Quinol Oxidases and/or Quinone Reductases Involved in Bacterial Extracellular Electron Transfer.

Frontiers in microbiology

Zhong Y, Shi L.
PMID: 30619124
Front Microbiol. 2018 Dec 10;9:3029. doi: 10.3389/fmicb.2018.03029. eCollection 2018.

To exchange electrons with extracellular substrates, some microorganisms employ extracellular electron transfer (EET) pathways that physically connect extracellular redox reactions to intracellular metabolic activity. These pathways are made of redox and structural proteins that work cooperatively to transfer electrons...

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Zhong Y, Shi L. Genomic Analyses of the Quinol Oxidases and/or Quinone Reductases Involved in Bacterial Extracellular Electron Transfer. Front Microbiol. 2018;9:3029doi: 10.3389/fmicb.2018.03029.
Zhong, Y., & Shi, L. (2018). Genomic Analyses of the Quinol Oxidases and/or Quinone Reductases Involved in Bacterial Extracellular Electron Transfer. Frontiers in microbiology, 93029. https://doi.org/10.3389/fmicb.2018.03029
Zhong, Yuhong, and Shi, Liang. "Genomic Analyses of the Quinol Oxidases and/or Quinone Reductases Involved in Bacterial Extracellular Electron Transfer." Frontiers in microbiology vol. 9 (2018): 3029. doi: https://doi.org/10.3389/fmicb.2018.03029
Zhong Y, Shi L. Genomic Analyses of the Quinol Oxidases and/or Quinone Reductases Involved in Bacterial Extracellular Electron Transfer. Front Microbiol. 2018 Dec 10;9:3029. doi: 10.3389/fmicb.2018.03029. eCollection 2018. PMID: 30619124; PMCID: PMC6295460.
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Cyclic Changes in Active Site Polarization and Dynamics Drive the 'Ping-pong' Kinetics in NRH:Quinone Oxidoreductase 2: An Insight from QM/MM Simulations.

ACS catalysis

Reinhardt CR, Hu QH, Bresnahan CG, Hati S, Bhattacharyya S.
PMID: 31583178
ACS Catal. 2018 Dec 07;8(12):12015-12029. doi: 10.1021/acscatal.8b04193. Epub 2018 Nov 14.

Quinone reductases belong to the family of flavin-dependent oxidoreductases. With the redox active cofactor, flavin adenine dinucleotide, quinone reductases are known to utilize a 'ping-pong' kinetic mechanism during catalysis in which a hydride is bounced back and forth between...

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Reinhardt CR, Hu QH, Bresnahan CG, et al. Cyclic Changes in Active Site Polarization and Dynamics Drive the 'Ping-pong' Kinetics in NRH:Quinone Oxidoreductase 2: An Insight from QM/MM Simulations. ACS Catal. 2018;8(12):12015-12029doi: 10.1021/acscatal.8b04193.
Reinhardt, C. R., Hu, Q. H., Bresnahan, C. G., Hati, S., & Bhattacharyya, S. (2018). Cyclic Changes in Active Site Polarization and Dynamics Drive the 'Ping-pong' Kinetics in NRH:Quinone Oxidoreductase 2: An Insight from QM/MM Simulations. ACS catalysis, 8(12), 12015-12029. https://doi.org/10.1021/acscatal.8b04193
Reinhardt, Clorice R, et al. "Cyclic Changes in Active Site Polarization and Dynamics Drive the 'Ping-pong' Kinetics in NRH:Quinone Oxidoreductase 2: An Insight from QM/MM Simulations." ACS catalysis vol. 8,12 (2018): 12015-12029. doi: https://doi.org/10.1021/acscatal.8b04193
Reinhardt CR, Hu QH, Bresnahan CG, Hati S, Bhattacharyya S. Cyclic Changes in Active Site Polarization and Dynamics Drive the 'Ping-pong' Kinetics in NRH:Quinone Oxidoreductase 2: An Insight from QM/MM Simulations. ACS Catal. 2018 Dec 07;8(12):12015-12029. doi: 10.1021/acscatal.8b04193. Epub 2018 Nov 14. PMID: 31583178; PMCID: PMC6776251.
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Showing 1 to 5 of 5 entries