Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 1 to 12 of 327 entries
Sorted by: Best Match Show Resources per page
Overcoming the Gas-Liquid Mass Transfer of Oxygen by Coupling Photosynthetic Water Oxidation with Biocatalytic Oxyfunctionalization.

Angewandte Chemie (International ed. in English)

Hoschek A, Bühler B, Schmid A.
PMID: 28945948
Angew Chem Int Ed Engl. 2017 Nov 20;56(47):15146-15149. doi: 10.1002/anie.201706886. Epub 2017 Oct 27.

Gas-liquid mass transfer of gaseous reactants is a major limitation for high space-time yields, especially for O

Cite
Hoschek A, Bühler B, Schmid A. Overcoming the Gas-Liquid Mass Transfer of Oxygen by Coupling Photosynthetic Water Oxidation with Biocatalytic Oxyfunctionalization. Angew Chem Int Ed Engl. 2017;56(47):15146-15149doi: 10.1002/anie.201706886.
Hoschek, A., Bühler, B., & Schmid, A. (2017). Overcoming the Gas-Liquid Mass Transfer of Oxygen by Coupling Photosynthetic Water Oxidation with Biocatalytic Oxyfunctionalization. Angewandte Chemie (International ed. in English), 56(47), 15146-15149. https://doi.org/10.1002/anie.201706886
Hoschek, Anna, et al. "Overcoming the Gas-Liquid Mass Transfer of Oxygen by Coupling Photosynthetic Water Oxidation with Biocatalytic Oxyfunctionalization." Angewandte Chemie (International ed. in English) vol. 56,47 (2017): 15146-15149. doi: https://doi.org/10.1002/anie.201706886
Hoschek A, Bühler B, Schmid A. Overcoming the Gas-Liquid Mass Transfer of Oxygen by Coupling Photosynthetic Water Oxidation with Biocatalytic Oxyfunctionalization. Angew Chem Int Ed Engl. 2017 Nov 20;56(47):15146-15149. doi: 10.1002/anie.201706886. Epub 2017 Oct 27. PMID: 28945948; PMCID: PMC5708270.
Copy Download .nbib Format: NLM
Structure and properties of the catalytic site of nitric oxide reductase at ambient temperature.

Biochimica et biophysica acta

Daskalakis V, Ohta T, Kitagawa T, Varotsis C.
PMID: 26140941
Biochim Biophys Acta. 2015 Oct;1847(10):1240-4. doi: 10.1016/j.bbabio.2015.06.014. Epub 2015 Jul 02.

Nitric oxide reductase (Nor) is the third of the four enzymes of bacterial denitrification responsible for the catalytic formation of laughing gas (N2O). Here we report the detection of the hyponitrite (HO-N=N-O(-)) species (νN-N=1332cm(-1)) in the heme b3 Fe-FeB...

Cite
Daskalakis V, Ohta T, Kitagawa T, et al. Structure and properties of the catalytic site of nitric oxide reductase at ambient temperature. Biochim Biophys Acta. 2015;1847(10):1240-4doi: 10.1016/j.bbabio.2015.06.014.
Daskalakis, V., Ohta, T., Kitagawa, T., & Varotsis, C. (2015). Structure and properties of the catalytic site of nitric oxide reductase at ambient temperature. Biochimica et biophysica acta, 1847(10), 1240-4. https://doi.org/10.1016/j.bbabio.2015.06.014
Daskalakis, Vangelis, et al. "Structure and properties of the catalytic site of nitric oxide reductase at ambient temperature." Biochimica et biophysica acta vol. 1847,10 (2015): 1240-4. doi: https://doi.org/10.1016/j.bbabio.2015.06.014
Daskalakis V, Ohta T, Kitagawa T, Varotsis C. Structure and properties of the catalytic site of nitric oxide reductase at ambient temperature. Biochim Biophys Acta. 2015 Oct;1847(10):1240-4. doi: 10.1016/j.bbabio.2015.06.014. Epub 2015 Jul 02. PMID: 26140941.
Copy Download .nbib Format: NLM
17(R)-resolvin D1 ameliorates bleomycin-induced pulmonary fibrosis in mice.

Physiological reports

Yatomi M, Hisada T, Ishizuka T, Koga Y, Ono A, Kamide Y, Seki K, Aoki-Saito H, Tsurumaki H, Sunaga N, Kaira K, Dobashi K, Yamada M, Okajima F.
PMID: 26660549
Physiol Rep. 2015 Dec;3(12). doi: 10.14814/phy2.12628.

Idiopathic pulmonary fibrosis (IPF) is a destructive inflammatory disease with limited therapeutic options. Inflammation plays an integral role in the development of pulmonary fibrosis. Unresolved inflammatory responses can lead to substantial tissue injury, chronic inflammation, and fibrosis. The resolvins...

Cite
Yatomi M, Hisada T, Ishizuka T, et al. 17(R)-resolvin D1 ameliorates bleomycin-induced pulmonary fibrosis in mice. Physiol Rep. 2015;3(12)doi: 10.14814/phy2.12628.
Yatomi, M., Hisada, T., Ishizuka, T., Koga, Y., Ono, A., Kamide, Y., Seki, K., Aoki-Saito, H., Tsurumaki, H., Sunaga, N., Kaira, K., Dobashi, K., Yamada, M., & Okajima, F. (2015). 17(R)-resolvin D1 ameliorates bleomycin-induced pulmonary fibrosis in mice. Physiological reports, 3(12), . https://doi.org/10.14814/phy2.12628
Yatomi, Masakiyo, et al. "17(R)-resolvin D1 ameliorates bleomycin-induced pulmonary fibrosis in mice." Physiological reports vol. 3,12 (2015). doi: https://doi.org/10.14814/phy2.12628
Yatomi M, Hisada T, Ishizuka T, Koga Y, Ono A, Kamide Y, Seki K, Aoki-Saito H, Tsurumaki H, Sunaga N, Kaira K, Dobashi K, Yamada M, Okajima F. 17(R)-resolvin D1 ameliorates bleomycin-induced pulmonary fibrosis in mice. Physiol Rep. 2015 Dec;3(12). doi: 10.14814/phy2.12628. PMID: 26660549; PMCID: PMC4760456.
Copy Download .nbib Format: NLM
Transmembrane thioredoxin-related protein TMX1 is reversibly oxidized in response to protein accumulation in the endoplasmic reticulum.

FEBS open bio

Matsuo Y, Hirota K.
PMID: 29123984
FEBS Open Bio. 2017 Oct 03;7(11):1768-1777. doi: 10.1002/2211-5463.12319. eCollection 2017 Nov.

Numerous secretory and membrane proteins undergo post-translational modifications in the endoplasmic reticulum (ER), and the formation of disulfide bonds is a modification that is critical for proper protein folding. The mammalian ER contains a large family of oxidoreductases that...

Cite
Matsuo Y, Hirota K. Transmembrane thioredoxin-related protein TMX1 is reversibly oxidized in response to protein accumulation in the endoplasmic reticulum. FEBS Open Bio. 2017;7(11):1768-1777doi: 10.1002/2211-5463.12319.
Matsuo, Y., & Hirota, K. (2017). Transmembrane thioredoxin-related protein TMX1 is reversibly oxidized in response to protein accumulation in the endoplasmic reticulum. FEBS open bio, 7(11), 1768-1777. https://doi.org/10.1002/2211-5463.12319
Matsuo, Yoshiyuki, and Hirota, Kiichi. "Transmembrane thioredoxin-related protein TMX1 is reversibly oxidized in response to protein accumulation in the endoplasmic reticulum." FEBS open bio vol. 7,11 (2017): 1768-1777. doi: https://doi.org/10.1002/2211-5463.12319
Matsuo Y, Hirota K. Transmembrane thioredoxin-related protein TMX1 is reversibly oxidized in response to protein accumulation in the endoplasmic reticulum. FEBS Open Bio. 2017 Oct 03;7(11):1768-1777. doi: 10.1002/2211-5463.12319. eCollection 2017 Nov. PMID: 29123984; PMCID: PMC5666389.
Copy Download .nbib Format: NLM
Switching between Inner- and Outer-Sphere PCET Mechanisms of Small-Molecule Activation: Superoxide Dismutation and Oxygen/Superoxide Reduction Reactivity Deriving from the Same Manganese Complex.

Journal of the American Chemical Society

Kenkel I, Franke A, Dürr M, Zahl A, Dücker-Benfer C, Langer J, Filipović MR, Yu M, Puchta R, Fiedler SR, Shores MP, Goldsmith CR, Ivanović-Burmazović I.
PMID: 28111938
J Am Chem Soc. 2017 Feb 01;139(4):1472-1484. doi: 10.1021/jacs.6b08394. Epub 2017 Jan 23.

Readily exchangeable water molecules are commonly found in the active sites of oxidoreductases, yet the overwhelming majority of studies on small-molecule mimics of these enzymes entirely ignores the contribution of water to the reactivity. Studies of how these enzymes...

Cite
Kenkel I, Franke A, Dürr M, et al. Switching between Inner- and Outer-Sphere PCET Mechanisms of Small-Molecule Activation: Superoxide Dismutation and Oxygen/Superoxide Reduction Reactivity Deriving from the Same Manganese Complex. J Am Chem Soc. 2017;139(4):1472-1484doi: 10.1021/jacs.6b08394.
Kenkel, I., Franke, A., Dürr, M., Zahl, A., Dücker-Benfer, C., Langer, J., Filipović, M. R., Yu, M., Puchta, R., Fiedler, S. R., Shores, M. P., Goldsmith, C. R., & Ivanović-Burmazović, I. (2017). Switching between Inner- and Outer-Sphere PCET Mechanisms of Small-Molecule Activation: Superoxide Dismutation and Oxygen/Superoxide Reduction Reactivity Deriving from the Same Manganese Complex. Journal of the American Chemical Society, 139(4), 1472-1484. https://doi.org/10.1021/jacs.6b08394
Kenkel, Isabell, et al. "Switching between Inner- and Outer-Sphere PCET Mechanisms of Small-Molecule Activation: Superoxide Dismutation and Oxygen/Superoxide Reduction Reactivity Deriving from the Same Manganese Complex." Journal of the American Chemical Society vol. 139,4 (2017): 1472-1484. doi: https://doi.org/10.1021/jacs.6b08394
Kenkel I, Franke A, Dürr M, Zahl A, Dücker-Benfer C, Langer J, Filipović MR, Yu M, Puchta R, Fiedler SR, Shores MP, Goldsmith CR, Ivanović-Burmazović I. Switching between Inner- and Outer-Sphere PCET Mechanisms of Small-Molecule Activation: Superoxide Dismutation and Oxygen/Superoxide Reduction Reactivity Deriving from the Same Manganese Complex. J Am Chem Soc. 2017 Feb 01;139(4):1472-1484. doi: 10.1021/jacs.6b08394. Epub 2017 Jan 23. PMID: 28111938.
Copy Download .nbib Format: NLM
Syntrophic butyrate and propionate oxidation processes: from genomes to reaction mechanisms.

Environmental microbiology reports

Müller N, Worm P, Schink B, Stams AJ, Plugge CM.
PMID: 23766220
Environ Microbiol Rep. 2010 Aug;2(4):489-99. doi: 10.1111/j.1758-2229.2010.00147.x. Epub 2010 Mar 03.

In anoxic environments such as swamps, rice fields and sludge digestors, syntrophic microbial communities are important for decomposition of organic matter to CO2 and CH4 . The most difficult step is the fermentative degradation of short-chain fatty acids such...

Cite
Müller N, Worm P, Schink B, et al. Syntrophic butyrate and propionate oxidation processes: from genomes to reaction mechanisms. Environ Microbiol Rep. 2010;2(4):489-99doi: 10.1111/j.1758-2229.2010.00147.x.
Müller, N., Worm, P., Schink, B., Stams, A. J., & Plugge, C. M. (2010). Syntrophic butyrate and propionate oxidation processes: from genomes to reaction mechanisms. Environmental microbiology reports, 2(4), 489-99. https://doi.org/10.1111/j.1758-2229.2010.00147.x
Müller, Nicolai, et al. "Syntrophic butyrate and propionate oxidation processes: from genomes to reaction mechanisms." Environmental microbiology reports vol. 2,4 (2010): 489-99. doi: https://doi.org/10.1111/j.1758-2229.2010.00147.x
Müller N, Worm P, Schink B, Stams AJ, Plugge CM. Syntrophic butyrate and propionate oxidation processes: from genomes to reaction mechanisms. Environ Microbiol Rep. 2010 Aug;2(4):489-99. doi: 10.1111/j.1758-2229.2010.00147.x. Epub 2010 Mar 03. PMID: 23766220.
Copy Download .nbib Format: NLM
Tomato expressing Arabidopsis glutaredoxin gene AtGRXS17 confers tolerance to chilling stress via modulating cold responsive components.

Horticulture research

Hu Y, Wu Q, Sprague SA, Park J, Oh M, Rajashekar CB, Koiwa H, Nakata PA, Cheng N, Hirschi KD, White FF, Park S.
PMID: 26623076
Hortic Res. 2015 Nov 11;2:15051. doi: 10.1038/hortres.2015.51. eCollection 2015.

Chilling stress is a production constraint of tomato, a tropical origin, chilling-sensitive horticultural crop. The development of chilling tolerant tomato thus has significant potential to impact tomato production. Glutaredoxins (GRXs) are ubiquitous oxidoreductases, which utilize the reducing power of...

Cite
Hu Y, Wu Q, Sprague SA, et al. Tomato expressing Arabidopsis glutaredoxin gene AtGRXS17 confers tolerance to chilling stress via modulating cold responsive components. Hortic Res. 2015;2:15051doi: 10.1038/hortres.2015.51.
Hu, Y., Wu, Q., Sprague, S. A., Park, J., Oh, M., Rajashekar, C. B., Koiwa, H., Nakata, P. A., Cheng, N., Hirschi, K. D., White, F. F., & Park, S. (2015). Tomato expressing Arabidopsis glutaredoxin gene AtGRXS17 confers tolerance to chilling stress via modulating cold responsive components. Horticulture research, 215051. https://doi.org/10.1038/hortres.2015.51
Hu, Ying, et al. "Tomato expressing Arabidopsis glutaredoxin gene AtGRXS17 confers tolerance to chilling stress via modulating cold responsive components." Horticulture research vol. 2 (2015): 15051. doi: https://doi.org/10.1038/hortres.2015.51
Hu Y, Wu Q, Sprague SA, Park J, Oh M, Rajashekar CB, Koiwa H, Nakata PA, Cheng N, Hirschi KD, White FF, Park S. Tomato expressing Arabidopsis glutaredoxin gene AtGRXS17 confers tolerance to chilling stress via modulating cold responsive components. Hortic Res. 2015 Nov 11;2:15051. doi: 10.1038/hortres.2015.51. eCollection 2015. PMID: 26623076; PMCID: PMC4641303.
Copy Download .nbib Format: NLM
Effect of Eclipta prostrata on 11Beta-Hydroxysteroid Dehydrogenase in Rat Liver and Kidney.

Evidence-based complementary and alternative medicine : eCAM

Xu C, Wei B, Fu X, Luo M, Liu S, Li R, Ren B, Tang L.
PMID: 24876875
Evid Based Complement Alternat Med. 2014;2014:651053. doi: 10.1155/2014/651053. Epub 2014 Apr 30.

Eclipta prostrata (EP) is often prescribed in combination with glucocorticoid to treat glomerular nephritis, nephrotic syndrome, and IgA nephropathy in clinical practice of Traditional Chinese Medicine. Previous studies from our laboratory revealed that coadministration of EP significantly increased the...

Cite
Xu C, Wei B, Fu X, et al. Effect of Eclipta prostrata on 11Beta-Hydroxysteroid Dehydrogenase in Rat Liver and Kidney. Evid Based Complement Alternat Med. 2014;2014:651053doi: 10.1155/2014/651053.
Xu, C., Wei, B., Fu, X., Luo, M., Liu, S., Li, R., Ren, B., & Tang, L. (2014). Effect of Eclipta prostrata on 11Beta-Hydroxysteroid Dehydrogenase in Rat Liver and Kidney. Evidence-based complementary and alternative medicine : eCAM, 2014651053. https://doi.org/10.1155/2014/651053
Xu, Chenshu, et al. "Effect of Eclipta prostrata on 11Beta-Hydroxysteroid Dehydrogenase in Rat Liver and Kidney." Evidence-based complementary and alternative medicine : eCAM vol. 2014 (2014): 651053. doi: https://doi.org/10.1155/2014/651053
Xu C, Wei B, Fu X, Luo M, Liu S, Li R, Ren B, Tang L. Effect of Eclipta prostrata on 11Beta-Hydroxysteroid Dehydrogenase in Rat Liver and Kidney. Evid Based Complement Alternat Med. 2014;2014:651053. doi: 10.1155/2014/651053. Epub 2014 Apr 30. PMID: 24876875; PMCID: PMC4021844.
Copy Download .nbib Format: NLM
DksA-Dependent Transcriptional Regulation in Salmonella Experiencing Nitrosative Stress.

Frontiers in microbiology

Crawford MA, Henard CA, Tapscott T, Porwollik S, McClelland M, Vázquez-Torres A.
PMID: 27065993
Front Microbiol. 2016 Mar 31;7:444. doi: 10.3389/fmicb.2016.00444. eCollection 2016.

Redox-based signaling is fundamental to the capacity of bacteria to sense, and respond to, nitrosative and oxidative stress encountered in natural and host environments. The conserved RNA polymerase regulatory protein DksA is a thiol-based sensor of reactive nitrogen and...

Cite
Crawford MA, Henard CA, Tapscott T, et al. DksA-Dependent Transcriptional Regulation in Salmonella Experiencing Nitrosative Stress. Front Microbiol. 2016;7:444doi: 10.3389/fmicb.2016.00444.
Crawford, M. A., Henard, C. A., Tapscott, T., Porwollik, S., McClelland, M., & Vázquez-Torres, A. (2016). DksA-Dependent Transcriptional Regulation in Salmonella Experiencing Nitrosative Stress. Frontiers in microbiology, 7444. https://doi.org/10.3389/fmicb.2016.00444
Crawford, Matthew A, et al. "DksA-Dependent Transcriptional Regulation in Salmonella Experiencing Nitrosative Stress." Frontiers in microbiology vol. 7 (2016): 444. doi: https://doi.org/10.3389/fmicb.2016.00444
Crawford MA, Henard CA, Tapscott T, Porwollik S, McClelland M, Vázquez-Torres A. DksA-Dependent Transcriptional Regulation in Salmonella Experiencing Nitrosative Stress. Front Microbiol. 2016 Mar 31;7:444. doi: 10.3389/fmicb.2016.00444. eCollection 2016. PMID: 27065993; PMCID: PMC4815678.
Copy Download .nbib Format: NLM
Analysis of nucleotide diphosphate sugar dehydrogenases reveals family and group-specific relationships.

FEBS open bio

Freas N, Newton P, Perozich J.
PMID: 27047744
FEBS Open Bio. 2016 Jan 11;6(1):77-89. doi: 10.1002/2211-5463.12022. eCollection 2016 Jan.

UNLABELLED: UDP-glucose dehydrogenase (UDPGDH), UDP-N-acetyl-mannosamine dehydrogenase (UDPNAMDH) and GDP-mannose dehydrogenase (GDPMDH) belong to a family of NAD (+)-linked 4-electron-transfering oxidoreductases called nucleotide diphosphate sugar dehydrogenases (NDP-SDHs). UDPGDH is an enzyme responsible for converting UDP-d-glucose to UDP-d-glucuronic acid, a product...

Cite
Freas N, Newton P, Perozich J. Analysis of nucleotide diphosphate sugar dehydrogenases reveals family and group-specific relationships. FEBS Open Bio. 2016;6(1):77-89doi: 10.1002/2211-5463.12022.
Freas, N., Newton, P., & Perozich, J. (2016). Analysis of nucleotide diphosphate sugar dehydrogenases reveals family and group-specific relationships. FEBS open bio, 6(1), 77-89. https://doi.org/10.1002/2211-5463.12022
Freas, Nicholas, et al. "Analysis of nucleotide diphosphate sugar dehydrogenases reveals family and group-specific relationships." FEBS open bio vol. 6,1 (2016): 77-89. doi: https://doi.org/10.1002/2211-5463.12022
Freas N, Newton P, Perozich J. Analysis of nucleotide diphosphate sugar dehydrogenases reveals family and group-specific relationships. FEBS Open Bio. 2016 Jan 11;6(1):77-89. doi: 10.1002/2211-5463.12022. eCollection 2016 Jan. PMID: 27047744; PMCID: PMC4794789.
Copy Download .nbib Format: NLM
Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1.

Frontiers in microbiology

Alves MN, Neto SE, Alves AS, Fonseca BM, Carrêlo A, Pacheco I, Paquete CM, Soares CM, Louro RO.
PMID: 26175726
Front Microbiol. 2015 Jun 29;6:665. doi: 10.3389/fmicb.2015.00665. eCollection 2015.

The versatile anaerobic metabolism of the Gram-negative bacterium Shewanella oneidensis MR-1 (SOMR-1) relies on a multitude of redox proteins found in its periplasm. Most are multiheme cytochromes that carry electrons to terminal reductases of insoluble electron acceptors located at...

Cite
Alves MN, Neto SE, Alves AS, et al. Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1. Front Microbiol. 2015;6:665doi: 10.3389/fmicb.2015.00665.
Alves, M. N., Neto, S. E., Alves, A. S., Fonseca, B. M., Carrêlo, A., Pacheco, I., Paquete, C. M., Soares, C. M., & Louro, R. O. (2015). Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1. Frontiers in microbiology, 6665. https://doi.org/10.3389/fmicb.2015.00665
Alves, Mónica N, et al. "Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1." Frontiers in microbiology vol. 6 (2015): 665. doi: https://doi.org/10.3389/fmicb.2015.00665
Alves MN, Neto SE, Alves AS, Fonseca BM, Carrêlo A, Pacheco I, Paquete CM, Soares CM, Louro RO. Characterization of the periplasmic redox network that sustains the versatile anaerobic metabolism of Shewanella oneidensis MR-1. Front Microbiol. 2015 Jun 29;6:665. doi: 10.3389/fmicb.2015.00665. eCollection 2015. PMID: 26175726; PMCID: PMC4484225.
Copy Download .nbib Format: NLM
A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E.

Biotechnology for biofuels

Clarkson SM, Hamilton-Brehm SD, Giannone RJ, Engle NL, Tschaplinski TJ, Hettich RL, Elkins JG.
PMID: 25506391
Biotechnol Biofuels. 2014 Dec 03;7(1):165. doi: 10.1186/s13068-014-0165-z. eCollection 2014.

BACKGROUND: Chemical and physical pretreatment of lignocellulosic biomass improves substrate reactivity for increased microbial biofuel production, but also restricts growth via the release of furan aldehydes, such as furfural and 5-hydroxymethylfurfural (5-HMF). The physiological effects of these inhibitors on...

Cite
Clarkson SM, Hamilton-Brehm SD, Giannone RJ, et al. A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E. Biotechnol Biofuels. 2014;7(1):165doi: 10.1186/s13068-014-0165-z.
Clarkson, S. M., Hamilton-Brehm, S. D., Giannone, R. J., Engle, N. L., Tschaplinski, T. J., Hettich, R. L., & Elkins, J. G. (2014). A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E. Biotechnology for biofuels, 7(1), 165. https://doi.org/10.1186/s13068-014-0165-z
Clarkson, Sonya M, et al. "A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E." Biotechnology for biofuels vol. 7,1 (2014): 165. doi: https://doi.org/10.1186/s13068-014-0165-z
Clarkson SM, Hamilton-Brehm SD, Giannone RJ, Engle NL, Tschaplinski TJ, Hettich RL, Elkins JG. A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E. Biotechnol Biofuels. 2014 Dec 03;7(1):165. doi: 10.1186/s13068-014-0165-z. eCollection 2014. PMID: 25506391; PMCID: PMC4265447.
Copy Download .nbib Format: NLM
Showing 1 to 12 of 327 entries