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Showing 37 to 45 of 45 entries
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HyPRP1 Gene Suppressed by Multiple Stresses Plays a Negative Role in Abiotic Stress Tolerance in Tomato.

Frontiers in plant science

Li J, Ouyang B, Wang T, Luo Z, Yang C, Li H, Sima W, Zhang J, Ye Z.
PMID: 27446190
Front Plant Sci. 2016 Jun 29;7:967. doi: 10.3389/fpls.2016.00967. eCollection 2016.

Many hybrid proline-rich protein (HyPRP) genes respond to biotic and abiotic stresses in plants, but little is known about their roles other than as putative cell-wall structural proteins. A HyPRP1 gene encodes a protein with proline-rich domain, and an...

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Li J, Ouyang B, Wang T, et al. HyPRP1 Gene Suppressed by Multiple Stresses Plays a Negative Role in Abiotic Stress Tolerance in Tomato. Front Plant Sci. 2016;7:967doi: 10.3389/fpls.2016.00967.
Li, J., Ouyang, B., Wang, T., Luo, Z., Yang, C., Li, H., Sima, W., Zhang, J., & Ye, Z. (2016). HyPRP1 Gene Suppressed by Multiple Stresses Plays a Negative Role in Abiotic Stress Tolerance in Tomato. Frontiers in plant science, 7967. https://doi.org/10.3389/fpls.2016.00967
Li, Jinhua, et al. "HyPRP1 Gene Suppressed by Multiple Stresses Plays a Negative Role in Abiotic Stress Tolerance in Tomato." Frontiers in plant science vol. 7 (2016): 967. doi: https://doi.org/10.3389/fpls.2016.00967
Li J, Ouyang B, Wang T, Luo Z, Yang C, Li H, Sima W, Zhang J, Ye Z. HyPRP1 Gene Suppressed by Multiple Stresses Plays a Negative Role in Abiotic Stress Tolerance in Tomato. Front Plant Sci. 2016 Jun 29;7:967. doi: 10.3389/fpls.2016.00967. eCollection 2016. PMID: 27446190; PMCID: PMC4925714.
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Structure and function of plant-type ferredoxins.

Photosynthesis research

Fukuyama K.
PMID: 16034533
Photosynth Res. 2004;81(3):289-301. doi: 10.1023/B:PRES.0000036882.19322.0a.

The plant-type ferredoxins (Fds) are the [2Fe-2S] proteins that function primarily in photosynthesis; they transfer electrons from photoreduced Photosystem I to ferredoxin NADP(+) reductase in which NADPH is produced for CO(2) assimilation. In addition, Fds partition electrons to various...

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Fukuyama K. Structure and function of plant-type ferredoxins. Photosynth Res. 2004;81(3):289-301doi: 10.1023/B:PRES.0000036882.19322.0a.
Fukuyama, K. (2004). Structure and function of plant-type ferredoxins. Photosynthesis research, 81(3), 289-301. https://doi.org/10.1023/B:PRES.0000036882.19322.0a
Fukuyama, Keiichi. "Structure and function of plant-type ferredoxins." Photosynthesis research vol. 81,3 (2004): 289-301. doi: https://doi.org/10.1023/B:PRES.0000036882.19322.0a
Fukuyama K. Structure and function of plant-type ferredoxins. Photosynth Res. 2004;81(3):289-301. doi: 10.1023/B:PRES.0000036882.19322.0a. PMID: 16034533.
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Sequence of the gene coding for the beta-subunit of dinitrogenase from the blue-green alga Anabaena.

Proceedings of the National Academy of Sciences of the United States of America

Mazur BJ, Chui CF.
PMID: 16593247
Proc Natl Acad Sci U S A. 1982 Nov;79(22):6782-6. doi: 10.1073/pnas.79.22.6782.

The nitrogen fixation nif K gene of the blue-green alga Anabaena, which codes for the beta-subunit of dinitrogenase, has been subjected to sequence analysis. The nif K protein is predicted to be 512 amino acids long, to have a...

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Mazur BJ, Chui CF. Sequence of the gene coding for the beta-subunit of dinitrogenase from the blue-green alga Anabaena. Proc Natl Acad Sci U S A. 1982;79(22):6782-6doi: 10.1073/pnas.79.22.6782.
Mazur, B. J., & Chui, C. F. (1982). Sequence of the gene coding for the beta-subunit of dinitrogenase from the blue-green alga Anabaena. Proceedings of the National Academy of Sciences of the United States of America, 79(22), 6782-6. https://doi.org/10.1073/pnas.79.22.6782
Mazur, B J, and Chui, C F. "Sequence of the gene coding for the beta-subunit of dinitrogenase from the blue-green alga Anabaena." Proceedings of the National Academy of Sciences of the United States of America vol. 79,22 (1982): 6782-6. doi: https://doi.org/10.1073/pnas.79.22.6782
Mazur BJ, Chui CF. Sequence of the gene coding for the beta-subunit of dinitrogenase from the blue-green alga Anabaena. Proc Natl Acad Sci U S A. 1982 Nov;79(22):6782-6. doi: 10.1073/pnas.79.22.6782. PMID: 16593247; PMCID: PMC347217.
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Ground spin state variability in [Fe4S4(SR)4]3-. Synthetic analogs of the reduced clusters in ferredoxins and other iron-sulfur proteins: cases of extreme sensitivity of electronic state and structure to extrinsic factors.

Journal of the American Chemical Society

Carney MJ, Papaefthymiou GC, Spartalian K, Frankel RB, Holm RH.
PMID: 22148785
J Am Chem Soc. 1988 Aug 01;110(18):6084-95. doi: 10.1021/ja00226a025.

No abstract available.

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Carney MJ, Papaefthymiou GC, Spartalian K, et al. Ground spin state variability in [Fe4S4(SR)4]3-. Synthetic analogs of the reduced clusters in ferredoxins and other iron-sulfur proteins: cases of extreme sensitivity of electronic state and structure to extrinsic factors. J Am Chem Soc. 1988;110(18):6084-95doi: 10.1021/ja00226a025.
Carney, M. J., Papaefthymiou, G. C., Spartalian, K., Frankel, R. B., & Holm, R. H. (1988). Ground spin state variability in [Fe4S4(SR)4]3-. Synthetic analogs of the reduced clusters in ferredoxins and other iron-sulfur proteins: cases of extreme sensitivity of electronic state and structure to extrinsic factors. Journal of the American Chemical Society, 110(18), 6084-95. https://doi.org/10.1021/ja00226a025
Carney, M J, et al. "Ground spin state variability in [Fe4S4(SR)4]3-. Synthetic analogs of the reduced clusters in ferredoxins and other iron-sulfur proteins: cases of extreme sensitivity of electronic state and structure to extrinsic factors." Journal of the American Chemical Society vol. 110,18 (1988): 6084-95. doi: https://doi.org/10.1021/ja00226a025
Carney MJ, Papaefthymiou GC, Spartalian K, Frankel RB, Holm RH. Ground spin state variability in [Fe4S4(SR)4]3-. Synthetic analogs of the reduced clusters in ferredoxins and other iron-sulfur proteins: cases of extreme sensitivity of electronic state and structure to extrinsic factors. J Am Chem Soc. 1988 Aug 01;110(18):6084-95. doi: 10.1021/ja00226a025. PMID: 22148785.
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[Ferredoxin from Bumilleriopsis filiformis Vischer].

Planta

Böger P.
PMID: 24500180
Planta. 1970 Jun;92(2):105-28. doi: 10.1007/BF00385204.

Ferredoxin from the alga Bumilleriopsis filiformis Vischer (Xanthophyceae) is characterized by comparing some of its properties with spinach ferredoxin.It is similar to the known plant ferredoxins in the following points: a) Absorption spectrum. b) Molecular weight. c) Amino acid...

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Böger P. Ferredoxin aus Bumilleriopsis filiformis Vischer. [Ferredoxin from Bumilleriopsis filiformis Vischer]. Planta. 1970;92(2):105-28doi: 10.1007/BF00385204.
Böger, P. (1970). Ferredoxin aus Bumilleriopsis filiformis Vischer. [Ferredoxin from Bumilleriopsis filiformis Vischer]. Planta, 92(2), 105-28. https://doi.org/10.1007/BF00385204
Böger, P. "Ferredoxin aus Bumilleriopsis filiformis Vischer." [Ferredoxin from Bumilleriopsis filiformis Vischer]. Planta vol. 92,2 (1970): 105-28. doi: https://doi.org/10.1007/BF00385204
Böger P. Ferredoxin aus Bumilleriopsis filiformis Vischer. [Ferredoxin from Bumilleriopsis filiformis Vischer]. Planta. 1970 Jun;92(2):105-28. doi: 10.1007/BF00385204. German. PMID: 24500180.
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[Influence of ferredoxin on ferredoxin-NADP reductase].

Planta

Böger P.
PMID: 24487683
Planta. 1971 Dec;99(4):319-38. doi: 10.1007/BF00385824.

Transhydrogenase and diaphorase activity of ferredoxin-NADP reductase are enhanced by plant ferredoxins. This stimulation is specific; ferredoxin cannot be replaced by sulfhydryl compounds such as cysteine or dithiothreitol, the apoprotein of ferredoxin or Fe(2+), Fe(3+) ions.The effect is particularly...

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Böger P. Einfluß von Ferredoxin auf Ferredoxin-NADP-Reduktase. [Influence of ferredoxin on ferredoxin-NADP reductase]. Planta. 1971;99(4):319-38doi: 10.1007/BF00385824.
Böger, P. (1971). Einfluß von Ferredoxin auf Ferredoxin-NADP-Reduktase. [Influence of ferredoxin on ferredoxin-NADP reductase]. Planta, 99(4), 319-38. https://doi.org/10.1007/BF00385824
Böger, P. "Einfluß von Ferredoxin auf Ferredoxin-NADP-Reduktase." [Influence of ferredoxin on ferredoxin-NADP reductase]. Planta vol. 99,4 (1971): 319-38. doi: https://doi.org/10.1007/BF00385824
Böger P. Einfluß von Ferredoxin auf Ferredoxin-NADP-Reduktase. [Influence of ferredoxin on ferredoxin-NADP reductase]. Planta. 1971 Dec;99(4):319-38. doi: 10.1007/BF00385824. German. PMID: 24487683.
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Qualitative and quantitative immunofluorescence studies of chloroplast ferredoxin : Application to investigations of ferredoxin inheritance in Nicotiana hybrids.

Planta

Huisman JG, Bernards A, Liebregts P, Gebbink MG, Stegwee D.
PMID: 24420666
Planta. 1977 Jan;137(3):279-86. doi: 10.1007/BF00388163.

Antibodies were raised in rabbits against 2Fe-2S ferredoxin from N. tabacum L. The antibodies showed partial cross-reactivity in the double diffusion test with ferredoxins from Spinacia oleracea L., Petunia inflata Fries., P. axillaris Lam., Phaseolus vulgaris L., Chlamydomonas remhardii...

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Huisman JG, Bernards A, Liebregts P, et al. Qualitative and quantitative immunofluorescence studies of chloroplast ferredoxin : Application to investigations of ferredoxin inheritance in Nicotiana hybrids. Planta. 1977;137(3):279-86doi: 10.1007/BF00388163.
Huisman, J. G., Bernards, A., Liebregts, P., Gebbink, M. G., & Stegwee, D. (1977). Qualitative and quantitative immunofluorescence studies of chloroplast ferredoxin : Application to investigations of ferredoxin inheritance in Nicotiana hybrids. Planta, 137(3), 279-86. https://doi.org/10.1007/BF00388163
Huisman, J G, et al. "Qualitative and quantitative immunofluorescence studies of chloroplast ferredoxin : Application to investigations of ferredoxin inheritance in Nicotiana hybrids." Planta vol. 137,3 (1977): 279-86. doi: https://doi.org/10.1007/BF00388163
Huisman JG, Bernards A, Liebregts P, Gebbink MG, Stegwee D. Qualitative and quantitative immunofluorescence studies of chloroplast ferredoxin : Application to investigations of ferredoxin inheritance in Nicotiana hybrids. Planta. 1977 Jan;137(3):279-86. doi: 10.1007/BF00388163. PMID: 24420666.
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Identification of the two-component guaiacol demethylase system from Rhodococcus rhodochrous and expression in Pseudomonas putida EM42 for guaiacol assimilation.

AMB Express

García-Hidalgo J, Ravi K, Kuré LL, Lidén G, Gorwa-Grauslund M.
PMID: 30859469
AMB Express. 2019 Mar 11;9(1):34. doi: 10.1186/s13568-019-0759-8.

A diversity of softwood lignin depolymerization processes yield guaiacol as the main low molecular weight product. This key aromatic compound can be utilized as a carbon source by several microbial species, most of which are Gram positive bacteria. Microbial...

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García-Hidalgo J, Ravi K, Kuré LL, et al. Identification of the two-component guaiacol demethylase system from Rhodococcus rhodochrous and expression in Pseudomonas putida EM42 for guaiacol assimilation. AMB Express. 2019;9(1):34doi: 10.1186/s13568-019-0759-8.
García-Hidalgo, J., Ravi, K., Kuré, L. L., Lidén, G., & Gorwa-Grauslund, M. (2019). Identification of the two-component guaiacol demethylase system from Rhodococcus rhodochrous and expression in Pseudomonas putida EM42 for guaiacol assimilation. AMB Express, 9(1), 34. https://doi.org/10.1186/s13568-019-0759-8
García-Hidalgo, Javier, et al. "Identification of the two-component guaiacol demethylase system from Rhodococcus rhodochrous and expression in Pseudomonas putida EM42 for guaiacol assimilation." AMB Express vol. 9,1 (2019): 34. doi: https://doi.org/10.1186/s13568-019-0759-8
García-Hidalgo J, Ravi K, Kuré LL, Lidén G, Gorwa-Grauslund M. Identification of the two-component guaiacol demethylase system from Rhodococcus rhodochrous and expression in Pseudomonas putida EM42 for guaiacol assimilation. AMB Express. 2019 Mar 11;9(1):34. doi: 10.1186/s13568-019-0759-8. PMID: 30859469; PMCID: PMC6411806.
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Proteomic response of the marine ammonia-oxidising archaeon Nitrosopumilus maritimus to iron limitation reveals strategies to compensate for nutrient scarcity.

Environmental microbiology

Shafiee RT, Snow JT, Hester S, Zhang Q, Rickaby REM.
PMID: 33876540
Environ Microbiol. 2021 Apr 19; doi: 10.1111/1462-2920.15491. Epub 2021 Apr 19.

Dissolved iron (Fe) is vanishingly low in the oceans, with ecological success conferred to microorganisms that can restructure their biochemistry to maintain high growth rates during Fe scarcity. Chemolithoautotrophic ammonia-oxidising archaea (AOA) are highly abundant in the oceans, constituting...

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Shafiee RT, Snow JT, Hester S, et al. Proteomic response of the marine ammonia-oxidising archaeon Nitrosopumilus maritimus to iron limitation reveals strategies to compensate for nutrient scarcity. Environ Microbiol. 2021;doi: 10.1111/1462-2920.15491.
Shafiee, R. T., Snow, J. T., Hester, S., Zhang, Q., & Rickaby, R. E. M. (2021). Proteomic response of the marine ammonia-oxidising archaeon Nitrosopumilus maritimus to iron limitation reveals strategies to compensate for nutrient scarcity. Environmental microbiology, . https://doi.org/10.1111/1462-2920.15491
Shafiee, Roxana T, et al. "Proteomic response of the marine ammonia-oxidising archaeon Nitrosopumilus maritimus to iron limitation reveals strategies to compensate for nutrient scarcity." Environmental microbiology vol. (2021). doi: https://doi.org/10.1111/1462-2920.15491
Shafiee RT, Snow JT, Hester S, Zhang Q, Rickaby REM. Proteomic response of the marine ammonia-oxidising archaeon Nitrosopumilus maritimus to iron limitation reveals strategies to compensate for nutrient scarcity. Environ Microbiol. 2021 Apr 19; doi: 10.1111/1462-2920.15491. Epub 2021 Apr 19. PMID: 33876540.
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Showing 37 to 45 of 45 entries