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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...

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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.
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Large-Scale Proteomics of the Cassava Storage Root and Identification of a Target Gene to Reduce Postharvest Deterioration.

The Plant cell

Vanderschuren H, Nyaboga E, Poon JS, Baerenfaller K, Grossmann J, Hirsch-Hoffmann M, Kirchgessner N, Nanni P, Gruissem W.
PMID: 24876255
Plant Cell. 2014 May;26(5):1913-1924. doi: 10.1105/tpc.114.123927. Epub 2014 May 29.

Cassava (Manihot esculenta) is the most important root crop in the tropics, but rapid postharvest physiological deterioration (PPD) of the root is a major constraint to commercial cassava production. We established a reliable method for image-based PPD symptom quantification...

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Vanderschuren H, Nyaboga E, Poon JS, et al. Large-Scale Proteomics of the Cassava Storage Root and Identification of a Target Gene to Reduce Postharvest Deterioration. Plant Cell. 2014;26(5):1913-1924doi: 10.1105/tpc.114.123927.
Vanderschuren, H., Nyaboga, E., Poon, J. S., Baerenfaller, K., Grossmann, J., Hirsch-Hoffmann, M., Kirchgessner, N., Nanni, P., & Gruissem, W. (2014). Large-Scale Proteomics of the Cassava Storage Root and Identification of a Target Gene to Reduce Postharvest Deterioration. The Plant cell, 26(5), 1913-1924. https://doi.org/10.1105/tpc.114.123927
Vanderschuren, Hervé, et al. "Large-Scale Proteomics of the Cassava Storage Root and Identification of a Target Gene to Reduce Postharvest Deterioration." The Plant cell vol. 26,5 (2014): 1913-1924. doi: https://doi.org/10.1105/tpc.114.123927
Vanderschuren H, Nyaboga E, Poon JS, Baerenfaller K, Grossmann J, Hirsch-Hoffmann M, Kirchgessner N, Nanni P, Gruissem W. Large-Scale Proteomics of the Cassava Storage Root and Identification of a Target Gene to Reduce Postharvest Deterioration. Plant Cell. 2014 May;26(5):1913-1924. doi: 10.1105/tpc.114.123927. Epub 2014 May 29. PMID: 24876255; PMCID: PMC4079358.
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Redox regulation by reversible protein S-thiolation in bacteria.

Frontiers in microbiology

Loi VV, Rossius M, Antelmann H.
PMID: 25852656
Front Microbiol. 2015 Mar 16;6:187. doi: 10.3389/fmicb.2015.00187. eCollection 2015.

Low molecular weight (LMW) thiols function as thiol-redox buffers to maintain the reduced state of the cytoplasm. The best studied LMW thiol is the tripeptide glutathione (GSH) present in all eukaryotes and Gram-negative bacteria. Firmicutes bacteria, including Bacillus and...

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Loi VV, Rossius M, Antelmann H. Redox regulation by reversible protein S-thiolation in bacteria. Front Microbiol. 2015;6:187doi: 10.3389/fmicb.2015.00187.
Loi, V. V., Rossius, M., & Antelmann, H. (2015). Redox regulation by reversible protein S-thiolation in bacteria. Frontiers in microbiology, 6187. https://doi.org/10.3389/fmicb.2015.00187
Loi, Vu Van, et al. "Redox regulation by reversible protein S-thiolation in bacteria." Frontiers in microbiology vol. 6 (2015): 187. doi: https://doi.org/10.3389/fmicb.2015.00187
Loi VV, Rossius M, Antelmann H. Redox regulation by reversible protein S-thiolation in bacteria. Front Microbiol. 2015 Mar 16;6:187. doi: 10.3389/fmicb.2015.00187. eCollection 2015. PMID: 25852656; PMCID: PMC4360819.
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S-nitrosoglutathione reductases are low-copy number, cysteine-rich proteins in plants that control multiple developmental and defense responses in Arabidopsis.

Frontiers in plant science

Xu S, Guerra D, Lee U, Vierling E.
PMID: 24204370
Front Plant Sci. 2013 Nov 05;4:430. doi: 10.3389/fpls.2013.00430. eCollection 2013.

S-nitrosoglutathione reductase (GSNOR) is believed to modulate effects of reactive oxygen and nitrogen species through catabolism of S-nitrosoglutathione (GSNO). We combined bioinformatics of plant GSNOR genes, localization of GSNOR in Arabidopsis thaliana, and microarray analysis of a GSNOR null...

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Xu S, Guerra D, Lee U, et al. S-nitrosoglutathione reductases are low-copy number, cysteine-rich proteins in plants that control multiple developmental and defense responses in Arabidopsis. Front Plant Sci. 2013;4:430doi: 10.3389/fpls.2013.00430.
Xu, S., Guerra, D., Lee, U., & Vierling, E. (2013). S-nitrosoglutathione reductases are low-copy number, cysteine-rich proteins in plants that control multiple developmental and defense responses in Arabidopsis. Frontiers in plant science, 4430. https://doi.org/10.3389/fpls.2013.00430
Xu, Shengbao, et al. "S-nitrosoglutathione reductases are low-copy number, cysteine-rich proteins in plants that control multiple developmental and defense responses in Arabidopsis." Frontiers in plant science vol. 4 (2013): 430. doi: https://doi.org/10.3389/fpls.2013.00430
Xu S, Guerra D, Lee U, Vierling E. S-nitrosoglutathione reductases are low-copy number, cysteine-rich proteins in plants that control multiple developmental and defense responses in Arabidopsis. Front Plant Sci. 2013 Nov 05;4:430. doi: 10.3389/fpls.2013.00430. eCollection 2013. PMID: 24204370; PMCID: PMC3817919.
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Redox regulation: an introduction.

Physiologia plantarum

Dietz KJ, Scheibe R.
PMID: 15032870
Physiol Plant. 2004 Jan;120(1):1-3. doi: 10.1111/j.0031-9317.2004.0277.x.

The redox-state is a critical determinate of cell function, and any major imbalances can cause severe damage or death. The cellular redox status therefore needs to be sensed and modulated before such imbalances occur. Various redox-active components are involved...

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Dietz KJ, Scheibe R. Redox regulation: an introduction. Physiol Plant. 2004;120(1):1-3doi: 10.1111/j.0031-9317.2004.0277.x.
Dietz, K. J., & Scheibe, R. (2004). Redox regulation: an introduction. Physiologia plantarum, 120(1), 1-3. https://doi.org/10.1111/j.0031-9317.2004.0277.x
Dietz, Karl-Josef, and Scheibe, Renate. "Redox regulation: an introduction." Physiologia plantarum vol. 120,1 (2004): 1-3. doi: https://doi.org/10.1111/j.0031-9317.2004.0277.x
Dietz KJ, Scheibe R. Redox regulation: an introduction. Physiol Plant. 2004 Jan;120(1):1-3. doi: 10.1111/j.0031-9317.2004.0277.x. PMID: 15032870.
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Thiol-based redox signaling in the nitrogen-fixing symbiosis.

Frontiers in plant science

Frendo P, Matamoros MA, Alloing G, Becana M.
PMID: 24133498
Front Plant Sci. 2013 Sep 26;4:376. doi: 10.3389/fpls.2013.00376.

In nitrogen poor soils legumes establish a symbiotic interaction with rhizobia that results in the formation of root nodules. These are unique plant organs where bacteria differentiate into bacteroids, which express the nitrogenase enzyme complex that reduces atmospheric N...

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Frendo P, Matamoros MA, Alloing G, et al. Thiol-based redox signaling in the nitrogen-fixing symbiosis. Front Plant Sci. 2013;4:376doi: 10.3389/fpls.2013.00376.
Frendo, P., Matamoros, M. A., Alloing, G., & Becana, M. (2013). Thiol-based redox signaling in the nitrogen-fixing symbiosis. Frontiers in plant science, 4376. https://doi.org/10.3389/fpls.2013.00376
Frendo, Pierre, et al. "Thiol-based redox signaling in the nitrogen-fixing symbiosis." Frontiers in plant science vol. 4 (2013): 376. doi: https://doi.org/10.3389/fpls.2013.00376
Frendo P, Matamoros MA, Alloing G, Becana M. Thiol-based redox signaling in the nitrogen-fixing symbiosis. Front Plant Sci. 2013 Sep 26;4:376. doi: 10.3389/fpls.2013.00376. PMID: 24133498; PMCID: PMC3783977.
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Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides.

Chemical science

Ukuwela AA, Bush AI, Wedd AG, Xiao Z.
PMID: 29675162
Chem Sci. 2017 Dec 06;9(5):1173-1183. doi: 10.1039/c7sc04416j. eCollection 2018 Feb 07.

Glutaredoxins (Grxs) are a family of glutathione (GSH)-dependent thiol-disulfide oxidoreductases. They feature GSH-binding sites that directly connect the reversible redox chemistry of protein thiols to the abundant cellular nonprotein thiol pool GSSG/GSH. This work studied the pathways for oxidation...

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Ukuwela AA, Bush AI, Wedd AG, et al. Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides. Chem Sci. 2017;9(5):1173-1183doi: 10.1039/c7sc04416j.
Ukuwela, A. A., Bush, A. I., Wedd, A. G., & Xiao, Z. (2018). Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides. Chemical science, 9(5), 1173-1183. https://doi.org/10.1039/c7sc04416j
Ukuwela, Ashwinie A, et al. "Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides." Chemical science vol. 9,5 (2018): 1173-1183. doi: https://doi.org/10.1039/c7sc04416j
Ukuwela AA, Bush AI, Wedd AG, Xiao Z. Glutaredoxins employ parallel monothiol-dithiol mechanisms to catalyze thiol-disulfide exchanges with protein disulfides. Chem Sci. 2017 Dec 06;9(5):1173-1183. doi: 10.1039/c7sc04416j. eCollection 2018 Feb 07. PMID: 29675162; PMCID: PMC5885593.
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Corrigendum: Phosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins.

Scientific reports

Domkin V, Chabes A.
PMID: 28387227
Sci Rep. 2017 Apr 07;7:45880. doi: 10.1038/srep45880.

No abstract available.

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Domkin V, Chabes A. Corrigendum: Phosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins. Sci Rep. 2017;7:45880doi: 10.1038/srep45880.
Domkin, V., & Chabes, A. (2017). Corrigendum: Phosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins. Scientific reports, 745880. https://doi.org/10.1038/srep45880
Domkin, Vladimir, and Chabes, Andrei. "Corrigendum: Phosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins." Scientific reports vol. 7 (2017): 45880. doi: https://doi.org/10.1038/srep45880
Domkin V, Chabes A. Corrigendum: Phosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins. Sci Rep. 2017 Apr 07;7:45880. doi: 10.1038/srep45880. PMID: 28387227; PMCID: PMC5383934.
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Overexpression of a CPYC-Type Glutaredoxin, .

Frontiers in plant science

Liu S, Fu H, Jiang J, Chen Z, Gao J, Shu H, Zhang S, Yang C, Liu J.
PMID: 31316541
Front Plant Sci. 2019 Jun 27;10:848. doi: 10.3389/fpls.2019.00848. eCollection 2019.

Glutaredoxins (Grxs) are a ubiquitous group of oxidoreductase enzymes that are important in plant growth and development; however, the functions of rice Grxs have not been fully elucidated. In this paper, we showed that one of the Grxs, encoded...

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Liu S, Fu H, Jiang J, et al. Overexpression of a CPYC-Type Glutaredoxin, . Front Plant Sci. 2019;10:848doi: 10.3389/fpls.2019.00848.
Liu, S., Fu, H., Jiang, J., Chen, Z., Gao, J., Shu, H., Zhang, S., Yang, C., & Liu, J. (2019). Overexpression of a CPYC-Type Glutaredoxin, . Frontiers in plant science, 10848. https://doi.org/10.3389/fpls.2019.00848
Liu, Shengjie, et al. "Overexpression of a CPYC-Type Glutaredoxin, ." Frontiers in plant science vol. 10 (2019): 848. doi: https://doi.org/10.3389/fpls.2019.00848
Liu S, Fu H, Jiang J, Chen Z, Gao J, Shu H, Zhang S, Yang C, Liu J. Overexpression of a CPYC-Type Glutaredoxin, . Front Plant Sci. 2019 Jun 27;10:848. doi: 10.3389/fpls.2019.00848. eCollection 2019. PMID: 31316541; PMCID: PMC6610441.
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Inhibition of PDIA3 in club cells attenuates osteopontin production and lung fibrosis.

Thorax

Kumar A, Elko E, Bruno SR, Mark ZF, Chamberlain N, Mihavics BK, Chandrasekaran R, Walzer J, Ruban M, Gold C, Lam YW, Ghandikota S, Jegga AG, Gomez JL, Janssen-Heininger YM, Anathy V.
PMID: 34400514
Thorax. 2021 Aug 16; doi: 10.1136/thoraxjnl-2021-216882. Epub 2021 Aug 16.

CONCLUSIONS: Our study reveals a new relationship with distally localised club cells, PDIA3 and SPP1 in lung fibrosis and inhibition of PDIA3 or SPP1 attenuates lung fibrosis.

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Kumar A, Elko E, Bruno SR, et al. Inhibition of PDIA3 in club cells attenuates osteopontin production and lung fibrosis. Thorax. 2021;doi: 10.1136/thoraxjnl-2021-216882.
Kumar, A., Elko, E., Bruno, S. R., Mark, Z. F., Chamberlain, N., Mihavics, B. K., Chandrasekaran, R., Walzer, J., Ruban, M., Gold, C., Lam, Y. W., Ghandikota, S., Jegga, A. G., Gomez, J. L., Janssen-Heininger, Y. M., & Anathy, V. (2021). Inhibition of PDIA3 in club cells attenuates osteopontin production and lung fibrosis. Thorax, . https://doi.org/10.1136/thoraxjnl-2021-216882
Kumar, Amit, et al. "Inhibition of PDIA3 in club cells attenuates osteopontin production and lung fibrosis." Thorax vol. (2021). doi: https://doi.org/10.1136/thoraxjnl-2021-216882
Kumar A, Elko E, Bruno SR, Mark ZF, Chamberlain N, Mihavics BK, Chandrasekaran R, Walzer J, Ruban M, Gold C, Lam YW, Ghandikota S, Jegga AG, Gomez JL, Janssen-Heininger YM, Anathy V. Inhibition of PDIA3 in club cells attenuates osteopontin production and lung fibrosis. Thorax. 2021 Aug 16; doi: 10.1136/thoraxjnl-2021-216882. Epub 2021 Aug 16. PMID: 34400514.
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Thiol-based redox-active proteins as cardioprotective therapeutic agents in cardiovascular diseases.

Basic research in cardiology

Andreadou I, Efentakis P, Frenis K, Daiber A, Schulz R.
PMID: 34275052
Basic Res Cardiol. 2021 Jul 17;116(1):44. doi: 10.1007/s00395-021-00885-5.

Thiol-based redox compounds, namely thioredoxins (Trxs), glutaredoxins (Grxs) and peroxiredoxins (Prxs), stand as a pivotal group of proteins involved in antioxidant processes and redox signaling. Glutaredoxins (Grxs) are considered as one of the major families of proteins involved in...

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Andreadou I, Efentakis P, Frenis K, et al. Thiol-based redox-active proteins as cardioprotective therapeutic agents in cardiovascular diseases. Basic Res Cardiol. 2021;116(1):44doi: 10.1007/s00395-021-00885-5.
Andreadou, I., Efentakis, P., Frenis, K., Daiber, A., & Schulz, R. (2021). Thiol-based redox-active proteins as cardioprotective therapeutic agents in cardiovascular diseases. Basic research in cardiology, 116(1), 44. https://doi.org/10.1007/s00395-021-00885-5
Andreadou, Ioanna, et al. "Thiol-based redox-active proteins as cardioprotective therapeutic agents in cardiovascular diseases." Basic research in cardiology vol. 116,1 (2021): 44. doi: https://doi.org/10.1007/s00395-021-00885-5
Andreadou I, Efentakis P, Frenis K, Daiber A, Schulz R. Thiol-based redox-active proteins as cardioprotective therapeutic agents in cardiovascular diseases. Basic Res Cardiol. 2021 Jul 17;116(1):44. doi: 10.1007/s00395-021-00885-5. PMID: 34275052.
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Chickpea glutaredoxin (.

Physiology and molecular biology of plants : an international journal of functional plant biology

Kumar A, Kumar V, Dubey AK, Ansari MA, Narayan S, Meenakshi, Kumar S, Pandey V, Pande V, Sanyal I.
PMID: 34092945
Physiol Mol Biol Plants. 2021 May;27(5):923-944. doi: 10.1007/s12298-021-00999-z. Epub 2021 May 06.

Glutaredoxins (Grxs) are short, cysteine-rich glutathione (GSH)-mediated oxidoreductases. In this study, a chickpea (SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s12298-021-00999-z.

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Kumar A, Kumar V, Dubey AK, et al. Chickpea glutaredoxin (. Physiol Mol Biol Plants. 2021;27(5):923-944doi: 10.1007/s12298-021-00999-z.
Kumar, A., Kumar, V., Dubey, A. K., Ansari, M. A., Narayan, S., Meenakshi, Kumar, S., Pandey, V., Pande, V., & Sanyal, I. (2021). Chickpea glutaredoxin (. Physiology and molecular biology of plants : an international journal of functional plant biology, 27(5), 923-944. https://doi.org/10.1007/s12298-021-00999-z
Kumar, Anil, et al. "Chickpea glutaredoxin (." Physiology and molecular biology of plants : an international journal of functional plant biology vol. 27,5 (2021): 923-944. doi: https://doi.org/10.1007/s12298-021-00999-z
Kumar A, Kumar V, Dubey AK, Ansari MA, Narayan S, Meenakshi, Kumar S, Pandey V, Pande V, Sanyal I. Chickpea glutaredoxin (. Physiol Mol Biol Plants. 2021 May;27(5):923-944. doi: 10.1007/s12298-021-00999-z. Epub 2021 May 06. PMID: 34092945; PMCID: PMC8140008.
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Showing 1 to 12 of 77 entries