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Identification of the Large Subunit of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase as a Substrate for Transglutaminase in Medicago sativa L. (Alfalfa).

Plant physiology

Margosiak SA, Dharma A, Bruce-Carver MR, Gonzales AP, Louie D, Kuehn GD.
PMID: 16667270
Plant Physiol. 1990 Jan;92(1):88-96. doi: 10.1104/pp.92.1.88.

Extracts prepared from floral meristematic tissue of alfalfa (Medicago sativa L.) were investigated for expression of the enzyme transglutaminase in order to identify the major protein substrate for transglutaminase-directed modifications among plant proteins. The large polymorphic subunits of ribulose...

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Margosiak SA, Dharma A, Bruce-Carver MR, et al. Identification of the Large Subunit of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase as a Substrate for Transglutaminase in Medicago sativa L. (Alfalfa). Plant Physiol. 1990;92(1):88-96doi: 10.1104/pp.92.1.88.
Margosiak, S. A., Dharma, A., Bruce-Carver, M. R., Gonzales, A. P., Louie, D., & Kuehn, G. D. (1990). Identification of the Large Subunit of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase as a Substrate for Transglutaminase in Medicago sativa L. (Alfalfa). Plant physiology, 92(1), 88-96. https://doi.org/10.1104/pp.92.1.88
Margosiak, S A, et al. "Identification of the Large Subunit of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase as a Substrate for Transglutaminase in Medicago sativa L. (Alfalfa)." Plant physiology vol. 92,1 (1990): 88-96. doi: https://doi.org/10.1104/pp.92.1.88
Margosiak SA, Dharma A, Bruce-Carver MR, Gonzales AP, Louie D, Kuehn GD. Identification of the Large Subunit of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase as a Substrate for Transglutaminase in Medicago sativa L. (Alfalfa). Plant Physiol. 1990 Jan;92(1):88-96. doi: 10.1104/pp.92.1.88. PMID: 16667270; PMCID: PMC1062252.
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Ubiquitin Pool Modulation and Protein Degradation in Wheat Roots during High Temperature Stress.

Plant physiology

Ferguson DL, Guikema JA, Paulsen GM.
PMID: 16667343
Plant Physiol. 1990 Mar;92(3):740-6. doi: 10.1104/pp.92.3.740.

Ubiquitin, a key component in an ATP-dependent proteolytic pathway, participates in the response of various eucaryotic organisms to high temperature stress. Our objective was to determine if ubiquitin serves a similar capacity for metabolizing altered proteins in higher plants...

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Ferguson DL, Guikema JA, Paulsen GM. Ubiquitin Pool Modulation and Protein Degradation in Wheat Roots during High Temperature Stress. Plant Physiol. 1990;92(3):740-6doi: 10.1104/pp.92.3.740.
Ferguson, D. L., Guikema, J. A., & Paulsen, G. M. (1990). Ubiquitin Pool Modulation and Protein Degradation in Wheat Roots during High Temperature Stress. Plant physiology, 92(3), 740-6. https://doi.org/10.1104/pp.92.3.740
Ferguson, D L, et al. "Ubiquitin Pool Modulation and Protein Degradation in Wheat Roots during High Temperature Stress." Plant physiology vol. 92,3 (1990): 740-6. doi: https://doi.org/10.1104/pp.92.3.740
Ferguson DL, Guikema JA, Paulsen GM. Ubiquitin Pool Modulation and Protein Degradation in Wheat Roots during High Temperature Stress. Plant Physiol. 1990 Mar;92(3):740-6. doi: 10.1104/pp.92.3.740. PMID: 16667343; PMCID: PMC1062362.
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OUR PRESENT KNOWLEDGE OF PLANT PROTEINS.

Science (New York, N.Y.)

Osborne TB.
PMID: 17771936
Science. 1908 Oct 02;28(718):417-27. doi: 10.1126/science.28.718.417.

No abstract available.

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Osborne TB. OUR PRESENT KNOWLEDGE OF PLANT PROTEINS. Science. 1908;28(718):417-27doi: 10.1126/science.28.718.417.
Osborne, T. B. (1908). OUR PRESENT KNOWLEDGE OF PLANT PROTEINS. Science (New York, N.Y.), 28(718), 417-27. https://doi.org/10.1126/science.28.718.417
Osborne, T B. "OUR PRESENT KNOWLEDGE OF PLANT PROTEINS." Science (New York, N.Y.) vol. 28,718 (1908): 417-27. doi: https://doi.org/10.1126/science.28.718.417
Osborne TB. OUR PRESENT KNOWLEDGE OF PLANT PROTEINS. Science. 1908 Oct 02;28(718):417-27. doi: 10.1126/science.28.718.417. PMID: 17771936.
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Assaying protein palmitoylation in plants.

Plant methods

Hemsley PA, Taylor L, Grierson CS.
PMID: 18190696
Plant Methods. 2008 Jan 11;4:2. doi: 10.1186/1746-4811-4-2.

BACKGROUND: Protein S-acylation (also known as palmitoylation) is the reversible post-translational addition of acyl lipids to cysteine residues in proteins through a thioester bond. It allows strong association with membranes. Whilst prediction methods for S-acylation exist, prediction is imperfect....

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Hemsley PA, Taylor L, Grierson CS. Assaying protein palmitoylation in plants. Plant Methods. 2008;4:2doi: 10.1186/1746-4811-4-2.
Hemsley, P. A., Taylor, L., & Grierson, C. S. (2008). Assaying protein palmitoylation in plants. Plant methods, 42. https://doi.org/10.1186/1746-4811-4-2
Hemsley, Piers A, et al. "Assaying protein palmitoylation in plants." Plant methods vol. 4 (2008): 2. doi: https://doi.org/10.1186/1746-4811-4-2
Hemsley PA, Taylor L, Grierson CS. Assaying protein palmitoylation in plants. Plant Methods. 2008 Jan 11;4:2. doi: 10.1186/1746-4811-4-2. PMID: 18190696; PMCID: PMC2244627.
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Heterelogous expression of plant genes.

International journal of plant genomics

Yesilirmak F, Sayers Z.
PMID: 19672459
Int J Plant Genomics. 2009;2009:296482. doi: 10.1155/2009/296482. Epub 2009 Aug 06.

Heterologous expression allows the production of plant proteins in an organism which is simpler than the natural source. This technology is widely used for large-scale purification of plant proteins from microorganisms for biochemical and biophysical analyses. Additionally expression in...

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Yesilirmak F, Sayers Z. Heterelogous expression of plant genes. Int J Plant Genomics. 2009;2009:296482doi: 10.1155/2009/296482.
Yesilirmak, F., & Sayers, Z. (2009). Heterelogous expression of plant genes. International journal of plant genomics, 2009296482. https://doi.org/10.1155/2009/296482
Yesilirmak, Filiz, and Sayers, Zehra. "Heterelogous expression of plant genes." International journal of plant genomics vol. 2009 (2009): 296482. doi: https://doi.org/10.1155/2009/296482
Yesilirmak F, Sayers Z. Heterelogous expression of plant genes. Int J Plant Genomics. 2009;2009:296482. doi: 10.1155/2009/296482. Epub 2009 Aug 06. PMID: 19672459; PMCID: PMC2722100.
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From host recognition to T-DNA integration: the function of bacterial and plant genes in the Agrobacterium-plant cell interaction.

Molecular plant pathology

Tzfira T, Citovsky V.
PMID: 20572967
Mol Plant Pathol. 2000 Jul 01;1(4):201-12. doi: 10.1046/j.1364-3703.2000.00026.x.

UNLABELLED: Abstract Agrobacterium tumefaciens and its related species, A. rhizogenes and A. vitis, are the only known bacterial pathogens which 'genetically invade' host plants and stably integrate part of their genetic material into the host cell genome. Thus, A....

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Tzfira T, Citovsky V. From host recognition to T-DNA integration: the function of bacterial and plant genes in the Agrobacterium-plant cell interaction. Mol Plant Pathol. 2000;1(4):201-12doi: 10.1046/j.1364-3703.2000.00026.x.
Tzfira, T., & Citovsky, V. (2000). From host recognition to T-DNA integration: the function of bacterial and plant genes in the Agrobacterium-plant cell interaction. Molecular plant pathology, 1(4), 201-12. https://doi.org/10.1046/j.1364-3703.2000.00026.x
Tzfira, T, and Citovsky, V. "From host recognition to T-DNA integration: the function of bacterial and plant genes in the Agrobacterium-plant cell interaction." Molecular plant pathology vol. 1,4 (2000): 201-12. doi: https://doi.org/10.1046/j.1364-3703.2000.00026.x
Tzfira T, Citovsky V. From host recognition to T-DNA integration: the function of bacterial and plant genes in the Agrobacterium-plant cell interaction. Mol Plant Pathol. 2000 Jul 01;1(4):201-12. doi: 10.1046/j.1364-3703.2000.00026.x. PMID: 20572967.
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Storage proteins.

The arabidopsis book

Fujiwara T, Nambara E, Yamagishi K, Goto DB, Naito S.
PMID: 22303197
Arabidopsis Book. 2002;1:e0020. doi: 10.1199/tab.0020. Epub 2002 Sep 30.

Plants accumulate storage substances such as starch, lipids and proteins in certain phases of development. Storage proteins accumulate in both vegetative and reproductive tissues and serve as a reservoir to be used in later stages of plant development. The...

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Fujiwara T, Nambara E, Yamagishi K, et al. Storage proteins. Arabidopsis Book. 2002;1:e0020doi: 10.1199/tab.0020.
Fujiwara, T., Nambara, E., Yamagishi, K., Goto, D. B., & Naito, S. (2002). Storage proteins. The arabidopsis book, 1e0020. https://doi.org/10.1199/tab.0020
Fujiwara, Toru, et al. "Storage proteins." The arabidopsis book vol. 1 (2002): e0020. doi: https://doi.org/10.1199/tab.0020
Fujiwara T, Nambara E, Yamagishi K, Goto DB, Naito S. Storage proteins. Arabidopsis Book. 2002;1:e0020. doi: 10.1199/tab.0020. Epub 2002 Sep 30. PMID: 22303197; PMCID: PMC3243327.
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Cross-reactivity between natural rubber latex and food allergens.

Environmental toxicology and pharmacology

Raulf-Heimsoth M, Posch A, Chen Z, Baur X.
PMID: 21781817
Environ Toxicol Pharmacol. 1997 Nov;4(1):169-73. doi: 10.1016/s1382-6689(97)10059-x.

Immediate-type hypersensitivity to latex is a growing problem, especially among health care workers (HCWs) and patients requiring long-term catheterization and multiple operations. The responsible allergens are latex proteins, which are found in raw latex, as well as in various...

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Raulf-Heimsoth M, Posch A, Chen Z, et al. Cross-reactivity between natural rubber latex and food allergens. Environ Toxicol Pharmacol. 1997;4(1):169-73doi: 10.1016/s1382-6689(97)10059-x.
Raulf-Heimsoth, M., Posch, A., Chen, Z., & Baur, X. (1997). Cross-reactivity between natural rubber latex and food allergens. Environmental toxicology and pharmacology, 4(1), 169-73. https://doi.org/10.1016/s1382-6689(97)10059-x
Raulf-Heimsoth, M, et al. "Cross-reactivity between natural rubber latex and food allergens." Environmental toxicology and pharmacology vol. 4,1 (1997): 169-73. doi: https://doi.org/10.1016/s1382-6689(97)10059-x
Raulf-Heimsoth M, Posch A, Chen Z, Baur X. Cross-reactivity between natural rubber latex and food allergens. Environ Toxicol Pharmacol. 1997 Nov;4(1):169-73. doi: 10.1016/s1382-6689(97)10059-x. PMID: 21781817.
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Dual or Not Dual?-Comparative Analysis of Fluorescence Microscopy-Based Approaches to Study Organelle Targeting Specificity of Nuclear-Encoded Plant Proteins.

Frontiers in plant science

Sharma M, Bennewitz B, Klösgen RB.
PMID: 30298079
Front Plant Sci. 2018 Sep 19;9:1350. doi: 10.3389/fpls.2018.01350. eCollection 2018.

Plant cells are unique as they carry two organelles of endosymbiotic origin, namely mitochondria and chloroplasts (plastids) which have specific but partially overlapping functions, e. g., in energy and redox metabolism. Despite housing residual genomes of limited coding capacity,...

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Sharma M, Bennewitz B, Klösgen RB. Dual or Not Dual?-Comparative Analysis of Fluorescence Microscopy-Based Approaches to Study Organelle Targeting Specificity of Nuclear-Encoded Plant Proteins. Front Plant Sci. 2018;9:1350doi: 10.3389/fpls.2018.01350.
Sharma, M., Bennewitz, B., & Klösgen, R. B. (2018). Dual or Not Dual?-Comparative Analysis of Fluorescence Microscopy-Based Approaches to Study Organelle Targeting Specificity of Nuclear-Encoded Plant Proteins. Frontiers in plant science, 91350. https://doi.org/10.3389/fpls.2018.01350
Sharma, Mayank, et al. "Dual or Not Dual?-Comparative Analysis of Fluorescence Microscopy-Based Approaches to Study Organelle Targeting Specificity of Nuclear-Encoded Plant Proteins." Frontiers in plant science vol. 9 (2018): 1350. doi: https://doi.org/10.3389/fpls.2018.01350
Sharma M, Bennewitz B, Klösgen RB. Dual or Not Dual?-Comparative Analysis of Fluorescence Microscopy-Based Approaches to Study Organelle Targeting Specificity of Nuclear-Encoded Plant Proteins. Front Plant Sci. 2018 Sep 19;9:1350. doi: 10.3389/fpls.2018.01350. eCollection 2018. PMID: 30298079; PMCID: PMC6160753.
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Computational studies on Begomoviral AC2/C2 proteins.

Bioinformation

Babu KSD, Manoharan P, Pandi G.
PMID: 30237675
Bioinformation. 2018 Jun 30;14(6):294-303. doi: 10.6026/97320630014294. eCollection 2018.

Geminiviridae is a large family of circular, single stranded DNA viruses, which infects and causes devastating diseases on economically important crops. They are subdivided into nine genera. Members of the genus begomovirus encode a pathogenic protein called AC2/C2 which...

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Babu KSD, Manoharan P, Pandi G. Computational studies on Begomoviral AC2/C2 proteins. Bioinformation. 2018;14(6):294-303doi: 10.6026/97320630014294.
Babu, K. S. D., Manoharan, P., & Pandi, G. (2018). Computational studies on Begomoviral AC2/C2 proteins. Bioinformation, 14(6), 294-303. https://doi.org/10.6026/97320630014294
Babu, Kanthalu Shagadevan Dinesh, et al. "Computational studies on Begomoviral AC2/C2 proteins." Bioinformation vol. 14,6 (2018): 294-303. doi: https://doi.org/10.6026/97320630014294
Babu KSD, Manoharan P, Pandi G. Computational studies on Begomoviral AC2/C2 proteins. Bioinformation. 2018 Jun 30;14(6):294-303. doi: 10.6026/97320630014294. eCollection 2018. PMID: 30237675; PMCID: PMC6137562.
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Foaming properties of acid-soluble protein-rich ingredient obtained from industrial rapeseed meal.

Journal of food science and technology

Ivanova P, Kalaydzhiev H, Dessev TT, Silva CLM, Rustad T, Chalova VI.
PMID: 30150839
J Food Sci Technol. 2018 Sep;55(9):3792-3798. doi: 10.1007/s13197-018-3311-y. Epub 2018 Aug 09.

The use of the rapeseed meal as a source for preparation of protein-rich ingredients for the food industry is an alternative to the current limited application as a feed additive. The aim of this study was to evaluate foaming...

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Ivanova P, Kalaydzhiev H, Dessev TT, et al. Foaming properties of acid-soluble protein-rich ingredient obtained from industrial rapeseed meal. J Food Sci Technol. 2018;55(9):3792-3798doi: 10.1007/s13197-018-3311-y.
Ivanova, P., Kalaydzhiev, H., Dessev, T. T., Silva, C. L. M., Rustad, T., & Chalova, V. I. (2018). Foaming properties of acid-soluble protein-rich ingredient obtained from industrial rapeseed meal. Journal of food science and technology, 55(9), 3792-3798. https://doi.org/10.1007/s13197-018-3311-y
Ivanova, Petya, et al. "Foaming properties of acid-soluble protein-rich ingredient obtained from industrial rapeseed meal." Journal of food science and technology vol. 55,9 (2018): 3792-3798. doi: https://doi.org/10.1007/s13197-018-3311-y
Ivanova P, Kalaydzhiev H, Dessev TT, Silva CLM, Rustad T, Chalova VI. Foaming properties of acid-soluble protein-rich ingredient obtained from industrial rapeseed meal. J Food Sci Technol. 2018 Sep;55(9):3792-3798. doi: 10.1007/s13197-018-3311-y. Epub 2018 Aug 09. PMID: 30150839; PMCID: PMC6098807.
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Cut intake of saturated fats to stave off coronary heart disease.

Nursing standard (Royal College of Nursing (Great Britain) : 1987)

[No authors listed]
PMID: 27977344
Nurs Stand. 2016 Dec 14;31(16):18. doi: 10.7748/ns.31.16-18.18.s19.

Replacing major saturated fatty acids with unsaturated fats, whole grain carbohydrates or plant proteins is an effective way to prevent coronary heart disease, say researchers.

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Cut intake of saturated fats to stave off coronary heart disease. Nurs Stand. 2016;31(16):18doi: 10.7748/ns.31.16-18.18.s19.
(2016). Cut intake of saturated fats to stave off coronary heart disease. Nursing standard (Royal College of Nursing (Great Britain) : 1987), 31(16), 18. https://doi.org/10.7748/ns.31.16-18.18.s19
"Cut intake of saturated fats to stave off coronary heart disease." Nursing standard (Royal College of Nursing (Great Britain) : 1987) vol. 31,16 (2016): 18. doi: https://doi.org/10.7748/ns.31.16-18.18.s19
Cut intake of saturated fats to stave off coronary heart disease. Nurs Stand. 2016 Dec 14;31(16):18. doi: 10.7748/ns.31.16-18.18.s19. PMID: 27977344.
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Showing 13 to 24 of 271 entries