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Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture.

Planta

Hei WG, Senger H.
PMID: 24241856
Planta. 1986 Feb;167(2):233-9. doi: 10.1007/BF00391420.

The phosphorylation of thylakoid proteins, which comprise apoproteins of the light-harvesting chlorophyll a/b-protein complex (LHCP), was investigated in vivo and in vitro during the development of Scenedesmus obliquus in synchronous cultures. The in-vitro and in-vivo protein phosphorylation exhibited a...

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Hei WG, Senger H. Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture. Planta. 1986;167(2):233-9doi: 10.1007/BF00391420.
Hei, W. G., & Senger, H. (1986). Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture. Planta, 167(2), 233-9. https://doi.org/10.1007/BF00391420
Hei, W G, and Senger, H. "Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture." Planta vol. 167,2 (1986): 233-9. doi: https://doi.org/10.1007/BF00391420
Hei WG, Senger H. Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture. Planta. 1986 Feb;167(2):233-9. doi: 10.1007/BF00391420. PMID: 24241856.
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Sequence of two genes in pea chloroplast DNA coding for 84 and 82 kD polypeptides of the photosystem I complex.

Plant molecular biology

Lehmbeck J, Rasmussen OF, Bookjans GB, Jepsen BR, Stummann BM, Henningsen KW.
PMID: 24302152
Plant Mol Biol. 1986 Jan;7(1):3-10. doi: 10.1007/BF00020126.

The genes encoding the two P700 chlorophyll a-apoproteins of the photosystem I complex were localized on the pea (Pisum sativum) chloroplast genome. The nucleotide sequence of the genes and the flanking regions has been determined. The genes are separated...

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Lehmbeck J, Rasmussen OF, Bookjans GB, et al. Sequence of two genes in pea chloroplast DNA coding for 84 and 82 kD polypeptides of the photosystem I complex. Plant Mol Biol. 1986;7(1):3-10doi: 10.1007/BF00020126.
Lehmbeck, J., Rasmussen, O. F., Bookjans, G. B., Jepsen, B. R., Stummann, B. M., & Henningsen, K. W. (1986). Sequence of two genes in pea chloroplast DNA coding for 84 and 82 kD polypeptides of the photosystem I complex. Plant molecular biology, 7(1), 3-10. https://doi.org/10.1007/BF00020126
Lehmbeck, J, et al. "Sequence of two genes in pea chloroplast DNA coding for 84 and 82 kD polypeptides of the photosystem I complex." Plant molecular biology vol. 7,1 (1986): 3-10. doi: https://doi.org/10.1007/BF00020126
Lehmbeck J, Rasmussen OF, Bookjans GB, Jepsen BR, Stummann BM, Henningsen KW. Sequence of two genes in pea chloroplast DNA coding for 84 and 82 kD polypeptides of the photosystem I complex. Plant Mol Biol. 1986 Jan;7(1):3-10. doi: 10.1007/BF00020126. PMID: 24302152.
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Translation and Co-translational Membrane Engagement of Plastid-encoded Chlorophyll-binding Proteins Are Not Influenced by Chlorophyll Availability in Maize.

Frontiers in plant science

Zoschke R, Chotewutmontri P, Barkan A.
PMID: 28400776
Front Plant Sci. 2017 Mar 28;8:385. doi: 10.3389/fpls.2017.00385. eCollection 2017.

Chlorophyll is an indispensable constituent of the photosynthetic machinery in green organisms. Bound by apoproteins of photosystems I and II, chlorophyll performs light-harvesting and charge separation. Due to the phototoxic nature of free chlorophyll and its precursors, chlorophyll synthesis...

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Zoschke R, Chotewutmontri P, Barkan A. Translation and Co-translational Membrane Engagement of Plastid-encoded Chlorophyll-binding Proteins Are Not Influenced by Chlorophyll Availability in Maize. Front Plant Sci. 2017;8:385doi: 10.3389/fpls.2017.00385.
Zoschke, R., Chotewutmontri, P., & Barkan, A. (2017). Translation and Co-translational Membrane Engagement of Plastid-encoded Chlorophyll-binding Proteins Are Not Influenced by Chlorophyll Availability in Maize. Frontiers in plant science, 8385. https://doi.org/10.3389/fpls.2017.00385
Zoschke, Reimo, et al. "Translation and Co-translational Membrane Engagement of Plastid-encoded Chlorophyll-binding Proteins Are Not Influenced by Chlorophyll Availability in Maize." Frontiers in plant science vol. 8 (2017): 385. doi: https://doi.org/10.3389/fpls.2017.00385
Zoschke R, Chotewutmontri P, Barkan A. Translation and Co-translational Membrane Engagement of Plastid-encoded Chlorophyll-binding Proteins Are Not Influenced by Chlorophyll Availability in Maize. Front Plant Sci. 2017 Mar 28;8:385. doi: 10.3389/fpls.2017.00385. eCollection 2017. PMID: 28400776; PMCID: PMC5368244.
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In vitro reconstitution of the photosystem I light-harvesting complex LHCI-730: heterodimerization is required for antenna pigment organization.

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

Schmid VH, Cammarata KV, Bruns BU, Schmidt GW.
PMID: 11038558
Proc Natl Acad Sci U S A. 1997 Jul 08;94(14):7667-72. doi: 10.1073/pnas.94.14.7667.

Here we describe the in vitro reconstitution of photosystem I light-harvesting complexes with pigments and proteins (Lhca1 and Lhca4) obtained by overexpression of tomato Lhca genes in Escherichia coli. Using Lhca1 and Lhca4 individually for reconstitution results in monomeric...

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Schmid VH, Cammarata KV, Bruns BU, et al. In vitro reconstitution of the photosystem I light-harvesting complex LHCI-730: heterodimerization is required for antenna pigment organization. Proc Natl Acad Sci U S A. 1997;94(14):7667-72doi: 10.1073/pnas.94.14.7667.
Schmid, V. H., Cammarata, K. V., Bruns, B. U., & Schmidt, G. W. (1997). In vitro reconstitution of the photosystem I light-harvesting complex LHCI-730: heterodimerization is required for antenna pigment organization. Proceedings of the National Academy of Sciences of the United States of America, 94(14), 7667-72. https://doi.org/10.1073/pnas.94.14.7667
Schmid, V H, et al. "In vitro reconstitution of the photosystem I light-harvesting complex LHCI-730: heterodimerization is required for antenna pigment organization." Proceedings of the National Academy of Sciences of the United States of America vol. 94,14 (1997): 7667-72. doi: https://doi.org/10.1073/pnas.94.14.7667
Schmid VH, Cammarata KV, Bruns BU, Schmidt GW. In vitro reconstitution of the photosystem I light-harvesting complex LHCI-730: heterodimerization is required for antenna pigment organization. Proc Natl Acad Sci U S A. 1997 Jul 08;94(14):7667-72. doi: 10.1073/pnas.94.14.7667. PMID: 11038558; PMCID: PMC23880.
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Stability of the Apoproteins of Light-Harvesting Complex I and II during Biogenesis of Thylakoids in the Chlorophyll b-less Barley Mutant Chlorina f2.

Plant physiology

Preiss S, Thornber JP.
PMID: 12228395
Plant Physiol. 1995 Mar;107(3):709-717. doi: 10.1104/pp.107.3.709.

Transcription and translation of Lhc (cab) genes have been compared in the chlorina f2 mutant of barley (Hordeum vulgare) and its wild type to study the effect of chlorophyll b's absence on the regulation of assembly of the light-harvesting...

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Preiss S, Thornber JP. Stability of the Apoproteins of Light-Harvesting Complex I and II during Biogenesis of Thylakoids in the Chlorophyll b-less Barley Mutant Chlorina f2. Plant Physiol. 1995;107(3):709-717doi: 10.1104/pp.107.3.709.
Preiss, S., & Thornber, J. P. (1995). Stability of the Apoproteins of Light-Harvesting Complex I and II during Biogenesis of Thylakoids in the Chlorophyll b-less Barley Mutant Chlorina f2. Plant physiology, 107(3), 709-717. https://doi.org/10.1104/pp.107.3.709
Preiss, S., and Thornber, J. P.. "Stability of the Apoproteins of Light-Harvesting Complex I and II during Biogenesis of Thylakoids in the Chlorophyll b-less Barley Mutant Chlorina f2." Plant physiology vol. 107,3 (1995): 709-717. doi: https://doi.org/10.1104/pp.107.3.709
Preiss S, Thornber JP. Stability of the Apoproteins of Light-Harvesting Complex I and II during Biogenesis of Thylakoids in the Chlorophyll b-less Barley Mutant Chlorina f2. Plant Physiol. 1995 Mar;107(3):709-717. doi: 10.1104/pp.107.3.709. PMID: 12228395; PMCID: PMC157186.
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Two Sweetclover (Melilotus alba Desr.) Mutants Temperature Sensitive for Chlorophyll Expression.

Plant physiology

Bevins MA, Madhavan S, Markwell J.
PMID: 12232006
Plant Physiol. 1993 Dec;103(4):1123-1131. doi: 10.1104/pp.103.4.1123.

The nonallelic sweetclover (Melilotus alba Desr.) mutants U371 (ch10/ch10 genotype) and U372 (ch11/ch11 genotype) are derived from the U389 (+/+ genotype) parental strain. Growth of the U389 strain at a temperature of 17 or 26[deg]C results in plants normally...

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Bevins MA, Madhavan S, Markwell J. Two Sweetclover (Melilotus alba Desr.) Mutants Temperature Sensitive for Chlorophyll Expression. Plant Physiol. 1993;103(4):1123-1131doi: 10.1104/pp.103.4.1123.
Bevins, M. A., Madhavan, S., & Markwell, J. (1993). Two Sweetclover (Melilotus alba Desr.) Mutants Temperature Sensitive for Chlorophyll Expression. Plant physiology, 103(4), 1123-1131. https://doi.org/10.1104/pp.103.4.1123
Bevins, M. A., et al. "Two Sweetclover (Melilotus alba Desr.) Mutants Temperature Sensitive for Chlorophyll Expression." Plant physiology vol. 103,4 (1993): 1123-1131. doi: https://doi.org/10.1104/pp.103.4.1123
Bevins MA, Madhavan S, Markwell J. Two Sweetclover (Melilotus alba Desr.) Mutants Temperature Sensitive for Chlorophyll Expression. Plant Physiol. 1993 Dec;103(4):1123-1131. doi: 10.1104/pp.103.4.1123. PMID: 12232006; PMCID: PMC159097.
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Cooperation of cytoplasmic and plastidial translation in formation of the photosynthetic apparatus and its stage-specific efficiency.

Plant physiology

Brandt P, von Kessel B.
PMID: 16663055
Plant Physiol. 1983 Jul;72(3):616-9. doi: 10.1104/pp.72.3.616.

In synchronized Euglena gracilis, strain Z, the synthesis of the apoproteins for the chlorophyll-protein-complexes CPI, CPa, and LHCP is light-dependent and takes place in the light period in a characteristic consecutive fashion: CPI at 1 to 2 hours, CPa...

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Brandt P, von Kessel B. Cooperation of cytoplasmic and plastidial translation in formation of the photosynthetic apparatus and its stage-specific efficiency. Plant Physiol. 1983;72(3):616-9doi: 10.1104/pp.72.3.616.
Brandt, P., & von Kessel, B. (1983). Cooperation of cytoplasmic and plastidial translation in formation of the photosynthetic apparatus and its stage-specific efficiency. Plant physiology, 72(3), 616-9. https://doi.org/10.1104/pp.72.3.616
Brandt, P, and von Kessel, B. "Cooperation of cytoplasmic and plastidial translation in formation of the photosynthetic apparatus and its stage-specific efficiency." Plant physiology vol. 72,3 (1983): 616-9. doi: https://doi.org/10.1104/pp.72.3.616
Brandt P, von Kessel B. Cooperation of cytoplasmic and plastidial translation in formation of the photosynthetic apparatus and its stage-specific efficiency. Plant Physiol. 1983 Jul;72(3):616-9. doi: 10.1104/pp.72.3.616. PMID: 16663055; PMCID: PMC1066290.
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Light-Dependent Accumulation of Radiolabeled Plastid-Encoded Chlorophyll a-Apoproteins Requires Chlorophyll a: I. Analysis of Chlorophyll-Deficient Mutants and Phytochrome Involvement.

Plant physiology

Klein RR, Gamble PE, Mullet JE.
PMID: 16666451
Plant Physiol. 1988 Dec;88(4):1246-56. doi: 10.1104/pp.88.4.1246.

The accumulation of radiolabeled plastid-encoded chlorophyll a-apoproteins is light dependent and is controlled at a posttranscriptional level. Illumination of dark-grown barley (Hordeum vulgare L.) with a brief pulse of red light induced the accumulation of radiolabeled chlorophyll a-apoproteins in...

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Klein RR, Gamble PE, Mullet JE. Light-Dependent Accumulation of Radiolabeled Plastid-Encoded Chlorophyll a-Apoproteins Requires Chlorophyll a: I. Analysis of Chlorophyll-Deficient Mutants and Phytochrome Involvement. Plant Physiol. 1988;88(4):1246-56doi: 10.1104/pp.88.4.1246.
Klein, R. R., Gamble, P. E., & Mullet, J. E. (1988). Light-Dependent Accumulation of Radiolabeled Plastid-Encoded Chlorophyll a-Apoproteins Requires Chlorophyll a: I. Analysis of Chlorophyll-Deficient Mutants and Phytochrome Involvement. Plant physiology, 88(4), 1246-56. https://doi.org/10.1104/pp.88.4.1246
Klein, R R, et al. "Light-Dependent Accumulation of Radiolabeled Plastid-Encoded Chlorophyll a-Apoproteins Requires Chlorophyll a: I. Analysis of Chlorophyll-Deficient Mutants and Phytochrome Involvement." Plant physiology vol. 88,4 (1988): 1246-56. doi: https://doi.org/10.1104/pp.88.4.1246
Klein RR, Gamble PE, Mullet JE. Light-Dependent Accumulation of Radiolabeled Plastid-Encoded Chlorophyll a-Apoproteins Requires Chlorophyll a: I. Analysis of Chlorophyll-Deficient Mutants and Phytochrome Involvement. Plant Physiol. 1988 Dec;88(4):1246-56. doi: 10.1104/pp.88.4.1246. PMID: 16666451; PMCID: PMC1055749.
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Effects of rice policosanol on serum lipoproteins, homocysteine, fibrinogen and C-reactive protein in hypercholesterolaemic patients.

Clinical drug investigation

Reiner Z, Tedeschi-Reiner E, Romić Z.
PMID: 17532716
Clin Drug Investig. 2005;25(11):701-7. doi: 10.2165/00044011-200525110-00003.

BACKGROUND: Policosanol is an agent that includes mixtures of aliphatic primary alcohols extracted primarily from sugar-cane wax. This mixture has been shown to lower total and low-density lipoprotein (LDL) cholesterol in animal models, healthy volunteers and hypercholesterolaemic patients.PATIENTS AND...

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Reiner Z, Tedeschi-Reiner E, Romić Z. Effects of rice policosanol on serum lipoproteins, homocysteine, fibrinogen and C-reactive protein in hypercholesterolaemic patients. Clin Drug Investig. 2005;25(11):701-7doi: 10.2165/00044011-200525110-00003.
Reiner, Z., Tedeschi-Reiner, E., & Romić, Z. (2005). Effects of rice policosanol on serum lipoproteins, homocysteine, fibrinogen and C-reactive protein in hypercholesterolaemic patients. Clinical drug investigation, 25(11), 701-7. https://doi.org/10.2165/00044011-200525110-00003
Reiner, Zeljko, et al. "Effects of rice policosanol on serum lipoproteins, homocysteine, fibrinogen and C-reactive protein in hypercholesterolaemic patients." Clinical drug investigation vol. 25,11 (2005): 701-7. doi: https://doi.org/10.2165/00044011-200525110-00003
Reiner Z, Tedeschi-Reiner E, Romić Z. Effects of rice policosanol on serum lipoproteins, homocysteine, fibrinogen and C-reactive protein in hypercholesterolaemic patients. Clin Drug Investig. 2005;25(11):701-7. doi: 10.2165/00044011-200525110-00003. PMID: 17532716.
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Human Lp(a): regions in sequences of apoproteins similar to domains in signal transduction proteins.

Endocrine practice : official journal of the American College of Endocrinology and the American Association of Clinical Endocrinologists

Guevara J, Valentinova NV, Davison D, Morrisett JD, Sparrow JT.
PMID: 15251573
Endocr Pract. 1995 Nov-Dec;1(6):440-8. doi: 10.4158/EP.1.6.440.

The major apoproteins of Lp(a)--apo(a) and apo B-100--are linked by only one intermolecular disulfide bond. This linkage has been suggested to be located between apo(a) Cys4057 and apo B-100 Cys3734. Several studies, however, have suggested other noncovalent interactions between...

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Guevara J, Valentinova NV, Davison D, et al. Human Lp(a): regions in sequences of apoproteins similar to domains in signal transduction proteins. Endocr Pract. 1995;1(6):440-8doi: 10.4158/EP.1.6.440.
Guevara, J., Valentinova, N. V., Davison, D., Morrisett, J. D., & Sparrow, J. T. (1995). Human Lp(a): regions in sequences of apoproteins similar to domains in signal transduction proteins. Endocrine practice : official journal of the American College of Endocrinology and the American Association of Clinical Endocrinologists, 1(6), 440-8. https://doi.org/10.4158/EP.1.6.440
Guevara, J, et al. "Human Lp(a): regions in sequences of apoproteins similar to domains in signal transduction proteins." Endocrine practice : official journal of the American College of Endocrinology and the American Association of Clinical Endocrinologists vol. 1,6 (1995): 440-8. doi: https://doi.org/10.4158/EP.1.6.440
Guevara J, Valentinova NV, Davison D, Morrisett JD, Sparrow JT. Human Lp(a): regions in sequences of apoproteins similar to domains in signal transduction proteins. Endocr Pract. 1995 Nov-Dec;1(6):440-8. doi: 10.4158/EP.1.6.440. PMID: 15251573.
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Nitrogen-dependent regulation of photosynthetic gene expression.

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

Plumley FG, Schmidt GW.
PMID: 16594026
Proc Natl Acad Sci U S A. 1989 Apr;86(8):2678-82. doi: 10.1073/pnas.86.8.2678.

Nitrogen-limited Chlamydomonas reinhardtii is chlorotic and very deficient in chlorophyll a/b light-harvesting complexes (LHC). Rates of synthesis of photosynthetic proteins, but especially the LHC apoproteins, are reduced 10- to 40-fold. Moderately high levels of chloroplast transcripts accumulate in nitrogen-limited...

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Plumley FG, Schmidt GW. Nitrogen-dependent regulation of photosynthetic gene expression. Proc Natl Acad Sci U S A. 1989;86(8):2678-82doi: 10.1073/pnas.86.8.2678.
Plumley, F. G., & Schmidt, G. W. (1989). Nitrogen-dependent regulation of photosynthetic gene expression. Proceedings of the National Academy of Sciences of the United States of America, 86(8), 2678-82. https://doi.org/10.1073/pnas.86.8.2678
Plumley, F G, and Schmidt, G W. "Nitrogen-dependent regulation of photosynthetic gene expression." Proceedings of the National Academy of Sciences of the United States of America vol. 86,8 (1989): 2678-82. doi: https://doi.org/10.1073/pnas.86.8.2678
Plumley FG, Schmidt GW. Nitrogen-dependent regulation of photosynthetic gene expression. Proc Natl Acad Sci U S A. 1989 Apr;86(8):2678-82. doi: 10.1073/pnas.86.8.2678. PMID: 16594026; PMCID: PMC286981.
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Effect of periportal- and centrilobular-equivalent oxygen tension on liver specific functions in long-term rat hepatocyte cultures.

Toxicology in vitro : an international journal published in association with BIBRA

Maier P, Saad B, Schawalder HP.
PMID: 20692934
Toxicol In Vitro. 1994 Jun;8(3):423-35. doi: 10.1016/0887-2333(94)90164-3.

The influence of periportal- and centrilobular-equivalent oxygen tensions on cellular functions and xenobiotic metabolism was investigated in rat hepatocytes cultured under 20% (air/CO(2)), 13% or 4% O(2) for up to 9 days on teflon membrane dishes, coated with crude...

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Maier P, Saad B, Schawalder HP. Effect of periportal- and centrilobular-equivalent oxygen tension on liver specific functions in long-term rat hepatocyte cultures. Toxicol In Vitro. 1994;8(3):423-35doi: 10.1016/0887-2333(94)90164-3.
Maier, P., Saad, B., & Schawalder, H. P. (1994). Effect of periportal- and centrilobular-equivalent oxygen tension on liver specific functions in long-term rat hepatocyte cultures. Toxicology in vitro : an international journal published in association with BIBRA, 8(3), 423-35. https://doi.org/10.1016/0887-2333(94)90164-3
Maier, P, et al. "Effect of periportal- and centrilobular-equivalent oxygen tension on liver specific functions in long-term rat hepatocyte cultures." Toxicology in vitro : an international journal published in association with BIBRA vol. 8,3 (1994): 423-35. doi: https://doi.org/10.1016/0887-2333(94)90164-3
Maier P, Saad B, Schawalder HP. Effect of periportal- and centrilobular-equivalent oxygen tension on liver specific functions in long-term rat hepatocyte cultures. Toxicol In Vitro. 1994 Jun;8(3):423-35. doi: 10.1016/0887-2333(94)90164-3. PMID: 20692934.
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Showing 1 to 12 of 88 entries