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Alteration in catalytic properties of human CYP2D6 caused by substitution of glycine-42 with arginine, lysine and glutamic acid.

Drug metabolism and pharmacokinetics

Tsuzuki D, Hichiya H, Okuda Y, Yamamoto S, Tamagake K, Shinoda S, Narimatsu S.
PMID: 15618721
Drug Metab Pharmacokinet. 2003;18(1):79-85. doi: 10.2133/dmpk.18.79.

The effects of the substitution of glycine at position 42 with various other amino acid residues on the functions of CYP2D6 were studied using debrisoquine (DB) and bunitrolol (BTL) 4-hydroxylations as indices of drug-metabolizing enzymes. The substitution with hydrophobic...

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Tsuzuki D, Hichiya H, Okuda Y, et al. Alteration in catalytic properties of human CYP2D6 caused by substitution of glycine-42 with arginine, lysine and glutamic acid. Drug Metab Pharmacokinet. 2003;18(1):79-85doi: 10.2133/dmpk.18.79.
Tsuzuki, D., Hichiya, H., Okuda, Y., Yamamoto, S., Tamagake, K., Shinoda, S., & Narimatsu, S. (2003). Alteration in catalytic properties of human CYP2D6 caused by substitution of glycine-42 with arginine, lysine and glutamic acid. Drug metabolism and pharmacokinetics, 18(1), 79-85. https://doi.org/10.2133/dmpk.18.79
Tsuzuki, Daisuke, et al. "Alteration in catalytic properties of human CYP2D6 caused by substitution of glycine-42 with arginine, lysine and glutamic acid." Drug metabolism and pharmacokinetics vol. 18,1 (2003): 79-85. doi: https://doi.org/10.2133/dmpk.18.79
Tsuzuki D, Hichiya H, Okuda Y, Yamamoto S, Tamagake K, Shinoda S, Narimatsu S. Alteration in catalytic properties of human CYP2D6 caused by substitution of glycine-42 with arginine, lysine and glutamic acid. Drug Metab Pharmacokinet. 2003;18(1):79-85. doi: 10.2133/dmpk.18.79. PMID: 15618721.
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Mutants of Sweetclover (Melilotus alba) Lacking Chlorophyll b: Studies on Pigment-Protein Complexes and Thylakoid Protein Phosphorylation.

Plant physiology

Markwell JP, Webber AN, Lake B.
PMID: 16664169
Plant Physiol. 1985 Apr;77(4):948-51. doi: 10.1104/pp.77.4.948.

Mutants of sweetclover (Melilotus alba) with defects in the nuclear ch5 locus were examined. Using thin-layer chromatography and absorption spectroscopy, three of these mutants were found to lack chlorophyll (Chl) b. One of these three mutants, U374, possessed thylakoid...

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Markwell JP, Webber AN, Lake B. Mutants of Sweetclover (Melilotus alba) Lacking Chlorophyll b: Studies on Pigment-Protein Complexes and Thylakoid Protein Phosphorylation. Plant Physiol. 1985;77(4):948-51doi: 10.1104/pp.77.4.948.
Markwell, J. P., Webber, A. N., & Lake, B. (1985). Mutants of Sweetclover (Melilotus alba) Lacking Chlorophyll b: Studies on Pigment-Protein Complexes and Thylakoid Protein Phosphorylation. Plant physiology, 77(4), 948-51. https://doi.org/10.1104/pp.77.4.948
Markwell, J P, et al. "Mutants of Sweetclover (Melilotus alba) Lacking Chlorophyll b: Studies on Pigment-Protein Complexes and Thylakoid Protein Phosphorylation." Plant physiology vol. 77,4 (1985): 948-51. doi: https://doi.org/10.1104/pp.77.4.948
Markwell JP, Webber AN, Lake B. Mutants of Sweetclover (Melilotus alba) Lacking Chlorophyll b: Studies on Pigment-Protein Complexes and Thylakoid Protein Phosphorylation. Plant Physiol. 1985 Apr;77(4):948-51. doi: 10.1104/pp.77.4.948. PMID: 16664169; PMCID: PMC1064638.
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Chemical Cross-linking of Neighboring Thylakoid Membrane Polypeptides.

Plant physiology

Novak-Hofer I, Siegenthaler PA.
PMID: 16660519
Plant Physiol. 1978 Sep;62(3):368-72. doi: 10.1104/pp.62.3.368.

Cross-linking between protein components of whole spinach (Spinacia oleracea var. Nobel) thylakoids and of photosystem I- and II-enriched thylakoid fractions has been produced by reaction with the bifunctional imidoester dimethyl-3,3'-dithiobispropionimidate dihydrochloride as well as by the oxidation of intrinsic...

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Novak-Hofer I, Siegenthaler PA. Chemical Cross-linking of Neighboring Thylakoid Membrane Polypeptides. Plant Physiol. 1978;62(3):368-72doi: 10.1104/pp.62.3.368.
Novak-Hofer, I., & Siegenthaler, P. A. (1978). Chemical Cross-linking of Neighboring Thylakoid Membrane Polypeptides. Plant physiology, 62(3), 368-72. https://doi.org/10.1104/pp.62.3.368
Novak-Hofer, I, and Siegenthaler, P A. "Chemical Cross-linking of Neighboring Thylakoid Membrane Polypeptides." Plant physiology vol. 62,3 (1978): 368-72. doi: https://doi.org/10.1104/pp.62.3.368
Novak-Hofer I, Siegenthaler PA. Chemical Cross-linking of Neighboring Thylakoid Membrane Polypeptides. Plant Physiol. 1978 Sep;62(3):368-72. doi: 10.1104/pp.62.3.368. PMID: 16660519; PMCID: PMC1092128.
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Protein domains required for formation of stable monomeric Lhca1- and Lhca4-complexes.

Photosynthesis research

Rupprecht J, Paulsen H, Schmid VH.
PMID: 16228432
Photosynth Res. 2000;63(3):217-24. doi: 10.1023/A:1006499517613.

The peripheral light-harvesting complex of Photosystem I consists of two subpopulations, LHCI-680 and LHCI-730. The latter is composed of the two apoproteins Lhca1 and Lhca4. Recently, reconstitution of monomeric LHCI using bacterially overexpressed Lhca1 or Lhca4 was achieved. In...

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Rupprecht J, Paulsen H, Schmid VH. Protein domains required for formation of stable monomeric Lhca1- and Lhca4-complexes. Photosynth Res. 2000;63(3):217-24doi: 10.1023/A:1006499517613.
Rupprecht, J., Paulsen, H., & Schmid, V. H. (2000). Protein domains required for formation of stable monomeric Lhca1- and Lhca4-complexes. Photosynthesis research, 63(3), 217-24. https://doi.org/10.1023/A:1006499517613
Rupprecht, J, et al. "Protein domains required for formation of stable monomeric Lhca1- and Lhca4-complexes." Photosynthesis research vol. 63,3 (2000): 217-24. doi: https://doi.org/10.1023/A:1006499517613
Rupprecht J, Paulsen H, Schmid VH. Protein domains required for formation of stable monomeric Lhca1- and Lhca4-complexes. Photosynth Res. 2000;63(3):217-24. doi: 10.1023/A:1006499517613. PMID: 16228432.
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Antisense inhibition of the beta-carotene hydroxylase enzyme in Arabidopsis and the implications for carotenoid accumulation, photoprotection and antenna assembly.

Photosynthesis research

Rissler HM, Pogson BJ.
PMID: 16228322
Photosynth Res. 2001;67(1):127-37. doi: 10.1023/A:1010669404183.

The xanthophylls are oxygenated carotenoids and are important structural components of the photosynthetic apparatus. Xanthophylls contribute to the assembly and stability of light-harvesting complex apoproteins (LHC) and contribute to photoprotection via non-photochemical quenching of chlorophyll fluorescence (NPQ) in oxygenic...

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Rissler HM, Pogson BJ. Antisense inhibition of the beta-carotene hydroxylase enzyme in Arabidopsis and the implications for carotenoid accumulation, photoprotection and antenna assembly. Photosynth Res. 2001;67(1):127-37doi: 10.1023/A:1010669404183.
Rissler, H. M., & Pogson, B. J. (2001). Antisense inhibition of the beta-carotene hydroxylase enzyme in Arabidopsis and the implications for carotenoid accumulation, photoprotection and antenna assembly. Photosynthesis research, 67(1), 127-37. https://doi.org/10.1023/A:1010669404183
Rissler, H M, and Pogson, B J. "Antisense inhibition of the beta-carotene hydroxylase enzyme in Arabidopsis and the implications for carotenoid accumulation, photoprotection and antenna assembly." Photosynthesis research vol. 67,1 (2001): 127-37. doi: https://doi.org/10.1023/A:1010669404183
Rissler HM, Pogson BJ. Antisense inhibition of the beta-carotene hydroxylase enzyme in Arabidopsis and the implications for carotenoid accumulation, photoprotection and antenna assembly. Photosynth Res. 2001;67(1):127-37. doi: 10.1023/A:1010669404183. PMID: 16228322.
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Transcription of three sets of genes coding for the core light-harvesting proteins in the purple sulfur bacterium, Allochromatium vinosum.

Photosynthesis research

Nagashima S, Shimada K, Matsuura K, Nagashima KV.
PMID: 16245138
Photosynth Res. 2002;74(3):269-80. doi: 10.1023/A:1021280104053.

The nucleotide sequence of the puf operon coding for the subunits of the photosynthetic reaction center and the core light-harvesting complex (LH1) of the purple sulfur bacterium, Allochromatium (A.) vinosum (formally Chromatium vinosum), was completely determined. Unlike other known...

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Nagashima S, Shimada K, Matsuura K, et al. Transcription of three sets of genes coding for the core light-harvesting proteins in the purple sulfur bacterium, Allochromatium vinosum. Photosynth Res. 2002;74(3):269-80doi: 10.1023/A:1021280104053.
Nagashima, S., Shimada, K., Matsuura, K., & Nagashima, K. V. (2002). Transcription of three sets of genes coding for the core light-harvesting proteins in the purple sulfur bacterium, Allochromatium vinosum. Photosynthesis research, 74(3), 269-80. https://doi.org/10.1023/A:1021280104053
Nagashima, Sakiko, et al. "Transcription of three sets of genes coding for the core light-harvesting proteins in the purple sulfur bacterium, Allochromatium vinosum." Photosynthesis research vol. 74,3 (2002): 269-80. doi: https://doi.org/10.1023/A:1021280104053
Nagashima S, Shimada K, Matsuura K, Nagashima KV. Transcription of three sets of genes coding for the core light-harvesting proteins in the purple sulfur bacterium, Allochromatium vinosum. Photosynth Res. 2002;74(3):269-80. doi: 10.1023/A:1021280104053. PMID: 16245138.
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Species-related differences in the electrophoretic behavior of CP 29 and CP 26: An immunochemical analysis.

Photosynthesis research

Falbel TG, Staehelin LA.
PMID: 24408776
Photosynth Res. 1992 Nov;34(2):249-62. doi: 10.1007/BF00033442.

The monomeric chlorophyll-protein complexes, CP 29 and CP 26 seen in the Camm and Green (1980) and Dunahay and Staehelin (1986) green gels do not always migrate in the order of the apparent molecular weight of their apoproteins as...

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Falbel TG, Staehelin LA. Species-related differences in the electrophoretic behavior of CP 29 and CP 26: An immunochemical analysis. Photosynth Res. 1992;34(2):249-62doi: 10.1007/BF00033442.
Falbel, T. G., & Staehelin, L. A. (1992). Species-related differences in the electrophoretic behavior of CP 29 and CP 26: An immunochemical analysis. Photosynthesis research, 34(2), 249-62. https://doi.org/10.1007/BF00033442
Falbel, T G, and Staehelin, L A. "Species-related differences in the electrophoretic behavior of CP 29 and CP 26: An immunochemical analysis." Photosynthesis research vol. 34,2 (1992): 249-62. doi: https://doi.org/10.1007/BF00033442
Falbel TG, Staehelin LA. Species-related differences in the electrophoretic behavior of CP 29 and CP 26: An immunochemical analysis. Photosynth Res. 1992 Nov;34(2):249-62. doi: 10.1007/BF00033442. PMID: 24408776.
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The localization of genes for ribosomal, cytochrome b6/f complex and photosystems I and II polypeptides on the chloroplast chromosome of Vicia faba.

Plant molecular biology

Ko K, Straus NA.
PMID: 24302308
Plant Mol Biol. 1986 May;7(3):219-28. doi: 10.1007/BF00021334.

Detailed studies of rearranged chloroplast genomes such as Vicia faba should give insights into the constraints governing the positional organization of the various gene clusters on the chloroplast chromosome. Seven polypeptide genes have already been mapped on the Vicia...

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Ko K, Straus NA. The localization of genes for ribosomal, cytochrome b6/f complex and photosystems I and II polypeptides on the chloroplast chromosome of Vicia faba. Plant Mol Biol. 1986;7(3):219-28doi: 10.1007/BF00021334.
Ko, K., & Straus, N. A. (1986). The localization of genes for ribosomal, cytochrome b6/f complex and photosystems I and II polypeptides on the chloroplast chromosome of Vicia faba. Plant molecular biology, 7(3), 219-28. https://doi.org/10.1007/BF00021334
Ko, K, and Straus, N A. "The localization of genes for ribosomal, cytochrome b6/f complex and photosystems I and II polypeptides on the chloroplast chromosome of Vicia faba." Plant molecular biology vol. 7,3 (1986): 219-28. doi: https://doi.org/10.1007/BF00021334
Ko K, Straus NA. The localization of genes for ribosomal, cytochrome b6/f complex and photosystems I and II polypeptides on the chloroplast chromosome of Vicia faba. Plant Mol Biol. 1986 May;7(3):219-28. doi: 10.1007/BF00021334. PMID: 24302308.
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Synthesis and turnover of the light-harvesting chlorophylla/b-protein inLemna gibba grown with intermittent red light: possible translational control.

Planta

Slovin JP, Tobin EM.
PMID: 24276276
Planta. 1982 Sep;154(5):465-72. doi: 10.1007/BF01267815.

Lemna gibba L. G-3 plants grown heterotrophically in the dark with intermittent red light (2 min every 8 h) contain a substantial amount of translatable mRNA encoding the light-harvesting chlorophyll (Chl)a/b-protein. However, very little [(35)S]methionine is incorporated into the...

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Slovin JP, Tobin EM. Synthesis and turnover of the light-harvesting chlorophylla/b-protein inLemna gibba grown with intermittent red light: possible translational control. Planta. 1982;154(5):465-72doi: 10.1007/BF01267815.
Slovin, J. P., & Tobin, E. M. (1982). Synthesis and turnover of the light-harvesting chlorophylla/b-protein inLemna gibba grown with intermittent red light: possible translational control. Planta, 154(5), 465-72. https://doi.org/10.1007/BF01267815
Slovin, J P, and Tobin, E M. "Synthesis and turnover of the light-harvesting chlorophylla/b-protein inLemna gibba grown with intermittent red light: possible translational control." Planta vol. 154,5 (1982): 465-72. doi: https://doi.org/10.1007/BF01267815
Slovin JP, Tobin EM. Synthesis and turnover of the light-harvesting chlorophylla/b-protein inLemna gibba grown with intermittent red light: possible translational control. Planta. 1982 Sep;154(5):465-72. doi: 10.1007/BF01267815. PMID: 24276276.
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Molecular cloning and nucleotide sequence of the psaA and psaB genes of the cyanobacterium Synechococcus sp. PCC 7002.

Plant molecular biology

Cantrell A, Bryant DA.
PMID: 24277132
Plant Mol Biol. 1987 Sep;9(5):453-68. doi: 10.1007/BF00015877.

The psaA and psaB genes, which encode the P700 chlorophyll a apoproteins of the Photosystem I complex, have been cloned from the unicellular, transformable cyanobacterium Synechococcus sp. PCC 7002. The nucleotide sequence of these genes and of their flanking...

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Cantrell A, Bryant DA. Molecular cloning and nucleotide sequence of the psaA and psaB genes of the cyanobacterium Synechococcus sp. PCC 7002. Plant Mol Biol. 1987;9(5):453-68doi: 10.1007/BF00015877.
Cantrell, A., & Bryant, D. A. (1987). Molecular cloning and nucleotide sequence of the psaA and psaB genes of the cyanobacterium Synechococcus sp. PCC 7002. Plant molecular biology, 9(5), 453-68. https://doi.org/10.1007/BF00015877
Cantrell, A, and Bryant, D A. "Molecular cloning and nucleotide sequence of the psaA and psaB genes of the cyanobacterium Synechococcus sp. PCC 7002." Plant molecular biology vol. 9,5 (1987): 453-68. doi: https://doi.org/10.1007/BF00015877
Cantrell A, Bryant DA. Molecular cloning and nucleotide sequence of the psaA and psaB genes of the cyanobacterium Synechococcus sp. PCC 7002. Plant Mol Biol. 1987 Sep;9(5):453-68. doi: 10.1007/BF00015877. PMID: 24277132.
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Nucleotide sequence of the clustered genes for the 44 kd chlorophyll a apoprotein and the "32 kd"-like protein of the photosystem II reaction center in the spinach plastid chromosome.

Current genetics

Alt J, Morris J, Westhoff P, Herrmann RG.
PMID: 24177999
Curr Genet. 1984 Oct;8(8):597-606. doi: 10.1007/BF00395705.

A 2,900 base pair DNA segment of the spinach plastid chromosome which encodes the genes for the 44 kd chlorophyll a apoprotein and a "32 kd"-like protein of the photosystem II reaction center has been subjected to sequence and...

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Alt J, Morris J, Westhoff P, et al. Nucleotide sequence of the clustered genes for the 44 kd chlorophyll a apoprotein and the "32 kd"-like protein of the photosystem II reaction center in the spinach plastid chromosome. Curr Genet. 1984;8(8):597-606doi: 10.1007/BF00395705.
Alt, J., Morris, J., Westhoff, P., & Herrmann, R. G. (1984). Nucleotide sequence of the clustered genes for the 44 kd chlorophyll a apoprotein and the "32 kd"-like protein of the photosystem II reaction center in the spinach plastid chromosome. Current genetics, 8(8), 597-606. https://doi.org/10.1007/BF00395705
Alt, J, et al. "Nucleotide sequence of the clustered genes for the 44 kd chlorophyll a apoprotein and the "32 kd"-like protein of the photosystem II reaction center in the spinach plastid chromosome." Current genetics vol. 8,8 (1984): 597-606. doi: https://doi.org/10.1007/BF00395705
Alt J, Morris J, Westhoff P, Herrmann RG. Nucleotide sequence of the clustered genes for the 44 kd chlorophyll a apoprotein and the "32 kd"-like protein of the photosystem II reaction center in the spinach plastid chromosome. Curr Genet. 1984 Oct;8(8):597-606. doi: 10.1007/BF00395705. PMID: 24177999.
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N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization.

Nature communications

Freibert SA, Boniecki MT, Stümpfig C, Schulz V, Krapoth N, Winge DR, Mühlenhoff U, Stehling O, Cygler M, Lill R.
PMID: 34824239
Nat Commun. 2021 Nov 25;12(1):6902. doi: 10.1038/s41467-021-27122-w.

Synthesis of iron-sulfur (Fe/S) clusters in living cells requires scaffold proteins for both facile synthesis and subsequent transfer of clusters to target apoproteins. The human mitochondrial ISCU2 scaffold protein is part of the core ISC (iron-sulfur cluster assembly) complex...

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Freibert SA, Boniecki MT, Stümpfig C, et al. N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization. Nat Commun. 2021;12(1):6902doi: 10.1038/s41467-021-27122-w.
Freibert, S. A., Boniecki, M. T., Stümpfig, C., Schulz, V., Krapoth, N., Winge, D. R., Mühlenhoff, U., Stehling, O., Cygler, M., & Lill, R. (2021). N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization. Nature communications, 12(1), 6902. https://doi.org/10.1038/s41467-021-27122-w
Freibert, Sven-A, et al. "N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization." Nature communications vol. 12,1 (2021): 6902. doi: https://doi.org/10.1038/s41467-021-27122-w
Freibert SA, Boniecki MT, Stümpfig C, Schulz V, Krapoth N, Winge DR, Mühlenhoff U, Stehling O, Cygler M, Lill R. N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization. Nat Commun. 2021 Nov 25;12(1):6902. doi: 10.1038/s41467-021-27122-w. PMID: 34824239; PMCID: PMC8617193.
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Showing 25 to 36 of 88 entries