Academic literature on the topic 'Molecular cloning; Mutagenesis; 4-HPPD'

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Journal articles on the topic "Molecular cloning; Mutagenesis; 4-HPPD"

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Stirdivant, Steven M., Janet Ahern, Robert R. Conroy, Stanley F. Barnett, Lynette M. Ledder, Allen Oliff, and David C. Heimbrook. "Cloning and mutagenesis of the p110α subunit of human phosphoinositide 3′-hydroxykinase." Bioorganic & Medicinal Chemistry 5, no. 1 (January 1997): 65–74. http://dx.doi.org/10.1016/s0968-0896(96)00196-4.

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FAVALORO, Bartolo, Antonio TAMBURRO, Stefania ANGELUCCI, Antonella DE LUCA, Sonia MELINO, Carmine DI ILIO, and Domenico ROTILIO. "Molecular cloning, expression and site-directed mutagenesis of glutathione S-transferase from Ochrobactrum anthropi." Biochemical Journal 335, no. 3 (November 1, 1998): 573–79. http://dx.doi.org/10.1042/bj3350573.

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The gene coding for a novel glutathione S-transferase (GST) has been isolated from the bacterium Ochrobactrum anthropi. A PCR fragment of 230 bp was obtained using oligonucleotide primers deduced from N-terminal and ‘internal ’ sequences of the purified enzyme. The gene was obtained by screening of a genomic DNA partial library from O. anthropi constructed in pBluescript with a PCR fragment probe. The gene encodes a protein (OaGST) of 201 amino acids with a calculated molecular mass of 21738 Da. The product of the gene was expressed and characterized; it showed GST activity with substrates 1-chloro-2,4-dinitrobenzene (CDNB), p-nitrobenzyl chloride and 4-nitroquinoline 1-oxide, and glutathione-dependent peroxidase activity towards cumene hydroperoxide. The overexpressed product of the gene was also confirmed to have in vivo GST activity towards CDNB. The interaction of the recombinant GST with several antibiotics indicated that the enzyme is involved in the binding of rifamycin and tetracycline. The OaGST amino acid sequence showed the greatest identity (45%) with a GST from Pseudomonas sp. strain LB400. A serine residue in the N-terminal region is conserved in almost all known bacterial GSTs, and it appears to be the counterpart of the catalytic serine residue present in Theta-class GSTs. Substitution of the Ser-11 residue resulted in a mutant OaGST protein lacking CDNB-conjugating activity; moreover the mutant enzyme was not able to bind Sepharose–GSH affinity matrices. The amino acid and nucleotide sequences reported in this paper have been submitted to the EMBL Data Bank with the accession number Y17279.
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Garfinkel, D. J., M. F. Mastrangelo, N. J. Sanders, B. K. Shafer, and J. N. Strathern. "Transposon tagging using Ty elements in yeast." Genetics 120, no. 1 (September 1, 1988): 95–108. http://dx.doi.org/10.1093/genetics/120.1.95.

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Abstract We have used the ability to induce high levels of Ty transposition to develop a method for transposon mutagenesis in Saccharomyces cerevisiae. To facilitate genetic and molecular analysis, we have constructed GAL1-promoted TyH3 or Ty917 elements that contain unique cloning sites, and marked these elements with selectable genes. These genes include the yeast HIS3 gene, and the plasmid PiAN7 containing the Tn903 NEO gene. The marked Ty elements retain their ability to transpose, to mutate the LYS2, LYS5, or STE2 genes, and to activate the promoterless his3 delta 4 target gene. Ty elements containing selectable genes are also useful in strain construction, in chromosomal mapping, and in gene cloning strategies.
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Park, I. K., P. Roach, J. Bondor, S. P. Fox, and A. A. DePaoli-Roach. "Molecular mechanism of the synergistic phosphorylation of phosphatase inhibitor-2. Cloning, expression, and site-directed mutagenesis of inhibitor-2." Journal of Biological Chemistry 269, no. 2 (January 1994): 944–54. http://dx.doi.org/10.1016/s0021-9258(17)42203-4.

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Popham, D. L., and P. Setlow. "Cloning, nucleotide sequence, mutagenesis, and mapping of the Bacillus subtilis pbpD gene, which codes for penicillin-binding protein 4." Journal of Bacteriology 176, no. 23 (1994): 7197–205. http://dx.doi.org/10.1128/jb.176.23.7197-7205.1994.

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Richard, Nathalie, Horacio Salomon, Robert Rando, Tarek Mansour, Terry L. Bowlin, and Mark A. Wainberg. "Selection and Characterization of Human Immunodeficiency Virus Type 1 Variants Resistant to the (+) and (−) Enantiomers of 2′-Deoxy-3′-Oxa-4′-Thio-5-Fluorocytidine." Antimicrobial Agents and Chemotherapy 44, no. 5 (May 1, 2000): 1127–31. http://dx.doi.org/10.1128/aac.44.5.1127-1131.2000.

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ABSTRACT Human immunodeficiency virus (HIV) type 1 (HIV-1) variants were selected for resistance to the (+) and (−) enantiomers of a novel nucleoside analogue, 2′-deoxy-3′-oxa-4′-thio-5-fluorocytidine (dOTFC), by use of the infectious molecular clone HIV HXB2D and the human T-cell line MT-4. The dOTFC-resistant variants that were selected were 10-fold less sensitive than wild-type virus, and cloning and sequencing of the complete reverse transcriptase (RT)-coding region identified the mutation M184V. Studies with mutated recombinant HXB2D virus confirmed the importance of the M184V mutation in conferring resistance to (−)dOTFC in MT-4 cells, although no difference in sensitivity was observed in primary cells. The M184V substitution also displayed decreased susceptibility to (+)dOTFC. Selection with (+)dOTFC also produced variants which were 10-fold more resistant than the wild type, and a novel mutation, D67G, was identified following cloning and sequencing of the RT genes. The D67G mutation was introduced into HXB2D by site-directed mutagenesis, and the data obtained confirmed the importance of this mutation in conferring resistance to both (+)dOTFC and (−)dOTFC. Mutated recombinant molecular clone HXB2D-D67G was further selected with (+)dOTFC, and three of six clones sequenced contained both the D67G and M184V mutations, while the other three of the six clones contained only the D67G mutation. Clinical isolates of HIV-1 which are (−) 2′-deoxy-3′-thiacytidine-resistant also displayed resistance to both (+)dOTFC and (−)dOTFC.
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Betz, Andrea, Sandra J. Facey, Bernhard Hauer, Barbara Tshisuaka, and Franz Lingens. "Molecular cloning, sequencing, expression, and site-directed mutagenesis of the 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase gene fromArthrobacter spec. R?61a." Journal of Basic Microbiology 40, no. 1 (February 2000): 7–23. http://dx.doi.org/10.1002/(sici)1521-4028(200002)40:1<7::aid-jobm7>3.0.co;2-5.

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Chitnis, P. R., D. Purvis, and N. Nelson. "Molecular cloning and targeted mutagenesis of the gene psaF encoding subunit III of photosystem I from the cyanobacterium Synechocystis sp. PCC 6803." Journal of Biological Chemistry 266, no. 30 (October 1991): 20146–51. http://dx.doi.org/10.1016/s0021-9258(18)54902-4.

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Jia, Airong, and Xiao-Hua Zhang. "Molecular Cloning, Characterization, and Expression Analysis of the CXCR4 Gene from Turbot:Scophthalmus maximus." Journal of Biomedicine and Biotechnology 2009 (2009): 1–8. http://dx.doi.org/10.1155/2009/767893.

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Chemokine receptor 4 (CXCR4) belongs to the large superfamily of G protein-coupled receptors. The EST sequence of CXCR4 from turbot (Scophthalmus maximusL.) was obtained from a subtractive cDNA library. In the present study, the full-length cDNA sequence of turbot CXCR4 was obtained, and sequence analysis indicated that its primary structure was highly similar to CXCR4 from other vertebrates. Quantitative real-time PCR demonstrated that the highest expression level of turbot CXCR4 was in the spleen following injection with physiological saline (PS). After turbot were challenged withVibrio harveyi, the lowest expression level of CXCR4 was detected at 8 hours in the spleen and 12 hours in the head kidney, and then increased gradually to 36 hours. These findings suggested that CXCR4 may play a significant role in the immune response of turbot.
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Dai, Ding, Re Bai, Ernest Hodgson, and Randy L. Rose. "Cloning, sequencing, heterologous expression, and characterization of murine cytochrome P450 3a25*(Cyp3a25), a testosterone 6?-hydroxylase." Journal of Biochemical and Molecular Toxicology 15, no. 2 (2001): 90–99. http://dx.doi.org/10.1002/jbt.4.

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Dissertations / Theses on the topic "Molecular cloning; Mutagenesis; 4-HPPD"

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Lee, Meng Huee. "Studies on ketoacid-dependent dioxygenases involved in amino acid metabolism." Thesis, University of Oxford, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.362049.

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