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Journal articles on the topic 'Site directed mutagensis'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Gudynaite-Savitch, Loreta, Christelle Loiselay, Leonid V. Savitch, et al. "The small domain of cytochromeffrom the psychrophileChlamydomonas raudensisUWO 241 modulates the apparent molecular mass and decreases the accumulation of cytochromefin the mesophileChlamydomonas reinhardtii." Biochemistry and Cell Biology 85, no. 5 (2007): 616–27. http://dx.doi.org/10.1139/o07-066.

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Cytochrome f from the psychrophile Chlamydomonas raudensis UWO 241 has a lower thermostability of its c-type heme and an apparent molecular mass that is 7 kDa lower than that of the model mesophilic green alga Chlamydomonas reinhardtii. We combined chloroplast transformation, site-directed mutagensis, and the creation of chimeric fusion constructs to assess the contribution of specific domains and (or) amino acids residues to the structure, stability, and accumulation of cytochrome f, as well as its function in photosynthetic intersystem electron transport. We demonstrate that differences in t

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2

de Vries, G. E. "Site-directed mutagenesis." Trends in Plant Science 5, no. 7 (2000): 276. http://dx.doi.org/10.1016/s1360-1385(00)01699-x.

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3

Carter, P. "Site-directed mutagenesis." Biochemical Journal 237, no. 1 (1986): 1–7. http://dx.doi.org/10.1042/bj2370001.

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4

Nybo, Kristie. "Site-directed mutagenesis: colony growth." BioTechniques 50, no. 2 (2011): 87–89. http://dx.doi.org/10.2144/000113609.

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5

Weiner, M. P., and G. L. Costa. "Rapid PCR site-directed mutagenesis." Genome Research 4, no. 3 (1994): S131—S136. http://dx.doi.org/10.1101/gr.4.3.s131.

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6

MacDonald, Nicholas J., José M. P. Freije, Mary L. Stracke, Richard E. Manrow, and Patricia S. Steeg. "Site-directed Mutagenesis ofnm23-H1." Journal of Biological Chemistry 271, no. 41 (1996): 25107–16. http://dx.doi.org/10.1074/jbc.271.41.25107.

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7

Vallone, B., P. Vecchini, V. Cavalli, and M. Brunori. "Site-directed mutagenesis in hemoglobin." FEBS Letters 324, no. 2 (1993): 117–22. http://dx.doi.org/10.1016/0014-5793(93)81375-a.

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8

Carey, Michael F., Craig L. Peterson, and Stephen T. Smale. "PCR-Mediated Site-Directed Mutagenesis." Cold Spring Harbor Protocols 2013, no. 8 (2013): pdb.prot076505. http://dx.doi.org/10.1101/pdb.prot076505.

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9

Costa, Gina L., and Michael P. Weiner. "Rapid PCR Site-Directed Mutagenesis." Cold Spring Harbor Protocols 2006, no. 1 (2006): pdb.prot4144. http://dx.doi.org/10.1101/pdb.prot4144.

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10

Erb, Laurie, Richard Garrad, Yanjun Wang, Tom Quinn, John T. Turner, and Gary A. Weisman. "Site-directed Mutagenesis of P2UPurinoceptors." Journal of Biological Chemistry 270, no. 9 (1995): 4185–88. http://dx.doi.org/10.1074/jbc.270.9.4185.

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11

Imai, Kiyohiro, Kenzo Fushitani, Gentaro Miyazaki, et al. "Site-directed mutagenesis in haemoglobin." Journal of Molecular Biology 218, no. 4 (1991): 769–78. http://dx.doi.org/10.1016/0022-2836(91)90265-8.

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12

Nadin-Davis, Susan A., and Shirley C. Chang. "Site-Directed Mutagenesis of Large Plasmids." BioTechniques 25, no. 6 (1998): 1014–19. http://dx.doi.org/10.2144/98256st04.

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13

Schildkraut, Ezra, and Peichung Hsieh. "Site-Directed Mutagenesis by Gibson Assembly." Genetic Engineering & Biotechnology News 33, no. 4 (2013): 18–19. http://dx.doi.org/10.1089/gen.33.4.08.

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14

Richardson, Richard T., and Michael G. O'Rand. "Site-directed Mutagenesis of Rabbit Proacrosin." Journal of Biological Chemistry 271, no. 39 (1996): 24069–74. http://dx.doi.org/10.1074/jbc.271.39.24069.

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15

Okamoto, Yasuo, Silvia Vaena de Avalos, and Yusuf A. Hannun. "Functional Analysis ofISC1by Site-Directed Mutagenesis†." Biochemistry 42, no. 25 (2003): 7855–62. http://dx.doi.org/10.1021/bi0341354.

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16

Cavallius, Jens, and William C. Merrick. "Site-directed Mutagenesis of Yeast eEF1A." Journal of Biological Chemistry 273, no. 44 (1998): 28752–58. http://dx.doi.org/10.1074/jbc.273.44.28752.

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17

Abe, Ikuro, Yukie Sano, Yusuke Takahashi, and Hiroshi Noguchi. "Site-directed Mutagenesis of Benzalacetone Synthase." Journal of Biological Chemistry 278, no. 27 (2003): 25218–26. http://dx.doi.org/10.1074/jbc.m303276200.

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18

Benjamin, David C., and Samuel S. Perdue. "Site-Directed Mutagenesis in Epitope Mapping." Methods 9, no. 3 (1996): 508–15. http://dx.doi.org/10.1006/meth.1996.0058.

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19

Bielli, Pamela, Gian Carlo Bellenchi, and Lilia Calabrese. "Site-directed Mutagenesis of Human Ceruloplasmin." Journal of Biological Chemistry 276, no. 4 (2000): 2678–85. http://dx.doi.org/10.1074/jbc.m007176200.

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20

DAHAI, Tang, Shoji ANDO, Yozo TAKASAKI, and Jutaro TADANO. "Site-Directed Mutagenesis of Restriction EndonucleaseHindIII." Bioscience, Biotechnology, and Biochemistry 63, no. 10 (1999): 1703–7. http://dx.doi.org/10.1271/bbb.63.1703.

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21

Amerik, Alexander Yu, Vladimir K. Antonov, Alexander E. Gorbalenya, Svetlana A. Kotova, Tatyana V. Rotanova, and Elena V. Shimbarevich. "Site-directed mutagenesis of La protease." FEBS Letters 287, no. 1-2 (1991): 211–14. http://dx.doi.org/10.1016/0014-5793(91)80053-6.

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22

Andag, Reiner, and Ekkehard Schütz. "General Method for Site-Directed Mutagenesis." BioTechniques 30, no. 3 (2001): 486–88. http://dx.doi.org/10.2144/01303bm04.

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23

Hussain, Hasnain, and Nikson Fatt-Ming Chong. "Combined Overlap Extension PCR Method for Improved Site Directed Mutagenesis." BioMed Research International 2016 (2016): 1–7. http://dx.doi.org/10.1155/2016/8041532.

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The combined overlap extension PCR (COE-PCR) method developed in this work combines the strengths of the overlap extension PCR (OE-PCR) method with the speed and ease of the asymmetrical overlap extension (AOE-PCR) method. This combined method allows up to 6 base pairs to be mutated at a time and requires a total of 40–45 PCR cycles. A total of eight mutagenesis experiments were successfully carried out, with each experiment mutating between two to six base pairs. Up to four adjacent codons were changed in a single experiment. This method is especially useful for codon optimization, where doub

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24

Loke, Paxton, and Tiow-Suan Sim. "A Comparison of Three Site-Directed Mutagenesis Kits." Zeitschrift für Naturforschung C 56, no. 9-10 (2001): 810–13. http://dx.doi.org/10.1515/znc-2001-9-1021.

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Abstract In this comparative study, three different mutagenesis kits, namely the MutaGene phagemid in vitro mutagenesis kit (Bio-Rad), the Transformerä Site-Directed mutagenesis kit (Clontech) and the Quik-change site-directed mutagenesis kit (Stratagene) were used for the mutagenesis of IPNS genes. However, a large difference in mutation efficiencies among these kits was encountered. Furthermore, these kits employ different strategies with its own individual strengths and weaknesses. Thus, a comparison among these three kits to evaluate their usefulness and improvements on the strategy adopte

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25

Shenoy, Avinash R., and Sandhya S. Visweswariah. "Site-directed mutagenesis using a single mutagenic oligonucleotide and DpnI digestion of template DNA." Analytical Biochemistry 319, no. 2 (2003): 335–36. http://dx.doi.org/10.1016/s0003-2697(03)00286-0.

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26

Diner, Bruce A., Peter J. Nixon, and Joseph W. Farchaus. "Site-directed mutagenesis of photosynthetic reaction centers." Current Opinion in Structural Biology 1, no. 4 (1991): 546–54. http://dx.doi.org/10.1016/s0959-440x(05)80076-4.

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27

Lamandé, ShireenR, Emanouil Sigalas, SuzanneB Golub, et al. "Site-directed mutagenesis of type VI collagen." Matrix Biology 16, no. 2 (1997): 74–75. http://dx.doi.org/10.1016/s0945-053x(97)90092-5.

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28

Molina-Heredia, Fernando P., Antonio Dı́az-Quintana, Manuel Hervás, José A. Navarro, and Miguel A. De la Rosa. "Site-directed Mutagenesis of Cytochromec6fromAnabaenaSpecies PCC 7119." Journal of Biological Chemistry 274, no. 47 (1999): 33565–70. http://dx.doi.org/10.1074/jbc.274.47.33565.

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29

Fraser, C. M. "Site-directed Mutagenesis of β-Adrenergic Receptors". Journal of Biological Chemistry 264, № 16 (1989): 9266–70. http://dx.doi.org/10.1016/s0021-9258(18)60524-1.

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30

Kuipers, Oscar P., Hein J. Boot, and Willem M. de Vos. "Improved site-directed mutagenesis method using PCR." Nucleic Acids Research 19, no. 16 (1991): 4558. http://dx.doi.org/10.1093/nar/19.16.4558.

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31

De la Cerda, Berta, Antonio Dı́az-Quintana, José A. Navarro, Manuel Hervás, and Miguel A. De la Rosa. "Site-directed Mutagenesis of Cytochromec6fromSynechocystissp. PCC 6803." Journal of Biological Chemistry 274, no. 19 (1999): 13292–97. http://dx.doi.org/10.1074/jbc.274.19.13292.

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32

Storici, Francesca, L. Kevin Lewis, and Michael A. Resnick. "In vivo site-directed mutagenesis using oligonucleotides." Nature Biotechnology 19, no. 8 (2001): 773–76. http://dx.doi.org/10.1038/90837.

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33

Barber, Michael D., Steven J. Gambling, Herman C. Watson, and Jennifer A. Littlechild. "Site-directed mutagenesis of yeast phosphoglycerate kinase." FEBS Letters 320, no. 3 (1993): 193–97. http://dx.doi.org/10.1016/0014-5793(93)80584-h.

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34

Rodríguez-Lecompte, Juan Carlos, and Frederick S. B. Kibenge. "Site-Directed Mutagenesis of Avibirnavirus VP4 Gene." Virology 292, no. 2 (2002): 241–46. http://dx.doi.org/10.1006/viro.2001.1260.

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35

Schirwitz, K., A. Schmidt, and V. Lamzin. "Modelling crystal contacts by site-directed mutagenesis." Acta Crystallographica Section A Foundations of Crystallography 60, a1 (2004): s131. http://dx.doi.org/10.1107/s0108767304097429.

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36

Lam, Bing K., John F. Penrose, Kongyi Xu, Mathew H. Baldasaro, and K. Frank Austen. "Site-directed Mutagenesis of Human Leukotriene C4Synthase." Journal of Biological Chemistry 272, no. 21 (1997): 13923–28. http://dx.doi.org/10.1074/jbc.272.21.13923.

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37

Kim, Eugene J., Rui-Guang Zhen, and Philip A. Rea. "Site-directed Mutagenesis of Vacuolar H+-pyrophosphatase." Journal of Biological Chemistry 270, no. 6 (1995): 2630–35. http://dx.doi.org/10.1074/jbc.270.6.2630.

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38

Garrett, Robert M., and K. V. Rajagopalan. "Site-directed Mutagenesis of Recombinant Sulfite Oxidase." Journal of Biological Chemistry 271, no. 13 (1996): 7387–91. http://dx.doi.org/10.1074/jbc.271.13.7387.

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39

Zhuang-Jackson, H., J. M. Moulis, and J. Meyer. "Site-directed mutagenesis of Clostridium pasteurianum rubredoxin." Journal of Inorganic Biochemistry 59, no. 2-3 (1995): 524. http://dx.doi.org/10.1016/0162-0134(95)97619-2.

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40

Murase, Sachiko, Jun S. Takagi, Yasuyuki Higashi, Hiromasa Imaishi, Noboru Yumoto, and Masanobu Tokushige. "Activation of aspartase by site-directed mutagenesis." Biochemical and Biophysical Research Communications 177, no. 1 (1991): 414–19. http://dx.doi.org/10.1016/0006-291x(91)91999-s.

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41

Bohnsack, Richard N. "Site-directed mutagenesis using positive antibiotic selection." Molecular Biotechnology 7, no. 2 (1997): 181–88. http://dx.doi.org/10.1007/bf02761754.

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42

Bi, Wanli, and Peter J. Stambrook. "Site-Directed Mutagenesis by Combined Chain Reaction." Analytical Biochemistry 256, no. 1 (1998): 137–40. http://dx.doi.org/10.1006/abio.1997.2516.

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43

Lee, Norman H., Susan M. Pellegrino та Claire M. Fraser. "Site-Directed Mutagenesis of α-Adrenergic Receptors". Neuroprotocols 4, № 1 (1994): 20–31. http://dx.doi.org/10.1006/ncmn.1994.1004.

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44

Climie, S., L. Ruiz-Perez, D. Gonzalez-Pacanowska, et al. "Saturation site-directed mutagenesis of thymidylate synthase." Journal of Biological Chemistry 265, no. 31 (1990): 18776–79. http://dx.doi.org/10.1016/s0021-9258(17)30579-3.

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45

Hashimoto-Gotoh, Tamotsu, Toshiki Mizuno, Yuko Ogasahara, and Masao Nakagawa. "An oligodeoxyribonucleotide-directed dual amber method for site-directed mutagenesis." Gene 152, no. 2 (1995): 271–75. http://dx.doi.org/10.1016/0378-1119(94)00750-m.

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46

Mogi, Tatsushi, Satoru Akimoto, Sachiko Endou, Takahiro Watanabe-Nakayama, Eri Mizuochi-Asai, and Hideto Miyoshi. "Probing the Ubiquinol-Binding Site in Cytochromebdby Site-Directed Mutagenesis†." Biochemistry 45, no. 25 (2006): 7924–30. http://dx.doi.org/10.1021/bi060192w.

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47

Redick, Sambra D., Daniel L. Settles, Gina Briscoe, and Harold P. Erickson. "Defining Fibronectin's Cell Adhesion Synergy Site by Site-Directed Mutagenesis." Journal of Cell Biology 149, no. 2 (2000): 521–27. http://dx.doi.org/10.1083/jcb.149.2.521.

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Fibronectin's RGD-mediated binding to the α5β1 integrin is dramatically enhanced by a synergy site within fibronectin III domain 9 (FN9). Guided by the crystal structure of the cell-binding domain, we selected amino acids in FN9 that project in the same direction as the RGD, presumably toward the integrin, and mutated them to alanine. R1379 in the peptide PHSRN, and the nearby R1374 have been shown previously to be important for α5β1-mediated adhesion (Aota, S., M. Nomizu, and K.M. Yamada. 1994. J. Biol. Chem. 269:24756–24761). Our more extensive set of mutants showed that R1379 is the key res

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48

Woodyer, Ryan, Joshua L. Wheatley, Heather A. Relyea, Stacey Rimkus, and Wilfred A. van der Donk. "Site-Directed Mutagenesis of Active Site Residues of Phosphite Dehydrogenase†." Biochemistry 44, no. 12 (2005): 4765–74. http://dx.doi.org/10.1021/bi047868c.

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49

Fisher, Constance L., and Guo Kui Pei. "Modification of a PCRBased Site-Directed Mutagenesis Method." BioTechniques 23, no. 4 (1997): 570–74. http://dx.doi.org/10.2144/97234bm01.

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50

Boyd, A. Christopher, and David J. Porteous. "PCR-Generated Crossover Linkers for Site-Directed Mutagenesis." BioTechniques 23, no. 5 (1997): 827–30. http://dx.doi.org/10.2144/97235bm13.

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