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Articles de revues sur le sujet « Site-Directed Mutagenesi »

Auteur : Grafiati

Publié le 9 mars 2023

Mis à jour le 31 juillet 2025

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1

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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2

Sil, Kallol, and Soumendra Nath Talapatra. "Prediction of Site Directed Mutagenesis of Acetylcholinesterase by Using Hotspot Wizard Tool." International Journal of Science and Research (IJSR) 13, no. 9 (2024): 1597–600. http://dx.doi.org/10.21275/sr24926121958.

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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

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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5

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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6

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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7

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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8

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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9

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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10

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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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

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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13

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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14

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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15

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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16

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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17

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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18

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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19

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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20

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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21

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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22

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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23

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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24

Pai, Dhungat Jayant. "Michael Smith and Site-directed Mutagenesis." Journal of the Association of Physicians of India 72, no. 7 (2024): 108. https://doi.org/10.59556/japi.72.0587.

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25

Cupples, C. G., M. Cabrera, C. Cruz, and J. H. Miller. "A set of lacZ mutations in Escherichia coli that allow rapid detection of specific frameshift mutations." Genetics 125, no. 2 (1990): 275–80. http://dx.doi.org/10.1093/genetics/125.2.275.

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Abstract We have used site-directed mutagenesis to alter bases in lacZ near the region encoding essential residues in the active site of beta-galactosidase. The altered sequences generate runs of six or seven identical base pairs which create a frameshift, resulting in a Lac- phenotype. Reversion to Lac+ in each strain can occur only by a specific frameshift at these sequences. Monotonous runs of A's (or of T's on the opposite strand) and G's (or C's) have been constructed, as has an alternating -C-G- sequence. These specific frameshift indicator strains complement a set of six previously desc

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26

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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27

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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28

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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29

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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30

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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31

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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32

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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33

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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34

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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35

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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36

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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37

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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38

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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39

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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40

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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41

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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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

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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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

Subedi, Mamata, Pratikshya Paudel, Shubham Gopera, Abhishek Sharma, and Sanjeet Singh Sandal. "Site-directed Mutagenesis's Prospective Uses in Enhancing Cereal Crops." Journal of Advances in Biology & Biotechnology 27, no. 6 (2024): 868–77. http://dx.doi.org/10.9734/jabb/2024/v27i6950.

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By 2050, there will be 9.8 billion people on the planet, which means that food production must grow by 50% globally. Using conventional plant breeding techniques alone may not be able to meet these increasing demands. A crop's yield, nutritional value, and stress tolerance may all be precisely and quickly improved with the use of genetic engineering tools like site-directed mutagenesis. The most recent site-directed mutagenesis methods—such as genome editing with CRISPR/Cas9—and their uses for crop improvement are covered in this study. A comparison is made between the advantages and disadvant

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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

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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49

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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50

Chen, Shaorong, Shawanda Wilson-Stanford, William Cromwell, et al. "Site-Directed Mutations in the Lanthipeptide Mutacin 1140." Applied and Environmental Microbiology 79, no. 13 (2013): 4015–23. http://dx.doi.org/10.1128/aem.00704-13.

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ABSTRACTThe oral bacteriumStreptococcus mutans, strain JH1140, produces the antibiotic mutacin 1140. Mutacin 1140 belongs to a group of antibiotics called lanthipeptides. More specifically, mutacin 1140 is related to the epidermin type A(I) lanthipeptides. Mutagenesis experiments of this group of lanthipeptides have been primarily restricted to the posttranslationally modifiedmeso-lanthionine and 3-methyllanthionine residues. Site-directed mutagenesis of the core peptide of mutacin 1140 was performed using the suicide vector pVA891. Substitutions of the N-terminal residue, the charged residue

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