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Готові списки джерел за темами / Molecular cloning / Статті в журналах

Статті в журналах з теми "Molecular cloning"

Щоб переглянути інші типи публікацій з цієї теми, перейдіть за посиланням: Molecular cloning.

Автор: Grafiati

Опубліковано: 4 червня 2021

Оновлено: 6 вересня 2023

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1

Kwak, Inseok. "Molecular Cloning and Characterization of Bovine CYP26A1 Promoter." Journal of Life Science 26, no. 1 (January 30, 2016): 42–49. http://dx.doi.org/10.5352/jls.2016.26.1.42.

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2

Xu, Libing, Yuhong Chen, Qiuhua Li, Tianliang He, and Xinhua Chen. "Molecular cloning." Fish & Shellfish Immunology 98 (March 2020): 981–87. http://dx.doi.org/10.1016/j.fsi.2019.10.064.

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3

Morimura, Naoko, Yoko Tezuka, Naoko Watanabe, Masafumi Yasuda, Seiji Miyatani, Nobumichi Hozumi, and Ken-ichi Tezuka. "Molecular Cloning of POEM." Journal of Biological Chemistry 276, no. 45 (September 6, 2001): 42172–81. http://dx.doi.org/10.1074/jbc.m103216200.

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4

Ashwini, Malla, Shanmugaraj Bala Murugan, Srinivasan Balamurugan, and Ramalingam Sathishkumar. "Advances in molecular cloning." Molecular Biology 50, no. 1 (January 2016): 1–6. http://dx.doi.org/10.1134/s0026893316010131.

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5

Tu, Kevin, Angela Sun, and Daniel Levin. "A Sweet Method of Modeling Restriction Endonuclease-Based Molecular Cloning." American Biology Teacher 85, no. 1 (January 1, 2023): 52–54. http://dx.doi.org/10.1525/abt.2023.85.1.52.

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Анотація:

Molecular cloning is an invaluable research tool in modern molecular biology. However, it is often difficult for students to grasp conceptually without visual aids and even more difficult to understand how to successfully set up a cloning experiment. Here, we describe a flipped classroom activity that simulates cloning using donuts as models of plasmids. Students noted in semistructured interviews that the interactive nature of this activity made it an engaging introduction to molecular cloning.

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6

Taylor, D. W., J. S. Cordingley, D. W. Dunne, K. S. Johnson, W. J. Haddow, C. E. Hormaeche, V. Nene, and A. E. Butterworth. "Molecular cloning of schistosome genes." Parasitology 92, S1 (January 1986): S73—S81. http://dx.doi.org/10.1017/s003118200008570x.

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As part of an integrated programme investigating human schistosomiasis, work which involves epidemiological surveys and detailed immunological studies as well as biochemical investigations, we have, over the last three years, been cloning schistosome genes in a variety of plasmid and lambda vector systems. In this lecture we present a review of some selected aspects of work primarily aimed at production of experimental vaccines against the disease but which, on a broader front, is also concerned with developmental regulation of gene expression around the parasite's life-cycle. Specifically, we are interested in cloning three groups of genes. First, those encoding surface antigens; second, those associated with sexual maturity and egg production; and third, antigens which may provide a basis for a specific immunodiagnostic test.

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7

Yamamoto, Kosuke, Suguru Oguri, Susumu Chiba, and Yoshie S. Momonoki. "Molecular cloning ofacetylcholinesterasegene fromSalicornia europaeaL." Plant Signaling & Behavior 4, no. 5 (May 2009): 361–66. http://dx.doi.org/10.4161/psb.4.5.8360.

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8

Iwaki, Daisuke, Shun-ichiro Kawabata, Yoshiki Miura, Atsuko Kato, Peter B. Armstrong, James P. Quigley, Kare Lehmann Nielsen, Klavs Dolmer, Lars Sottrup-Jensen, and Sadaaki Iwanaga. "Molecular Cloning of Limulusalpha2-Macroglobulin." European Journal of Biochemistry 242, no. 3 (December 15, 1996): 822–31. http://dx.doi.org/10.1111/j.1432-1033.1996.0822r.x.

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9

Malcolm, S. "Guide to Molecular Cloning Techniques." Journal of Medical Genetics 27, no. 1 (January 1, 1990): 70. http://dx.doi.org/10.1136/jmg.27.1.70.

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10

Reuter, Harald, and Hartmut Porzig. "Muscle disease and molecular cloning." Nature 336, no. 6195 (November 1988): 113. http://dx.doi.org/10.1038/336113b0.

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11

Etchegaray, Jean Pierre, Maria Adela MartÃnez, Manuel Krauskopf, and Gloria LeÃ³n. "Molecular cloning ofRenibacterium salmoninarumDNA fragments." FEMS Microbiology Letters 79, no. 1 (March 1991): 61–64. http://dx.doi.org/10.1111/j.1574-6968.1991.tb04505.x.

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12

Vannahme, Christian, Sabine Schübel, Marcus Herud, Silke Gösling, Hanni Hülsmann, Mats Paulsson, Ursula Hartmann, and Patrik Maurer. "Molecular Cloning of Testican-2." Journal of Neurochemistry 73, no. 1 (January 18, 2002): 12–20. http://dx.doi.org/10.1046/j.1471-4159.1999.0730012.x.

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13

Iwahana, H., T. Yamaoka, M. Mizutani, N. Mizusawa, S. Ii, K. Yoshimoto, and M. Itakura. "Molecular cloning of rat amidophosphoribosyltransferase." Journal of Biological Chemistry 268, no. 10 (April 1993): 7225–37. http://dx.doi.org/10.1016/s0021-9258(18)53167-7.

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14

Yogalingam, Gouri, and Donald S. Anson. "Molecular cloning of feline CD34." Veterinary Immunology and Immunopathology 95, no. 1-2 (September 2003): 53–61. http://dx.doi.org/10.1016/s0165-2427(03)00102-8.

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15

Darlison, Mark G. "Guide to molecular cloning techniques." Trends in Neurosciences 11, no. 11 (January 1988): 510–11. http://dx.doi.org/10.1016/0166-2236(88)90014-8.

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16

Smith, Annabel N., Karin E. Finberg, Carsten A. Wagner, Richard P. Lifton, Mark A. J. Devonald, Ya Su, and Fiona E. Karet. "Molecular Cloning and Characterization ofAtp6n1b." Journal of Biological Chemistry 276, no. 45 (August 8, 2001): 42382–88. http://dx.doi.org/10.1074/jbc.m107267200.

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17

Chandrasekaran, L., and M. L. Tanzer. "Molecular cloning of chicken aggrecan." Biochemical Journal 296, no. 3 (December 15, 1993): 885–87. http://dx.doi.org/10.1042/bj2960885b.

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18

Zhyvoloup, Alexander, Ivan Nemazanyy, Aleksei Babich, Ganna Panasyuk, Natalya Pobigailo, Mariya Vudmaska, Valeriy Naidenov, et al. "Molecular Cloning of CoA Synthase." Journal of Biological Chemistry 277, no. 25 (April 29, 2002): 22107–10. http://dx.doi.org/10.1074/jbc.c200195200.

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19

Kawai, Shuji, Hiroyuki Honda, Takaaki Tanase, Masahito Taya, Shinji Iijima, and Takeshi Kobayashi. "Molecular Cloning ofRuminococcus albusCellulase Gene." Agricultural and Biological Chemistry 51, no. 1 (January 1987): 59–63. http://dx.doi.org/10.1080/00021369.1987.10867974.

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20

Rowley, R. Bruce, Joseph B. Bolen, and Joseph Fargnoli. "Molecular Cloning of Rodent p72Syk." Journal of Biological Chemistry 270, no. 21 (May 26, 1995): 12659–64. http://dx.doi.org/10.1074/jbc.270.21.12659.

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21

Deininger, Prescott. "Molecular cloning: A laboratory manual." Analytical Biochemistry 186, no. 1 (April 1990): 182–83. http://dx.doi.org/10.1016/0003-2697(90)90595-z.

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22

Tokuhara, Makoto, Momoki Hirai, Yutaka Atomi, Masaaki Terada, and Masaru Katoh. "Molecular Cloning of HumanFrizzled-6." Biochemical and Biophysical Research Communications 243, no. 2 (February 1998): 622–27. http://dx.doi.org/10.1006/bbrc.1998.8143.

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23

Tokuhara, Makoto, Momoki Hirai, Yutaka Atomi, Masaaki Terada, and Masaru Katoh. "Molecular Cloning of HumanFrizzled-6,." Biochemical and Biophysical Research Communications 247, no. 3 (June 1998): 910. http://dx.doi.org/10.1006/bbrc.1998.8859.

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24

Iwahana, H., J. Oka, N. Mizusawa, E. Kudo, S. Ii, K. Yoshimoto, E. W. Holmes, and M. Itakura. "Molecular Cloning of Human Amidophosphoribosyltransferase." Biochemical and Biophysical Research Communications 190, no. 1 (January 1993): 192–200. http://dx.doi.org/10.1006/bbrc.1993.1030.

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25

Fugier-Vivier, Isabelle, Odette de Bouteiller, Christiane Guret, François Fossiez, Jacques Banchereau, Marie-Geneviève Mattei, Smina Aït-Yahia, Eric Garcia, Serge Lebecque, and Yong-Jun Liu. "Molecular cloning of human RP105." European Journal of Immunology 27, no. 7 (July 1997): 1824–27. http://dx.doi.org/10.1002/eji.1830270734.

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26

Ishikawa, H., Y. Shinkai, H. Yagita, C. C. Yue, P. A. Henkart, S. Sawada, H. A. Young, C. W. Reynolds, and K. Okumura. "Molecular cloning of rat cytolysin." Journal of Immunology 143, no. 9 (November 1, 1989): 3069–73. http://dx.doi.org/10.4049/jimmunol.143.9.3069.

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Анотація:

Abstract Rat cytolysin is one of the cytolytic factors present in the cytoplasmic granules of rat NK-like cytolytic cells and purified cytolysin exhibits an apparent Mr or 70 kDa. Cytolysis produced by cytolysin occurs in the presence of Ca2+ and is accompanied by the formation of membrane lesions of 160 A diameter. We have isolated a cDNA encoding rat cytolysin from the cDNA library of a rat large granular lymphocyte (LGL) cell line, by hybridization of the rat library with a cDNA probe for mouse perforin. The amino acid sequence deduced from the nucleotide sequence of the isolated cDNA insert indicates that the mature cytolysin protein consist of 534 amino acids with a leader peptide of 20 amino acids. The protein contains two functionally important domains: the first domain is believed to contain the transmembrane channel and the second domain consists of an epidermal growth factor-type "class B" cysteine-rich region. A comparison with mouse perforin indicates that the two genes are very similar (89.9% nucleotide and 84.9% amino acid identity). Northern blot hybridization analysis indicates that cytolysin mRNA is expressed in rat lymphocytes (lymphokine-activated killer cells and LGL cells) and LGL cell lines.

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27

Tan, Lendl, Emily J. Strong, Kyra Woods, and Nicholas P. West. "Homologous alignment cloning: a rapid, flexible and highly efficient general molecular cloning method." PeerJ 6 (June 29, 2018): e5146. http://dx.doi.org/10.7717/peerj.5146.

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Анотація:

Homologous alignment cloning (HAC) is a rapid method of molecular cloning that facilitates low-cost, highly efficient cloning of polymerase chain reaction products into any plasmid vector in approximately 2 min. HAC facilitates insert integration due to a sequence alignment strategy, by way of short, vector-specific homology tails appended to insert during amplification. Simultaneous exposure of single-stranded fragment ends, utilising the 3′→5′ exonuclease activity of T4 DNA polymerase, creates overlapping homologous DNA on each molecule. The exonuclease activity of T4 polymerase is quenched simply by the addition of EDTA and a simple annealing step ensures high yield and high fidelity vector formation. The resultant recombinant plasmids are transformed into standardE. colicloning strains and screened via established methods as necessary. HAC exploits reagents commonly found in molecular research laboratories and achieves efficiencies that exceed conventional cloning methods, including another ligation-independent method we tested. HAC is also suitable for combining multiple fragments in a single reaction, thus extending its flexibility.

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28

Rebhun, John F., and J. Howard Pratt. "Molecular Cloning of Nedd4 fromXenopus Laevis." DNA Sequence 9, no. 5-6 (January 1998): 295–306. http://dx.doi.org/10.3109/10425179809008468.

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29

Sasaki, Katsutoshi. "Molecular Cloning and Characterization of Sialyltransferases." Trends in Glycoscience and Glycotechnology 8, no. 41 (1996): 195–215. http://dx.doi.org/10.4052/tigg.8.195.

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30

Iwamoto, Motohiro, and Takashi Oku. "Cloning and Molecular Characterization ofhrpXfromXanthomonas axonopodispv.citri." DNA Sequence 11, no. 1-2 (January 2000): 167–73. http://dx.doi.org/10.3109/10425170009033986.

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31

NISHIMURA, Motohiro, Daisuke ISHIYAMA, and Julian DAVIES. "Molecular Cloning ofStreptomycesGenes Encoding Vanillate Demethylase." Bioscience, Biotechnology, and Biochemistry 70, no. 9 (September 23, 2006): 2316–19. http://dx.doi.org/10.1271/bbb.60180.

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32

Gay, N. J., and J. E. Walker. "Molecular cloning of a bovine cathepsin." Biochemical Journal 225, no. 3 (February 1, 1985): 707–12. http://dx.doi.org/10.1042/bj2250707.

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Анотація:

A cDNA clone for a thiol endoproteinase has been isolated from a bovine heart cDNA library by using a mixture of 32 synthetic oligonucleotides as a hybridization probe. The inserted region is 672 base pairs in length. It contains a sequence encoding the C-terminal region of a protein that is homologous to rat liver cathepsins B and H and to plant thiol proteinases. In addition, it contains the sequence of 442 bases corresponding to the 3′ untranslated region of the mRNA. The inserted region was used as a specific probe in RNA transfer analysis; the size of the mRNA encoding the thiol endoproteinase is estimated to be approx. 1.7 kilobases. Thus, the maximum size of the encoded protein is about 350-400 amino acids.

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33

Appleton, Evan, Jenhan Tao, Traci Haddock, and Douglas Densmore. "Interactive assembly algorithms for molecular cloning." Nature Methods 11, no. 6 (April 28, 2014): 657–62. http://dx.doi.org/10.1038/nmeth.2939.

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34

Ziegler, Jörg, Irene Stenzel, Bettina Hause, Helmut Maucher, Mats Hamberg, Rudi Grimm, Martin Ganal, and Claus Wasternack. "Molecular Cloning of Allene Oxide Cyclase." Journal of Biological Chemistry 275, no. 25 (April 6, 2000): 19132–38. http://dx.doi.org/10.1074/jbc.m002133200.

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35

Hashimoto, T., K. Tamaki, K. i. Suzuki, and Y. Yamada. "Molecular Cloning of Plant Spermidine Synthases." Plant and Cell Physiology 39, no. 1 (January 1, 1998): 73–79. http://dx.doi.org/10.1093/oxfordjournals.pcp.a029291.

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36

WOODHEAD, L. "A Practical Guide to Molecular Cloning." Biochemical Society Transactions 13, no. 4 (August 1, 1985): 801. http://dx.doi.org/10.1042/bst0130801a.

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37

Kawabata, Hiroshi, Rong Yang, Toshiyasu Hirama, Peter T. Vuong, Seiji Kawano, Adrian F. Gombart, and H. Phillip Koeffler. "Molecular Cloning of Transferrin Receptor 2." Journal of Biological Chemistry 274, no. 30 (July 23, 1999): 20826–32. http://dx.doi.org/10.1074/jbc.274.30.20826.

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38

Kohler, Stefan A., Eric Menotti, and Lukas C. Kühn. "Molecular Cloning of Mouse Glycolate Oxidase." Journal of Biological Chemistry 274, no. 4 (January 22, 1999): 2401–7. http://dx.doi.org/10.1074/jbc.274.4.2401.

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39

He, Xiao-Ping, Zhao-Shen Li, Zhen-Xing Tu, Xue Pan, Yan-Fang Gong, Jun Gao, and Jing Jin. "Molecular cloning of human canstatin gene." World Chinese Journal of Digestology 12, no. 10 (2004): 2329. http://dx.doi.org/10.11569/wcjd.v12.i10.2329.

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40

Madsen, Hans O., and J. Peter Hjorth. "Molecular cloning of mouse PSP mRNA." Nucleic Acids Research 13, no. 1 (1985): 1–13. http://dx.doi.org/10.1093/nar/13.1.1.

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41

MIN, Kwan-Sik, Kunio SHIOTA, and Tomoya OGAWA. "Molecular Cloning of Equine Preprorelaxin cDNA." Journal of Reproduction and Development 42, no. 3 (1996): 171–78. http://dx.doi.org/10.1262/jrd.42.171.

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42

Murphy, Thomas J., Kasuhisa Takeuchi, and R. Wayne Alexander. "Molecular Cloning of AT1 Angiotensin Receptors." American Journal of Hypertension 5, no. 12_Pt_2 (December 1992): 236S—242S. http://dx.doi.org/10.1093/ajh/5.12.236s.

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43

Namba, Tsunehisa, Hiroji Oida, Akira Kakizuka, Yukihiko Sugimoto, Manabu Negishi, Atsushi Ichikawa, and Shuh Narumiya. "Molecular Cloning of a Prostacyclin Receptor." Japanese Journal of Pharmacology 64 (1994): 146. http://dx.doi.org/10.1016/s0021-5198(19)50228-1.

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44

PENG, Shi-Qing, Jing XU, Hui-Liang LI, and Wei-Min TIAN. "Cloning and Molecular Characterization ofHbCOI1fromHevea brasiliensis." Bioscience, Biotechnology, and Biochemistry 73, no. 3 (March 23, 2009): 665–70. http://dx.doi.org/10.1271/bbb.80721.

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45

Jiang, Pan Hong, Françoise Chany-Fournier, and Charles Chany. "Sarcolectin: Complete purification for molecular cloning." Biochimie 81, no. 7 (July 1999): 701–7. http://dx.doi.org/10.1016/s0300-9084(99)80127-8.

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46

Tsao, Der-An, Cheng-Wen Wu, and Young-Sun Lin. "Molecular cloning of bovine telomerase RNA." Gene 221, no. 1 (October 1998): 51–58. http://dx.doi.org/10.1016/s0378-1119(98)00432-6.

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47

Kawai, Hidehiko, Takahide Ota, Fumio Suzuki, and Masaaki Tatsuka. "Molecular cloning of mouse thioredoxin reductases." Gene 242, no. 1-2 (January 2000): 321–30. http://dx.doi.org/10.1016/s0378-1119(99)00498-9.

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48

Mi, Lixin. "Molecular Cloning of Protein-Based Polymers." Biomacromolecules 7, no. 7 (July 2006): 2099–107. http://dx.doi.org/10.1021/bm050158h.

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49

Grusby, Michael J., Steve C. Mitchell, and Laurie H. Glimcher. "Molecular cloning of mouse cathepsin D." Nucleic Acids Research 18, no. 13 (1990): 4008. http://dx.doi.org/10.1093/nar/18.13.4008.

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50

Zubriene, Asta, Saulute Budriene, Judita Lubiene, and Gervydas Dienys. "Immobilized Alkaline Phosphatase for Molecular Cloning." Biocatalysis and Biotransformation 20, no. 6 (January 2002): 423–27. http://dx.doi.org/10.1080/1024242021000040873.

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