Artigos de revistas: "Molecular cloning"

1

Kwak, Inseok. "Molecular Cloning and Characterization of Bovine CYP26A1 Promoter". Journal of Life Science 26, n.º 1 (30 de janeiro de 2016): 42–49. http://dx.doi.org/10.5352/jls.2016.26.1.42.

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

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Morimura, Naoko, Yoko Tezuka, Naoko Watanabe, Masafumi Yasuda, Seiji Miyatani, Nobumichi Hozumi e Ken-ichi Tezuka. "Molecular Cloning of POEM". Journal of Biological Chemistry 276, n.º 45 (6 de setembro de 2001): 42172–81. http://dx.doi.org/10.1074/jbc.m103216200.

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4

Ashwini, Malla, Shanmugaraj Bala Murugan, Srinivasan Balamurugan e Ramalingam Sathishkumar. "Advances in molecular cloning". Molecular Biology 50, n.º 1 (janeiro de 2016): 1–6. http://dx.doi.org/10.1134/s0026893316010131.

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5

Tu, Kevin, Angela Sun e Daniel Levin. "A Sweet Method of Modeling Restriction Endonuclease-Based Molecular Cloning". American Biology Teacher 85, n.º 1 (1 de janeiro de 2023): 52–54. http://dx.doi.org/10.1525/abt.2023.85.1.52.

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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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Taylor, D. W., J. S. Cordingley, D. W. Dunne, K. S. Johnson, W. J. Haddow, C. E. Hormaeche, V. Nene e A. E. Butterworth. "Molecular cloning of schistosome genes". Parasitology 92, S1 (janeiro de 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.

7

Yamamoto, Kosuke, Suguru Oguri, Susumu Chiba e Yoshie S. Momonoki. "Molecular cloning ofacetylcholinesterasegene fromSalicornia europaeaL." Plant Signaling & Behavior 4, n.º 5 (maio de 2009): 361–66. http://dx.doi.org/10.4161/psb.4.5.8360.

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Iwaki, Daisuke, Shun-ichiro Kawabata, Yoshiki Miura, Atsuko Kato, Peter B. Armstrong, James P. Quigley, Kare Lehmann Nielsen, Klavs Dolmer, Lars Sottrup-Jensen e Sadaaki Iwanaga. "Molecular Cloning of Limulusalpha2-Macroglobulin". European Journal of Biochemistry 242, n.º 3 (15 de dezembro de 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, n.º 1 (1 de janeiro de 1990): 70. http://dx.doi.org/10.1136/jmg.27.1.70.

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10

Reuter, Harald, e Hartmut Porzig. "Muscle disease and molecular cloning". Nature 336, n.º 6195 (novembro de 1988): 113. http://dx.doi.org/10.1038/336113b0.

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11

Etchegaray, Jean Pierre, Maria Adela MartÃnez, Manuel Krauskopf e Gloria LeÃ³n. "Molecular cloning ofRenibacterium salmoninarumDNA fragments". FEMS Microbiology Letters 79, n.º 1 (março de 1991): 61–64. http://dx.doi.org/10.1111/j.1574-6968.1991.tb04505.x.

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Vannahme, Christian, Sabine Schübel, Marcus Herud, Silke Gösling, Hanni Hülsmann, Mats Paulsson, Ursula Hartmann e Patrik Maurer. "Molecular Cloning of Testican-2". Journal of Neurochemistry 73, n.º 1 (18 de janeiro de 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 e M. Itakura. "Molecular cloning of rat amidophosphoribosyltransferase." Journal of Biological Chemistry 268, n.º 10 (abril de 1993): 7225–37. http://dx.doi.org/10.1016/s0021-9258(18)53167-7.

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14

Yogalingam, Gouri, e Donald S. Anson. "Molecular cloning of feline CD34". Veterinary Immunology and Immunopathology 95, n.º 1-2 (setembro de 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, n.º 11 (janeiro de 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 e Fiona E. Karet. "Molecular Cloning and Characterization ofAtp6n1b". Journal of Biological Chemistry 276, n.º 45 (8 de agosto de 2001): 42382–88. http://dx.doi.org/10.1074/jbc.m107267200.

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17

Chandrasekaran, L., e M. L. Tanzer. "Molecular cloning of chicken aggrecan". Biochemical Journal 296, n.º 3 (15 de dezembro de 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, n.º 25 (29 de abril de 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 e Takeshi Kobayashi. "Molecular Cloning ofRuminococcus albusCellulase Gene". Agricultural and Biological Chemistry 51, n.º 1 (janeiro de 1987): 59–63. http://dx.doi.org/10.1080/00021369.1987.10867974.

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20

Rowley, R. Bruce, Joseph B. Bolen e Joseph Fargnoli. "Molecular Cloning of Rodent p72Syk." Journal of Biological Chemistry 270, n.º 21 (26 de maio de 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, n.º 1 (abril de 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 e Masaru Katoh. "Molecular Cloning of HumanFrizzled-6". Biochemical and Biophysical Research Communications 243, n.º 2 (fevereiro de 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 e Masaru Katoh. "Molecular Cloning of HumanFrizzled-6",. Biochemical and Biophysical Research Communications 247, n.º 3 (junho de 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 e M. Itakura. "Molecular Cloning of Human Amidophosphoribosyltransferase". Biochemical and Biophysical Research Communications 190, n.º 1 (janeiro de 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 e Yong-Jun Liu. "Molecular cloning of human RP105". European Journal of Immunology 27, n.º 7 (julho de 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 e K. Okumura. "Molecular cloning of rat cytolysin." Journal of Immunology 143, n.º 9 (1 de novembro de 1989): 3069–73. http://dx.doi.org/10.4049/jimmunol.143.9.3069.

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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.

27

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

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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.

28

Rebhun, John F., e J. Howard Pratt. "Molecular Cloning of Nedd4 fromXenopus Laevis". DNA Sequence 9, n.º 5-6 (janeiro de 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, n.º 41 (1996): 195–215. http://dx.doi.org/10.4052/tigg.8.195.

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30

Iwamoto, Motohiro, e Takashi Oku. "Cloning and Molecular Characterization ofhrpXfromXanthomonas axonopodispv.citri". DNA Sequence 11, n.º 1-2 (janeiro de 2000): 167–73. http://dx.doi.org/10.3109/10425170009033986.

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31

NISHIMURA, Motohiro, Daisuke ISHIYAMA e Julian DAVIES. "Molecular Cloning ofStreptomycesGenes Encoding Vanillate Demethylase". Bioscience, Biotechnology, and Biochemistry 70, n.º 9 (23 de setembro de 2006): 2316–19. http://dx.doi.org/10.1271/bbb.60180.

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32

Gay, N. J., e J. E. Walker. "Molecular cloning of a bovine cathepsin". Biochemical Journal 225, n.º 3 (1 de fevereiro de 1985): 707–12. http://dx.doi.org/10.1042/bj2250707.

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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.

33

Appleton, Evan, Jenhan Tao, Traci Haddock e Douglas Densmore. "Interactive assembly algorithms for molecular cloning". Nature Methods 11, n.º 6 (28 de abril de 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 e Claus Wasternack. "Molecular Cloning of Allene Oxide Cyclase". Journal of Biological Chemistry 275, n.º 25 (6 de abril de 2000): 19132–38. http://dx.doi.org/10.1074/jbc.m002133200.

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35

Hashimoto, T., K. Tamaki, K. i. Suzuki e Y. Yamada. "Molecular Cloning of Plant Spermidine Synthases". Plant and Cell Physiology 39, n.º 1 (1 de janeiro de 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, n.º 4 (1 de agosto de 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 e H. Phillip Koeffler. "Molecular Cloning of Transferrin Receptor 2". Journal of Biological Chemistry 274, n.º 30 (23 de julho de 1999): 20826–32. http://dx.doi.org/10.1074/jbc.274.30.20826.

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38

Kohler, Stefan A., Eric Menotti e Lukas C. Kühn. "Molecular Cloning of Mouse Glycolate Oxidase". Journal of Biological Chemistry 274, n.º 4 (22 de janeiro de 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 e Jing Jin. "Molecular cloning of human canstatin gene". World Chinese Journal of Digestology 12, n.º 10 (2004): 2329. http://dx.doi.org/10.11569/wcjd.v12.i10.2329.

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40

Madsen, Hans O., e J. Peter Hjorth. "Molecular cloning of mouse PSP mRNA". Nucleic Acids Research 13, n.º 1 (1985): 1–13. http://dx.doi.org/10.1093/nar/13.1.1.

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41

MIN, Kwan-Sik, Kunio SHIOTA e Tomoya OGAWA. "Molecular Cloning of Equine Preprorelaxin cDNA". Journal of Reproduction and Development 42, n.º 3 (1996): 171–78. http://dx.doi.org/10.1262/jrd.42.171.

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42

Murphy, Thomas J., Kasuhisa Takeuchi e R. Wayne Alexander. "Molecular Cloning of AT1 Angiotensin Receptors". American Journal of Hypertension 5, n.º 12_Pt_2 (dezembro de 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 e 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 e Wei-Min TIAN. "Cloning and Molecular Characterization ofHbCOI1fromHevea brasiliensis". Bioscience, Biotechnology, and Biochemistry 73, n.º 3 (23 de março de 2009): 665–70. http://dx.doi.org/10.1271/bbb.80721.

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45

Jiang, Pan Hong, Françoise Chany-Fournier e Charles Chany. "Sarcolectin: Complete purification for molecular cloning". Biochimie 81, n.º 7 (julho de 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 e Young-Sun Lin. "Molecular cloning of bovine telomerase RNA". Gene 221, n.º 1 (outubro de 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 e Masaaki Tatsuka. "Molecular cloning of mouse thioredoxin reductases". Gene 242, n.º 1-2 (janeiro de 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, n.º 7 (julho de 2006): 2099–107. http://dx.doi.org/10.1021/bm050158h.

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49

Grusby, Michael J., Steve C. Mitchell e Laurie H. Glimcher. "Molecular cloning of mouse cathepsin D". Nucleic Acids Research 18, n.º 13 (1990): 4008. http://dx.doi.org/10.1093/nar/18.13.4008.

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50

Zubriene, Asta, Saulute Budriene, Judita Lubiene e Gervydas Dienys. "Immobilized Alkaline Phosphatase for Molecular Cloning". Biocatalysis and Biotransformation 20, n.º 6 (janeiro de 2002): 423–27. http://dx.doi.org/10.1080/1024242021000040873.

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Artigos de revistas sobre o tema "Molecular cloning"

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