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Artículos de revistas sobre el tema "Mutagenesi sito specifica"

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Publicado: 11 de marzo de 2023

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1

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 described strains which detect each of the base substitutions. We have examined a variety of mutagens and mutators for their ability to cause reversion to Lac+. Surprisingly, frameshifts are well stimulated at many of these runs by ethyl methanesulfonate, N-methyl-N'-nitro-N-nitrosoguanidine and 2-amino-purine, mutagens not widely known to induce frameshifts. A comparison of ethyl methanesulfonate, N-methyl-N'-nitro-N-nitrosoguanidine and 2-aminopurine frameshift specificity with that found with a mutH strain suggests that these mutagens partially or fully saturate or inactivate the methylation-directed mismatch repair system and allow replication errors leading to frameshifts to escape repair. This results in a form of indirect mutagenesis, which can be detected at certain sites.
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2

KURAMITSU, Seiki, and Hiroyuki KAGAMIYAMA. "Site-specific mutagenesis of aspartate aminotransferase." Seibutsu Butsuri 28, no. 1 (1988): 7–11. http://dx.doi.org/10.2142/biophys.28.7.

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3

Baldrich, Marcus, and Werner Goebel. "Rapid and efficient site-specific mutagenesis." "Protein Engineering, Design and Selection" 3, no. 6 (1990): 563. http://dx.doi.org/10.1093/protein/3.6.563.

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4

Inouye, Satoshi, Yili Guo, Nicholas Ling, and Shunichi Shimasaki. "Site-specific mutagenesis of human follistatin." Biochemical and Biophysical Research Communications 179, no. 1 (1991): 352–58. http://dx.doi.org/10.1016/0006-291x(91)91377-o.

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5

SOYFER, VALERY N. "Genetic Engineering and Site-Specific Mutagenesis." Annals of the New York Academy of Sciences 452, no. 1 (1985): 305–11. http://dx.doi.org/10.1111/j.1749-6632.1985.tb30017.x.

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6

Sambrook, Joseph, and David W. Russell. "Site-specific Mutagenesis by Overlap Extension." Cold Spring Harbor Protocols 2006, no. 1 (2006): pdb.prot3468. http://dx.doi.org/10.1101/pdb.prot3468.

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7

Foss, K., and William H. McClain. "Rapid site-specific mutagenesis in plasmids." Gene 59, no. 2-3 (1987): 285–90. http://dx.doi.org/10.1016/0378-1119(87)90336-2.

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8

Fujii, J., K. Maruyama, M. Tada, and D. H. MacLennan. "Expression and Site-specific Mutagenesis of Phospholamban." Journal of Biological Chemistry 264, no. 22 (1989): 12950–55. http://dx.doi.org/10.1016/s0021-9258(18)51579-9.

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9

Caffrey, Michael S., and Michael A. Cusanovich. "Site-specific mutagenesis studies of cytochromes c." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1187, no. 3 (1994): 277–88. http://dx.doi.org/10.1016/0005-2728(94)90001-9.

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10

Anthony-Cahill, Spencer J., Michael C. Griffith, Christopher J. Noren, Daniel J. Suich, and Peter G. Schultz. "Site-specific mutagenesis with unnatural amino acids." Trends in Biochemical Sciences 14, no. 10 (1989): 400–403. http://dx.doi.org/10.1016/0968-0004(89)90287-9.

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11

Mitchell, Nancy, and Gerhard Stöhrer. "Mutagenesis originating in site-specific DNA damage." Journal of Molecular Biology 191, no. 2 (1986): 177–80. http://dx.doi.org/10.1016/0022-2836(86)90254-8.

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12

Luisetti, Maurizio, та James Travis. "Bioengineering: α1-Proteinase Inhibitor Site-Specific Mutagenesis". Chest 110, № 6 (1996): 278S—283S. http://dx.doi.org/10.1378/chest.110.6_supplement.278s.

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13

MATTINGLY, JOSEPH R., and MARINO MARTINEZ-CARRION. "Site-Specific Mutagenesis in the Active Site of Aspartate Aminotransferase." Annals of the New York Academy of Sciences 585, no. 1 Vitamin B6 (1990): 526–28. http://dx.doi.org/10.1111/j.1749-6632.1990.tb28095.x.

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14

Char, Si Nian, Erica Unger-Wallace, Bronwyn Frame, et al. "Heritable site-specific mutagenesis using TALENs in maize." Plant Biotechnology Journal 13, no. 7 (2015): 1002–10. http://dx.doi.org/10.1111/pbi.12344.

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15

Larder, Brendan A., Dorothy J. M. Purifoy, Kenneth L. Powell, and Graham Darby. "Site-specific mutagenesis of AIDS virus reverse transcriptase." Nature 327, no. 6124 (1987): 716–17. http://dx.doi.org/10.1038/327716a0.

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16

Gupta, P. K., D. L. Johnson, T. M. Reid, M. S. Lee, L. J. Romano, and C. M. King. "Mutagenesis by single site-specific arylamine-DNA adducts." Journal of Biological Chemistry 264, no. 33 (1989): 20120–30. http://dx.doi.org/10.1016/s0021-9258(19)47227-x.

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17

Banga, S. S., and J. B. Boyd. "Oligonucleotide-directed site-specific mutagenesis in Drosophila melanogaster." Proceedings of the National Academy of Sciences 89, no. 5 (1992): 1735–39. http://dx.doi.org/10.1073/pnas.89.5.1735.

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18

Jenkins, Frank J., and Bernard Roizman. "Site-specific mutagenesis of large DNA viral genomes." BioEssays 5, no. 6 (1986): 244–47. http://dx.doi.org/10.1002/bies.950050603.

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19

Imai, Takeshi, Pierre Chambon, and Daniel Metzger. "Inducible site-specific somatic mutagenesis in mouse hepatocytes." genesis 26, no. 2 (2000): 147–48. http://dx.doi.org/10.1002/(sici)1526-968x(200002)26:2<147::aid-gene15>3.0.co;2-3.

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20

Chen, Jin-Tann, Ruth J. Mayer, Carol A. Fierke, and Stephen J. Benkovic. "Site-specific mutagenesis of dihydrofolate reductase fromEscherichia coli." Journal of Cellular Biochemistry 29, no. 2 (1985): 73–82. http://dx.doi.org/10.1002/jcb.240290203.

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21

Duran, Harry L., and Altaf A. Wani. "Site-specific gap-misrepair mutagenesis by O4-ethylthymine." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 908, no. 1 (1987): 60–69. http://dx.doi.org/10.1016/0167-4781(87)90022-4.

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22

Kunkel, T. A. "Rapid and efficient site-specific mutagenesis without phenotypic selection." Proceedings of the National Academy of Sciences 82, no. 2 (1985): 488–92. http://dx.doi.org/10.1073/pnas.82.2.488.

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23

CHANG, GWONG-JEN J., BARBARA J. B. JOHNSON, and DENNIS W. TRENT. "Site-Specific Oligonucleotide-Directed Mutagenesis Using T4 DNA Polymerase." DNA 7, no. 3 (1988): 211–17. http://dx.doi.org/10.1089/dna.1988.7.211.

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24

Carvalho, T. G., S. Thiberge, H. Sakamoto, and R. Menard. "Conditional mutagenesis using site-specific recombination in Plasmodium berghei." Proceedings of the National Academy of Sciences 101, no. 41 (2004): 14931–36. http://dx.doi.org/10.1073/pnas.0404416101.

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25

Tsuji, F. I., S. Inouye, T. Goto, and Y. Sakaki. "Site-specific mutagenesis of the calcium-binding photoprotein aequorin." Proceedings of the National Academy of Sciences 83, no. 21 (1986): 8107–11. http://dx.doi.org/10.1073/pnas.83.21.8107.

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26

Oda, Kimimitsu, Yoshio Misumi, Miwa Sohda, Noboru Takami, Yoshiyuki Sakaki, and Yukio Ikehara. "Selective processing of proalbumin determined by site-specific mutagenesis." Biochemical and Biophysical Research Communications 175, no. 2 (1991): 690–96. http://dx.doi.org/10.1016/0006-291x(91)91621-i.

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27

Page, John E., Chengyi Liang, Jane M. Sayer, Donald M. Jerina, and Anthony Dipple. "Site-Specific Mutagenesis with Benzo[a]Pyrene-Deoxyribonucleoside Adducts." Polycyclic Aromatic Compounds 16, no. 1-4 (2000): 99–108. http://dx.doi.org/10.1080/10406639908020577.

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28

Owens, Robert A., Rosemarie W. Hammond, Richard C. Gardner, Michael C. Kiefer, Susan M. Thompson, and Dean E. Cress. "Site-specific mutagenesis of potato spindle tuber viroid cDNA:." Plant Molecular Biology 6, no. 3 (1986): 179–92. http://dx.doi.org/10.1007/bf00021487.

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29

Miyazaki, Chie, Yoshitaka Iba, Yukio Yamada, Haruo Takahashi, Jun-ichi Sawada, and Yoshikazu Kurosawa. "Changes in the specificity of antibodies by site-specific mutagenesis followed by random mutagenesis." Protein Engineering, Design and Selection 12, no. 5 (1999): 407–15. http://dx.doi.org/10.1093/protein/12.5.407.

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30

Petrenko, V. A., S. M. Kipriyanov, A. N. Boldyrev, and P. I. Pozdnyakov. "Mutagenesis directed by phosphotriester analogues of oligonucleotides: A way to site-specific mutagenesis in vivo." FEBS Letters 238, no. 1 (1988): 109–12. http://dx.doi.org/10.1016/0014-5793(88)80236-9.

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31

Chen, I. T., and L. A. Chasin. "Direct selection for mutations affecting specific splice sites in a hamster dihydrofolate reductase minigene." Molecular and Cellular Biology 13, no. 1 (1993): 289–300. http://dx.doi.org/10.1128/mcb.13.1.289-300.1993.

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A Chinese hamster cell line containing an extra exon 2 (50 bp) inserted into a single intron of a dihydrofolate reductase (dhfr) minigene was constructed. The extra exon 2 was efficiently spliced into the RNA, resulting in an mRNA that is incapable of coding for the DHFR enzyme. Mutations that decreased splicing of this extra exon 2 caused it to be skipped and so produced normal dhfr mRNA. In contrast to the parental cell line, the splicing mutants display a DHFR-positive growth phenotype. Splicing mutants were isolated from this cell line after treatment with four different mutagens (racemic benzo[c]phenanthrene diol epoxide, ethyl methanesulfonate, ethyl nitrosourea, and UV irradiation). By polymerase chain reaction amplification and direct DNA sequencing, we determined the base changes in 66 mutants. Each of the mutagens generated highly specific base changes. All mutations were single-base substitutions and comprised 24 different changes distributed over 16 positions. Most of the mutations were within the consensus sequences at the exon 2 splice donor, acceptor, and branch sites. The RNA splicing patterns in the mutants were analyzed by quantitative reverse transcription-polymerase chain reaction. The recruitment of cryptic sites was rarely seen; simple exon skipping was the predominant mutant phenotype. The wide variety of mutations that produced exon skipping suggests that this phenotype is the typical consequence of splice site damage and supports the exon definition model of splice site selection. A few mutations were located outside the consensus sequences, in the exon or between the branch point and the polypyrimidine tract, identifying additional positions that play a role in splice site definition. That most of these 66 mutations fell within consensus sequences in this near-saturation mutagenesis suggests that splicing signals beyond the consensus may consist of robust RNA structures.
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32

Chen, I. T., and L. A. Chasin. "Direct selection for mutations affecting specific splice sites in a hamster dihydrofolate reductase minigene." Molecular and Cellular Biology 13, no. 1 (1993): 289–300. http://dx.doi.org/10.1128/mcb.13.1.289.

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A Chinese hamster cell line containing an extra exon 2 (50 bp) inserted into a single intron of a dihydrofolate reductase (dhfr) minigene was constructed. The extra exon 2 was efficiently spliced into the RNA, resulting in an mRNA that is incapable of coding for the DHFR enzyme. Mutations that decreased splicing of this extra exon 2 caused it to be skipped and so produced normal dhfr mRNA. In contrast to the parental cell line, the splicing mutants display a DHFR-positive growth phenotype. Splicing mutants were isolated from this cell line after treatment with four different mutagens (racemic benzo[c]phenanthrene diol epoxide, ethyl methanesulfonate, ethyl nitrosourea, and UV irradiation). By polymerase chain reaction amplification and direct DNA sequencing, we determined the base changes in 66 mutants. Each of the mutagens generated highly specific base changes. All mutations were single-base substitutions and comprised 24 different changes distributed over 16 positions. Most of the mutations were within the consensus sequences at the exon 2 splice donor, acceptor, and branch sites. The RNA splicing patterns in the mutants were analyzed by quantitative reverse transcription-polymerase chain reaction. The recruitment of cryptic sites was rarely seen; simple exon skipping was the predominant mutant phenotype. The wide variety of mutations that produced exon skipping suggests that this phenotype is the typical consequence of splice site damage and supports the exon definition model of splice site selection. A few mutations were located outside the consensus sequences, in the exon or between the branch point and the polypyrimidine tract, identifying additional positions that play a role in splice site definition. That most of these 66 mutations fell within consensus sequences in this near-saturation mutagenesis suggests that splicing signals beyond the consensus may consist of robust RNA structures.
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33

Li, Ming, Omar S. Akbari, and Bradley J. White. "Highly Efficient Site-Specific Mutagenesis in Malaria Mosquitoes Using CRISPR." G3&#58; Genes|Genomes|Genetics 8, no. 2 (2017): 653–58. http://dx.doi.org/10.1534/g3.117.1134.

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34

Yuan, Lin, and Hak-Jung Kim. "Characterization of Human Cytosolic Thioredoxin Reductase by Site-specific Mutagenesis." Bulletin of the Korean Chemical Society 31, no. 12 (2010): 3515–16. http://dx.doi.org/10.5012/bkcs.2010.31.12.3515.

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35

Baldwin, Jack E., Stephen L. Martin, and John D. Sutherland. "Site-specific forced misincorporation mutagenesis using modified T7 DNA polymerase." "Protein Engineering, Design and Selection" 4, no. 5 (1991): 579–84. http://dx.doi.org/10.1093/protein/4.5.579.

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36

Brocard, J., X. Warot, O. Wendling, et al. "Spatio-temporally controlled site-specific somatic mutagenesis in the mouse." Proceedings of the National Academy of Sciences 94, no. 26 (1997): 14559–63. http://dx.doi.org/10.1073/pnas.94.26.14559.

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37

Semler, Bert L., Victoria H. Johnson, Patricia Gillis Dewalt, and Mary Frances Ypma-Wong. "Site-specific mutagenesis of cDNA clones expressing a poliovirus proteinase." Journal of Cellular Biochemistry 33, no. 1 (1987): 39–51. http://dx.doi.org/10.1002/jcb.240330105.

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38

Pellar, Gregory J., and Patrick J. DiMario. "Deletion and site-specific mutagenesis of nucleolin's carboxy GAR domain." Chromosoma 111, no. 7 (2003): 461–69. http://dx.doi.org/10.1007/s00412-003-0231-y.

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39

Hung, Chih-Hung, Ming-Chih Lee, and Jung-Yaw Lin. "Inactivation of Acacia confusa trypsin inhibitor by site-specific mutagenesis." FEBS Letters 353, no. 3 (1994): 312–14. http://dx.doi.org/10.1016/0014-5793(94)01066-8.

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40

Zhang, Yang, and Evan R. Kantrowitz. "Probing the regulatory site of Escherichia coli aspartate transcarbamoylase by site-specific mutagenesis." Biochemistry 31, no. 3 (1992): 792–98. http://dx.doi.org/10.1021/bi00118a022.

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41

Eri Nobusawa, Katsuhisa Nakajima, and Setsuko Nakajima. "Investigation of an antigenic determinant site on haemagglutinin molecule by site specific mutagenesis." Virus Research 3 (September 1985): 58. http://dx.doi.org/10.1016/0168-1702(85)90367-3.

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42

Zeng, Chenbo, and Herbert J. Fromm. "Active Site Residues of Human Brain Hexokinase as Studied by Site-specific Mutagenesis." Journal of Biological Chemistry 270, no. 18 (1995): 10509–13. http://dx.doi.org/10.1074/jbc.270.18.10509.

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43

Inglese, James, John M. Smith, and Stephen J. Benkovic. "Active-site mapping and site-specific mutagenesis of glycinamide ribonucleotide transformylase from Escherichia coli." Biochemistry 29, no. 28 (1990): 6678–87. http://dx.doi.org/10.1021/bi00480a018.

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44

Chouljenko, Vladimir, Sukhanya Jayachandra, Galina Rybachuk, and Konstantin G. Kousoulas. "Efficient Long-PCR Site-Specific Mutagenesis of a High GC Template." BioTechniques 21, no. 3 (1996): 472–80. http://dx.doi.org/10.2144/96213st05.

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45

Eghtedarzadeh-Kondri, Mohammad, Michael A. Walls, and Scott M. Glaser. "Site-Specific Mutagenesis of Immunoglobulin Domains by Multiple-Fragment Homologous Recombination." BioTechniques 23, no. 5 (1997): 830–34. http://dx.doi.org/10.2144/97235bm14.

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46

Huang, Honglin, Denis Jeanteur, Franc Pattus, and Robert E. W. Hancock. "Membrane topology and site-specific mutagenesis of Pseudomonas aeruginosa porin OprD." Molecular Microbiology 16, no. 5 (1995): 931–41. http://dx.doi.org/10.1111/j.1365-2958.1995.tb02319.x.

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47

Cianciotto, Nicholas P., Robert Long, Barry I. Eisenstein, and N. Cary Engleberg. "Site-specific mutagenesis inLegionella pneumophilaby allelic exchange using counterselectable ColE1 vectors." FEMS Microbiology Letters 56, no. 2 (1988): 203–7. http://dx.doi.org/10.1111/j.1574-6968.1988.tb03178.x.

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48

GUINET, Francoise, Jean-Dominique GUITTON, Nathalie GAULT, et al. "Interleukin-1beta-specific partial agonists defined by site-directed mutagenesis studies." European Journal of Biochemistry 211, no. 3 (1993): 583–90. http://dx.doi.org/10.1111/j.1432-1033.1993.tb17585.x.

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49

Komissarov, Andrey A., Marie T. Marchbank, Michael J. Calcutt, Thomas P. Quinn, and Susan L. Deutscher. "Site-specific Mutagenesis of a Recombinant Anti-single-stranded DNA Fab." Journal of Biological Chemistry 272, no. 43 (1997): 26864–70. http://dx.doi.org/10.1074/jbc.272.43.26864.

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50

Nishimura, Chiaki, Kensuke Futatsugi, Kiyoshi Yasukawa, Tadamitsu Kishimoto, and Yoji Arata. "Site-specific mutagenesis of human interleukin-6 and its biological activity." FEBS Letters 281, no. 1-2 (1991): 167–69. http://dx.doi.org/10.1016/0014-5793(91)80384-f.

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