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Journal articles on the topic 'Human Mutagenesis'

Author: Grafiati

Published: 4 June 2021

Last updated: 3 February 2022

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1

Rosenkranz, Herbert S., Ying Ping Zhang, Orest T. Macina, Donald R. Mattison, and Gilles Klopman. "Human developmental toxicity and mutagenesis." Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis 422, no. 2 (1998): 347–50. http://dx.doi.org/10.1016/s0027-5107(98)00170-5.

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2

Everson, Richard B., Karen L. Milne, Dorothy Warburton, Howard D. McClamrock, and Philip D. Buchanan. "Mutagenesis assays of human amniotic fluid." Environmental Mutagenesis 7, no. 2 (1985): 171–84. http://dx.doi.org/10.1002/em.2860070206.

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3

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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4

Olins, Peter O., S. Christopher Bauer, Sarah Braford-Goldberg, et al. "Saturation Mutagenesis of Human Interleukin-3." Journal of Biological Chemistry 270, no. 40 (1995): 23754–60. http://dx.doi.org/10.1074/jbc.270.40.23754.

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5

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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6

Shedlovsky, A., J. D. McDonald, D. Symula, and W. F. Dove. "Mouse models of human phenylketonuria." Genetics 134, no. 4 (1993): 1205–10. http://dx.doi.org/10.1093/genetics/134.4.1205.

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Abstract Phenylketonuria (PKU) results from a deficiency in phenylalanine hydroxylase, the enzyme catalyzing the conversion of phenylalanine (PHE) to tyrosine. Although this inborn error of metabolism was among the first in humans to be understood biochemically and genetically, little is known of the mechanism(s) involved in the pathology of PKU. We have combined mouse germline mutagenesis with screens for hyperphenylalaninemia to isolate three mutants deficient in phenylalanine hydroxylase (PAH) activity and cross-reactive protein. Two of these have reduced PAH mRNA and display characteristic

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7

Kaluka, Daniel, Dipanwita Batabyal, Bing-Yu Chiang, Thomas L. Poulos, and Syun-Ru Yeh. "Spectroscopic and Mutagenesis Studies of Human PGRMC1." Biochemistry 54, no. 8 (2015): 1638–47. http://dx.doi.org/10.1021/bi501177e.

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8

Marcelino, Luisa A., and William G. Thilly. "Mitochondrial mutagenesis in human cells and tissues." Mutation Research/DNA Repair 434, no. 3 (1999): 177–203. http://dx.doi.org/10.1016/s0921-8777(99)00028-2.

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9

Gang, Spencer S., Michelle L. Castelletto, Astra S. Bryant, et al. "Targeted mutagenesis in a human-parasitic nematode." PLOS Pathogens 13, no. 10 (2017): e1006675. http://dx.doi.org/10.1371/journal.ppat.1006675.

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10

Barbone, Francis P., Steven A. Middleton, Dana L. Johnson, et al. "Mutagenesis Studies of the Human Erythropoietin Receptor." Journal of Biological Chemistry 272, no. 8 (1997): 4985–92. http://dx.doi.org/10.1074/jbc.272.8.4985.

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11

Dellarco, Vicki L., Robert P. Erickson, Susan E. Lewis, and Michael D. Shelby. "Mutagenesis and human genetic disease: An introduction." Environmental and Molecular Mutagenesis 25, S2 (1995): 2–6. http://dx.doi.org/10.1002/em.2850250603.

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12

Kukimoto, Iwao. "Human Papillomavirus Carcinogenesis Mediated by APOBEC Mutagenesis." YAKUGAKU ZASSHI 139, no. 1 (2019): 75–79. http://dx.doi.org/10.1248/yakushi.18-00164-3.

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13

Oliveriusová, Jana, Vladimı́r Kery, Kenneth N. Maclean та Jan P. Kraus. "Deletion Mutagenesis of Human Cystathionine β-Synthase". Journal of Biological Chemistry 277, № 50 (2002): 48386–94. http://dx.doi.org/10.1074/jbc.m207087200.

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14

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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15

Kuga, Tetsuro, Yoshinori Komatsu, Motoo Yamasaki, et al. "Mutagenesis of human granulocyte colony stimulating factor." Biochemical and Biophysical Research Communications 159, no. 1 (1989): 103–11. http://dx.doi.org/10.1016/0006-291x(89)92410-8.

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16

Chatterjee, Nimrat, Yunfu Lin, Beatriz A. Santillan, Patricia Yotnda, and John H. Wilson. "Environmental stress induces trinucleotide repeat mutagenesis in human cells." Proceedings of the National Academy of Sciences 112, no. 12 (2015): 3764–69. http://dx.doi.org/10.1073/pnas.1421917112.

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The dynamic mutability of microsatellite repeats is implicated in the modification of gene function and disease phenotype. Studies of the enhanced instability of long trinucleotide repeats (TNRs)—the cause of multiple human diseases—have revealed a remarkable complexity of mutagenic mechanisms. Here, we show that cold, heat, hypoxic, and oxidative stresses induce mutagenesis of a long CAG repeat tract in human cells. We show that stress-response factors mediate the stress-induced mutagenesis (SIM) of CAG repeats. We show further that SIM of CAG repeats does not involve mismatch repair, nucleot

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17

Mackay, Graham A., Mark D. Hulett, Justin P. D. Cook та ін. "Mutagenesis Within Human FcεRIα Differentially Affects Human and Murine IgE Binding". Journal of Immunology 168, № 4 (2002): 1787–95. http://dx.doi.org/10.4049/jimmunol.168.4.1787.

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18

Gerdin, Matthew J., Faika Mseeh, and Margarita L. Dubocovich. "Mutagenesis studies of the human MT2 melatonin receptor." Biochemical Pharmacology 66, no. 2 (2003): 315–20. http://dx.doi.org/10.1016/s0006-2952(03)00239-9.

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19

AMUNDSON, S. A. "Alpha particle mutagenesis of human lymphoblastoid cell lines." International Journal of Radiation Biology 70, no. 2 (1996): 219–26. http://dx.doi.org/10.1080/095530096145210.

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20

Vallone, Beatrice, Andrea Bellelli, Adriana E. Miele, Maurizio Brunori та Giulio Fermi. "Probing the α1β2Interface of Human Hemoglobin by Mutagenesis". Journal of Biological Chemistry 271, № 21 (1996): 12472–80. http://dx.doi.org/10.1074/jbc.271.21.12472.

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21

Chan, Danny, Yi Ma Weng, Anne M. Hocking, Sue Golub, David J. McQuillan, and John F. Bateman. "Site-directed Mutagenesis of Human Type X Collagen." Journal of Biological Chemistry 271, no. 23 (1996): 13566–72. http://dx.doi.org/10.1074/jbc.271.23.13566.

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22

Ericson, Nolan G., Mariola Kulawiec, Marc Vermulst, et al. "Decreased Mitochondrial DNA Mutagenesis in Human Colorectal Cancer." PLoS Genetics 8, no. 6 (2012): e1002689. http://dx.doi.org/10.1371/journal.pgen.1002689.

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23

Besaratinia, Ahmad, and Gerd P. Pfeifer. "Sunlight ultraviolet irradiation andBRAFV600 mutagenesis in human melanoma." Human Mutation 29, no. 8 (2008): 983–91. http://dx.doi.org/10.1002/humu.20802.

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24

Liber, Howard L., Rupa Idate, Christy Warner, and Susan M. Bailey. "Radiation Quality and Mutagenesis in Human Lymphoblastoid Cells." Radiation Research 182, no. 4 (2014): 390. http://dx.doi.org/10.1667/rr13817.1.

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25

Burns, Michael B., Nuri A. Temiz, and Reuben S. Harris. "Evidence for APOBEC3B mutagenesis in multiple human cancers." Nature Genetics 45, no. 9 (2013): 977–83. http://dx.doi.org/10.1038/ng.2701.

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26

Molyneux, Sam D., Paul D. Waterhouse, Dawne Shelton, et al. "Human somatic cell mutagenesis creates genetically tractable sarcomas." Nature Genetics 46, no. 9 (2014): 964–72. http://dx.doi.org/10.1038/ng.3065.

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27

Schultz, Eric P., Jean-Marc Lanchy, Erin E. Ellerbeck, and Brent J. Ryckman. "Scanning Mutagenesis of Human Cytomegalovirus Glycoprotein gH/gL." Journal of Virology 90, no. 5 (2015): 2294–305. http://dx.doi.org/10.1128/jvi.01875-15.

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ABSTRACTThe core, conserved function of the herpesvirus gH/gL is to promote gB-mediated membrane fusion during entry, although the mechanism is poorly understood. The human cytomegalovirus (HCMV) gH/gL can exist as either the gH/gL/gO trimer or the gH/gL/UL128/UL130/UL131 (gH/gL/UL128-131) pentamer. One model suggests that gH/gL/gO provides the core fusion role during entry into all cells within the broad tropism of HCMV, whereas gH/gL/UL128-131 acts at an earlier stage, by a distinct receptor-binding mechanism to enhance infection of select cell types, such as epithelial cells, endothelial ce

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28

von Wurmb-Schwark, N., I. Jelkmann, H. D. Bruhn, and M. Oehmichen. "Variability of mitochondrial DNA mutagenesis in human blood." International Congress Series 1288 (April 2006): 112–14. http://dx.doi.org/10.1016/j.ics.2005.09.157.

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29

Iskow, Rebecca C., Michael T. McCabe, Ryan E. Mills, et al. "Natural Mutagenesis of Human Genomes by Endogenous Retrotransposons." Cell 141, no. 7 (2010): 1253–61. http://dx.doi.org/10.1016/j.cell.2010.05.020.

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30

Skafar, Debra F., and Shohei Koide. "Understanding the human estrogen receptor-alpha using targeted mutagenesis." Molecular and Cellular Endocrinology 246, no. 1-2 (2006): 83–90. http://dx.doi.org/10.1016/j.mce.2005.12.015.

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31

Zhou, D. J., K. R. Korzekwa, T. Poulos, and S. A. Chen. "A site-directed mutagenesis study of human placental aromatase." Journal of Biological Chemistry 267, no. 2 (1992): 762–68. http://dx.doi.org/10.1016/s0021-9258(18)48349-4.

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32

Grånäs, Charlotta, Gunnar Nordvall, and Dan Larhammar. "Site-directed mutagenesis of the human 5-HT1B receptor." European Journal of Pharmacology 349, no. 2-3 (1998): 367–75. http://dx.doi.org/10.1016/s0014-2999(98)00213-1.

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33

Kronenberg, Amy. "Perspectives on Fast-Neutron Mutagenesis of Human Lymphoblastoid Cells." Radiation Research 128, no. 1 (1991): S87. http://dx.doi.org/10.2307/3578008.

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34

Cipres-Palacin, Guadalupe, and Caroline M. Kane. "Alanine-Scanning Mutagenesis of Human Transcript Elongation Factor TFIIS." Biochemistry 34, no. 46 (1995): 15375–80. http://dx.doi.org/10.1021/bi00046a046.

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35

MARSH, KATHERINE L., EMMA L. MECZES, RONALD THORN, RICHARD MARSHALL та CAROLINE A. AUSTIN. "103 Site-directed mutagenesis of human DNA topoisomerase IIβ". Biochemical Society Transactions 25, № 4 (1997): S638. http://dx.doi.org/10.1042/bst025s638.

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36

Prendergast, Neal J., Tavner J. Delcamp, Philip L. Smith, and James H. Freisheim. "Expression and site-directed mutagenesis of human dihydrofolate reductase." Biochemistry 27, no. 10 (1988): 3664–71. http://dx.doi.org/10.1021/bi00410a022.

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37

Gao, Zhan-Guo, Qiaoling Jiang, Kenneth A. Jacobson, and Adriaan P. Ijzerman. "Site-directed mutagenesis studies of human A2A adenosine receptors." Biochemical Pharmacology 60, no. 5 (2000): 661–68. http://dx.doi.org/10.1016/s0006-2952(00)00357-9.

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38

Kikuchi, Norihisa, Kiyoshi Nagata, Masaru Shin, Kenji Mitsushima, Hiroshi Teraoka, and Nobuo Yoshida. "Site-Directed Mutagenesis of Human Pancreatic Secretory Trypsin Inhibitor." Journal of Biochemistry 106, no. 6 (1989): 1059–63. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a122964.

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39

Yang, In-Young, Grace Chan, Holly Miller, et al. "Mutagenesis by Acrolein-Derived Propanodeoxyguanosine Adducts in Human Cells†." Biochemistry 41, no. 46 (2002): 13826–32. http://dx.doi.org/10.1021/bi0264723.

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40

NICOLE, PASCAL, KAI DU, ALAIN COUVINEAU, and MARC LABURTHE. "Site-Directed Mutagenesis of Human VIP1 versus VIP2 Receptors." Annals of the New York Academy of Sciences 865, no. 1 VIP, PACAP, A (1998): 378–81. http://dx.doi.org/10.1111/j.1749-6632.1998.tb11199.x.

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41

Spaete, R. R., and E. S. Mocarski. "Insertion and deletion mutagenesis of the human cytomegalovirus genome." Proceedings of the National Academy of Sciences 84, no. 20 (1987): 7213–17. http://dx.doi.org/10.1073/pnas.84.20.7213.

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42

Fu, Yiping, Hong Wei Liu, Sean M. Forsythe, et al. "Mutagenesis analysis of human SM22: characterization of actin binding." Journal of Applied Physiology 89, no. 5 (2000): 1985–90. http://dx.doi.org/10.1152/jappl.2000.89.5.1985.

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SM22 is a 201-amino acid actin-binding protein expressed at high levels in smooth muscle cells. It has structural homology to calponin, but how SM22 binds to actin remains unknown. We performed site-directed mutagenesis to generate a series of NH2-terminal histidine (His)-tagged mutants of human SM22 in Escherichia coli and used these to analyze the functional importance of potential actin binding domains. Purified full-length recombinant SM22 bound to actin in vitro, as demonstrated by cosedimentation assay. Binding did not vary with calcium concentration. The COOH-terminal domain of SM22 is

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43

Ohare, M. C., V. A. Curry, R. E. Mitchell, and T. E. Cawston. "Stabilization of Purified Human Collagenase by Site-Directed Mutagenesis." Biochemical and Biophysical Research Communications 216, no. 1 (1995): 329–37. http://dx.doi.org/10.1006/bbrc.1995.2628.

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44

Armarego, Wilfred L. F., Hong-Ping Zhang, and Nan Yang. "In-vitro Site-directed Mutagenesis of Human Dihydropteridine Reductase." Pteridines 7, no. 3 (1996): 88–89. http://dx.doi.org/10.1515/pteridines.1996.7.3.88.

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45

Nault, Jean-Charles, Shalini Datta, Sandrine Imbeaud, et al. "Recurrent AAV2-related insertional mutagenesis in human hepatocellular carcinomas." Nature Genetics 47, no. 10 (2015): 1187–93. http://dx.doi.org/10.1038/ng.3389.

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46

Wang, Yan, Kazunori Yamaguchi, Yukiko Shimada, Xuejian Zhao, and Taeko Miyagi. "Site-directed mutagenesis of human membrane-associated ganglioside sialidase." European Journal of Biochemistry 268, no. 8 (2001): 2201–8. http://dx.doi.org/10.1046/j.1432-1327.2001.02069.x.

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47

Cho, Sung-Woo, Hye-Young Yoon, Jee-Yin Ahn, Eun-Young Lee, and Jongweon Lee. "Cassette mutagenesis of lysine 130 of human glutamate dehydrogenase." European Journal of Biochemistry 268, no. 11 (2001): 3205–13. http://dx.doi.org/10.1046/j.1432-1327.2001.02209.x.

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48

Chen, Junjian Z., and Fred F. Kadlubar. "Mitochondrial Mutagenesis and Oxidative Stress in Human Prostate Cancer." Journal of Environmental Science and Health, Part C 22, no. 1 (2004): 1–12. http://dx.doi.org/10.1081/gnc-120037931.

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49

Ricci, Giorgio, Mario Lo Bello, Anna Maria Caccuri, et al. "Site-directed Mutagenesis of Human Glutathione Transferase P1-1." Journal of Biological Chemistry 270, no. 3 (1995): 1243–48. http://dx.doi.org/10.1074/jbc.270.3.1243.

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50

Bello, Mario Lo, Andrea Battistoni, Anna P. Mazzetti, et al. "Site-directed Mutagenesis of Human Glutathione Transferase P1-1." Journal of Biological Chemistry 270, no. 3 (1995): 1249–53. http://dx.doi.org/10.1074/jbc.270.3.1249.

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