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Journal articles on the topic 'Gene family'

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Author: Grafiati

Published: 4 June 2021

Last updated: 20 February 2023

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1

Alam, S. M. Khorshed, Rupasri Ain, Toshihiro Konno, Jennifer K. Ho-Chen, and Michael J. Soares. "The rat prolactin gene family locus: species-specific gene family expansion." Mammalian Genome 17, no. 8 (August 2006): 858–77. http://dx.doi.org/10.1007/s00335-006-0010-1.

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2

Ehsani, Sepehr, Hairu Huo, Ashkan Salehzadeh, Cosmin L. Pocanschi, Joel C. Watts, Holger Wille, David Westaway, Ekaterina Rogaeva, Peter H. St. George-Hyslop, and Gerold Schmitt-Ulms. "Family reunion – The ZIP/prion gene family." Progress in Neurobiology 93, no. 3 (March 2011): 405–20. http://dx.doi.org/10.1016/j.pneurobio.2010.12.001.

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3

Töpel, Mats, and Paul Jarvis. "The Tic20 gene family." Plant Signaling & Behavior 6, no. 7 (July 2011): 1046–48. http://dx.doi.org/10.4161/psb.6.7.15631.

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4

Kaelin, William G. "The p53 gene family." Oncogene 18, no. 53 (December 1999): 7701–5. http://dx.doi.org/10.1038/sj.onc.1202955.

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5

Wong, Howard, and Michael C. Schotz. "The lipase gene family." Journal of Lipid Research 43, no. 7 (July 2002): 993–99. http://dx.doi.org/10.1194/jlr.r200007-jlr200.

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6

Mendoza, Michael, Garni Mandani, and Jamil Momand. "The MDM2 gene family." BioMolecular Concepts 5, no. 1 (March 1, 2014): 9–19. http://dx.doi.org/10.1515/bmc-2013-0027.

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AbstractMDM2 is an oncoprotein that blocks p53 tumor suppressor-mediated transcriptional transactivation, escorts p53 from the cell nucleus to the cytoplasm, and polyubiquitylates p53. Polyubiquitylated p53 is rapidly degraded in the cytoplasm by the 26S proteasome. MDM2 is abnormally upregulated in several types of cancers, especially those of mesenchymal origin. MDM4 is a homolog of MDM2 that also inhibits p53 by blocking p53-mediated transactivation. MDM4 is required for MDM2-mediated polyubiquitylated of p53 and is abnormally upregulated in several cancer types. MDM2 and MDM4 genes have been detected in all vertebrates to date and only a single gene homolog, named MDM, has been detected in some invertebrates. MDM2, MDM4, and MDM have similar gene structures, suggesting that MDM2 and MDM4 arose through a duplication event more than 440 million years ago. All members of this small MDM2 gene family contain a single really interesting new gene (RING) domain (with the possible exception of lancelet MDM) which places them in the RING-domain superfamily. Similar to MDM2, the vast majority of proteins with RING domains are E3 ubiquitin ligases. Other RING domain E3 ubiquitin ligases that target p53 are COP1, Pirh2, and MSL2. In this report, we present evidence that COP1, Pirh2, and MSL2 evolved independently of MDM2 and MDM4. We also show, through structure homology models of invertebrate MDM RING domains, that MDM2 is more evolutionarily conserved than MDM4.

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7

Liberles, David A., and Katharina Dittmar. "Characterizing gene family evolution." Biological Procedures Online 10, no. 1 (December 2008): 66–73. http://dx.doi.org/10.1251/bpo144.

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8

Parenti, Giancarlo, Germana Meroni, and Andrea Ballabio. "The sulfatase gene family." Current Opinion in Genetics & Development 7, no. 3 (June 1997): 386–91. http://dx.doi.org/10.1016/s0959-437x(97)80153-0.

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9

Bahram, S., and T. Spies. "The MIC gene family." Human Immunology 47, no. 1-2 (April 1996): 64. http://dx.doi.org/10.1016/0198-8859(96)85038-5.

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10

Macleod, Kay, Dominique Leprince, and Dominique Stehelin. "The ets gene family." Trends in Biochemical Sciences 17, no. 7 (July 1992): 251–56. http://dx.doi.org/10.1016/0968-0004(92)90404-w.

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11

Bahram, S., and T. Spies. "The MIC gene family." Research in Immunology 147, no. 5 (January 1996): 328–33. http://dx.doi.org/10.1016/0923-2494(96)89646-5.

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12

Kwon, Byoung S. "Pigmentation Genes: the Tyrosinase Gene Family and the pmel 17 Gene Family." Journal of Investigative Dermatology 100, s2 (February 1993): 134S—140. http://dx.doi.org/10.1111/1523-1747.ep12465022.

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13

Kwon, Byoung S. "Pigmentation Genes: the Tyrosinase Gene Family and the pmel 17 Gene Family." Journal of Investigative Dermatology 100, no. 2 (February 1993): S134—S140. http://dx.doi.org/10.1038/jid.1993.2.

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14

White, Mary E., and Brian I. Crother. "Gene Conversions May Obscure Actin Gene Family Relationships." Journal of Molecular Evolution 50, no. 2 (February 2000): 170–74. http://dx.doi.org/10.1007/s002399910018.

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15

Tang, D., H. Jiang, Y. Zhang, Y. Li, X. Zhang, and T. Zhou. "Cloning and sequencing of the complicated rDNA gene family of Bos taurus." Czech Journal of Animal Science 51, No. 10 (December 5, 2011): 425–28. http://dx.doi.org/10.17221/3960-cjas.

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The rDNA genes coding for ribosomal RNA (rRNA) in animals are repeat sequences with high GC content and complicated structure. Based on the sequences of human ribosomal DNA repeat unit and transcription unit and the long and accurate PCR method with LA Taq DNA polymerase and GC buffer, we were able to amplify the complicated repeat sequences of rDNA genes in Bos taurus. Three rDNA genes and 2 internal transcribed spacer (ITS) fragments were cloned and confirmed by sequencing. The conditions for the cloning of complicated DNA sequences such as special rules of primer design, improvement of the reaction system, selection of DNA polymerase and adjustment of cycle parameters were discussed.  

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16

Yang, Baoxue. "The Human Aquaporin Gene Family." Current Genomics 1, no. 1 (July 1, 2000): 91–102. http://dx.doi.org/10.2174/1389202003351832.

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17

Larsen, Knud. "The porcine cerebellin gene family." Gene 799 (October 2021): 145852. http://dx.doi.org/10.1016/j.gene.2021.145852.

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18

Fensterl, Volker, and Ganes C. Sen. "The ISG56/IFIT1 Gene Family." Journal of Interferon & Cytokine Research 31, no. 1 (January 2011): 71–78. http://dx.doi.org/10.1089/jir.2010.0101.

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19

Sleegers, Kristel, and Christine Van Broeckhoven. "Rogue gene in the family." Nature 458, no. 7237 (March 2009): 415–16. http://dx.doi.org/10.1038/458415a.

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20

Romano, Patrick G. N., Peter Horton, and Julie E. Gray. "The Arabidopsis Cyclophilin Gene Family." Plant Physiology 134, no. 4 (March 29, 2004): 1268–82. http://dx.doi.org/10.1104/pp.103.022160.

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21

Kaelin, W. G. "The Emerging p53 Gene Family." JNCI Journal of the National Cancer Institute 91, no. 7 (April 7, 1999): 594–98. http://dx.doi.org/10.1093/jnci/91.7.594.

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22

Strommer, Judith. "The plant ADH gene family." Plant Journal 66, no. 1 (March 28, 2011): 128–42. http://dx.doi.org/10.1111/j.1365-313x.2010.04458.x.

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23

Alt, F. W., R. DePinho, K. Zimmerman, E. Legouy, K. Hatton, P. Ferrier, A. Tesfaye, G. Yancopoulos, and P. Nisen. "The Human myc Gene Family." Cold Spring Harbor Symposia on Quantitative Biology 51 (January 1, 1986): 931–41. http://dx.doi.org/10.1101/sqb.1986.051.01.106.

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24

Farber, S. A. "The Zebrafish Annexin Gene Family." Genome Research 13, no. 6 (May 12, 2003): 1082–96. http://dx.doi.org/10.1101/gr.479603.

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25

Herz, J. "The LDL gene receptor family." Atherosclerosis 144 (May 1999): 3. http://dx.doi.org/10.1016/s0021-9150(99)80005-7.

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26

Acampora, Dario, Maurizio D'Esposito, Antonio Faiella, Maria Pannese, Enrica Migliaccio, Franco Morelli, Anna Stornaiuolo, Vincenzo Nigro, Antonio Simeone, and Edoardo Boncinelli. "The human HOX gene family." Nucleic Acids Research 17, no. 24 (1989): 10385–402. http://dx.doi.org/10.1093/nar/17.24.10385.

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27

Herz, Joachim. "The LDL Receptor Gene Family." Neuron 29, no. 3 (March 2001): 571–81. http://dx.doi.org/10.1016/s0896-6273(01)00234-3.

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28

Davis, J. Nathan, Laura McGhee, and Shari Meyers. "The ETO (MTG8) gene family." Gene 303 (January 2003): 1–10. http://dx.doi.org/10.1016/s0378-1119(02)01172-1.

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29

Akhtar, Tariq A., Yuki Matsuba, Ines Schauvinhold, Geng Yu, Hazel A. Lees, Samuel E. Klein, and Eran Pichersky. "The tomatocis-prenyltransferase gene family." Plant Journal 73, no. 4 (December 31, 2012): 640–52. http://dx.doi.org/10.1111/tpj.12063.

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30

Nuzzo, Regina. "Family history wins gene debate." Nature 509, no. 7501 (May 2014): 403. http://dx.doi.org/10.1038/509403e.

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31

Yoshida, Akira, Andrey Rzhetsky, Lily C. Hsu, and Cheng Chang. "Human aldehyde dehydrogenase gene family." European Journal of Biochemistry 251, no. 3 (February 1998): 549–57. http://dx.doi.org/10.1046/j.1432-1327.1998.2510549.x.

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32

Oates, Andrew C., Stephen J. Pratt, Brenda Vail, Yi-lin Yan, Robert K. Ho, Stephen L. Johnson, John H. Postlethwait, and Leonard I. Zon. "The zebrafish klf gene family." Blood 98, no. 6 (September 15, 2001): 1792–801. http://dx.doi.org/10.1182/blood.v98.6.1792.

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Abstract The Krüppel-like factor(KLF) family of genes encodes transcriptional regulatory proteins that play roles in differentiation of a diverse set of cells in mammals. For instance, the founding memberKLF1 (also known as EKLF) is required for normal globin production in mammals. Five new KLF genes have been isolated from the zebrafish, Danio rerio, and the structure of their products, their genetic map positions, and their expression during development of the zebrafish have been characterized. Three genes closely related to mammalian KLF2 andKLF4 were found, as was an ortholog of mammalianKLF12. A fifth gene, apparently missing from the genome of mammals and closely related to KLF1 and KLF2,was also identified. Analysis demonstrated the existence of novel conserved domains in the N-termini of these proteins. Developmental expression patterns suggest potential roles for these zebrafish genes in diverse processes, including hematopoiesis, blood vessel function, and fin and epidermal development. The studies imply a high degree of functional conservation of the zebrafish genes with their mammalian homologs. These findings further the understanding of theKLF genes in vertebrate development and indicate an ancient role in hematopoiesis for the Krüppel-like factorgene family.

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33

Hwang, Sue-Yun, Bermseok Oh, Zheng Zhang, Webb Miller, Davor Solter, and B. B. Knowles. "The mouse cornichon gene family." Development Genes and Evolution 209, no. 2 (February 15, 1999): 120–25. http://dx.doi.org/10.1007/s004270050234.

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34

Vogt, Richard G., Natalie E. Miller, Rachel Litvack, Richard A. Fandino, Jackson Sparks, Jon Staples, Robert Friedman, and Joseph C. Dickens. "The insect SNMP gene family." Insect Biochemistry and Molecular Biology 39, no. 7 (July 2009): 448–56. http://dx.doi.org/10.1016/j.ibmb.2009.03.007.

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35

Nakayama, Tatsuo, Shinji Takechi, and Yasunari Takami. "The chicken histone gene family." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 104, no. 4 (April 1993): 635–39. http://dx.doi.org/10.1016/0305-0491(93)90189-c.

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36

Papaioannou, Virginia E., and Lee M. Silver. "The T-box gene family." BioEssays 20, no. 1 (December 6, 1998): 9–19. http://dx.doi.org/10.1002/(sici)1521-1878(199801)20:1<9::aid-bies4>3.0.co;2-q.

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37

Sánchez, Rosario, Laura Arroyo, Pilar Luaces, Carlos Sanz, and Ana Pérez. "Olive Polyphenol Oxidase Gene Family." International Journal of Molecular Sciences 24, no. 4 (February 6, 2023): 3233. http://dx.doi.org/10.3390/ijms24043233.

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The phenolic compounds containing hydroxytyrosol are the minor components of virgin olive oil (VOO) with the greatest impact on its functional properties and health benefits. Olive breeding for improving the phenolic composition of VOO is strongly dependent on the identification of the key genes determining the biosynthesis of these compounds in the olive fruit and also their transformation during the oil extraction process. In this work, olive polyphenol oxidase (PPO) genes have been identified and fully characterized in order to evaluate their specific role in the metabolism of hydroxytyrosol-derived compounds by combining gene expression analysis and metabolomics data. Four PPO genes have been identified, synthesized, cloned and expressed in Escherichia coli, and the functional identity of the recombinant proteins has been verified using olive phenolic substrates. Among the characterized genes, two stand out: (i) OePPO2 with its diphenolase activity, which is very active in the oxidative degradation of phenols during oil extraction and also seems to be highly involved in the natural defense mechanism in response to biotic stress, and (ii) OePPO3, which codes for a tyrosinase protein, having diphenolase but also monophenolase activity, which catalyzes the hydroxylation of tyrosol to form hydroxytyrosol.

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38

Yao, Xiaohua, Yue Wang, Youhua Yao, Likun An, Yixiong Bai, Xin Li, Kunlun Wu, and Youming Qiao. "Use of gene family analysis to discover argonaut (AGO) genes for increasing the resistance of Tibetan hull-less barley to leaf stripe disease." Plant Protection Science 57, No. 3 (June 10, 2021): 226–39. http://dx.doi.org/10.17221/180/2020-pps.

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Leaf stripe is a common, but major infectious disease of barley, severely affecting the yield and quality. However, only a few genes have been identified by conventional gene mapping. Gene family analysis has become a fast and efficient strategy for gene discovery. Studies demonstrated that Argonaute (AGO) proteins play an important role in plant disease resistance. Thus, we obtained nine HvAGO genes via mRNA sequencing before and after a Pyrenophora graminea infection of a disease-resistant variety "Kunlun 14" and a susceptible variety "Z1141". We analysed the physicochemical characteristics, gene structures, and motifs of the HvAGO gene sequences and found that these proteins were divided into four clusters by evolutionary distance. There was high consistency in the number of exons, size, and the number and type of motifs in the different clusters. Based on protein phylogenetics, they could be divided into three branches. A collinearity analysis of Tibetan hull-less barley and Arabidopsis thaliana, rice, and maize showed that four genes were collinear with respect to the other three species. The qRT-PCR showed the expression levels of HvAGO1, HvAGO2 and HvAGO4 were significantly increased after infection with Pyrenophora graminea. These three members of the AGO gene family are, thus, speculated to play an important role in barley leaf stripe resistance. The results provide reference for the application of HvAGO genes in the leaf stripe control and the exploration of disease resistance genes in other crops.

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39

MacLean, James A., Diego Lorenzetti, Zhiying Hu, Will J. Salerno, Jonathan Miller, and Miles F. Wilkinson. "Rhox homeobox gene cluster: recent duplication of three family members." genesis 44, no. 3 (2006): 122–29. http://dx.doi.org/10.1002/gene.20193.

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40

Morisaki, T., K. Sermsuvitayawong, S. H. Byun, Y. Matsuda, K. Hidaka, H. Morisaki, and T. Mukai. "Mouse Mef2b Gene: Unique Member of MEF2 Gene Family." Journal of Biochemistry 122, no. 5 (November 1, 1997): 939–46. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a021855.

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41

Atchison, M., and M. Adesnik. "Gene conversion in a cytochrome P-450 gene family." Proceedings of the National Academy of Sciences 83, no. 8 (April 1, 1986): 2300–2304. http://dx.doi.org/10.1073/pnas.83.8.2300.

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42

Keebaugh, Alaine C., Robert T. Sullivan, and James W. Thomas. "Gene duplication and inactivation in the HPRT gene family." Genomics 89, no. 1 (January 2007): 134–42. http://dx.doi.org/10.1016/j.ygeno.2006.07.003.

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43

Tantikanjana, Titima, Mikhail E. Nasrallah, and June B. Nasrallah. "TheBrassica S gene family: Molecular characterization of theSLR2 gene." Sexual Plant Reproduction 9, no. 2 (March 1996): 107–16. http://dx.doi.org/10.1007/bf02153058.

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44

Liu, Ying, Yi-Bing Zhang, Ting-Kai Liu, and Jian-Fang Gui. "Lineage-Specific Expansion of IFIT Gene Family: An Insight into Coevolution with IFN Gene Family." PLoS ONE 8, no. 6 (June 20, 2013): e66859. http://dx.doi.org/10.1371/journal.pone.0066859.

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45

Janoušek, Václav, Robert C. Karn, and Christina M. Laukaitis. "The role of retrotransposons in gene family expansions: insights from the mouse Abp gene family." BMC Evolutionary Biology 13, no. 1 (2013): 107. http://dx.doi.org/10.1186/1471-2148-13-107.

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46

Wise, Dawnne O'Neal, Ralf Krahe, and Berl R. Oakley. "The γ-Tubulin Gene Family in Humans." Genomics 67, no. 2 (July 2000): 164–70. http://dx.doi.org/10.1006/geno.2000.6247.

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47

Kumar, Sudhir, Kristi A. Balczarek, and Zhi-Chun Lai. "Evolution of the hedgehog Gene Family." Genetics 142, no. 3 (March 1, 1996): 965–72. http://dx.doi.org/10.1093/genetics/142.3.965.

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Abstract Effective intercellular communication is an important feature in the development of multicellular organisms. Secreted hedgehog (hh) protein is essential for both long- and short-range cellular signaling required for body pattern formation in animals. In a molecular evolutionary study, we find that the vertebrate homologs of the Drosophila hh gene arose by two gene duplications: the first gave rise to Desert hh, whereas the second produced the Indian and Sonic hh genes. Both duplications occurred before the emergence of vertebrates and probably before the evolution of chordates. The amino-terminal fragment of the hh precursor, crucial in long- and short-range intercellular communication, evolves two to four times slower than the carboxyl-terminal fragment in both Drosophila hh and its vertebrate homologues, suggesting conservation of mechanism of hh action in animals. A majority of amino acid substitutions in the amino- and carboxyl-terminal fragments are conservative, but the carboxyl-terminal domain has undergone extensive insertion-deletion events while maintaining its autocleavage protease activity. Our results point to similarity of evolutionary constraints among sites of Drosophila and vertebrate hh homologs and suggest some future directions for understanding the role of hh genes in the evolution of developmental complexity in animals.

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48

Morisaki, Takayuki, and Hiroko Morisaki. "Ampd gene family in cardiac development." Gout and Nucleic Acid Metabolism 23, no. 1 (1999): 11–15. http://dx.doi.org/10.6032/gnam1999.23.1_11.

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49

Tayengwa, Reuben, Jianfei Zhao, Courtney F. Pierce, Breanna E. Werner, and Michael M. Neff. "Synopsis of theSOFLPlant-Specific Gene Family." G3: Genes|Genomes|Genetics 8, no. 4 (February 21, 2018): 1281–90. http://dx.doi.org/10.1534/g3.118.200040.

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50

Ye, Xin, Nikolas Nikolaidis, Masatoshi Nei, and Zhi-Chun Lai. "Evolution of the mob Gene Family." Open Cell Signaling Journal 1 (January 14, 2009): 1–11. http://dx.doi.org/10.2174/1876390100901010001.

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