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Journal articles on the topic 'Encoding genes'

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Published: 10 March 2023

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1

Grierson, Don, Colin Bird, Dean DellaPenna, and Régie Mache. "Genes encoding polygalacturonases." Plant Molecular Biology Reporter 12, no. 2 (June 1994): S57. http://dx.doi.org/10.1007/bf02671571.

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2

Weeks, Don, Carolyn Silflow, Pete Snustad, and Don Fosket. "Genes encoding tubulins." Plant Molecular Biology Reporter 12, no. 2 (June 1994): S76. http://dx.doi.org/10.1007/bf02671579.

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3

Boon, T. "Genes encoding melanoma antigens." Melanoma Research 3, no. 1 (March 1993): 5. http://dx.doi.org/10.1097/00008390-199303000-00008.

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4

Xavier-Filho, J., and F. A. Paiva Campos. "Genes encoding protease inhibitors." Plant Molecular Biology Reporter 12, no. 2 (June 1994): S58—S59. http://dx.doi.org/10.1007/bf02671572.

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5

Zilinskas, Barbara A., Kozi Asada, Esra Galun, Dirk Inze, and Kunisuke Tanaka. "Genes encoding superoxide dismutases." Plant Molecular Biology Reporter 12, no. 2 (June 1994): S73—S74. http://dx.doi.org/10.1007/bf02671577.

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6

PARNES, JANE R. "Genes Encoding T-cell Antigens." Annals of the New York Academy of Sciences 546, no. 1 Molecular Bas (December 1988): 109–15. http://dx.doi.org/10.1111/j.1749-6632.1988.tb21625.x.

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7

Beyer, E., and V. Berthoud. "Mutations in Connexin-encoding genes." Acta Ophthalmologica 93 (September 23, 2015): n/a. http://dx.doi.org/10.1111/j.1755-3768.2015.0167.

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8

Gigot, Claude, and Steven Spiker. "Nomenclature of genes encoding histones." Plant Molecular Biology Reporter 12, no. 2 (June 1994): S39—S40. http://dx.doi.org/10.1007/bf02671566.

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9

Mundy, John, Robert Leah, Rebecca Boston, Yaeta Endo, and Fiorenzo Stirpe. "Genes encoding ribosome-inactivating proteins." Plant Molecular Biology Reporter 12, no. 2 (June 1994): S60—S62. http://dx.doi.org/10.1007/bf02671573.

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10

Showalter, Allan, Marcia Kieliszewski, Alice Cheung, and Mary Tierney. "Genes encoding cell wall proteins." Plant Molecular Biology Reporter 14, no. 1 (March 1996): 9–10. http://dx.doi.org/10.1007/bf02671896.

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11

Doran, James L., Wade H. Bingle, and Kenneth L. Roy. "Two human genes encoding tRNAGlyGCC." Gene 65, no. 2 (May 1988): 329–36. http://dx.doi.org/10.1016/0378-1119(88)90471-4.

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12

Valihrach, L., K. Demnerová, R. Karpíšková, and I. Melenová. "The expression of selected genes encoding enterotoxins in Staphylococcus aureus strains." Czech Journal of Food Sciences 27, Special Issue 2 (January 3, 2010): 56–65. http://dx.doi.org/10.17221/208/2009-cjfs.

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Staphylococcus aureus is an important food-borne pathogen, which produces many toxic substances that cause a variety of illnesses. Some strains of S. aureus produce thermostable enterotoxins that can be responsible for alimentary intoxication. The aim of this work was to establish a protocol for the study of 9 enterotoxin genes expression (sea-sej). First, a method for the detection of genes encoding enterotoxins was established and then a method for the determination of the expression of these genes was optimised, using a range of the PCR techniques (multiplex, touchdown and real-time). The expression of staphylococcal enterotoxin genes was evaluated both qualitatively and quantitatively. In present study were used S. aureus strains from culture collections as well as those newly-isolated from raw milk samples. The obtained results indicate the various expression of the different genes for enterotoxin. However the main benefit of this work is the established protocol for the study of enterotoxin gene expression, which can provide a better understanding of the conditions for the enterotoxins production.
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13

Klochko, V. V. "GENES ENCODING SYNTHESIS OF PHENAZINE-1-CARBOXYLIC ACID IN Pseudomonas batumici." Biotechnologia Acta 9, no. 5 (October 2016): 45–53. http://dx.doi.org/10.15407/biotech9.05.045.

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14

Deneris, E. S., J. Boulter, J. Connolly, E. Wada, K. Wada, D. Goldman, L. W. Swanson, J. Patrick, and S. Heinemann. "Genes encoding neuronal nicotinic acetylcholine receptors." Clinical Chemistry 35, no. 5 (May 1, 1989): 731–37. http://dx.doi.org/10.1093/clinchem/35.5.731.

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Abstract Four genes (alpha 2, alpha 3, alpha 4, and beta 2), which encode proteins homologous to the Torpedo electric organ and vertebrate muscle nicotinic acetylcholine receptors, have been identified by cloning rat brain cDNAs. Injection of transcripts derived from these cDNAs into Xenopus laevis oocytes results in the formation of three nicotinic acetylcholine receptors. Two of these receptors, alpha 3/beta 2 and alpha 4/beta 2, have the characteristics of ganglionic nicotinic receptors. The third (alpha 2/beta 2) exhibits a previously undescribed pharmacology and thus represents a novel subtype that may be expressed in the brain. The wide distribution of alpha 2, alpha 3, alpha 4, and beta 2 transcripts in the brain indicates that neuronal nicotinic acetylcholine receptors are a major neurotransmitter receptor system.
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15

Baumg�rtner, B., C. Klett, H. Hameister, A. Richter, and R. Knippers. "Mouse genes encoding DNA topoisomerase I." Mammalian Genome 5, no. 1 (January 1994): 19–25. http://dx.doi.org/10.1007/bf00360563.

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16

Weisberg, Robert A., Martin Freundlich, David Friedman, Jeffrey Gardner, Nora Goosen, Howard Nash, Amos Oppenheim, and Josette Rouvière‐Yaniv. "Nomenclature of the genes encoding IHF." Molecular Microbiology 19, no. 3 (February 1996): 642. http://dx.doi.org/10.1046/j.1365-2958.1996.t01-2-442924.x.

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17

Iacoviello, Licia, Michela Vischetti, Francesco Zito, and Maria Benedetta Donati. "Genes Encoding Fibrinogen and Cardiovascular Risk." Hypertension 38, no. 5 (November 2001): 1199–203. http://dx.doi.org/10.1161/hy1101.099478.

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18

Vierstra, Richard. "Genes encoding ubiquitin and related proteins." Plant Molecular Biology Reporter 12, no. 2 (June 1994): S77—S78. http://dx.doi.org/10.1007/bf02671580.

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19

Miller, Walter L. "Structure of genes encoding steroidogenic enzymes." Journal of Steroid Biochemistry 27, no. 4-6 (January 1987): 759–66. http://dx.doi.org/10.1016/0022-4731(87)90147-6.

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20

Bao, Wei-Guo, and Hiroshi Fukuhara. "The ubiquitin-encoding genes ofKluyveromyces lactis." Yeast 16, no. 4 (March 15, 2000): 343–51. http://dx.doi.org/10.1002/1097-0061(20000315)16:4<343::aid-yea534>3.0.co;2-f.

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21

Waryah, Charlene Babra, Jully Gogoi-Tiwari, Kelsi Wells, Karina Yui Eto, Elnaz Masoumi, Paul Costantino, Michael Kotiw, and Trilochan Mukkur. "Diversity of Virulence Factors Associated with West Australian Methicillin-SensitiveStaphylococcus aureusIsolates of Human Origin." BioMed Research International 2016 (2016): 1–10. http://dx.doi.org/10.1155/2016/8651918.

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An extensive array of virulence factors associated withS. aureushas contributed significantly to its success as a major nosocomial pathogen in hospitals and community causing variety of infections in affected patients. Virulence factors include immune evading capsular polysaccharides, poly-N-acetyl glucosamine, and teichoic acid in addition to damaging toxins including hemolytic toxins, enterotoxins, cytotoxins, exfoliative toxin, and microbial surface components recognizing adhesive matrix molecules (MSCRAMM). In this investigation, 31 West AustralianS. aureusisolates of human origin and 6 controls were analyzed for relative distribution of virulence-associated genes using PCR and/or an immunoassay kit and MSCRAMM by PCR-based typing. Genes encoding MSCRAMM, namely, Spa, ClfA, ClfB, SdrE, SdrD, IsdA, and IsdB, were detected in >90% of isolates. Gene encodingα-toxin was detected in >90% of isolates whereas genes encodingβ-toxin and SEG were detectable in 50–60% of isolates. Genes encoding toxin proteins, namely, SEA, SEB, SEC, SED, SEE, SEH, SEI, SEJ, TSST, PVL, ETA, and ETB, were detectable in >50% of isolates. Use of RAPD-PCR for determining the virulence factor-based genetic relatedness among the isolates revealed five cluster groups confirming genetic diversity among the MSSA isolates, with the greatest majority of the clinicalS. aureus(84%) isolates clustering in group IIIa.
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22

Cao, Bang Phi, and Anh Thi Van Le. "Metal transporter encoding gene families in Fabaceae: II. Cation/H+ exchanger (CAX) encoding genes." Science and Technology Development Journal - Natural Sciences 1, T3 (September 30, 2017): 27–36. http://dx.doi.org/10.32508/stdjns.v1it3.462.

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The plant CAtion/H+ eXchangers (CAX) proteins belong to Ca2+/cation antiporter (CaCA) superfamily. By using in silico methods, the CAX encoding genes in the genome of six legume species have been identified in this work. In examined legume genomes, the CAX genes belong to a small multigenic family. The number of the CAX genes in these legume species is 17 (soybean), 6 (common bean and C. cajan), 5 (M. truncatula and C. arietinum) and 3 genes (L. japonicus), respectively. The legume CAX genes vary in genomic full-length ranging from 1,213 to 11,561 base pairs. All of the genes exhibit introns (from 4 to 11 introns). Their deduced full-length protein sequences range from 248 to 718 amino acids. Theoretical pI values of most (39/42) of legume CAX proteins were less than 7. The secondary structure modelling of protein exhibit transmembrane helix region (from 3 to 11 regions). Half of all (23/42) included 11 transmembrane helix regions. Based on phylogeny analysis, all of the legume CAX were divided into two groups, A and B, each consisting of two subgroups. The phylogeny suggested an ancient gene duplication in the genome of legumes ancestry. The recent gene duplication even was only detected in the soybean genome after the speciation. The expression analysis showed that all of 3 L. japonicus CAX genes expressed in all examined tissues. However, the expression of C. cajan CAX genes was not detected. For each of 4 remaining legumes, the CAX genes were differed in their expression level depending on studied tissues. The tissue-specific expressions of some CAX genes were observed in 5 out of the 6 legume species, except C. cajan.
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23

Gopalan, V. "Xpro: database of eukaryotic protein-encoding genes." Nucleic Acids Research 32, no. 90001 (January 1, 2004): 59D—63. http://dx.doi.org/10.1093/nar/gkh051.

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24

Dohmoto, M. "Genes Encoding Nitrilase-like Proteins from Tobacco." DNA Research 7, no. 5 (January 1, 2000): 283–89. http://dx.doi.org/10.1093/dnares/7.5.283.

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25

Mak, Tak W., Nicolette Caccia, Tammy Cook, Veronica Vadasz, Yasunobu Yoshikai, Uik Sohn, Nobuhiro Kimura, and Barry Toyonaga. "Genes Encoding the T-Cell Antigen Receptor." Journal of Investigative Dermatology 85, no. 1 (July 1985): S107—S109. http://dx.doi.org/10.1111/1523-1747.ep12275570.

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26

Hancock, Kathy, and Stephen L. Hajduk. "Sequence ofTrypanosoma bruceitRNA genes encoding cytosolic tRNAs." Nucleic Acids Research 20, no. 10 (1992): 2602. http://dx.doi.org/10.1093/nar/20.10.2602.

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27

Berg, Darwin K., and Stanley W. Halvorsen. "Genes encoding nicotinic receptor subtypes on neurons." Nature 334, no. 6181 (August 1988): 384–85. http://dx.doi.org/10.1038/334384a0.

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28

Vanhoof, Raymond, Eleonora Hannecart-Pokorni, and Jean Content. "Nomenclature of Genes Encoding Aminoglycoside-Modifying Enzymes." Antimicrobial Agents and Chemotherapy 42, no. 2 (February 1, 1998): 483. http://dx.doi.org/10.1128/aac.42.2.483.

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29

STRINGER, SAUNDRA L., THOMAS GARBE, SUSAN M. SUNKIN, and JAMES R. STRINGER. "Genes Encoding Antigenic Surface Glycoproteins inPneumocystisfrom Humans." Journal of Eukaryotic Microbiology 40, no. 6 (November 1993): 821–26. http://dx.doi.org/10.1111/j.1550-7408.1993.tb04481.x.

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30

Koper, Teresa E., Amal F. El-Sheikh, Jeanette M. Norton, and Martin G. Klotz. "Urease-Encoding Genes in Ammonia-Oxidizing Bacteria." Applied and Environmental Microbiology 70, no. 4 (April 2004): 2342–48. http://dx.doi.org/10.1128/aem.70.4.2342-2348.2004.

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ABSTRACT Many but not all ammonia-oxidizing bacteria (AOB) produce urease (urea amidohydrolase, EC 3.5.1.5) and are capable of using urea for chemolithotrophic growth. We sequenced the urease operons from two AOB, the β-proteobacterium Nitrosospira sp. strain NpAV and the γ-proteobacterium Nitrosococcus oceani. In both organisms, all seven urease genes were contiguous: the three structural urease genes ureABC were preceded and succeeded by the accessory genes ureD and ureEFG, respectively. Green fluorescent protein reporter gene fusions revealed that the ure genes were under control of a single operon promoter upstream of the ureD gene in Nitrosococcus oceani. Southern analyses revealed two copies of ureC in the Nitrosospira sp. strain NpAV genome, while a single copy of the ure operon was detected in the genome of Nitrosococcus oceani. The ureC gene encodes the alpha subunit protein containing the active site and conserved nickel binding ligands; these conserved regions were suitable primer targets for obtaining further ureC sequences from additional AOB. In order to develop molecular tools for detecting the ureolytic ecotype of AOB, ureC genes were sequenced from several β-proteobacterial AOB. Pairwise identity values ranged from 80 to 90% for the UreC peptides of AOB within a subdivision. UreC sequences deduced from AOB urease genes and available UreC sequences in the public databases were used to construct alignments and make phylogenetic inferences. The UreC proteins from β-proteobacterial AOB formed a distinct monophyletic group. Unexpectedly, the peptides from AOB did not group most closely with the UreC proteins from other β-proteobacteria. Instead, it appears that urease in β-proteobacterial autotrophic ammonia oxidizers is the product of divergent evolution in the common ancestor of γ- and β-proteobacteria that was initiated before their divergence during speciation. Sequence motifs conserved for the proteobacteria and variable regions possibly discriminatory for ureC from β-proteobacterial AOB were identified for future use in environmental analysis of ureolytic AOB. These gene sequences are the first publicly available for ure genes from autotrophic AOB.
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31

Liu, Q. R., S. Mandiyan, H. Nelson, and N. Nelson. "A family of genes encoding neurotransmitter transporters." Proceedings of the National Academy of Sciences 89, no. 14 (July 15, 1992): 6639–43. http://dx.doi.org/10.1073/pnas.89.14.6639.

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32

Saxe, Stephen A., and Alan R. Kimmel. "Genes encoding novel GTP-binding proteins inDictyostelium." Developmental Genetics 9, no. 4-5 (1988): 259–65. http://dx.doi.org/10.1002/dvg.1020090408.

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33

Li, Xin-Liang, Silvia Špániková, Ronald P. de Vries, and Peter Biely. "Identification of genes encoding microbial glucuronoyl esterases." FEBS Letters 581, no. 21 (July 26, 2007): 4029–35. http://dx.doi.org/10.1016/j.febslet.2007.07.041.

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34

Frasch, A. C. C., J. J. Cazzulo, L. Åslund, and U. Pettersson. "Comparison of genes encoding Trypanosoma cruzi antigens." Parasitology Today 7, no. 6 (January 1991): 148–51. http://dx.doi.org/10.1016/0169-4758(91)90284-u.

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35

Douglas, Michael, and Masaharu Takeda. "Nuclear genes encoding mitochondrial proteins in yeast." Trends in Biochemical Sciences 10, no. 5 (May 1985): 192–94. http://dx.doi.org/10.1016/0968-0004(85)90189-6.

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36

van Peij, Noël N. M. E., Marco M. C. Gielkens, Ronald P. de Vries, Jaap Visser, and Leo H. de Graaff. "The Transcriptional Activator XlnR Regulates Both Xylanolytic and Endoglucanase Gene Expression inAspergillus niger." Applied and Environmental Microbiology 64, no. 10 (October 1, 1998): 3615–19. http://dx.doi.org/10.1128/aem.64.10.3615-3619.1998.

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ABSTRACT The expression of genes encoding enzymes involved in xylan degradation and two endoglucanases involved in cellulose degradation was studied at the mRNA level in the filamentous fungusAspergillus niger. A strain with a loss-of-function mutation in the xlnR gene encoding the transcriptional activator XlnR and a strain with multiple copies of this gene were investigated in order to define which genes are controlled by XlnR. The data presented in this paper show that the transcriptional activator XlnR regulates the transcription of thexlnB, xlnC, and xlnD genes encoding the main xylanolytic enzymes (endoxylanases B and C and β-xylosidase, respectively). Also, the transcription of the genes encoding the accessory enzymes involved in xylan degradation, including α-glucuronidase A, acetylxylan esterase A, arabinoxylan arabinofuranohydrolase A, and feruloyl esterase A, was found to be controlled by XlnR. In addition, XlnR also activates transcription of two endoglucanase-encoding genes, eglA andeglB, indicating that transcriptional regulation by XlnR goes beyond the genes encoding xylanolytic enzymes and includes regulation of two endoglucanase-encoding genes.
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37

Markusková, Barbora, Aneta Lichvariková, Tomáš Szemes, Janka Koreňová, Tomáš Kuchta, and Hana Drahovská. "Genome analysis of lactic acid bacterial strains selected as potential starters for traditional Slovakian bryndza cheese." FEMS Microbiology Letters 366, Supplement_1 (October 22, 2018): i3—i9. http://dx.doi.org/10.1093/femsle/fny257s.

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ABSTRACT Genomes of 21 strains of lactic acid bacteria isolated from Slovakian traditional cheeses were sequenced on an Illumina MiSeq platform. Subsequently, they were analysed regarding taxonomic classification, presence of genes encoding defence systems, antibiotic resistance and production of biogenic amines. Thirteen strains were found to carry genes encoding at least one bacteriocin, 18 carried genes encoding at least one restriction–modification system, all strains carried 1–6 prophages and 9 strains had CRISPR-Cas systems. CRISPR-Cas type II-A was the most common, containing 0–24 spacers. Only 10% spacers were found to be homological to known bacteriophage or plasmid sequences in databases. Two Enterococcus faecium strains and a Lactococcus lactis strain carried antibiotic resistance genes. Genes encoding for ornithine decarboxylase were detected in four strains and genes encoding for agmatine deiminase were detected in four strains. Lactobacillus paraplantarum 251 L appeared to be the most interesting strain, as it contained genes encoding for two bacteriocins, a restriction–modification system, two CRISPR-Cas systems, four prophages and no genes connected with antibiotic resistance or production of biogenic amines.
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38

White, P. C., D. Grossberger, B. J. Onufer, D. D. Chaplin, M. I. New, B. Dupont, and J. L. Strominger. "Two genes encoding steroid 21-hydroxylase are located near the genes encoding the fourth component of complement in man." Proceedings of the National Academy of Sciences 82, no. 4 (February 1, 1985): 1089–93. http://dx.doi.org/10.1073/pnas.82.4.1089.

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39

Kumar, T. Rajendra, and Martin M. Matzuk. "Cloning of the mouse gonadotropin β-subunit-encoding genes, II. Structure of the luteinizing hormone β-subunit-encoding genes." Gene 166, no. 2 (December 1995): 335–36. http://dx.doi.org/10.1016/0378-1119(96)81753-7.

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40

Osorio, Héctor, Patricio Tapia-Reyes, Daniela Espinoza, Daniel Laporte, Alberto González, Eduardo Castro-Nallar, and Alejandra Moenne. "The Genome of the Marine Alga Ulva compressa (Chlorophyta) Reveals Protein-Coding Genes with Similarity to Plants and Green Microalgae, but Also to Animal, Bacterial, and Fungal Genes." International Journal of Molecular Sciences 23, no. 13 (June 30, 2022): 7279. http://dx.doi.org/10.3390/ijms23137279.

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The genome of the marine alga Ulva compressa was assembled using long and short reads. The genome assembly was 80.8 Mb in size and encoded 19,207 protein-coding genes. Several genes encoding antioxidant enzymes and a few genes encoding enzymes that synthesize ascorbate and glutathione were identified, showing similarity to plant and bacterial enzymes. Additionally, several genes encoding signal transduction protein kinases, such as MAPKs, CDPKS, CBLPKs, and CaMKs, were also detected, showing similarity to plants, green microalgae, and bacterial proteins. Regulatory transcription factors, such as ethylene- and ABA-responsive factors, MYB, WRKY, and HSTF, were also present and showed similarity to plant and green microalgae transcription factors. Genes encoding enzymes that synthesize ACC and ABA-aldehyde were also identified, but oxidases that synthesize ethylene and ABA, as well as enzymes that synthesize other plant hormones, were absent. Interestingly, genes involved in plant cell wall synthesis and proteins related to animal extracellular matrix were also detected. Genes encoding cyclins and CDKs were also found, and CDKs showed similarity to animal and fungal CDKs. Few genes encoding voltage-dependent calcium channels and ionotropic glutamate receptors were identified as showing similarity to animal channels. Genes encoding Transient Receptor Potential (TRP) channels were not identified, even though TRPs have been experimentally detected, indicating that the genome is not yet complete. Thus, protein-coding genes present in the genome of U. compressa showed similarity to plant and green microalgae, but also to animal, bacterial, and fungal genes.
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41

Krogh, Susanne, Steen T. Jørgensen, and Kevin M. Devine. "Lysis Genes of the Bacillus subtilisDefective Prophage PBSX." Journal of Bacteriology 180, no. 8 (April 15, 1998): 2110–17. http://dx.doi.org/10.1128/jb.180.8.2110-2117.1998.

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ABSTRACT Four genes identified within the late operon of PBSX show characteristics expected of a host cell lysis system; they arexepA, encoding an exported protein; xhlA, encoding a putative membrane-associated protein; xhlB, encoding a putative holin; and xlyA, encoding a putative endolysin. In this work, we have assessed the contribution of each gene to host cell lysis by expressing the four genes in different combinations under the control of their natural promoter located on the chromosome of Bacillus subtilis 168. The results show thatxepA is unlikely to be involved in host cell lysis. Expression of both xhlA and xhlB is necessary to effect host cell lysis of B. subtilis. Expression ofxhlB (encoding the putative holin) together withxlyA (encoding the endolysin) cannot effect cell lysis, indicating that the PBSX lysis system differs from those identified in the phages of gram-negative bacteria. Since host cell lysis can be achieved when xlyA is inactivated, it is probable that PBSX encodes a second endolysin activity which also uses XhlA and XhlB for export from the cell. The chromosome-based expression system developed in this study to investigate the functions of the PBSX lysis genes should be a valuable tool for the analysis of other host cell lysis systems and for expression and functional analysis of other lethal gene products in gram-positive bacteria.
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42

Shramko, S. V., L. F. Gulyaeva, V. N. Zorina, and T. V. Tretyakova. "Proliferative diseases of the uterus: clinical, immunological, and molecular aspects." Voprosy ginekologii, akušerstva i perinatologii 19, no. 5 (2020): 13–21. http://dx.doi.org/10.20953/1726-1678-2020-5-13-21.

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Objective. To perform comparative analysis of clinical data, serum levels of acute-phase proteins, cytokines, steroid hormones, and expression of genes encoding sex hormone receptors in tissues of patients with proliferative diseases of the uterus. Patients and methods. We analyzed clinical data of 349 patients with various proliferative diseases of the uterus. We also evaluated their serum levels of α2-macroglobulin, pregnancy-associated α2-glycoprotein, their immunocomplexes with IgG, lactoferrin, VEGF, IL-6, TNFa, IL-8, and sex hormones. Uterine tissue samples were tested for the expression of genes encoding estrogen receptors α and β (ЕRα, ЕRβ) and progesterone receptors (PGR). Data analysis was performed using the statistical packages of SAS 9.4, STATISTICA12, and IBM-SPSS Statistics 22. Results. The changes in the level of acute-phase proteins indicated inflammation. In isolated uterine fibroids, expression of genes encoding progesterone receptors prevailed, whereas in isolated adenomyosis, expression of genes encoding estrogen receptors prevailed. Patients with both uterine fibroids and adenomyosis demonstrated similar levels of expression of genes encoding sex steroid hormone receptors. Tissues of uterine leiomyosarcoma were characterized by downregulated expression of genes encoding sex steroid hormone receptors. Conclusion. Upregulation of genes encoding progesterone receptors in isolated uterine fibroids confirms that therapy with progesterone receptor blockers is appropriate in this case. The predominance of expression of genes encoding estrogen receptors in isolated adenomyosis indicates local hyperestrogenism, justifying the use of progestogens and antiestrogens. Equal expression of genes encoding estrogen and progesterone receptors in patients with combined disease, as wells as high frequency of inflammatory changes in tissues and increased serum levels of inflammatory markers, proves the need for antiinflammatory therapy. Key words: adenomyosis, inflammation, steroid receptor genes, leiomyosarcoma, uterine fibroids, gene expression
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43

Vijayasarathy, S., Isabelle Ernest, Jane E. ltzhaki, David Sherman, Michael R. Mowatt, Paul A. M. Michael, and Christine E. Clayton. "The genes encoding fructose bisphosphate aldolase inTrypanosoma bruceiare interspersed with unrelated genes." Nucleic Acids Research 18, no. 10 (1990): 2967. http://dx.doi.org/10.1093/nar/18.10.2967.

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44

Urbanovich, O. Yu, P. V. Kuzmitskaya, and G. B. Borovskiy. "Polymorphism of two wheat degydrines genes." Faktori eksperimental'noi evolucii organizmiv 25 (August 30, 2019): 172–77. http://dx.doi.org/10.7124/feeo.v25.1160.

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Aim. The aim of this work is to study the nucleotide sequences variability of two genes encoding wheat dehydrins. One of them belong to K-2 group, the other refers to K-3 type (respectively, TaDHN18 and TaDHN19.3 according to the classification of Wang et al.). These loci sre interesting due to their's genes participation in protection of plants from the various adverse abioti ecffects. Methods. Polymorphism of two genes encoding dehydrins was investigated using 6 wheat varieties as examples, among which were spring and winter varieties with different cold resistance, using PCR-based cloning, sequencing, and data processing softwares. Results. An analysis of the obtained nucleotide and hypothetical protein sequences alignment showed that the locus under study in the genomes of different wheat varieties, both spring and winter, is characterized by a high identity degree. Conclusions. The high conservatism of two loci encoding K-2 and K-3 dehydrins was demonstrated. Keywords: wheat, dehydrins, polymorphism.
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TAMIYA, Toru. "Genes Encoding Snake Neurotoxins and Their Expression Products." Journal of the Mass Spectrometry Society of Japan 51, no. 1 (2003): 96–100. http://dx.doi.org/10.5702/massspec.51.96.

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Sundheim, Leif. "Cloning and conjugational transfer of chitinase encoding genes." Agricultural and Food Science 59, no. 3 (July 1, 1987): 209–15. http://dx.doi.org/10.23986/afsci.72265.

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A genomic library of chromosomal DNA from Serratia marcescens was constructed in the broad host range cosmid pLAFR3. Chitinase positive clones were identified on a chitin medium. By conjugational transfer chitinase encoding plasmids were transferred to Pseudomonas spp.
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Klenke, Stefanie, and Winfried Siffert. "SNPs in genes encoding G proteins in pharmacogenetics." Pharmacogenomics 12, no. 5 (May 2011): 633–54. http://dx.doi.org/10.2217/pgs.10.203.

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48

Surmacz, Liliana, Jolanta Wiejak, and Elzbieta Wyroba. "Cloning of two genes encoding Rab7 in Paramecium." Acta Biochimica Polonica 53, no. 1 (December 19, 2005): 149–56. http://dx.doi.org/10.18388/abp.2006_3373.

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Rab7 is a small GTPase that plays a crucial role in the regulation of transport from early to late endosomes and lysosomes, phagosome maturation and in lysosomal biogenesis in mammalian cells. It contains conserved and unique sequence elements that mediate its function. Two Rab7 genes, Rab7a (703 bp) and Rab7b (707 bp) were identified in the unicellular eukaryote Paramecium by PCR amplification. They contain three short introns of different lengths (28-32 bp) and sequence located at identical positions in both genes. The presence of two Rab7 genes in the Paramecium genome was confirmed by Southern hybridization analysis performed with six different restriction enzymes. Expression of both genes was assessed by Northern blot and RT-PCR. Two transcripts of 1.8 and 2.2 kb were identified by hybridization analysis. The cloned complementary DNAs, both of 618 nucleotides in length, encode polypeptides of 206 amino acids that are 97.6% identical and differ in their C-termini. The predicted protein sequences of Rab7a and Rab7b contain all characteristic domains essential for Rab function: the effector domain (YRATVGADF) and four GTP-binding consensus sequences (GDSGVGKT, WDTAGQ, NKLD, SAK) as well as the prenylation motif (-CC) at the C-terminus indispensable for Rab binding to the membrane. Similarity searches revealed 81.6-82.1% homology of Paramecium Rab7 isoforms to human Rab7 and a lack of an insert typical for the Kinetoplastida - the species that appeared earlier in evolution. Paramecium is the first free-living lower eukaryote in which homologues of Rab7 have been identified that exhibit features similar to those of mammalian Rab7.
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McMillan, R. Andrew, Terrence A. T. Lee, and Vincent P. Conticello. "Rapid Assembly of Synthetic Genes Encoding Protein Polymers." Macromolecules 32, no. 11 (June 1999): 3643–48. http://dx.doi.org/10.1021/ma981660f.

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Sakellaris, H., J. M. Pemberton, and J. M. Manners. "Genes from Cellvibrio mixtus encoding beta-1,3 endoglucanase." Applied and Environmental Microbiology 56, no. 10 (1990): 3204–8. http://dx.doi.org/10.1128/aem.56.10.3204-3208.1990.

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