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Relevant bibliographies by topics / 3’ terminal exon

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Academic literature on the topic '3’ terminal exon'

Author: Grafiati

Published: 9 March 2023

Last updated: 11 March 2023

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Journal articles on the topic "3’ terminal exon"

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Davis, Mary Beth, Jon Dietz, David M. Standiford, and Charles P. Emerson. "Transposable Element Insertions Respecify Alternative Exon Splicing in Three Drosophila Myosin Heavy Chain Mutants." Genetics 150, no. 3 (1998): 1105–14. http://dx.doi.org/10.1093/genetics/150.3.1105.

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Abstract Insertions of transposable elements into the myosin heavy chain (Mhc) locus disrupt the regulation of alternative pre-mRNA splicing for multi-alternative exons in the Mhc2, Mhc3, and Mhc4 mutants in Drosophila. Sequence and expression analyses show that each inserted element introduces a strong polyadenylation signal that defines novel terminal exons, which are then differentially recognized by the alternative splicing apparatus. Mhc2 and Mhc4 have insertion elements located within intron 7c and exon 9a, respectively, and each expresses a single truncated transcript that contains an a

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Lou, Hua, Karla M. Neugebauer, Robert F. Gagel, and Susan M. Berget. "Regulation of Alternative Polyadenylation by U1 snRNPs and SRp20." Molecular and Cellular Biology 18, no. 9 (1998): 4977–85. http://dx.doi.org/10.1128/mcb.18.9.4977.

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ABSTRACT Although considerable information is currently available about the factors involved in constitutive vertebrate polyadenylation, the factors and mechanisms involved in facilitating communication between polyadenylation and splicing are largely unknown. Even less is known about the regulation of polyadenylation in genes in which 3′-terminal exons are alternatively recognized. Here we demonstrate that an SR protein, SRp20, affects recognition of an alternative 3′-terminal exon via an effect on the efficiency of binding of a polyadenylation factor to an alternative polyadenylation site. T

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Lou, Hua, David M. Helfman, Robert F. Gagel, and Susan M. Berget. "Polypyrimidine Tract-Binding Protein Positively Regulates Inclusion of an Alternative 3′-Terminal Exon." Molecular and Cellular Biology 19, no. 1 (1999): 78–85. http://dx.doi.org/10.1128/mcb.19.1.78.

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ABSTRACT Polypyrimidine tract-binding protein (PTB) is an abundant vertebrate hnRNP protein. PTB binding sites have been found within introns both upstream and downstream of alternative exons in a number of genes that are negatively controlled by the binding of PTB. We have previously reported that PTB binds to a pyrimidine tract within an RNA processing enhancer located adjacent to an alternative 3′-terminal exon within the gene coding for calcitonin and calcitonin gene-related peptide. The enhancer consists of a pyrimidine tract and CAG directly abutting on a 5′ splice site sequence to form

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Le Sommer, Caroline, Michelle Lesimple, Agnès Mereau, Severine Menoret, Marie-Rose Allo, and Serge Hardy. "PTB Regulates the Processing of a 3′-Terminal Exon by Repressing both Splicing and Polyadenylation." Molecular and Cellular Biology 25, no. 21 (2005): 9595–607. http://dx.doi.org/10.1128/mcb.25.21.9595-9607.2005.

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ABSTRACT The polypyrimidine tract binding protein (PTB) has been described as a global repressor of regulated exons. To investigate PTB functions in a physiological context, we used a combination of morpholino-mediated knockdown and transgenic overexpression strategies in Xenopus laevis embryos. We show that embryonic endoderm and skin deficient in PTB displayed a switch of the α-tropomyosin pre-mRNA 3′ end processing to the somite-specific pattern that results from the utilization of an upstream 3′-terminal exon designed exon 9A9′. Conversely, somitic targeted overexpression of PTB resulted i

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Kim, J., J. J. Yim, S. Wang, and D. Dorsett. "Alternate use of divergent forms of an ancient exon in the fructose-1,6-bisphosphate aldolase gene of Drosophila melanogaster." Molecular and Cellular Biology 12, no. 2 (1992): 773–83. http://dx.doi.org/10.1128/mcb.12.2.773-783.1992.

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The fructose-1,6-bisphosphate aldolase gene of Drosophila melanogaster contains three divergent copies of an evolutionarily conserved 3' exon. Two mRNAs encoding aldolase contain three exons and differ only in the poly(A) site. The first exon is small and noncoding. The second encodes the first 332 amino acids, which form the catalytic domain, and is homologous to exons 2 through 8 of vertebrates. The third exon encodes the last 29 amino acids, thought to control substrate specificity, and is homologous to vertebrate exon 9. A third mRNA substitutes a different 3' exon (4a) for exon 3 and enco

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Kim, J., J. J. Yim, S. Wang, and D. Dorsett. "Alternate use of divergent forms of an ancient exon in the fructose-1,6-bisphosphate aldolase gene of Drosophila melanogaster." Molecular and Cellular Biology 12, no. 2 (1992): 773–83. http://dx.doi.org/10.1128/mcb.12.2.773.

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The fructose-1,6-bisphosphate aldolase gene of Drosophila melanogaster contains three divergent copies of an evolutionarily conserved 3' exon. Two mRNAs encoding aldolase contain three exons and differ only in the poly(A) site. The first exon is small and noncoding. The second encodes the first 332 amino acids, which form the catalytic domain, and is homologous to exons 2 through 8 of vertebrates. The third exon encodes the last 29 amino acids, thought to control substrate specificity, and is homologous to vertebrate exon 9. A third mRNA substitutes a different 3' exon (4a) for exon 3 and enco

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Parra, Marilyn K., Sherry L. Gee, Mark J. Koury, Narla Mohandas, and John G. Conboy. "Alternative 5′ exons and differential splicing regulate expression of protein 4.1R isoforms with distinct N-termini." Blood 101, no. 10 (2003): 4164–71. http://dx.doi.org/10.1182/blood-2002-06-1796.

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Abstract Among the alternative pre-mRNA splicing events that characterize protein 4.1R gene expression, one involving exon 2′ plays a critical role in regulating translation initiation and N-terminal protein structure. Exon 2′ encompasses translation initiation site AUG1 and is located between alternative splice acceptor sites at the 5′ end of exon 2; its inclusion or exclusion from mature 4.1R mRNA regulates expression of longer or shorter isoforms of 4.1R protein, respectively. The current study reports unexpected complexity in the 5′ region of the 4.1R gene that directly affects alternative

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Lou, H., Y. Yang, G. J. Cote, S. M. Berget, and R. F. Gagel. "An intron enhancer containing a 5' splice site sequence in the human calcitonin/calcitonin gene-related peptide gene." Molecular and Cellular Biology 15, no. 12 (1995): 7135–42. http://dx.doi.org/10.1128/mcb.15.12.7135.

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Regulation of calcitonin (CT)/calcitonin gene-related peptide (CGRP) RNA processing involves the use of alternative 3' terminal exons. In most tissues and cell lines, the CT terminal exon is recognized. In an attempt to define regulatory sequences involved in the utilization of the CT-specific terminal exon, we performed deletion and mutation analyses of a mini-gene construct that contains the CT terminal exon and mimics the CT processing choice in vivo. These studies identified a 127-nucleotide intron enhancer located approximately 150 nucleotides downstream of the CT exon poly(A) cleavage si

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Datson, Nicole A., Geoffrey M. Duyk, Gert-Jan B. van Ommen, and Johan T. Den Dunnen. "Specific isolation of 3′-terminal exons of human genes by exon trapping." Nucleic Acids Research 22, no. 20 (1994): 4148–53. http://dx.doi.org/10.1093/nar/22.20.4148.

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Tabaska, J. E., R. V. Davuluri, and M. Q. Zhang. "Identifying the 3'-terminal exon in human DNA." Bioinformatics 17, no. 7 (2001): 602–7. http://dx.doi.org/10.1093/bioinformatics/17.7.602.

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Dissertations / Theses on the topic "3’ terminal exon"

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Anquetil, Vincent. "Régulation tissulaire de l'épissage alternatif : Caractérisation fonctionnelle d'une séquence activatrice de la maturation d'un exon 3' terminal." Phd thesis, Université Rennes 1, 2009. http://tel.archives-ouvertes.fr/tel-00462347.

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La maturation des ARN pré-messagers est le fruit d'un ensemble de processus nucléaires interconnectés qui sont soumis à de nombreuses régulations. L'épissage alternatif des exons 3' terminaux joue un rôle majeur dans l'expression des gènes car il permet de réguler qualitativement et quantitativement leur expression. Nous étudions les déterminants de la régulation tissulaire de l'épissage et de la polyadénylation en utilisant comme modèle le gène de la tropomyosine α de xénope. Ce gène contient, dans sa région 3' terminale, un exon composite interne/3' terminal nommé 9A9' qui est utilisé comme

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Anquetil, Vincent. "Régulation tissulaire de l’épissage alternatif : caractérisation fonctionnelle d’une séquence activatrice de la maturation d’un exon 3’ terminal." Rennes 1, 2009. https://theses.hal.science/tel-00462347.

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L’épissage alternatif des exons 3’ terminaux permet de réguler qualitativement et quantitativement la production d’ARN messagers. Nous étudions les déterminants de la régulation tissulaire de l’épissage et de la polyadénylation en utilisant comme modèle le gène de la tropomyosine α de xénope qui contient, dans sa région 3’ terminale, l’exon composite interne/3’ terminal 9A9’, dont l’expression est tissu-spécifique. Les études in vivo précédemment réalisées au laboratoire ont permis d’identifier un élément intronique qui réprime l’exon 9A9’ dans les cellules non musculaires. La protéine PTB se

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FONTANA, GABRIELE ALESSANDRO. "Mitochondrial stress deregulates the expression of Brahma, a chromatin - remodeling factor that controls transcription and splicing of genes involved in axon growth and guidance." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2012. http://hdl.handle.net/10281/29856.

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The human protein Brahma (Brm), encoded by the SMARCA2 gene, is one of the two mutually exclusive ATPase subunits of the mammalian SWI/SNF-BAF chromatin-remodelling complex. Brm-containing BAF complexes are enriched in neurons, where they play crucial roles in the regulation of genes involved in neuronal differentiation. Moreover, it has been reported that Brm associates with components of the spliceosome to regulate the inclusion of alternative internal exons. While investigating with splicing-sensitive microarrays the gene expression changes triggered by mitochondrial stress, I found that

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Hamon, Gouault Sandra. "Etude de la maturation différentielle du gène alpha-fast tropomyosine chez xénopus Laevis : identifications d'éléments en cis régulant l'utilisation d'un exon composite interne/3' terminal." Rennes 1, 2002. http://www.theses.fr/2002REN10046.

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L'exon 9A/9' du gène de l'alpha-tropomyosine de Xenopus laevis est utilisé en tant qu'exon 3' terminal dans les cellules musculaires embryonnaires ou en tant qu'exon interne dans les muscles striés embryonnaires et adultes. Il est par contre exclu dans les cellules non musculaires. L'exon 9A/9' se caractérise par des sites d'épissage et un signal de polyadénylation suboptimaux ainsi que par un point de branchement éloigné situé à 274 pb en amont du site d'épissage 3'. Une approche par transgenèse transitoire dans l'embryon a permis de mettre en évidence deux éléments régulateurs chevauchants e

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ARNAULT, FREDERIC. "Contribution a l'etude du gene de la lipoproteine lipase (lpl) : etude de la partie 3' terminale du gene (exon 9-exon 10)." Paris 6, 1997. http://www.theses.fr/1997PA066203.

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Le gene de la lipoproteine lipase (lpl) code un enzyme triacylglycerol hydrolase (ec 3. 1. 1. 34) a role central dans le metabolisme des lipoparticules riches en triglycerides : il reste de nombreuses imprecisions quant aux motifs moleculaires participant aux interactions de la lpl avec ses effecteurs. Les regulations intervenant sur l'expression du gene, ou l'activite lpl, sont tres complexes et encore mal precisees. La lpl est impliquee dans certaines pathologies complexes : obesite, diabete, atherosclerose. Dans un travail preliminaire nous avons compare les sequences lpl actuellement connu

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Book chapters on the topic "3’ terminal exon"

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Krizman, David B. "Gene Identification by 3′ Terminal Exon Trapping." In Genetic Engineering. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4899-1766-9_4.

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Conference papers on the topic "3’ terminal exon"

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Bernaedi, F., V. Bertagnolo, S. Bartolai, L. Rossi, F. Panicucci, and F. Conconi. "A POINT MUTATION AND A GENE DELETION OF FVIII GENE IN SEVERE HAEMOPHILIA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644047.

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The presence of Factor VIII (FVIII) gene lesions has been investigated in 100 haemophilia A patients using cDNA probes for the 3'part of FVIII gene (exons 14-26 ).In two related severe patients without inhibitor a deletion removesthe exon 26; the gene lesion has been confirmed with several restriction enzymes and has been shown by densitometry of the autoradiographic pattern in a woman of the same family. The complete deletionof the exon 26 has been described by Gitschier et al. in a patient with inhibitor. Thus the comparison of the end points of the two deletions could help to define the mec

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Ploos van Amstel, J. K., A. L. van der Zanden, P. H. Reitsma, and R. M. Bertina. "RESTRICTION ANALYSIS AND SOUTHERN BLOTTING OF TOTAL HUMAN DNA REVEALS THE EXISTENCE OF MORE THAN ONE GENE HOMOLOGOUS WITH PROTEIN S cDNA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644639.

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A deficiency in protein S, the cofactor of activated protein C, is associated with an increased risk for the development of venous thrombosis. It is inherited as an autosomal dominant disorder. To improve the detection of heterozygotes in affected families, we have started to search for restriction fragment length polymorphism (RFLP) in the protein S gene. This study revealed the existence of two genes containing sequences homologous to protein S cDNA.Three non-overlapping fragments of clone pSUL5, which codes for the carboxy-terminal part of protein S and contains the complete 3' untranslated

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Loskutoff, D. J., J. Mimuro, and C. Hekman. "PLASMINOGEN ACTIVATOR INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644763.

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Plasminogen activation provides an important source of localized proteolytic activity not only during fibrinolysis, but also during ovulation, cell migration, epithelial cell differentiation, tumor invasion and a variety of other physiological processes. Precise regulation of plasminogen activator (PA) activity thus constitutes a critical feature of many biological processes. This control is achieved in large part through the action of specific PA inhibitors (PAIs). Although 4 distinct PAIs have been detected,1the endothelial cellTderived inhibitor (PAI-1) is the only one that efficiently inhi

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