Výsledky vyhledávání - "Justine Southby"

Repression of α-actinin SM exon splicing by assisted binding of PTB to the polypyrimidine tract

Autor: Clare Gooding, Christopher W.J. Smith, Justine Southby, Arianne J. Matlin

Publikováno v: RNA. 13:1214-1223

Polypyrimidine tract binding protein (PTB) acts as a regulatory repressor of a large number of alternatively spliced exons, often requiring multiple binding sites in order to repress splicing. In one case, cooperative binding of PTB has been shown to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e86fd42982ea7d110c3a61271660e6f4
https://doi.org/10.1261/rna.219607

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Polypyrimidine Tract Binding Protein Functions as a Repressor To Regulate Alternative Splicing of α-Actinin Mutally Exclusive Exons

Autor: Justine Southby, Christopher W.J. Smith, Clare Gooding

Publikováno v: Molecular and Cellular Biology. 19:2699-2711

The smooth muscle (SM) and nonmuscle (NM) isoforms of alpha-actinin are produced by mutually exclusive splicing of an upstream NM exon and a downstream SM-specific exon. A rat alpha-actinin genomic clone encompassing the mutually exclusive exons was

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62be720f47b39cb90b001a236fe06df2
https://doi.org/10.1128/mcb.19.4.2699

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Comparison of the pharmacokinetics of apricitabine in the presence and absence of ritonavir-boosted tipranavir: a phase I, open-label, controlled, single-centre study

Autor: Susan Cox, Otto Linet, Karie Tackwell, Marie Borin, Justine Southby, Kim Perry

Publikováno v: Clinical drug investigation. 29(11)

Apricitabine is a deoxycytidine analogue nucleoside reverse transcriptase inhibitor for the treatment of HIV infection. The aim of this phase I study was to investigate whether administration of apricitabine with the HIV protease inhibitor tipranavir

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::969819157dc7e41cf08abfada6dfb7bf
https://pubmed.ncbi.nlm.nih.gov/19813775

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Apricitabine--a novel nucleoside reverse transcriptase inhibitor for the treatment of HIV infection that is refractory to existing drugs

Autor: Susan Cox, Justine Southby

Publikováno v: Expert opinion on investigational drugs. 18(2)

Background: Apricitabine (ATC) is a nucleoside reverse transcriptase inhibitor (NRTI) being developed for the treatment of HIV. ATC has promising antiviral activity, including against HIV-1 containing reverse transcriptase mutations that confer resis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b23b475fa640e50dbbfb4f39cc1343e
https://pubmed.ncbi.nlm.nih.gov/19236266

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Regulation of alternative splicing by PTB and associated factors

Autor: Alexis P Rideau, Justine Southby, Nicholas J. McGlincy, Fiona Robinson, Matthew C Wollerton, Arianne J. Matlin, Sushma Nagaraja Grellscheid, Clare Gooding, Christopher W.J. Smith, R. Spellman

Publikováno v: Biochemical Society transactions. 33(Pt 3)

PTB (polypyrimidine tract-binding protein) is a repressive regulator of alternative splicing. We have investigated the role of PTB in three model alternative splicing systems. In the α-actinin gene, PTB represses the SM (smooth muscle) exon by bindi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::399f88bf39a41bbab773aafc825dddc5
https://pubmed.ncbi.nlm.nih.gov/15916540

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The PTB interacting protein raver1 regulates alpha-tropomyosin alternative splicing

Autor: A. D. J. Scadden, Justine Southby, Clare Gooding, Alexis P Rideau, Robert H. Singer, Stefan Hüttelmaier, Christopher W.J. Smith, Natalia Gromak

Publikováno v: The EMBO journal. 22(23)

Regulated switching of the mutually exclusive exons 2 and 3 of alpha-tropomyosin (TM) involves repression of exon 3 in smooth muscle cells. Polypyrimidine tract-binding protein (PTB) is necessary but not sufficient for regulation of TM splicing. Rave

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::437b3262e6e61b1da6a3d2c1e8bcaf0a
http://ora.ox.ac.uk/objects/uuid:b70ebd3f-7d51-4332-93cc-2da2781ac60b

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