Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Stephen H. Munroe"'
Publikováno v:
PLoS ONE, Vol 10, Iss 9, p e0137893 (2015)
The α-thyroid hormone receptor gene (TRα) codes for two functionally distinct proteins: TRα1, the α-thyroid hormone receptor; and TRα2, a non-hormone-binding variant. The final exon of TRα2 mRNA overlaps the 3' end of Rev-erbα mRNA, which enco
Externí odkaz:
https://doaj.org/article/985b297c94334dbfb21d395c3e255144
Publikováno v:
PLoS ONE, Vol 9, Iss 6, p e99430 (2014)
RNA surveillance plays an important role in posttranscriptional regulation. Seminal work in this field has largely focused on yeast as a model system, whereas exploration of RNA surveillance in mammals is only recently begun. The increased transcript
Externí odkaz:
https://doaj.org/article/84088b8eeaa44035bdac7476e9024d89
Publikováno v:
RNA Biology. 7:179-190
The discovery of increasing numbers of genes with overlapping sequences highlights the problem of expression in the context of constraining regulatory elements from more than one gene. This study identifies regulatory sequences encompassed within two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a194861a8f91ec37ec9f60fbbe49948
https://doi.org/10.4161/rna.7.2.11182
https://doi.org/10.4161/rna.7.2.11182
Publikováno v:
PLoS ONE, Vol 10, Iss 9, p e0137893 (2015)
PLoS ONE
PLoS ONE
The α-thyroid hormone receptor gene (TRα) codes for two functionally distinct proteins: TRα1, the α-thyroid hormone receptor; and TRα2, a non-hormone-binding variant. The final exon of TRα2 mRNA overlaps the 3’ end of Rev-erbα mRNA, which en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d41ad7b2c618b4cee140278e76e3804
http://europepmc.org/articles/PMC4569393?pdf=render
http://europepmc.org/articles/PMC4569393?pdf=render
Publikováno v:
Journal of Biological Chemistry. 275:11507-11513
Thyroid hormone (T(3)) coordinates growth, differentiation, and metabolism by binding to nuclear thyroid hormone receptors (TRs). The TRalpha gene encodes T(3)-activated TRalpha1 (NR1A1a) as well as an antagonistic, non-T(3)-binding alternatively spl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c75a217124b8603afaa08d39069a058
https://doi.org/10.1074/jbc.275.15.11507
https://doi.org/10.1074/jbc.275.15.11507
Publikováno v:
RNA. 4:1111-1123
hnRNP A1 regulates alternative splicing by antagonizing SR proteins. It consists of two closely related, tandem RNA-recognition motifs (RRMs), followed by a glycine-rich domain. Analysis of variant proteins with duplications, deletions, or swaps of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdacaef39feaa32de7a14e5a27382001
https://doi.org/10.1017/s135583829898089x
https://doi.org/10.1017/s135583829898089x
Autor:
Stephen H. Munroe
Publikováno v:
The FASEB Journal. 27
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::42900ca11a17861ff226bcdb59375d28
https://doi.org/10.1096/fasebj.27.1_supplement.775.2
https://doi.org/10.1096/fasebj.27.1_supplement.775.2
Publikováno v:
The EMBO Journal. 13:5483-5495
hnRNP A1 is a pre-mRNA binding protein that antagonizes the alternative splicing activity of splicing factors SF2/ASF or SC35, causing activation of distal 5' splice sites. The structural requirements for hnRNP A1 function were determined by mutagene
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad9c0c0f5849d91d85cacf5eabde6901
https://doi.org/10.1002/j.1460-2075.1994.tb06883.x
https://doi.org/10.1002/j.1460-2075.1994.tb06883.x
Publikováno v:
BMC Molecular Biology
BMC Molecular Biology, Vol 11, Iss 1, p 97 (2010)
BMC Molecular Biology, Vol 11, Iss 1, p 97 (2010)
Background Alternative processing of α-thyroid hormone receptor (TRα, NR1A1) mRNAs gives rise to two functionally antagonistic nuclear receptors: TRα1, the α-type receptor, and TRα2, a non-hormone binding variant that is found only in mammals. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb11d2c1e9af03bde8d04872c6158058
https://doi.org/10.1186/1471-2199-11-97
https://doi.org/10.1186/1471-2199-11-97
Autor:
Mitchell A. Lazar, Stephen H. Munroe
Publikováno v:
Journal of Biological Chemistry. 266:22083-22086
The rat erbA alpha locus encodes two overlapping mRNAs, alpha 1 and alpha 2, which are identical except for their most 3' exons. alpha 1 mRNA encodes a thyroid hormone receptor, while alpha 2 encodes an altered ligand binding domain of unknown functi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36cf37917108e9174938160be2aa76df
https://doi.org/10.1016/s0021-9258(18)54535-x
https://doi.org/10.1016/s0021-9258(18)54535-x