Výsledky vyhledávání - "Claudia Lamprecht"

A Serine/Threonine-rich Motif Is One of Three Nuclear Localization Signals That Determine Unidirectional Transport of the Mineralocorticoid Receptor to the Nucleus

Autor: Amanda Carrigan, Laura Visentin, Ella Atlas, Gregory C. Addicks, Yanouchka Rouleau, Allison Edgecombe, Claudia Lamprecht, Yvonne A. Lefebvre, Robert J. G. Haché, Rhian F. Walther

Publikováno v: Journal of Biological Chemistry. 280:17549-17561

The mineralocorticoid receptor (MR) is a tightly regulated nuclear hormone receptor that selectively transmits corticosteroid signals. Steroid treatment transforms MR from a transcriptionally inert state, in which it is distributed equally between th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bdb218f176f3d8cd9928c1cf00a9bc0
https://doi.org/10.1074/jbc.m501548200

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Nuclear Export of the Glucocorticoid Receptor Is Accelerated by Cell Fusion-dependent Release of Calreticulin

Autor: Isabelle Groulx, Stephen Lee, Andrew Ridsdale, Robert J. G. Haché, Yvonne A. Lefebvre, Rhian F. Walther, Claudia Lamprecht

Publikováno v: Journal of Biological Chemistry. 278:37858-37864

Nucleocytoplasmic exchange of nuclear hormone receptors is hypothesized to allow for rapid and direct interactions with cytoplasmic signaling factors. In addition to recycling between a naïve, chaperone-associated cytoplasmic complex and a liganded

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::209205b25433402cd20a22c22ad1f6c4
https://doi.org/10.1074/jbc.m306356200

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Glucocorticoid Receptor Homodimers and Glucocorticoid-Mineralocorticoid Receptor Heterodimers Form in the Cytoplasm through Alternative Dimerization Interfaces

Autor: Yvonne A. Lefebvre, Claudia Lamprecht, Mingmin Liao, Gratien G. Prefontaine, Robert J. G. Haché, Rhian F. Walther, Joanne G.A. Savory

Publikováno v: Molecular and Cellular Biology. 21:781-793

Steroid hormone receptors act to regulate specific gene transcription primarily as steroid-specific dimers bound to palindromic DNA response elements. DNA-dependent dimerization contacts mediated between the receptor DNA binding domains stabilize DNA

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53bb3cfc6a86b821fb8459b536eea808
https://doi.org/10.1128/mcb.21.3.781-793.2001

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D-site binding protein transactivation requires the proline- and acid-rich domain and involves the coactivator p300

Autor: Claudia Lamprecht, Christopher R. Mueller

Publikováno v: The Journal of biological chemistry. 274(25)

The D-site binding protein (DBP) is a member of the proline- and acid-rich (PAR) domain subfamily of basic/leucine zipper proteins and is involved in transcriptional regulation in the liver. Deletion analysis of the DBP protein was carried out in an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03c0d98ee168e24cacb29ce92fc07887
https://pubmed.ncbi.nlm.nih.gov/10364202

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