Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Stephanie C. Wright"'
Publikováno v:
Structure (London, England : 1993). 30(3)
Summary B cell lymphoma 6 (BCL6) is a transcriptional repressor that is deregulated in diffuse large B cell lymphoma, and the peptide aptamer, Apt48, inhibits BCL6 by an unknown mechanism. We report the crystal structure of BCL6 in complex with an Ap
Publikováno v:
IUCrJ
'IUCrJ ', vol: 8, pages: 154-160 (2021)
IUCrJ, Vol 8, Iss 2, Pp 154-160 (2021)
'IUCrJ ', vol: 8, pages: 154-160 (2021)
IUCrJ, Vol 8, Iss 2, Pp 154-160 (2021)
The BCL6 BTB domain has been adapted to form a promiscuous assembly block as a basis for affinity-capture crystallography.
The production of diffraction-quality protein crystals is challenging and often requires bespoke, time-consuming and expen
The production of diffraction-quality protein crystals is challenging and often requires bespoke, time-consuming and expen
Autor:
Stephen B. Carr, Stephanie C. Wright, Jonathan M. Hadden, Mark A. Stead, Chi H. Trinh, Gareth O. Rosbrook
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 64:1101-1104
BCL6 is a transcriptional repressor that is overexpressed in diffuse large B-cell lymphoma and follicular lymphoma. The N-terminal POZ domain of BCL6 interacts with transcriptional corepressors and targeting these associations is a promising therapeu
Autor:
Chi H. Trinh, Stephanie C. Wright, Thomas A. Edwards, James A. Garnett, Mark A. Stead, Stephen B. Carr, Andrew J. Baron
Publikováno v:
Journal of Molecular Biology. 373:820-826
The POZ/BTB domain is an evolutionarily conserved motif found in approximately 40 zinc-finger transcription factors (POZ-ZF factors). Several POZ-ZF factors are implicated in human cancer, and POZ domain interaction interfaces represent an attractive
Autor:
Elizabeth J. Fox, Stephanie C. Wright
Publikováno v:
Biochemical Journal. 370:307-313
Mad family proteins are transcriptional repressors that antagonize the activity of the c-Myc proto-oncogene product. Mad3 is expressed specifically during the S-phase of the cell cycle in both proliferating and differentiating cells, suggesting that
Autor:
Louise Kime, Stephanie C. Wright
Publikováno v:
Biochemical Journal. 370:291-298
Myc and Mad family proteins are central regulators of cellular proliferation and differentiation. We show that various Mad family genes have distinct patterns of expression during the chemically induced differentiation of mouse erythroleukaemia (MEL)
Autor:
Stephanie C. Wright, Mark A. Stead
Publikováno v:
Acta crystallographica. Section F, Structural biology communications. 70(Pt 12)
The POZ domain is an evolutionarily conserved protein–protein interaction domain that is found in approximately 40 mammalian transcription factors. POZ domains mediate both homodimerization and the heteromeric interactions of different POZ-domain t
Autor:
Mark A. Stead, Stephanie C. Wright
Publikováno v:
Bioscience Reports, Vol 34, Iss 3, p e00110 (2014)
Bioscience Reports
Bioscience Reports
Nac1 (nucleus accumbens 1) is a POZ (poxvirus and zinc finger)-domain transcriptional repressor that is expressed at high levels in ovarian serous carcinoma. Here we identify Nac1 as a novel interacting partner of the POZ-domain transcriptional activ
Autor:
Stephanie C. Wright, Elizabeth J. Fox
Publikováno v:
Biochemical Journal. 359:361-367
The Myc/Max/Mad transcription factor network plays a central role in the control of cellular proliferation, differentiation and apoptosis. In order to elucidate the biological function of Mad3, we have analysed the precise temporal patterns of Mad3 m
Autor:
Stephanie C. Wright, Gareth O. Rosbrook, Simon D. Connell, Stephen B. Carr, Helen J. Close, Christopher M. Harrison, Mark A. Stead, Laura K. van Geersdaele
Protein ubiquitination in eukaryotic cells is mediated by diverse E3 ligase enzymes that each target specific substrates. The cullin E3 ligase complexes are the most abundant class of E3 ligases; they contain various cullin components that serve as s
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https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c13a6cff8717d607cbb9d70a87a2f9b