Výsledky vyhledávání - "O S, Gabrielsen"

Redox regulation of AMP synthesis in yeast: a role of the Bas1p and Bas2p transcription factors

Autor: B, Pinson, O S, Gabrielsen, B, Daignan-Fornier

Publikováno v: Molecular microbiology. 36(6)

Expression of yeast AMP synthesis genes (ADE genes) was severely affected when cells were grown under oxidative stress conditions. To get an insight into the molecular mechanisms of this new transcriptional regulation, the role of the Bas1p and Bas2p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d312c39c0ff4585226af45c6aad29975
https://pubmed.ncbi.nlm.nih.gov/10931295

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Sequence selectivity of c-Myb in vivo. Resolution of a DNA target specificity paradox

Autor: K B, Andersson, T, Berge, V, Matre, O S, Gabrielsen

Publikováno v: The Journal of biological chemistry. 274(31)

We have investigated the basis for the striking difference between the broad DNA sequence selectivity of the c-Myb transcription factor minimal DNA-binding domain R(2)R(3) in vitro and the more restricted preference of a R(2)R(3)VP16 protein for Myb-

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https://pubmed.ncbi.nlm.nih.gov/10419522

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Capillary electrophoretic mobility shift assay (CEMSA) of a protein-DNA complex

Autor: B, Xue, O S, Gabrielsen, A H, Myrset

Publikováno v: Journal of capillary electrophoresis. 4(5)

The utility of capillary electrophoresis in the study of DNA-protein binding is demonstrated, using the minimal DNA binding domain of the onco-protein c-Myb (R2R3) and a specific target DNA sequence as a model system. The capillary electrophoresis me

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https://pubmed.ncbi.nlm.nih.gov/9725121

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Flexibility in the second half-site sequence recognised by the c-Myb R2 domain--in vitro and in vivo analysis

Autor: E, Ording, S, Bergholtz, E M, Brendeford, N, Jamin, O S, Gabrielsen

Publikováno v: Oncogene. 13(5)

The oncoprotein c-Myb is a transcription factor that recognises its specific target sequences through two subdomains. The R3-domain binds the first half-site, YAAC, and plays a dominant role in sequence recognition, while the homologous R2-domain int

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8f851bb480cfebf66895241b8edc8352
https://pubmed.ncbi.nlm.nih.gov/8806694

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DNA-binding domain and recognition sequence of the yeast BAS1 protein, a divergent member of the Myb family of transcription factors

Autor: I, Høvring, A, Bostad, E, Ording, A H, Myrset, O S, Gabrielsen

Publikováno v: The Journal of biological chemistry. 269(26)

The yeast BAS1 protein is a transcriptional activator with an amino-terminal domain homologous to the DNA-binding domain of the oncoprotein Myb containing three imperfect tryptophan-rich repeats. In contrast to Myb-related transcription factors from

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https://pubmed.ncbi.nlm.nih.gov/8021277

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Magnetic DNA affinity purification of yeast transcription factor

Autor: O S, Gabrielsen, J, Huet

Publikováno v: Methods in enzymology. 218

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4a17f6134cc554c488eaeb01400845e6
https://pubmed.ncbi.nlm.nih.gov/8510544

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Direct mobilization of retinol from hepatic perisinusoidal stellate cells to plasma

Autor: K B, Andersen, A, Nilsson, H K, Blomhoff, T B, Oyen, O S, Gabrielsen, K R, Norum, R, Blomhoff

Publikováno v: The Journal of biological chemistry. 267(2)

We have studied the mechanism for mobilization of retinol from stellate cells. Our data show that perisinusoidal stellate cells isolated from liver contained retinol-binding protein (RBP) mRNA. By Western blot analysis we found that cultivated liver

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https://pubmed.ncbi.nlm.nih.gov/1730653

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Characterization of a K26Q site-directed mutant of human parathyroid hormone expressed in yeast

Autor: S, Reppe, O S, Gabrielsen, O K, Olstad, N, Morrison, O, Saether, O R, Blingsmo, V T, Gautvik, J, Gordeladze, A K, Haflan, E F, Voelkel

Publikováno v: The Journal of biological chemistry. 266(22)

Human parathyroid hormone (hPTH) is susceptible to proteolytical cleavage both in humans and when expressed as a secretory product in Escherichia coli (Høgseth, A., Blingsmo, O. R., Saether, O., Gautvik, V. T., Holmgren, E., Hartmanis, M., Josephson

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https://pubmed.ncbi.nlm.nih.gov/1860837

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Two polypeptide chains in yeast transcription factor tau interact with DNA

Autor: O S, Gabrielsen, N, Marzouki, A, Ruet, A, Sentenac, P, Fromageot

Publikováno v: The Journal of biological chemistry. 264(13)

Yeast transcription factor tau interacts with the A and B blocks of the intragenic promoter of tRNA genes. The structure of tau was investigated by identifying the polypeptide chains specifically complexed to the tRNA3Glu gene. Highly purified factor

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https://pubmed.ncbi.nlm.nih.gov/2651441

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