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C.E. Sekeris

Researcher at University of Marburg

Publications -  10
Citations -  382

C.E. Sekeris is an academic researcher from University of Marburg. The author has contributed to research in topics: Cytosol & Cortisol binding. The author has an hindex of 8, co-authored 10 publications receiving 382 citations.

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Cleavage of high-molecular-weight DNA-like RNA by a nuclease present in 30-S ribonucleoprotein particles of rat liver nuclei

TL;DR: It is concluded that the protein from 30-S nuclear particles contains an endonuclease which in vivo might be involved in the cleavage of high-molecular-weight DNA-like RNA.
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Further studies on nuclear ribonucleoprotein particles containing DNA-like RNA from rat liver

TL;DR: Nuclear ribonucleoprotein particles containing DNA-like RNA have been extracted from purified rat liver nuclei in the presence of high levels of cytoplasmic ribonuclease inhibitor and the sedimentation behavior of the RNA is correlated to the size of ribon nucleop protein particles from which the RNA had been extracted.
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On the mechanism of hormone action: XVI. Transfer of [1,2-3H2]cortisol from the cytoplasm to the nucleus of rat-liver cells

TL;DR: It is concluded that the cytoplasmic cortisol receptor facilitates the interaction of the hormone with the chromosomal proteins, resulting in increased transcription of rat-liver chromatin.
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Two cortisol binding proteins from rat liver cytosol.

TL;DR: Kinetic experiments in vivo show that the incorporation of radioactivity into Peak B follows a hyperbolic curve and levels off after 10 min whereas incorporation into Peak A is linear up to 10 min, and it is suggested that cortisol is first bound to Binders B and then transferred to Binder A.
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Dexamethasone-binding proteins in cytosol and nucleus of rat thymocytes. Purification of three receptor proteins.

TL;DR: Three receptor proteins were highly purified from cytosol, with molecular weights of 45 000, 72 000 and 90 000 and one from nuclear extracts with molecular weight of 72 000, and may represent degradation products of the cytoplasmic receptor upon entrance into the nucleus.