Results 351 to 360 of about 8,751,128 (381)
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Identification of a nuclear receptor for bile acids.
Science, 1999Bile acids are essential for the solubilization and transport of dietary lipids and are the major products of cholesterol catabolism. Results presented here show that bile acids are physiological ligands for the farnesoid X receptor (FXR), an orphan ...
M. Makishima +9 more
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Evidence for a role of CRM1 in signal-mediated nuclear protein export.
Science, 1997Chromosome maintenance region 1 (CRM1), a protein that shares sequence similarities with the karyopherin beta family of proteins involved in nuclear import pathway, was shown to form a complex with the leucine-rich nuclear export signal (NES).
B. Ossareh-Nazari +2 more
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Studies of the nuclear residual proteins
Archives of Biochemistry and Biophysics, 1968Abstract The nuclear residual proteins of rat liver have been prepared by solubilization with sodium deoxycholate and Sephadex gel filtration. These proteins were examined by analytical ultracentrifugation, DEAE-cellulose chromatography, starch gel electrophoresis, amino acid composition, and alkali-labile phosphorus analysis.
V. Patel +7 more
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Identity of nuclear membrane and non-histone nuclear proteins
Biochemistry, 1976The fate of plasma and nuclear membrane polypeptides in preparations of acidic chromosomal protein from chicken erythrocytes has been investigated. It is shown that detergent extraction procedures (Nonidet P-40, Triton X-100, and saponin), commonly employed in the preparation of acidic chromosomal protein, cannot be relied upon to remove plasma and ...
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Annual Review of Biochemistry, 2015
Lamins are intermediate filament proteins that form a scaffold, termed nuclear lamina, at the nuclear periphery. A small fraction of lamins also localize throughout the nucleoplasm.
Y. Gruenbaum, R. Foisner
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Lamins are intermediate filament proteins that form a scaffold, termed nuclear lamina, at the nuclear periphery. A small fraction of lamins also localize throughout the nucleoplasm.
Y. Gruenbaum, R. Foisner
semanticscholar +1 more source
ADP-ribosylation of nuclear proteins
Advances in Enzyme Regulation, 1979Covalent modification of nuclear proteins by mono ADP-ribosylation and poly ADP-ribosylation was studied in various tissues and under various growth conditions with the aid of a newly developed radioimmunoassay. Two types of (ADPR)n protein conjugates were found in vitro and in intact tissues which could be differentiated by their sensitivity towards ...
Peter Adamietz +3 more
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2007
Entry into the eukaryotic cell nucleus occurs through multiple pathways involving specific targeting signals, and intracellular receptor molecules of the importin/karyopherin superfamily which recognise and dock the nuclear import substrates carrying these signals at the nuclear pore.
Jade K. Forwood, David A. Jans
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Entry into the eukaryotic cell nucleus occurs through multiple pathways involving specific targeting signals, and intracellular receptor molecules of the importin/karyopherin superfamily which recognise and dock the nuclear import substrates carrying these signals at the nuclear pore.
Jade K. Forwood, David A. Jans
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Binding of nuclear proteins to DNA
Archives of Biochemistry and Biophysics, 1974Nonhistone proteins from rat liver nuclei prepared either by the phenol procedure of Teng et al. (1) or according to Richter and Sekeris (2) and labeled with 125 J (3) were recombined with DNA by stepwise dialysis from high salt-urea solutions. Recombination was evaluated by sucrose gradient centrifugation.
Walter Röwekamp, Constantin E. Sekeris
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Immunolocalization of Nuclear Proteins [PDF]
, 1994 Immunohistochemistry permits the localization at the tissue and subcellular level of antigens for which specific antisera or monoclonal antibodies are available. A wide variety of methods are used for this purpose, and the best method for any particular application must unfortunately be determined empirically.
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Pest sequences in nuclear proteins
International Journal of Biochemistry, 19931. Most of proteins which are rapidly degraded inside eukaryotic cells have been found to contain amino acid sequences (PEST sequences) enriched in proline, acidic residues (glutamic acid and/or aspartic acid) and hydrophilic residues (serine and threonine) (Rogers et al. (1986) Science 234, 364-368). 2.
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