Results 251 to 260 of about 3,196,863 (318)
Structural analysis of the lncRNA SChLAP1 reveals protein binding interfaces and a conformationally heterogenous retroviral insertion. [PDF]
RNAFalese JP +3 more
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VN-EGNN: E(3)- and SE(3)-Equivariant Graph Neural Networks with Virtual Nodes Enhance Protein Binding Site Identification. [PDF]
J CheminformSestak F +5 more
europepmc +1 more source
Correction to “Differential activity of MEK and ERK inhibitors in BRAF inhibitor resistant melanoma”
Molecular Oncology, EarlyView.
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Critical Reviews in Biochemistry and Molecular Biology, 1994
Odorant-binding proteins (OBPs) are low-molecular-weight soluble proteins highly concentrated in the nasal mucus of vertebrates and in the sensillar lymph of insects. Their affinity toward odors and pheromones suggests a role in olfactory perception, but their physiological function has not been clearly defined.
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Odorant-binding proteins (OBPs) are low-molecular-weight soluble proteins highly concentrated in the nasal mucus of vertebrates and in the sensillar lymph of insects. Their affinity toward odors and pheromones suggests a role in olfactory perception, but their physiological function has not been clearly defined.
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Chemistry and Physics of Lipids, 1985
A binding protein is described for certain oxygenated derivatives of cholesterol which suppress 3-hydroxy-3-methylglutaryl coenzyme A reductase and cholesterol synthesis in cultured mammalian cells. This protein is found in the cytosolic fraction of many cell types and is distinct from cytosolic proteins which bind cholesterol.
Taylor, F R, Kandutsch, A A
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A binding protein is described for certain oxygenated derivatives of cholesterol which suppress 3-hydroxy-3-methylglutaryl coenzyme A reductase and cholesterol synthesis in cultured mammalian cells. This protein is found in the cytosolic fraction of many cell types and is distinct from cytosolic proteins which bind cholesterol.
Taylor, F R, Kandutsch, A A
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Chemistry and Physics of Lipids, 1985
Proteins which bind glycolipids with high specificity are tentatively divided into two groups. One group consists of activator proteins involved in the catabolism of glycolipids by acid lysosomal hydrolases. Two activator proteins, GM2-activator and sphingolipid activator protein-1, are critically appraised on their glycolipid-binding properties and on
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Proteins which bind glycolipids with high specificity are tentatively divided into two groups. One group consists of activator proteins involved in the catabolism of glycolipids by acid lysosomal hydrolases. Two activator proteins, GM2-activator and sphingolipid activator protein-1, are critically appraised on their glycolipid-binding properties and on
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Protein binding of enprofylline
European Journal of Clinical Pharmacology, 1983The protein binding of enprofylline, 3-propylxanthine, in plasma was studied by equilibrium dialysis and ultrafiltration under various experimental conditions. A limited comparison with theophylline was also undertaken. The mean fraction of enprofylline bound in human plasma at 20 degrees C was 47.3 +/- 1.1% (SD), which was only 2% less than ...
K, Tegnér, O, Borgå, I, Svensson
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Frontiers in Bioscience, 1999
PCNA (proliferating cell nuclear antigen), originally characterized as a DNA polymerase accessory protein, functions as a DNA sliding clamp for DNA polymerase delta and is an essential component for eukaryotic chromosomal DNA replication. Recent studies have revealed a striking feature of PCNA in its ability to interact with multiple partners, involved,
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PCNA (proliferating cell nuclear antigen), originally characterized as a DNA polymerase accessory protein, functions as a DNA sliding clamp for DNA polymerase delta and is an essential component for eukaryotic chromosomal DNA replication. Recent studies have revealed a striking feature of PCNA in its ability to interact with multiple partners, involved,
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Annual Review of Nutrition, 1990
Folate-binding proteins of three major classes have been observed in various bodily fluids and in the plasma membrane and cytoplasm of normal and neoplastic cells. A major class, the high-affinity folate-binding proteins, show a preferential and tight binding of folic acid relative to reduced folates and methotrexate and consist of water-soluble and ...
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Folate-binding proteins of three major classes have been observed in various bodily fluids and in the plasma membrane and cytoplasm of normal and neoplastic cells. A major class, the high-affinity folate-binding proteins, show a preferential and tight binding of folic acid relative to reduced folates and methotrexate and consist of water-soluble and ...
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