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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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Interaction entropy for computational alanine scanning in protein–protein binding
, 2018Protein–protein interactions (PPIs) are at the heart of signal transduction and are central to the function of protein machine in biology. The highly specific protein–protein binding is quantitatively characterized by the binding free energy whose ...
Linqiong Qiu+4 more
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Physical Chemistry, Chemical Physics - PCCP, 2016
Understanding protein-protein interactions (PPIs) is quite important to elucidate crucial biological processes and even design compounds that interfere with PPIs with pharmaceutical significance.
Fu Chen+6 more
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Understanding protein-protein interactions (PPIs) is quite important to elucidate crucial biological processes and even design compounds that interfere with PPIs with pharmaceutical significance.
Fu Chen+6 more
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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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[38] Sulfatide-binding proteins
Chemistry and Physics of Lipids, 1986Sulfatides (galactosyl ceramide-I3-sulfate) and other sulfated glycolipids are found in many tissues. The cell adhesion proteins laminin, thrombospondin, and von Willebrand factor bind specifically to sulfated glycolipids. Methods for characterizing the specificity of these interactions using surface-adsorbed glycolipids are reviewed.
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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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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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Cellular and Molecular Life Sciences (CMLS), 1999
Nickel enzymes are a relatively new class of metalloenzymes. The seven known nickel enzymes are urease, hydrogenase, CO-dehydrogenase, methyl-coenzyme M reductase, Ni-superoxide dismutase, glyoxalase I and cis-trans isomerase. The requirement for nickel implies the presence of a nickel-processing system, since free transition metals are harmful to the ...
R K Wattt, P W Ludden
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Nickel enzymes are a relatively new class of metalloenzymes. The seven known nickel enzymes are urease, hydrogenase, CO-dehydrogenase, methyl-coenzyme M reductase, Ni-superoxide dismutase, glyoxalase I and cis-trans isomerase. The requirement for nickel implies the presence of a nickel-processing system, since free transition metals are harmful to the ...
R K Wattt, P W Ludden
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Science, 1988
Study of proteins that recognize specific DNA sequences has yielded much information, but the field is still in its infancy. Already two major structural motifs have been discovered, the helix-turn-helix and zinc finger, and numerous examples of DNA-binding proteins containing either of them are known. The restriction enzyme Eco RI uses yet a different
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Study of proteins that recognize specific DNA sequences has yielded much information, but the field is still in its infancy. Already two major structural motifs have been discovered, the helix-turn-helix and zinc finger, and numerous examples of DNA-binding proteins containing either of them are known. The restriction enzyme Eco RI uses yet a different
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CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein.
Science, 1990Leukocytes respond to lipopolysaccharide (LPS) at nanogram per milliliter concentrations with secretion of cytokines such as tumor necrosis factor-alpha (TNF-alpha).
S. D. Wright+4 more
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