Results 271 to 280 of about 8,850,756 (327)
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BioEssays, 1991
AbstractCells express many proteins that bind to laminin, the major adhesive component of basement membranes. Some of these, specifically integrins, function as transmembrane receptors that ‘signal’ the presence of laminin on the cell surface to the cytoplasm.
Mercurio, Arthur M., Shaw, Leslie M.
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AbstractCells express many proteins that bind to laminin, the major adhesive component of basement membranes. Some of these, specifically integrins, function as transmembrane receptors that ‘signal’ the presence of laminin on the cell surface to the cytoplasm.
Mercurio, Arthur M., Shaw, Leslie M.
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Plasma Protein Binding of Challenging Compounds.
Journal of Pharmacy and Science, 2015Accurately determining fraction unbound (fu ) with currently available methods has been challenging for certain compounds. Inaccurate fu values can lead to the misinterpretation of important attributes of a drug candidate.
K. Riccardi +7 more
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The Thyroxine-Binding Proteins
Thyroid, 2000The slow clearance, prolonged half-life, and high serum concentration of thyroxine (T4) are largely due to strong binding by the principal plasma thyroid hormone-binding proteins, thyroxine-binding globulin (TBG), transthyretin (TTR), and albumin. These proteins, which shield the hydrophobic thyroid hormones from their aqueous environment, buffer a ...
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British Journal of Haematology, 1975
The physical and physiologic properties of serum, milk and cellular FABP have been presented. Several investigators have shown that FABP with similar characteristics is present throughout the body fluids and tissue. Thus, FABP appears to be established as a protein which can significantly influence folate metabolism.
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The physical and physiologic properties of serum, milk and cellular FABP have been presented. Several investigators have shown that FABP with similar characteristics is present throughout the body fluids and tissue. Thus, FABP appears to be established as a protein which can significantly influence folate metabolism.
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Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2006
Emerging information on sphingolipid metabolism and signaling is leading to a better understanding of cellular processes such as apoptosis, cancer, cell survival and aging. In this review, we discuss the involvement of sphingolipids in these processes and focus on underlying mechanisms based on sphingolipid:protein interactions.
Jeffrey A. Jones +2 more
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Emerging information on sphingolipid metabolism and signaling is leading to a better understanding of cellular processes such as apoptosis, cancer, cell survival and aging. In this review, we discuss the involvement of sphingolipids in these processes and focus on underlying mechanisms based on sphingolipid:protein interactions.
Jeffrey A. Jones +2 more
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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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Clinical Pharmacology & Therapeutics, 1978
The protein binding of the new nonsteroidal anti‐inflammatory agent tolmetin to human serum albumin (HSA) and to the plasma of 8 healthy subjects was studied by equilibrium dialysis at 37° and pH 7.4 with 14C‐tolmetin. Over the total concentration (Ct) range 3.0 to 28.7 µg/ml (therapeutic range), the fraction oftolmetin unbound to 4% HSA was largely ...
J. Thomas, Barry W. Madsen, M. L. Selley
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The protein binding of the new nonsteroidal anti‐inflammatory agent tolmetin to human serum albumin (HSA) and to the plasma of 8 healthy subjects was studied by equilibrium dialysis at 37° and pH 7.4 with 14C‐tolmetin. Over the total concentration (Ct) range 3.0 to 28.7 µg/ml (therapeutic range), the fraction oftolmetin unbound to 4% HSA was largely ...
J. Thomas, Barry W. Madsen, M. L. Selley
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Journal of Protein Chemistry, 2001
Using a new method recently published for analyzing the binding isotherms of biopolymers (Poland, 2000a), we calculate the complete binding polynomials for lysozyme, insulin, and serum albumin from published titration data. These three proteins have, respectively, 22, 32, and 184 dissociable protons and hence are represented by series in powers of the ...
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Using a new method recently published for analyzing the binding isotherms of biopolymers (Poland, 2000a), we calculate the complete binding polynomials for lysozyme, insulin, and serum albumin from published titration data. These three proteins have, respectively, 22, 32, and 184 dissociable protons and hence are represented by series in powers of the ...
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Protein Binding of Propisomide
Journal of Pharmaceutical Sciences, 1985This paper describes the protein binding of propisomide to human serum and isolated proteins using equilibrium dialysis. The drug is exclusively bound to alpha1-acid glycoprotein with high affinity. The binding is saturable even at low concentrations of the drug.
J P Jeanniot +5 more
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Annual Review of Nutrition, 1988
INTRODUCTION . . . . . . . . .... . . . . . . . . ..... . . . . . . . . . . . . . . . . . . . ... . . . . . . . ..... . . . . . . ... . . . . . . . .... . . . . . . 279 Perspectives on the Nature of Vitamins and Vitamin Transport Systems 279 Nomenclature ..... . . . . ,", . . . . . . . . ,"" . . . . . . . "" . . . . . . . . ,"" . . . . . , """ . . . .
Alfred H. Merrill, Harold B. White
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INTRODUCTION . . . . . . . . .... . . . . . . . . ..... . . . . . . . . . . . . . . . . . . . ... . . . . . . . ..... . . . . . . ... . . . . . . . .... . . . . . . 279 Perspectives on the Nature of Vitamins and Vitamin Transport Systems 279 Nomenclature ..... . . . . ,", . . . . . . . . ,"" . . . . . . . "" . . . . . . . . ,"" . . . . . , """ . . . .
Alfred H. Merrill, Harold B. White
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