Results 331 to 340 of about 411,207 (359)
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MARCKS, membranes, and calmodulin: kinetics of their interaction
Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1998It is well documented that membrane binding of MARCKS (Myristoylated Alanine-Rich C-Kinase Substrate) requires both hydrophobic insertion of the N-terminal myristate into the bilayer and electrostatic interaction of the basic effector region with acidic lipids. The structure of a membrane-bound peptide corresponding to the effector region, residues 151-
A, Arbuzova, D, Murray, S, McLaughlin
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Molecular interactions and kinetic properties of fats
Progress in Lipid Research, 1999This article has reviewed the recent work on the molecular interactions and kinetic properties of the polymorphic transformations of the TAGs in the single and mixed states. Progress has recently been made in the molecular-level understanding of the polymorphic transformations of the TAGs.
K, Sato, S, Ueno, J, Yano
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A kinetic study of protein-protein interactions
Biochemistry, 1976Kinetic studies have been carried out of the monomer-dimer interaction of insulin, beta-lactoglobulin, and alpha-chymotrypsin using stopped-flow and temperature-jump techniques. The pH indicators bromothymol blue, bromophenol blue, and phenol red were used to monitor pH changes associated with the monomer-dimer interaction. In all three cases a kinetic
R, Koren, G G, Hammes
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Stiripentol kinetics in epilepsy: Nonlinearity and interactions
Clinical Pharmacology and Therapeutics, 1984Stiripentol kinetics during oral therapy were assessed in six patients with epilepsy who were receiving other antiepileptic drugs. Steady-state levels at 600, 1200, and 2400 mg/day increased in a nonlinear fashion, indicating Michaelis-Menten kinetics.
R H, Levy +5 more
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Mechanisms and kinetics of liposome–cell interactions
Advanced Drug Delivery Reviews, 1999Although the possibility of targeting drugs to specific tissues and cells, as well as facilitating their uptake and cytoplasmic delivery has rendered liposomes a versatile drug carrier system with numerous potential applications in medicine, the molecular mechanisms of liposome-cell interactions are not understood well.
, Düzgüneş, , Nir
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Kinetic models of the drug-receptor interaction
Journal of Theoretical Biology, 1975Abstract A model of drug action is proposed which is based upon intramolecular rearrangement of the drug-receptor complex. The model is a modification of classical occupancy theory kinetics. It is able to account for the transient excitatory response that is evoked by some blocking agents; it can also account for the phenomenon of “fade” (Paton, 1961)
R, Wilbur, E R, Fernholz, C T, Wilson
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Kinetic Mechanism for the Interaction of Hirulog with Thrombin
Biochemistry, 1994Hirulog (D-FPRPGGGGDGDFEEIPEEYL) is a bivalent inhibitor of thrombin consisting of a moiety (D-FPRP) that binds to the active-site cleft and a hirudin-like C-terminal region (DGDFEEIPEEYL) that binds to the positively charged surface groove of thrombin known as the anion-binding exosite.
M A, Parry, J M, Maraganore, S R, Stone
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Kinetic simulation of anticancer drug interactions
International Journal of Bio-Medical Computing, 1980A model is described that simulates the biochemical pathways of folate and nucleotide metabolism involved in DNA precursor biosynthesis. Examples are given of use of the model to study various aspects of the biochemical pharmacology of antitumour drugs.
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On the Thermodynamics and Kinetics of Hydrophobic Interactions at Interfaces
The Journal of Physical Chemistry B, 2013We have studied how primitive hydrophobic interactions between two or more small nonpolar solutes are affected by the presence of surfaces. We show that the desolvation barriers present in the potential of mean force between the solutes in bulk water are significantly reduced near an extended hydrophobic surface.
Srivathsan, Vembanur +3 more
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Kinetic studies of protein–protein interactions
Current Opinion in Structural Biology, 2002The structure of a protein-protein interaction, its affinity and thermodynamic characteristics depict a 'frozen' state of a complex. This picture ignores the kinetic nature of complex formation and dissociation, which are of major biological and biophysical interest.
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