Results 271 to 280 of about 137,279 (309)
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Thermodynamics of allosteric transitions
Journal of Theoretical Biology, 1977Abstract A new thermodynamic description of allosteric transitions in enzymes is introduced. Distinguished from previous approaches, the new method accounts for the effect of temperature on ligand binding affinities as well as the effect of ligand concentration. When applied to hemoglobin, the method yields a generalized Hill equation.
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Allosteric Properties of Acetylcholinesterase
Nature New Biology, 1972SEVERAL reports1–3 have suggested that cholinergic ligands bind to acetylcholinesterase at sites distinct from the active centre. Changeux et al.4 demonstrated that acetylcholine binds to non-catalytic sites as well as to the active centre of the enzyme.
G, Kato, E, Tan, J, Yung
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Sigmoidicity in Allosteric Models
Mathematical Biosciences, 1983For the saturation function, the state function as well as for the steady-state rate function of the Monod-Wyman-Changeux allosteric model analytical conditions of sigmoidicity are derived. They are shown as regions of sigmoidicity in a parameter space constituted by the allosteric constant parameter and the nonexclusive binding coefficient for each ...
Demongeot, Jacques, Laurent, Michel
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A portable allosteric mechanism
Proteins: Structure, Function, and Bioinformatics, 2004Abstract The allosteric mechanism by which the gene expression regulatory protein AraC regulates its DNA‐binding activity is shown to be portable by grafting it to β‐galactosidase, generating an arabinose‐regulated β‐galactosidase.
Urszula, Gryczynski, Robert, Schleif
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Kinetics of Allosteric Enzymes
Annual Review of Biophysics and Bioengineering, 1974Within the cell, hundreds of different chemical reactions go on simultaneously, each requiring different substrates and producing different products. This array of rea,ctions must be carefully regulated in order to maintain the orderly function of a cell.
G G, Hammes, C W, Wu
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Journal of Receptors and Signal Transduction, 2007
This article discusses a model to describe the effects of molecules that bind to a site on the receptor separate from that of the endogenous agonist to actively produce receptor signals (direct agonism). In addition, these molecules also modify the biological responses of the endogenous agonist (either potentiation or antagonism).
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This article discusses a model to describe the effects of molecules that bind to a site on the receptor separate from that of the endogenous agonist to actively produce receptor signals (direct agonism). In addition, these molecules also modify the biological responses of the endogenous agonist (either potentiation or antagonism).
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Allosteric modulation of caspases
Pharmacology & Therapeutics, 2011Caspases are proteolytic enzymes mainly involved in the induction and execution phases of apoptosis. This type of programmed cell death is an essential regulatory process required to maintain the integrity and homeostasis of multicellular organisms. Inappropriate apoptosis is attributed a key role in many human diseases, including neurodegenerative ...
Hans-Georg, Häcker +2 more
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Biochemistry, 2006
Disulfide bonds have been generally considered to be either structural or catalytic. Structural bonds stabilize a protein, while catalytic bonds mediate thiol-disulfide interchange reactions in substrate proteins. There is emerging evidence for a third type of disulfide bond that can control protein function by triggering a conformational change when ...
Bryan, Schmidt +2 more
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Disulfide bonds have been generally considered to be either structural or catalytic. Structural bonds stabilize a protein, while catalytic bonds mediate thiol-disulfide interchange reactions in substrate proteins. There is emerging evidence for a third type of disulfide bond that can control protein function by triggering a conformational change when ...
Bryan, Schmidt +2 more
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Allosteric and non-allosteric E. coli phosphofructokinases: effects on growth
Biochemical and Biophysical Research Communications, 1978Abstract In wild type Escherichia coli K-12 ca. 90% of phosphofructokinase is known to be the allosteric enzyme Pfk-1, and the rest is Pfk-2, a non-allosteric enzyme. An isogenic strain series has now been constructed with varying combinations and amounts of Pfk-1 and Pfk-2 (e.g., no Pfk-1, high level of Pfk-2; normal level Pfk-1, high level ...
J P, Robinson, D G, Fraenkel
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