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7 The Molecular Basis for Enzyme Regulation
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title
7 The Molecular Basis for Enzyme Regulation
(English)
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author name string
D.E. Koshland
series ordinal
1
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publication date
1970
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published in
The Enzymes
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page(s)
341-396
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cites work
Intracellular Regulatory Mechanisms: Regulation in multicellular forms may be an elaboration upon the pattern evolved in microorganisms.
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The Catalytic and Regulatory Properties of Enzymes
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Application of a Theory of Enzyme Specificity to Protein Synthesis
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Enzyme flexibility and enzyme action
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Allosteric proteins and cellular control systems
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Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-A. resolution, obtained by X-ray analysis
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Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 Å Resolution
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THE STRUCTURE OF CARBOXYPEPTIDASE A, IV. PRELIMINARY RESULTS AT 2.8 Å RESOLUTION, AND A SUBSTRATE COMPLEX AT 6 Å RESOLUTION.
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Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*
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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL
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Relation of protein subunit interactions to the molecular species observed during cooperative binding of ligands
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Heme proteins.
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The Determination of Enzyme Dissociation Constants
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Ueber einen in biologischer Beziehung wichtigen Einfluss, den die Kohlensäurespannung des Blutes auf dessen Sauerstoffbindung übt1
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Negative cooperativity in regulatory enzymes
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Positive and negative cooperativity in yeast glyceraldehyde 3-phosphate dehydrogenase.
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Antagonistic homotropic interactions as a possible explanation of coenzyme activation of glutamate dehydrogenase
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THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS
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The binding of organic ions by proteins.
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Negative cooperativity in enzyme action. The binding of diphosphopyridine nucleotide to glyceraldehyde 3-phosphate dehydrogenase
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A general method for the quantitative determination of saturation curves for multisubunit proteins.
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Spin-label study of hemoglobin conformations in solution
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Measurement of ligand-induced conformational changes in hemoglobin by circular dichroism
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Allosteric Interactions in Aspartate Transcarbamylase. II. Evidence for Different Conformational States of the Protein in the Presence and Absence of Specific Ligands
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Nuclear magnetic resonance studies of the structure and binding sites of enzymes. IV. Cytidine 3'-monophosphate binding to ribonuclease
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The effect of NAD+ on the catalytic efficiency of glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle
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The reaction between NAD+ and rabbit-muscle glyceraldehydephosphate dehydrogenase.
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The preparation and properties of the isolated alpha and beta subunits of hemoglobin A
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Oxygen equilibria of human hemoglobin valency hybrids. Discussion on the intrinsic properties of alpha and beta chains in the native protein
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Evidence for β-β interactions during the binding of oxygen to hemoglobin
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The Croonian Lecture, 1968: The Haemoglobin Molecule
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Thioredoxin. A localized conformational change accompanying reduction of the protein to the sulfhydryl form
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Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli
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The binding of nicotinamide-adenine dinucleotide to yeast d-glyceraldehyde-3-phosphate dehydrogenase: temperature-jump relaxation studies on the mechanism of an allosteric enzyme
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The significance of intermediary plateau regions in enzyme saturation curves
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An alternative to allosterism and cooperativity in the interpretation of enzyme kinetic data
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Effect of adenylic acid on the regulatory nicotinamide-adenine dinucleotide specific isocitrate dehydrogenase
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A Theoretical Study of the Binding of Small Molecules to a Polymerizing Protein System. A Model for Allosteric Effects*
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Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution: The Atomic Model
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Hemoglobin and its reaction with ligands
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The Oxygen Equilibrium of Hemoglobin and Its Structural Interpretation
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The absence of "heme-heme" interactions in hemoglobin
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Subunit exchange and ligand binding: a new hypothesis for the mechanism of oxygenation of hemoglobin
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Distinct Subunits for the Regulation and Catalytic Activity of Aspartate Transcarbamylase*
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Cellular regulation of glutamine synthetase activity in Escherichia coli
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DOI
10.1016/S1874-6047(08)60170-5
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