| scholarly article | Q13442814 |
| P356 | DOI | 10.1016/S0076-6879(80)64009-9 |
| P698 | PubMed publication ID | 7374452 |
| P2093 | author name string | K E Neet | |
| P2860 | cites work | A ligand exclusion theory of allosteric effects | Q71591703 |
| A Theoretical Study of the Binding of Small Molecules to a Polymerizing Protein System. A Model for Allosteric Effects* | Q72284745 | ||
| THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS | Q26778400 | ||
| ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL | Q27861036 | ||
| Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase | Q29395244 | ||
| Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits* | Q29615452 | ||
| Energetics of the cooperative and noncooperative binding of nicotinamide adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase at pH 6.5 and pH 8.5. Equilibrium and calorimetric analysis over a range of temperature | Q30334515 | ||
| Analysis of kinetic data of allosteric enzymes by a linear plot | Q32080442 | ||
| A kinetic interpretation of the allosteric model of Monod, Wyman, and Changeux | Q33958545 | ||
| Antagonistic homotropic interactions as a possible explanation of coenzyme activation of glutamate dehydrogenase | Q33958549 | ||
| Allosteric proteins and cellular control systems | Q33970893 | ||
| Conformation and cooperativity in hemoglobin | Q34036396 | ||
| Cooperativity in associating proteins. Monomer-dimer equilibrium coupled to ligand binding. | Q34210117 | ||
| On the nature of allosteric transitions: implications of non-exclusive ligand binding | Q34242889 | ||
| Cooperative Interactions of Hemoglobin | Q34349288 | ||
| LINKED FUNCTIONS AND RECIPROCAL EFFECTS IN HEMOGLOBIN: A SECOND LOOK. | Q35493170 | ||
| Allosteric interpretation of haemoglobin properties | Q39065586 | ||
| Threonine inhibition of the aspartokinase-homoserine dehydrogenase I of Escherichia coli. Threonine binding studies | Q39207154 | ||
| Threonine inhibition of the aspartokinase-homoserine dehydrogenase I of Escherichia coli. Stopped-flow kinetics and the cooperativity of inhibition of the homoserine dehydrogenase activity | Q39207163 | ||
| Threonine inhibition of the aspartokinase-homoserine dehydrogenase I of Escherichia coli. A slow transient and cooperativity of inhibition of the aspartokinase activity | Q39207171 | ||
| A simple digital-computer program for estimating the parameters of the hill equation | Q39324760 | ||
| Structure, function, and possible origin of a bifunctional allosteric enzyme, Escherichia coli aspartokinase I-homoserine dehydrogenase I. | Q39875337 | ||
| Half-site reactivity | Q39901424 | ||
| Pseudoconservative transition: A two-state model for the co-operative behavior of oligomeric proteins | Q39938424 | ||
| Diagnostic uses of the Hill (logit and Nernst) plots | Q39958064 | ||
| Analysis of the allosteric basis for positive and negative co-operativity and half-of-the-sites reactivity in yeast and rabbit muscle glyceraldehyde 3-phosphate dehydrogenase | Q39958092 | ||
| The regulation of enzyme activity and allosteric transition | Q39991392 | ||
| Cooperativity and noncooperativity in the binding of NAD analogs to rabbit muscle glyceraldehyde-3-phosphate dehydrogenase | Q39993952 | ||
| Quaternary Structure of Proteins | Q39993997 | ||
| Evidence for induced interactions in the anticooperative binding of nicotinamide adenine dinucleotide to sturgeon muscle glyceraldehyde-3-phosphate dehydrogenase | Q40097080 | ||
| Studies of the self-association of bacteriophage T4 gene 32 protein by equilibrium sedimentation | Q40348789 | ||
| A kinetic model of cooperativity in aspartate transcarbamylase | Q40796205 | ||
| Allosteric regulation of aspartate transcarbamoylase. Analysis of the structural and functional behavior in terms of a two-state model | Q40817769 | ||
| Remarks on the kinetics of enzymes with interacting effector molecules. Tests of a configurational hypothesis in a quasi-equilibrium model | Q41521928 | ||
| The significance of abrupt transitions in Lineweaver-Burk plots with particular reference to glutamate dehydrogenase. Negative and positive co-operativity in catalytic rate constants | Q41905041 | ||
| Activation of brain hexokinase by magnesium ions and by magnesium ion–adenosine triphosphate complex | Q42919244 | ||
| States of hemoglobin in solution | Q43700461 | ||
| The 3:3 function in enzyme kinetics possible shapes of v/S and (1/v)/(1/S) plots for third degree steady-state rate equations | Q43819950 | ||
| Models for hemoglobin and allosteric enzymes | Q43937128 | ||
| Inhibition of co-operative enzymes by substrate-analogues: possible implications for the physiological significance of negative co-operativity illustrated by phenylalanine metabolism in higher plants | Q43983766 | ||
| Polysteric linkage | Q44206527 | ||
| Absence of kinetic negative co-operativity in the allosteric model of Monod, Wyman and Changeux | Q44221500 | ||
| Kinetic cooperativity in the concerted model for allosteric enzymes | Q44490900 | ||
| Active site-directed and allosteric effectors of regulatory enzymes: The activation of aspartate transcarbamylase by substrate and transition state analogues | Q44693841 | ||
| Properties of graphical representations of multiple classes of binding sites | Q44782312 | ||
| Structures and roles of the polymorphic forms of tobacco mosaic virus protein. I. Sedimentation studies | Q45813213 | ||
| Interpretation of nonlinear steady state enzyme kinetics--cyclic and mathematical properties of cooperative, second-site and random pathway models | Q46429009 | ||
| Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with carbamyl phosphate | Q47748340 | ||
| Subunit Interactions in Enzyme Catalysis. Kinetic Models for One-Substrate Polymeric Enzymes | Q47884341 | ||
| A general approach to co-operativity and its application to the oxygen equilibrium of hemoglobin and its effectors | Q47885537 | ||
| Dose any enzyme follow the Michaelis-Menten equation? | Q52438030 | ||
| An analysis on the slope of Scatchard plots | Q52837338 | ||
| Ligand-induced polymerization. | Q52846743 | ||
| A new plot for allosteric phenomena | Q52856758 | ||
| The Role of Negative Cooperativity and Half-of-the-Sites Reactivity in Enzyme Regulation | Q52859538 | ||
| Active site directed effectors of allosteric enzymes | Q52884068 | ||
| Letter: Kinetic negative co-operativity in the allosteric model of Monod, Wyman and Changeux. | Q52889206 | ||
| Regulatory behavior of monomeric enzymes. 1. The mnemonical enzyme concept. | Q52890154 | ||
| Subunit interactions in enzyme catalysis. Effect of interactions on transient kinetics. | Q52890164 | ||
| Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice. | Q52904158 | ||
| Ligand binding and internal equilibiums in proteins | Q52993539 | ||
| Mechanism of nicotinamide-adenine dinucleotide binding to rabbit muscle glyceraldehyde 3-phosphate dehydrogenase. | Q52998495 | ||
| A general method for the quantitative determination of saturation curves for multisubunit proteins. | Q53007756 | ||
| Positive and negative cooperativity in yeast glyceraldehyde 3-phosphate dehydrogenase. | Q53913851 | ||
| The quantitative interpretation of maximum in Scatchard plots. | Q54245116 | ||
| Half-of-the-sites and all-of-the-sites reactivity in rabbit muscle glyceraldehyde 3-phosphate dehydrogenase. | Q54335404 | ||
| Diagnostic relationships in the relaxation spectrometry of allosteric enzymes | Q67278491 | ||
| Ligand-induced self-association of human luteinizing hormone. Negative cooperativity in the binding of 8-anilino-1-naphthalenesulfonate | Q67322517 | ||
| Ligand-induced self-association of human chorionic gonadotropin. Positive cooperativity in the binding of 8-anilino-1-naphthalenesulfonate | Q67322519 | ||
| Thermodynamic restrictions on the allosteric models through an analysis of the free energy of interaction between sites | Q68236438 | ||
| Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli | Q68406872 | ||
| Negative cooperativity in enzyme action. The binding of diphosphopyridine nucleotide to glyceraldehyde 3-phosphate dehydrogenase | Q68586060 | ||
| The significance of intermediary plateau regions in enzyme saturation curves | Q68602031 | ||
| Studies on the allosteric modification of nucleoside diphosphatase activity by magnesium nucleoside triphosphates and inosine diphosphate | Q68632142 | ||
| Molecular basis of negative co-operativity in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase | Q68680352 | ||
| Structure of yeast hexokinase. 3. Low resolution structure of a second crystal form showing a different quaternary structure, heterologous interaction of subunits and substrate binding | Q68698202 | ||
| A mathematical model for structure-function relations in hemoglobin | Q69405790 | ||
| Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with aspartate analogs | Q69931027 | ||
| Regulation of enzyme activity. The activity of enzymes can be controlled by a multiplicity of conformational equilibria | Q69934779 | ||
| The action of hemoglobin. Cooperative effects in tetrameric proteins | Q70396646 | ||
| The Hill plot and the energy of interaction in hemoglobin | Q70453153 | ||
| Macromolecule--small molecule interactions: analytical and graphical reexamination | Q70588428 | ||
| Relation between allosteric effects and changes in the energy of bonding between molecular subunits | Q71252023 | ||
| P304 | page(s) | 139-192 | |
| P577 | publication date | 1980-01-01 | |
| P1433 | published in | Methods in Enzymology | Q2076903 |
| P1476 | title | Cooperativity in enzyme function: equilibrium and kinetic aspects | |
| P478 | volume | 64 |
| Q39511319 | (Na+ + K+)-ATPase: on the number of the ATP sites of the functional unit |
| Q67276825 | (Na+ + K+)-dependent adenosine triphosphatase. Regulation of inorganic phosphate, magnesium ion, and calcium ion interactions with the enzyme by ouabain |
| Q41788786 | 31 Generation of allosteric enzymes from nonallosteric forms |
| Q36091838 | A complementary pair of rapid molecular screening assays for RecA activities |
| Q37347206 | Allosteric cofactor-mediated enzyme cooperativity: a theoretical treatment |
| Q70724850 | Allosterism and Na(+)-D-glucose cotransport kinetics in rabbit jejunal vesicles: compatibility with mixed positive and negative cooperativities in a homo- dimeric or tetrameric structure and experimental evidence for only one transport protein invol |
| Q36078950 | Allostery vs. "allokairy". |
| Q52277635 | Binding of phosphate and sulfate anions by purine nucleoside phosphorylase from E. coli: ligand-dependent quenching of enzyme intrinsic fluorescence. |
| Q38205116 | Biochemical properties of isolated transverse tubular membranes |
| Q41630784 | Biosynthesis of (1-->3)-beta-D-glucan (callose) by detergent extracts of a microsomal fraction from Arabidopsis thaliana |
| Q70370222 | Bovine seminal ribonuclease: non-hyperbolic kinetics in the second reaction strep |
| Q42858651 | Co-operativity in seminal ribonuclease function. Kinetic studies |
| Q41910219 | Co-operativity in seminal ribonuclease function: binding studies |
| Q37538093 | Cooperativity in axonemal motion: analysis of a four-state, two-site kinetic model |
| Q27000989 | Cooperativity in monomeric enzymes with single ligand-binding sites |
| Q43793538 | Creation of an allosteric phosphofructokinase starting with a nonallosteric enzyme. The case of dictyostelium discoideum phosphofructokinase |
| Q43578182 | Determinants of directionality in lambda site-specific recombination |
| Q25257375 | Dimerization of the bacterial RsrI N6-adenine DNA methyltransferase |
| Q31868682 | Effects of EGF receptor ligands on fetal ovine myoblasts |
| Q41682456 | Effects of isoleucine 135 side chain length on the cofactor donor-acceptor distance within F420H2:NADP+ oxidoreductase: A kinetic analysis |
| Q28281319 | Evidence from Inhibitor Studies for Conformational Changes of Citrate Synthase |
| Q42744661 | Experimental approach to the kinetic study of unstable site-directed irreversible inhibitors: kinetic origin of the apparent positive co-operativity arising from inactivation of trypsin by p-amidinophenylmethanesulphonyl fluoride |
| Q52132111 | Formycin A and its N-methyl analogues, specific inhibitors of E. coli purine nucleoside phosphorylase (PNP): induced tautomeric shifts on binding to enzyme, and enzyme-->ligand fluorescence resonance energy transfer. |
| Q37059737 | Functional Interaction between the Herpes Simplex Virus Type 1 Polymerase Processivity Factor and Origin-Binding Proteins: Enhancement of UL9 Helicase Activity |
| Q36029187 | High-throughput screening for RecA inhibitors using a transcreener adenosine 5'-O-diphosphate assay |
| Q43684816 | Human glutathione transferase A1-1 demonstrates both half-of-the-sites and all-of-the-sites reactivity |
| Q44367155 | Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase |
| Q43722650 | Influence of ligand valency on ligand-influenced monomer-dimer equilibrium systems and biological control mechanisms |
| Q43600334 | Interaction of Escherichia coli purine nucleoside phosphorylase (PNP) with the cationic and zwitterionic forms of the fluorescent substrate N(7)-methylguanosine |
| Q72825069 | Interaction of calmodulin with muscle phosphofructokinase. Interplay with metabolic effectors of the enzyme under physiological conditions |
| Q71935735 | Kinetic analysis of 75selenium uptake by mitochondria of germinating Vigna radiata of different selenium status |
| Q37573473 | Kinetic analysis of mutations affecting the cII activation site at the PRE promoter of bacteriophage lambda |
| Q42858220 | Kinetic co-operativity of wheat-germ RNA polymerase II with adenosine 5'-[beta gamma-imido]triphosphate as substrate |
| Q33777643 | Kinetic cooperativity in Escherichia coli 30S ribosomal subunit reconstitution reveals additional complexity in the assembly landscape |
| Q73321079 | Kinetic measurements of binding of galectin 3 to a laminin substratum |
| Q42479072 | Mitochondrial selenium-75 uptake and regulation revealed by kinetic analysis. |
| Q40129842 | Na+, K+-ATPase: relation of conformational transitions to function |
| Q41842701 | Pig heart fumarase really does exhibit negative kinetic co-operativity at a constant ionic strength |
| Q52121118 | Potential memory and hysteretic effects in transcription. |
| Q46896653 | Pyrazolo[4,3-e][1,2,4]triazines: purine analogues with electronic absorption in the visible region. |
| Q34289327 | Quantitative relationships of site to site interaction in Escherichia coli D-3-phosphoglycerate dehydrogenase revealed by asymmetric hybrid tetramers |
| Q68506544 | Rat liver glycine methyltransferase. Cooperative binding of S-adenosylmethionine and loss of cooperativity by removal of a short NH2-terminal segment |
| Q70197611 | Reaction of (Na+ + K+)-dependent adenosine triphosphatase with inorganic phosphate. Regulation by Na+, K+, and nucleotides |
| Q69428426 | Role of association on protein adsorption isotherms. Beta-lactoglobulin A adsorbed on a weakly hydrophobic surface |
| Q51910123 | Role of ionization of the phosphate cosubstrate on phosphorolysis by purine nucleoside phosphorylase (PNP) of bacterial (E. coli) and mammalian (human) origin. |
| Q74212837 | Steady state kinetic model for the binding of substrates and allosteric effectors to Escherichia coli phosphoribosyl-diphosphate synthase |
| Q70945679 | Steady state kinetics of erythrocyte anion exchange. Evidence for site-site interactions |
| Q52427497 | Tabtoxinine-beta-Lactam Transport into Cultured Corn Cells : Uptake via an Amino Acid Transport System. |
| Q64056745 | The Central Role of Glucokinase in Glucose Homeostasis: A Perspective 50 Years After Demonstrating the Presence of the Enzyme in Islets of Langerhans |
| Q47834685 | The Escherichia coli RecQ helicase functions as a monomer |
| Q64116815 | The Oligomeric State of the Plasma Membrane H⁺-ATPase from |
| Q24801687 | The herpes simplex virus type 1 DNA polymerase processivity factor, UL42, does not alter the catalytic activity of the UL9 origin-binding protein but facilitates its loading onto DNA |
| Q69705904 | The regulatory kinetic properties of porcine hepatic glucokinase |
| Q40135308 | Virus-receptor interaction in the adenovirus system: characterization of the positive cooperative binding of virions on HeLa cells |
| Q36289552 | Zn(II)-induced cooperativity of Escherichia coli ornithine transcarbamoylase |
Search more.