(Q52451798)

English

A quantitative evaluation of the effect of enzyme complexes on the glycolytic rate in vivo: mathematical modeling of the glycolytic complex.

scientific article published in April 1991

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scholarly article

1 reference

Europe PubMed Central

1 May 2018

http://europepmc.org/abstract/MED/2062101

A quantitative evaluation of the effect of enzyme complexes on the glycolytic rate in vivo: mathematical modeling of the glycolytic complex. (English)

1 reference

Europe PubMed Central

1 May 2018

http://europepmc.org/abstract/MED/2062101

author name string

S P Brooks

1

1 reference

Europe PubMed Central

1 May 2018

http://europepmc.org/abstract/MED/2062101

K B Storey

2

1 reference

Europe PubMed Central

1 May 2018

http://europepmc.org/abstract/MED/2062101

language of work or name

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publication date

1 April 1991

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Europe PubMed Central

1 May 2018

http://europepmc.org/abstract/MED/2062101

number of pages

15

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Journal of Theoretical Biology

1 reference

Europe PubMed Central

1 May 2018

http://europepmc.org/abstract/MED/2062101

149

1 reference

Europe PubMed Central

1 May 2018

http://europepmc.org/abstract/MED/2062101

3

1 reference

Europe PubMed Central

1 May 2018

http://europepmc.org/abstract/MED/2062101

361-375

1 reference

Europe PubMed Central

1 May 2018

http://europepmc.org/abstract/MED/2062101

Quantitative Comparison of the Binding of Various Glycolytic Enzymes to F‐Actin and the Interaction of Aldolase with G‐Actin

1 reference

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Binding of Glycolytic Enzymes to Structure Proteins of the Muscle

1 reference

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Remarks on the supramolecular organization of the glycolytic system in vivo

1 reference

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Interaction of muscle glycolytic enzymes with thin filament proteins

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Reevaluation of the "glycolytic complex" in muscle: a multitechnique approach using trout white muscle

1 reference

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Metabolic dependence of glycolytic enzyme binding in rat and sheep heart

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Enzyme kinetic evidence of active-site involvement in the interaction between aldolase and muscle myofibrils

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Influence of substrates on the dissociation of rabbit muscle D-glyceraldehyde 3-phosphate dehydrogenase.

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Factors affecting the activation of rabbit muscle phosphofructokinase by actin.

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Supramolecular organization of glycolytic enzymes

1 reference

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Effect of ionic strength on the interaction between aldolase and actin-containing filaments

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Equilibrium partition studies of the interaction between aldolase and myofibrils

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A reappraisal of the binding of cytosolic enzymes to erythrocyte membranes

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Aldolase decreases the dissociation-induced inactivation of muscle phosphofructokinase

1 reference

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Modulation of phosphofructokinase action by macromolecular interactions. Quantitative analysis of the phosphofructokinase-aldolase-calmodulin system

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Dynamic interactions of enzymes involved in triosephosphate metabolism

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Old pathway--new concept: control of glycolysis by metabolite-modulated dynamic enzyme associations

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Phosphofructokinase and fructosebisphosphatase from muscle can interact at physiological concentrations with mutual effects on their kinetic behavior

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Effect of association-dissociation on the catalytic properties of glyceraldehyde 3-phosphate dehydrogenase

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Interaction of the dissociable glycerol-3-phosphate dehydrogenase and fructose-1,6-bisphosphate aldolase. Quantitative analysis by an extrinsic fluorescence probe

1 reference

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Physico-chemical evidence for the interaction between aldolase and glyceraldehyde-3-phosphate dehydrogenase

1 reference

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Glycolytic enzyme binding and metabolic control in anaerobiosis

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Binding of phosphofructokinase to filamentous actin

1 reference

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Feedforward inhibition in biosynthetic pathways: inhibition of the aminoacyl-tRNA synthetase by intermediates of the pathway

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Complexes of sequential metabolic enzymes

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The indirect binding of triose-phosphate isomerase to myofibrils to form a glycolytic enzyme mini-complex

1 reference

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Calmodulin: an introduction

1 reference

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Concentration of MgATP2- and other ions in solution. Calculation of the true concentrations of species present in mixtures of associating ions

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Interaction between D-glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase labeled by fluorescein-5'-isothiocyanate: evidence that the dye participates in the interaction

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Kinetics of metabolic pathways. A system in vitro to study the control of flux

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Study of the flux and transition time control coefficient profiles in a metabolic system in vitro and the effect of an external stimulator

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Mechanism of glyceraldehyde-3-phosphate transfer from aldolase to glyceraldehyde-3-phosphate dehydrogenase

1 reference

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Glycolytic enzyme interactions with tubulin and microtubules

1 reference

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The aldolase-substrate intermediates and their interaction with glyceraldehyde-3-phosphate dehydrogenase in a reconstructed glycolytic system

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

Enzyme-enzyme interactions and the regulation of metabolic reaction pathways

1 reference

https://api.crossref.org/works/10.1016%2FS0022-5193%2805%2980311-X

7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1016/S0022-5193(05)80311-X

1 reference

Europe PubMed Central

1 May 2018

http://europepmc.org/abstract/MED/2062101

1 reference

Europe PubMed Central

1 May 2018

http://europepmc.org/abstract/MED/2062101

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