@article{MTMT:1060973,
	title = {CHANNELING OF TCA CYCLE INTERMEDIATES IN CULTURED SACCHAROMYCES-CEREVISIAE},
	url = {https://m2.mtmt.hu/api/publication/1060973},
	author = {Sümegi, Balázs and Sherry, A D and Malloy, C R},
	doi = {10.1021/bi00491a002},
	journal-iso = {BIOCHEMISTRY-US},
	journal = {BIOCHEMISTRY},
	volume = {29},
	unique-id = {1060973},
	issn = {0006-2960},
	year = {1990},
	eissn = {1520-4995},
	pages = {9106-9110}
}

@article{MTMT:32006019,
	title = {Control of Metabolism by Dynamic Macromolecular Interactions},
	url = {https://m2.mtmt.hu/api/publication/32006019},
	author = {Keleti, T. and Ovádi, Judit},
	doi = {10.1016/B978-0-12-152829-4.50003-3},
	journal-iso = {CURR TOP CELL REGUL},
	journal = {CURRENT TOPICS IN CELLULAR REGULATION},
	volume = {29},
	unique-id = {32006019},
	issn = {0070-2137},
	abstract = {This chapter discusses the control of metabolism by dynamic macromolecular interactions. Metabolic pathways are controlled and directed by pacemaker, bottleneck, and key enzymes. In general, no single enzyme is responsible for the control of a whole metabolic pathway. In pursuing the pacemaker theory, attempts are made to quantify metabolic regulation, and one studies each enzyme in a sequence separately in situ, determines its kinetic properties in the greatest possible detail and accuracy, and then seeks to determine how it works when it is in the intact cell. In prokaryotes and in eukaryotes the largest macrocompartment is the cytoplasm, containing quantities of soluble enzymes and is full of membranes associated with a great variety of organelles. A theoretical analysis of glycolysis in human erythrocytes has been provided, implicitly assuming that it proceeds in a homogeneous bulk solution without any interaction among the participating enzymes. © 1988 ACADEMIC PRESS, INC.},
	keywords = {Animals; Humans; CELLS; metabolism; CELL; review; human; animal; Models, Biological; enzymology; Macromolecular Substances; Cytosol; Cytosol; biological model; energy metabolism; energy metabolism; macromolecule; Multienzyme Complexes; multienzyme complex},
	year = {1988},
	pages = {1-33}
}

@article{MTMT:1060979,
	title = {FURTHER CHARACTERIZATION OF THE KREBS TRICARBOXYLIC-ACID CYCLE METABOLON},
	url = {https://m2.mtmt.hu/api/publication/1060979},
	author = {Robinson, J B and Inman, L and Sümegi, Balázs and Srere, P A},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {262},
	unique-id = {1060979},
	issn = {0021-9258},
	year = {1987},
	eissn = {1083-351X},
	pages = {1786-1790}
}

@article{MTMT:1012878,
	title = {Phosphofructokinase and fructosebisphosphatase from muscle can interact at physiological concentrations with mutual effects on their kinetic behavior.},
	url = {https://m2.mtmt.hu/api/publication/1012878},
	author = {Ovádi, Judit and ARAGON, JJ and SOLS, A},
	journal-iso = {BIOCHEM BIOPH RES CO},
	journal = {BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS},
	volume = {135},
	unique-id = {1012878},
	issn = {0006-291X},
	year = {1986},
	eissn = {1090-2104},
	pages = {852-856}
}

@article{MTMT:1060989,
	title = {Association between the α-ketoglutarate dehydrogenase complex and succinate thiokinase},
	url = {https://m2.mtmt.hu/api/publication/1060989},
	author = {Porpáczy, Zoltán and Sümegi, Balázs and Alkonyi, István},
	doi = {10.1016/0167-4838(83)90249-2},
	journal-iso = {BIOCHIM BIOPHYS ACTA},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA},
	volume = {749},
	unique-id = {1060989},
	issn = {0006-3002},
	year = {1983},
	eissn = {1878-2434},
	pages = {172-179}
}

@article{MTMT:1060988,
	title = {A STUDY ON THE PHYSICAL INTERACTION BETWEEN THE PYRUVATE-DEHYDROGENASE COMPLEX AND CITRATE SYNTHASE},
	url = {https://m2.mtmt.hu/api/publication/1060988},
	author = {Sümegi, Balázs and Alkonyi, István},
	doi = {10.1016/0167-4838(83)90248-0},
	journal-iso = {BIOCHIM BIOPHYS ACTA},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA},
	volume = {749},
	unique-id = {1060988},
	issn = {0006-3002},
	year = {1983},
	eissn = {1878-2434},
	pages = {163-171}
}