@article{MTMT:27563081, title = {Glutamine via α-ketoglutarate dehydrogenase provides succinyl-CoA for heme synthesis during erythropoiesis}, url = {https://m2.mtmt.hu/api/publication/27563081}, author = {Burch, Joseph S and Marcero, Jason R and Maschek, John Alan and Cox, James E and Jackson, Laurie K and Medlock, Amy E and Phillips, John D and Dailey, Harry A}, doi = {10.1182/blood-2018-01-829036}, journal-iso = {BLOOD}, journal = {BLOOD}, volume = {132}, unique-id = {27563081}, issn = {0006-4971}, year = {2018}, eissn = {1528-0020}, pages = {987-998} } @article{MTMT:31340550, title = {Passing the baton: Substrate channelling in respiratory metabolism}, url = {https://m2.mtmt.hu/api/publication/31340550}, author = {Fernie, A.R. and Zhang, Y. and Sweetlove, L.J.}, doi = {10.1155/2018/1539325}, journal-iso = {RESEARCH}, journal = {RESEARCH (LAMBERTVILLE, N.J.)}, volume = {2018}, unique-id = {31340550}, abstract = {Despite species-specific differences in the pathways of respiratory metabolism are remarkably conserved across the kingdoms of life with glycolysis, the tricarboxylic acid cycle, and mitochondrial electron transport chain representing the major components of the process in the vast majority of organisms. In addition to being of critical importance in fueling life itself these pathways serve as interesting case studies for substrate channelling with research on this theme having been carried out for over 40 years. Here we provide a cross-kingdom review of the ample evidence for protein-protein interaction and enzyme assemblies within the three component pathways as well as describing the scarcer available evidence for substrate channelling itself. Copyright © 2018 Alisdair R. Fernie et al.}, year = {2018}, eissn = {2334-1009} } @{MTMT:33616850, title = {Mitochondria, Thiamine, and Autonomic Dysfunction}, url = {https://m2.mtmt.hu/api/publication/33616850}, author = {Lonsdale, Derrick and Marrs, Chandler}, booktitle = {Thiamine deficiency disease, dysautonomia, and high calorie malnutrition}, doi = {10.1016/B978-0-12-810387-6.00003-4}, unique-id = {33616850}, keywords = {LACTIC-ACIDOSIS; Oxidative stress; WERNICKES ENCEPHALOPATHY; metformin therapy; feeding systems; MEGALOBLASTIC-ANEMIA SYNDROME; RED-CELL TRANSKETOLASE; CEREBROCORTICAL NECROSIS; TETRAHYDROFURFURYL DISULFIDE}, year = {2017}, pages = {59-103} } @article{MTMT:26764931, title = {Protein-protein interactions and metabolite channelling in the plant tricarboxylic acid cycle}, url = {https://m2.mtmt.hu/api/publication/26764931}, author = {Zhang, Youjun and Beard, Katherine F M and Swart, Corne and Bergmann, Susan and Krahnert, Ina and Nikoloski, Zoran and Graf, Alexander and Ratcliffe, R George and Sweetlove, Lee J and Fernie, Alisdair R and Obata, Toshihiro}, doi = {10.1038/ncomms15212}, journal-iso = {NAT COMMUN}, journal = {NATURE COMMUNICATIONS}, volume = {8}, unique-id = {26764931}, issn = {2041-1723}, year = {2017}, eissn = {2041-1723}, orcid-numbers = {Graf, Alexander/0000-0002-6696-5206} } @article{MTMT:2228167, title = {The negative impact of alpha-ketoglutarate dehydrogenase complex deficiency on matrix substrate-level phosphorylation}, url = {https://m2.mtmt.hu/api/publication/2228167}, author = {Kiss, Gergely and Konrád, Csaba and Dóczi, Judit and Starkov, AA and Kawamata, H and Manfredi, G and Zhang, SF and Gibson, GE and Beal, MF and Ádám, Veronika and Chinopoulos, Christos}, doi = {10.1096/fj.12-220202}, journal-iso = {FASEB J}, journal = {FASEB JOURNAL}, volume = {27}, unique-id = {2228167}, issn = {0892-6638}, abstract = {A decline in alpha-ketoglutarate dehydrogenase complex (KGDHC) activity has been associated with neurodegeneration. Provision of succinyl-CoA by KGDHC is essential for generation of matrix ATP (or GTP) by substrate-level phosphorylation catalyzed by succinyl-CoA ligase. Here, we demonstrate ATP consumption in respiration-impaired isolated and in situ neuronal somal mitochondria from transgenic mice with a deficiency of either dihydrolipoyl succinyltransferase (DLST) or dihydrolipoyl dehydrogenase (DLD) that exhibit a 20-48% decrease in KGDHC activity. Import of ATP into the mitochondrial matrix of transgenic mice was attributed to a shift in the reversal potential of the adenine nucleotide translocase toward more negative values due to diminished matrix substrate-level phosphorylation, which causes the translocase to reverse prematurely. Immunoreactivity of all three subunits of succinyl-CoA ligase and maximal enzymatic activity were unaffected in transgenic mice as compared to wild-type littermates. Therefore, decreased matrix substrate-level phosphorylation was due to diminished provision of succinyl-CoA. These results were corroborated further by the finding that mitochondria from wild-type mice respiring on substrates supporting substrate-level phosphorylation exhibited approximately 30% higher ADP-ATP exchange rates compared to those obtained from DLST+/- or DLD+/- littermates. We propose that KGDHC-associated pathologies are a consequence of the inability of respiration-impaired mitochondria to rely on "in-house" mitochondrial ATP reserves.-Kiss, G., Konrad, C., Doczi, J., Starkov, A. A., Kawamata, H., Manfredi, G., Zhang, S. F., Gibson, G. E., Beal, M. F., Adam-Vizi, V., Chinopoulos, C. The negative impact of alpha-ketoglutarate dehydrogenase complex deficiency on matrix substrate-level phosphorylation.}, year = {2013}, eissn = {1530-6860}, pages = {2392-2406}, orcid-numbers = {Dóczi, Judit/0000-0002-5797-5074; Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149} } @article{MTMT:22836618, title = {Impaired TCA cycle flux in mitochondria in skeletal muscle from type 2 diabetic subjects: Marker or maker of the diabetic phenotype?}, url = {https://m2.mtmt.hu/api/publication/22836618}, author = {Michael, Gaster and Jan, O Nehlin and Ariane, D Minet}, doi = {10.3109/13813455.2012.656653}, journal-iso = {ARCH PHYSIOL BIOCHEM}, journal = {ARCHIVES OF PHYSIOLOGY AND BIOCHEMISTRY}, volume = {118}, unique-id = {22836618}, issn = {1381-3455}, year = {2012}, eissn = {1744-4160}, pages = {156-189} } @article{MTMT:23450895, title = {Development and characterization of polyspecific anti-mitochondrion antibodies for proteomics studies on in toto tissue homogenates}, url = {https://m2.mtmt.hu/api/publication/23450895}, author = {Loro, E and Gianazza, E and Cazzola, S and Malena, A and Wait, R and Begum, S and Brizio, C and Dabbeni-Sala, F and Vergani, L}, doi = {10.1002/elps.200800576}, journal-iso = {ELECTROPHORESIS}, journal = {ELECTROPHORESIS}, volume = {30}, unique-id = {23450895}, issn = {0173-0835}, year = {2009}, eissn = {1522-2683}, pages = {1329-1341} } @article{MTMT:22836933, title = {Protein folding dinamics study for protein-protein interactions}, url = {https://m2.mtmt.hu/api/publication/22836933}, author = {Patil, AG and Ojha, MD and Bhandari, PA and Kulkarni, S}, volume = {1}, unique-id = {22836933}, year = {2009}, pages = {18-23} } @mastersthesis{MTMT:22836898, title = {The role of Cyclophilin D and the adenine-nucleotide translocator in the impairment of mitochondrial functions}, url = {https://m2.mtmt.hu/api/publication/22836898}, author = {Vajda, Szilvia}, unique-id = {22836898}, year = {2009} } @article{MTMT:21210496, title = {Candida krusei produces ethanol without production of succinic acid; a potential advantage for ethanol recovery by pervaporation membrane separation.}, url = {https://m2.mtmt.hu/api/publication/21210496}, author = {Nakayama, S and Morita, T and Negishi, H and Ikegami, T and Sakaki, K and Kitamoto, D}, doi = {10.1111/j.1567-1364.2008.00384.x}, journal-iso = {FEMS YEAST RES}, journal = {FEMS YEAST RESEARCH}, volume = {8}, unique-id = {21210496}, issn = {1567-1356}, year = {2008}, eissn = {1567-1364}, pages = {706-714} } @{MTMT:22836833, title = {Methods for Protein Screening}, url = {https://m2.mtmt.hu/api/publication/22836833}, author = {Francis, Joseph Carr and Graham, Carter and Anita, Anne Hamilton and Fiona, Suzanne Adair and Stephen, Williams}, unique-id = {22836833}, year = {2005} } @article{MTMT:10242169, title = {The interaction of FBPase with aldolase: a kinetic and fluorescence investigation on chicken muscle enzymes}, url = {https://m2.mtmt.hu/api/publication/10242169}, author = {DZIEWULSKA, SZWAJKOWSKA D and ZMOJDZIAN, M and DOBRYSZYCKI, P and KOCHMAN, M and DZUGAJ, A}, doi = {10.1016/j.cbpc.2003.10.010}, journal-iso = {COMP BIOCHEM PHYS B}, journal = {COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY}, volume = {137}, unique-id = {10242169}, issn = {1096-4959}, year = {2004}, eissn = {1879-1107}, pages = {115-129} } @mastersthesis{MTMT:22836880, title = {AN INVESTIGATION INTO THE ROLE OF PROTEIN-LIGAND INTERACTIONS ON OBLIGATE AND TRANSIENT PROTEIN-PROTEIN INTERACTIONS}, url = {https://m2.mtmt.hu/api/publication/22836880}, author = {ROBERT, JASON QUINLAN}, unique-id = {22836880}, year = {2004} } @article{MTMT:32006096, title = {Macromolecular Compartmentation and Channeling}, url = {https://m2.mtmt.hu/api/publication/32006096}, author = {Ovádi, Judit and Srere, P.A.}, doi = {10.1016/s0074-7696(08)60529-x}, journal-iso = {INT REV CYTOL}, journal = {INTERNATIONAL REVIEW OF CYTOLOGY-A SURVEY OF CELL BIOLOGY}, volume = {192}, unique-id = {32006096}, issn = {0074-7696}, abstract = {One of the accepted characterizations of the living state is that it is complex to an extraordinary degree. Since our current understanding of the living condition is minimal and fragmentary, it is not surprising that our first descriptions are simplistic. However, in certain areas of metabolism, especially those that have been amenable to experimentation for the longest period of time, the simplistic explanations have been the most difficult to revise. For example, current texts of general biochemistry still view metabolism as occurring by a series of independent enzymes dispersed in a uniform aqueous environment. This notion has been shown to be deeply flawed by both experimental and theoretical considerations. Thus, there is ample evidence that, in many metabolic pathways, specific interactions between sequential enzymes occur as static and/or dynamic complexes. In addition, reversible interactions of enzymes with structural proteins and membranes is a common occurrence. The interactions of enzymes give rise to a higher level of complexity that must be accounted for when one wishes to understand the regulation of metabolism. One of the phenomena that occurs because of sequential enzyme interactions is the process of channeling. This article discusses enzyme interactions and channeling and summarizes experimental and theoretical results from a few well-studied examples. Copyright © 2000 by Academic Press. All rights of reproduction in any form reserved.}, keywords = {metabolism; ENZYME; review; priority journal; protein protein interaction; complex formation; channeling; cell metabolism; enzyme kinetics; macromolecule; cell compartmentalization; structural protein; Ambiquity; Enzyme structure protein interactions; Enzyme-enzyme interactions}, year = {1999}, pages = {255-280} } @article{MTMT:22882644, title = {Supramolecular Organization in Living Cells}, url = {https://m2.mtmt.hu/api/publication/22882644}, author = {Jayashree, Krishna SAINIS}, journal-iso = {PROC INDIAN NAT SCI ACAD PART A}, journal = {PROCEEDINGS OF THE INDIAN NATIONAL SCIENCE ACADEMY}, volume = {B64}, unique-id = {22882644}, issn = {0370-0046}, year = {1998}, pages = {197-212} } @article{MTMT:20172627, title = {Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes}, url = {https://m2.mtmt.hu/api/publication/20172627}, author = {Johnson, J D and Mehus, J G and Tews, K and Milavetz, B I and Lambeth, D O}, doi = {10.1074/jbc.273.42.27580}, journal-iso = {J BIOL CHEM}, journal = {JOURNAL OF BIOLOGICAL CHEMISTRY}, volume = {273}, unique-id = {20172627}, issn = {0021-9258}, year = {1998}, eissn = {1083-351X}, pages = {27580-27586} } @article{MTMT:22803059, title = {Interaction between citrate synthase and malate dehydrogenase - Substrate channeling of oxaloacetate}, url = {https://m2.mtmt.hu/api/publication/22803059}, author = {Morgunov, I and Srere, PA}, doi = {10.1074/jbc.273.45.29540}, journal-iso = {J BIOL CHEM}, journal = {JOURNAL OF BIOLOGICAL CHEMISTRY}, volume = {273}, unique-id = {22803059}, issn = {0021-9258}, year = {1998}, eissn = {1083-351X}, pages = {29540-29544} } @article{MTMT:20174278, title = {Channeling of TCA cycle intermediates in Saccharomyces cerevisiae}, url = {https://m2.mtmt.hu/api/publication/20174278}, author = {Sonawat, I and Sonawat, H M}, journal-iso = {INDIAN J BIOCHEM BIOPHYS}, journal = {INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS}, volume = {35}, unique-id = {20174278}, issn = {0301-1208}, year = {1998}, eissn = {0975-0959}, pages = {260-265} } @article{MTMT:23314257, title = {Mutations in the IDH2 gene encoding the catalytic subunit of the yeast NAD(+)-dependent isocitrate dehydrogenase can be suppressed by mutations in the CIT1 gene encoding citrate synthase and other genes of oxidative metabolism}, url = {https://m2.mtmt.hu/api/publication/23314257}, author = {Gadde, DM and McCammon, MT}, doi = {10.1006/abbi.1997.0191}, journal-iso = {ARCH BIOCHEM BIOPHYS}, journal = {ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS}, volume = {344}, unique-id = {23314257}, issn = {0003-9861}, year = {1997}, eissn = {1096-0384}, pages = {139-149} } @article{MTMT:23233028, title = {Effects of acetic acid on respiration of Debaryomyces hansenii: (Studies on the mechanism of the antifungal action of acetic acid, part III)}, url = {https://m2.mtmt.hu/api/publication/23233028}, author = {Maehashi, K and Yamamoto, Y and Higashi, K and Yoshii, H}, journal-iso = {J JPN SOC FOOD SCI}, journal = {NIPPON SHOKUHIN KAGAKU KOGAKU KAISHI / JOURNAL OF THE JAPANESE SOCIETY FOR FOOD SCIENCE AND TECHNOLOGY}, volume = {43}, unique-id = {23233028}, issn = {1341-027X}, year = {1996}, pages = {225-230} } @article{MTMT:23314184, title = {Identification of a multienzyme complex of the tricarboxylic acid cycle enzymes containing citrate synthase isoenzymes from Pseudomonas aeruginosa}, url = {https://m2.mtmt.hu/api/publication/23314184}, author = {Mitchell, CG}, doi = {10.1042/bj3130769}, journal-iso = {BIOCHEM J}, journal = {BIOCHEMICAL JOURNAL}, volume = {313}, unique-id = {23314184}, issn = {0264-6021}, year = {1996}, eissn = {1470-8728}, pages = {769-774} } @article{MTMT:21207460, title = {PROTEIN-PROTEIN INTERACTIONS - METHODS FOR DETECTION AND ANALYSIS}, url = {https://m2.mtmt.hu/api/publication/21207460}, author = {PHIZICKY, EM and FIELDS, S}, doi = {10.1128/MMBR.59.1.94-123.1995}, journal-iso = {MICROBIOL REV}, journal = {MICROBIOLOGICAL REVIEWS}, volume = {59}, unique-id = {21207460}, issn = {0146-0749}, year = {1995}, pages = {94-123} } @article{MTMT:20172764, title = {ENZYMATIC AND METABOLIC STUDIES ON RETROGRADE REGULATION MUTANTS OF YEAST}, url = {https://m2.mtmt.hu/api/publication/20172764}, author = {Small, W C and Brodeur, R D and Sandor, A and Fedorova, N and LI, G Y and Butow, R A and Srere, P A}, doi = {10.1021/bi00016a031}, journal-iso = {BIOCHEMISTRY-US}, journal = {BIOCHEMISTRY}, volume = {34}, unique-id = {20172764}, issn = {0006-2960}, year = {1995}, eissn = {1520-4995}, pages = {5569-5576} } @article{MTMT:23314266, title = {17TH LIPMANN,FRITZ LECTURE - WANDERINGS (WONDERINGS) IN METABOLISM}, url = {https://m2.mtmt.hu/api/publication/23314266}, author = {SRERE, PA}, doi = {10.1515/bchm3.1993.374.7-12.833}, journal-iso = {BIOL CHEM H-S}, journal = {BIOLOGICAL CHEMISTRY HOPPE-SEYLER}, volume = {374}, unique-id = {23314266}, issn = {0177-3593}, year = {1993}, pages = {833-842} } @article{MTMT:1060962, title = {EVIDENCE FOR ORIENTATION-CONSERVED TRANSFER IN THE TCA CYCLE IN SACCHAROMYCES-CEREVISIAE - C-13 NMR-STUDIES}, url = {https://m2.mtmt.hu/api/publication/1060962}, author = {Sümegi, Balázs and Sherry, A D and Malloy, C R and Srere, P A}, doi = {10.1021/bi00210a022}, journal-iso = {BIOCHEMISTRY-US}, journal = {BIOCHEMISTRY}, volume = {32}, unique-id = {1060962}, issn = {0006-2960}, year = {1993}, eissn = {1520-4995}, pages = {12725-12729} } @article{MTMT:23307238, title = {GLUTAMATE-MALATE METABOLISM IN LIVER-MITOCHONDRIA - A MODEL CONSTRUCTED ON THE BASIS OF MITOCHONDRIAL LEVELS OF ENZYMES, SPECIFICITY, DISSOCIATION-CONSTANTS, AND STOICHIOMETRY OF HETERO-ENZYME COMPLEXES}, url = {https://m2.mtmt.hu/api/publication/23307238}, author = {FAHIEN, LA and TELLER, JK}, journal-iso = {J BIOL CHEM}, journal = {JOURNAL OF BIOLOGICAL CHEMISTRY}, volume = {267}, unique-id = {23307238}, issn = {0021-9258}, year = {1992}, eissn = {1083-351X}, pages = {10411-10422} } @article{MTMT:20172636, title = {SUBUNIT INTERACTIONS OF RUBISCO ACTIVASE - POLYETHYLENE-GLYCOL PROMOTES SELF-ASSOCIATION, STIMULATES ATPASE AND ACTIVATION ACTIVITIES, AND ENHANCES INTERACTIONS WITH RUBISCO}, url = {https://m2.mtmt.hu/api/publication/20172636}, author = {Salvucci, M E}, doi = {10.1016/0003-9861(92)90467-B}, journal-iso = {ARCH BIOCHEM BIOPHYS}, journal = {ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS}, volume = {298}, unique-id = {20172636}, issn = {0003-9861}, year = {1992}, eissn = {1096-0384}, pages = {688-696} } @article{MTMT:1061520, title = {Regulatory Consequences of Organization of Citric Acid Cycle Enzymes}, url = {https://m2.mtmt.hu/api/publication/1061520}, author = {Sümegi, Balázs and Porpáczy, Zoltán and Mc, Cammon M T and Sherry, A D and Malloy, C R and Srere, PA}, doi = {10.1016/B978-0-12-152833-1.50019-8}, journal-iso = {CURR TOP CELL REGUL}, journal = {CURRENT TOPICS IN CELLULAR REGULATION}, volume = {33}, unique-id = {1061520}, issn = {0070-2137}, year = {1992}, pages = {249-260} } @article{MTMT:20172709, title = {REGULATION OF ENZYME-ACTIVITY IN THE CELL - EFFECT OF ENZYME CONCENTRATION}, url = {https://m2.mtmt.hu/api/publication/20172709}, author = {Aragon, J J and Sols, A}, doi = {10.1096/fasebj.5.14.1752361}, journal-iso = {FASEB J}, journal = {FASEB JOURNAL}, volume = {5}, unique-id = {20172709}, issn = {0892-6638}, year = {1991}, eissn = {1530-6860}, pages = {2945-2950} } @article{MTMT:1060971, title = {Kinetic advantage of the interaction between the fatty acid β-oxidation enzymes and the complexes of the respiratory chain}, url = {https://m2.mtmt.hu/api/publication/1060971}, author = {Sümegi, Balázs and Porpáczy, Zoltán and Alkonyi, István}, doi = {10.1016/0005-2760(91)90016-B}, journal-iso = {BIOCHIM BIOPHYS ACTA}, journal = {BIOCHIMICA ET BIOPHYSICA ACTA}, volume = {1081}, unique-id = {1060971}, issn = {0006-3002}, year = {1991}, eissn = {1878-2434}, pages = {121-128} } @article{MTMT:20173123, title = {CELLULAR CONCENTRATIONS OF ENZYMES AND THEIR SUBSTRATES}, url = {https://m2.mtmt.hu/api/publication/20173123}, author = {Albe, K R and Butler, M H and Wright, B E}, doi = {10.1016/S0022-5193(05)80266-8}, journal-iso = {J THEOR BIOL}, journal = {JOURNAL OF THEORETICAL BIOLOGY}, volume = {143}, unique-id = {20173123}, issn = {0022-5193}, year = {1990}, eissn = {1095-8541}, pages = {163-195} } @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:21502145, title = {THE VISUALIZATION BY AFFINITY ELECTROPHORESIS OF A SPECIFIC ASSOCIATION BETWEEN THE CONSECUTIVE CITRIC-ACID CYCLE ENZYMES FUMARASE AND MALATE-DEHYDROGENASE}, url = {https://m2.mtmt.hu/api/publication/21502145}, author = {BEECKMANS, S and VANDRIESSCHE, E and KANAREK, L}, doi = {10.1111/j.1432-1033.1989.tb14948.x}, journal-iso = {EUR J BIOCHEM}, journal = {EUROPEAN JOURNAL OF BIOCHEMISTRY}, volume = {183}, unique-id = {21502145}, issn = {0014-2956}, year = {1989}, eissn = {1432-1033}, pages = {449-454} } @article{MTMT:20173082, title = {KINETIC ADVANTAGES OF HETERO-ENZYME COMPLEXES WITH GLUTAMATE-DEHYDROGENASE AND THE ALPHA-KETOGLUTARATE DEHYDROGENASE COMPLEX}, url = {https://m2.mtmt.hu/api/publication/20173082}, author = {Fahien, L A and Macdonald, M J and Teller, J K and Fibich, B and Fahien, C M}, journal-iso = {J BIOL CHEM}, journal = {JOURNAL OF BIOLOGICAL CHEMISTRY}, volume = {264}, unique-id = {20173082}, issn = {0021-9258}, year = {1989}, eissn = {1083-351X}, pages = {12303-12312} } @article{MTMT:1012907, title = {Kinetic and physico-chemical analysis of enzyme complexes and their possible role in the control of metabolism.}, url = {https://m2.mtmt.hu/api/publication/1012907}, author = {KELETI, T and Ovádi, Judit and BATKE, J}, doi = {10.1016/0079-6107(89)90016-3}, journal-iso = {PROG BIOPHYS MOL BIO}, journal = {PROGRESS IN BIOPHYSICS AND MOLECULAR BIOLOGY}, volume = {53}, unique-id = {1012907}, issn = {0079-6107}, year = {1989}, eissn = {1873-1732}, pages = {105-152} } @article{MTMT:20172717, title = {SUPRAMOLECULAR ORGANIZATION OF TRICARBOXYLIC-ACID CYCLE ENZYMES}, url = {https://m2.mtmt.hu/api/publication/20172717}, author = {Lyubarev, A E and Kurganov, B I}, doi = {10.1016/0303-2647(89)90038-5}, journal-iso = {BIOSYSTEMS}, journal = {BIOSYSTEMS}, volume = {22}, unique-id = {20172717}, issn = {0303-2647}, year = {1989}, eissn = {1872-8324}, pages = {91-102} } @article{MTMT:20172653, title = {STRUCTURAL BETA-CELL CHANGES AND TRANSIENT HYPERGLYCEMIA IN MICE TREATED WITH COMPOUNDS INDUCING INHIBITED CITRIC-ACID CYCLE ENZYME-ACTIVITY}, url = {https://m2.mtmt.hu/api/publication/20172653}, author = {Boquist, L and Boquist, S and Ericsson, I}, doi = {10.2337/diabetes.37.1.89}, journal-iso = {DIABETES}, journal = {DIABETES}, volume = {37}, unique-id = {20172653}, issn = {0012-1797}, year = {1988}, eissn = {1939-327X}, pages = {89-98} } @article{MTMT:22803064, title = {Regulation of Malate-dehydrogenase Activity by Glutamate, Citrate, Alpha-ketoglutarate, And Multienzyme Interaction}, url = {https://m2.mtmt.hu/api/publication/22803064}, author = {Fahien, LA and Kmiotek, EH and Macdonald, MJ and Fibich, B and Mandic, M}, journal-iso = {J BIOL CHEM}, journal = {JOURNAL OF BIOLOGICAL CHEMISTRY}, volume = {263}, unique-id = {22803064}, issn = {0021-9258}, year = {1988}, eissn = {1083-351X}, pages = {10687-10697} } @article{MTMT:20172723, title = {CITRIC-ACID CYCLE AS A ONE-STEP REACTION}, url = {https://m2.mtmt.hu/api/publication/20172723}, author = {Forster, M E C}, doi = {10.1016/S0022-5193(88)80020-1}, journal-iso = {J THEOR BIOL}, journal = {JOURNAL OF THEORETICAL BIOLOGY}, volume = {133}, unique-id = {20172723}, issn = {0022-5193}, year = {1988}, eissn = {1095-8541}, pages = {1-11} } @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:20172724, title = {HETEROMEROUS INTERACTIONS AMONG GLYCOLYTIC-ENZYMES AND OF GLYCOLYTIC-ENZYMES WITH F-ACTIN - EFFECTS OF POLY(ETHYLENE GLYCOL)}, url = {https://m2.mtmt.hu/api/publication/20172724}, author = {Walsh, J L and Knull, H R}, doi = {10.1016/0167-4838(88)90104-5}, journal-iso = {BIOCHIM BIOPHYS ACTA}, journal = {BIOCHIMICA ET BIOPHYSICA ACTA}, volume = {952}, unique-id = {20172724}, issn = {0006-3002}, year = {1988}, eissn = {1878-2434}, pages = {83-91} } @article{MTMT:23233025, title = {ENZYME ENZYME INTERACTIONS AS MODULATORS OF THE METABOLIC FLUX THROUGH THE CITRIC-ACID CYCLE}, url = {https://m2.mtmt.hu/api/publication/23233025}, author = {BEECKMANS, S and KANAREK, L}, journal-iso = {BIOCHEM SOC SYMP}, journal = {BIOCHEMICAL SOCIETY SYMPOSIUM}, volume = {1987}, unique-id = {23233025}, issn = {0067-8694}, year = {1987}, eissn = {1744-1439}, pages = {163-172} } @article{MTMT:23233023, title = {THE SUBUNITS OF SUCCINYL-COENZYME-A SYNTHETASE - FUNCTION AND ASSEMBLY}, url = {https://m2.mtmt.hu/api/publication/23233023}, author = {BRIDGER, WA and WOLODKO, WT and HENNING, W and UPTON, C and MAJUMDAR, R and WILLIAMS, SP}, journal-iso = {BIOCHEM SOC SYMP}, journal = {BIOCHEMICAL SOCIETY SYMPOSIUM}, volume = {1987}, unique-id = {23233023}, issn = {0067-8694}, year = {1987}, eissn = {1744-1439}, pages = {103-111} } @article{MTMT:20172721, title = {SUPRAMOLECULAR ORGANIZATION OF ENZYMES OF THE TRICARBOXYLIC-ACID CYCLE}, url = {https://m2.mtmt.hu/api/publication/20172721}, author = {Lyubarev, A E and Kurganov, B I}, journal-iso = {MOL BIOL}, journal = {MOLECULAR BIOLOGY}, volume = {21}, unique-id = {20172721}, issn = {0026-8933}, year = {1987}, eissn = {1608-3245}, pages = {1062-1072} } @article{MTMT:1060978, title = {Interaction between NAD-dependent isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase complex, and NADH:ubiquinone oxidoreductase}, url = {https://m2.mtmt.hu/api/publication/1060978}, author = {Porpáczy, Zoltán and Sümegi, Balázs and Alkonyi, István}, journal-iso = {J BIOL CHEM}, journal = {JOURNAL OF BIOLOGICAL CHEMISTRY}, volume = {262}, unique-id = {1060978}, issn = {0021-9258}, year = {1987}, eissn = {1083-351X}, pages = {9509-9514} } @article{MTMT:1060975, title = {ORGANIZATIONAL ASPECTS OF THE CITRIC-ACID CYCLE}, url = {https://m2.mtmt.hu/api/publication/1060975}, author = {Srere, P A and Sümegi, Balázs and Sherry, A D}, journal-iso = {BIOCHEM SOC SYMP}, journal = {BIOCHEMICAL SOCIETY SYMPOSIUM}, volume = {1987}, unique-id = {1060975}, issn = {0067-8694}, year = {1987}, eissn = {1744-1439}, pages = {173-181} } @article{MTMT:30795153, title = {COMPLEXES OF SEQUENTIAL METABOLIC ENZYMES}, url = {https://m2.mtmt.hu/api/publication/30795153}, author = {SRERE, PA}, doi = {10.1146/annurev.bi.56.070187.000513}, journal-iso = {ANNU REV BIOCHEM}, journal = {ANNUAL REVIEW OF BIOCHEMISTRY}, volume = {56}, unique-id = {30795153}, issn = {0066-4154}, year = {1987}, eissn = {1545-4509}, pages = {89-124} } @article{MTMT:20172728, title = {BIOPHYSICAL CHEMISTRY OF METABOLIC REACTION SEQUENCES IN CONCENTRATED ENZYME SOLUTION AND IN THE CELL}, url = {https://m2.mtmt.hu/api/publication/20172728}, author = {Srivastava, D K and Bernhard, S A}, doi = {10.1146/annurev.biophys.16.1.175}, journal-iso = {ANNU REV BIOPHYS BIOENG}, journal = {ANNUAL REVIEW OF BIOPHYSICS AND BIOENGINEERING}, volume = {16}, unique-id = {20172728}, issn = {0084-6589}, year = {1987}, eissn = {2327-9885}, pages = {175-204} } @article{MTMT:1060977, title = {Electronmicroscopic study on the size of pyruvate dehydrogenase complex in situ}, url = {https://m2.mtmt.hu/api/publication/1060977}, author = {Sümegi, Balázs and Liposits, Zsolt and Inman, L and Paull, W K and Srere, P A}, doi = {10.1111/j.1432-1033.1987.tb13601.x}, journal-iso = {EUR J BIOCHEM}, journal = {EUROPEAN JOURNAL OF BIOCHEMISTRY}, volume = {169}, unique-id = {1060977}, issn = {0014-2956}, year = {1987}, eissn = {1432-1033}, pages = {223-230}, orcid-numbers = {Liposits, Zsolt/0000-0002-3508-2750} } @article{MTMT:20172730, title = {ORGANIZATION OF CITRIC-ACID CYCLE ENZYMES INTO A MULTIENZYME CLUSTER}, url = {https://m2.mtmt.hu/api/publication/20172730}, author = {Barnes, S J and Weitzman, P D J}, doi = {10.1016/0014-5793(86)80621-4}, journal-iso = {FEBS LETT}, journal = {FEBS LETTERS}, volume = {201}, unique-id = {20172730}, issn = {0014-5793}, year = {1986}, eissn = {1873-3468}, pages = {267-270} } @article{MTMT:1060980, title = {ISOLATION AND CHARACTERIZATION OF 3-HYDROXYACYL COENZYME-A DEHYDROGENASE-BINDING PROTEIN FROM PIG-HEART INNER MITOCHONDRIAL-MEMBRANE}, url = {https://m2.mtmt.hu/api/publication/1060980}, author = {Kispál, Gyula and Sümegi, Balázs and Alkonyi, István}, journal-iso = {J BIOL CHEM}, journal = {JOURNAL OF BIOLOGICAL CHEMISTRY}, volume = {261}, unique-id = {1060980}, issn = {0021-9258}, year = {1986}, eissn = {1083-351X}, pages = {14209-14213} } @article{MTMT:20173009, title = {SUCCINYL-COA SYNTHETASE STRUCTURE-FUNCTION-RELATIONSHIPS AND OTHER CONSIDERATIONS}, url = {https://m2.mtmt.hu/api/publication/20173009}, author = {Nishimura, J S}, journal-iso = {ADV ENZYMOL RAMB}, journal = {ADVANCES IN ENZYMOLOGY AND RELATED AREAS OF MOLECULAR BIOLOGY}, volume = {58}, unique-id = {20173009}, issn = {0065-258X}, year = {1986}, pages = {141-172} } @inproceedings{MTMT:1061506, title = {Organization of the Mitochondrial Matrix}, url = {https://m2.mtmt.hu/api/publication/1061506}, author = {Srere, P A and Sümegi, Balázs}, booktitle = {Miocardial and Skeletar Muscle Bio-energetics}, unique-id = {1061506}, keywords = {Animals; Fatty Acids/metabolism; Citric Acid Cycle; Mitochondria, Heart/enzymology/*ultrastructure}, year = {1986}, pages = {13-25} } @article{MTMT:22058588, title = {Enzyme Enzyme Interactions and the Regulation of Metabolic Reaction Pathways.}, url = {https://m2.mtmt.hu/api/publication/22058588}, author = {Srivastava, DK and Bernhard, SA}, doi = {10.1016/B978-0-12-152828-7.50003-2}, journal-iso = {CURR TOP CELL REGUL}, journal = {CURRENT TOPICS IN CELLULAR REGULATION}, volume = {28}, unique-id = {22058588}, issn = {0070-2137}, year = {1986}, pages = {1-68} } @article{MTMT:20172663, title = {PRIMARY STRUCTURE OF THE SUCCINYL-COA SYNTHETASE OF ESCHERICHIA-COLI}, url = {https://m2.mtmt.hu/api/publication/20172663}, author = {Buck, D and Spencer, M E and Guest, J R}, doi = {10.1021/bi00343a031}, journal-iso = {BIOCHEMISTRY-US}, journal = {BIOCHEMISTRY}, volume = {24}, unique-id = {20172663}, issn = {0006-2960}, year = {1985}, eissn = {1520-4995}, pages = {6245-6252} } @article{MTMT:20172731, title = {SUBSTRATE CHANNELING OF OXALACETATE IN SOLID-STATE COMPLEXES OF MALATE-DEHYDROGENASE AND CITRATE SYNTHASE}, url = {https://m2.mtmt.hu/api/publication/20172731}, author = {Datta, A and Merz, J M and Spivey, H O}, journal-iso = {J BIOL CHEM}, journal = {JOURNAL OF BIOLOGICAL CHEMISTRY}, volume = {260}, unique-id = {20172731}, issn = {0021-9258}, year = {1985}, eissn = {1083-351X}, pages = {5008-5012} } @article{MTMT:22836694, title = {Purification and Characterization of the Pea Chloroplast Pyruvate Dehydrogenase Complex 1. A Source of Acetyl-CoA and NADH for Fatty Acid Biosynthesis}, url = {https://m2.mtmt.hu/api/publication/22836694}, author = {Pamela, J Camp and Douglas, D Randall}, doi = {10.​1104/​pp.​77.​3.​571}, journal-iso = {PLANT PHYSIOL}, journal = {PLANT PHYSIOLOGY}, volume = {77}, unique-id = {22836694}, issn = {0032-0889}, year = {1985}, eissn = {1532-2548}, pages = {571-577} } @article{MTMT:20172664, title = {ORGANIZATION OF KREBS TRICARBOXYLIC-ACID CYCLE ENZYMES IN MITOCHONDRIA}, url = {https://m2.mtmt.hu/api/publication/20172664}, author = {Robinson, J B and Srere, P A}, journal-iso = {J BIOL CHEM}, journal = {JOURNAL OF BIOLOGICAL CHEMISTRY}, volume = {260}, unique-id = {20172664}, issn = {0021-9258}, year = {1985}, eissn = {1083-351X}, pages = {800-805} } @article{MTMT:1060983, title = {INTERACTION BETWEEN CITRATE SYNTHASE AND THIOLASE}, url = {https://m2.mtmt.hu/api/publication/1060983}, author = {Sümegi, Balázs and Gilbert, H F and Srere, P A}, journal-iso = {J BIOL CHEM}, journal = {JOURNAL OF BIOLOGICAL CHEMISTRY}, volume = {260}, unique-id = {1060983}, issn = {0021-9258}, year = {1985}, eissn = {1083-351X}, pages = {188-190} } @article{MTMT:20172667, title = {WHY ARE ENZYMES SO BIG}, url = {https://m2.mtmt.hu/api/publication/20172667}, author = {Srere, P A}, doi = {10.1016/0968-0004(84)90221-4}, journal-iso = {TRENDS BIOCHEM SCI}, journal = {TRENDS IN BIOCHEMICAL SCIENCES}, volume = {9}, unique-id = {20172667}, issn = {0968-0004}, year = {1984}, eissn = {1362-4326}, pages = {387-390} } @article{MTMT:1060986, title = {BINDING OF THE ENZYMES OF FATTY-ACID BETA-OXIDATION AND SOME RELATED ENZYMES TO PIG-HEART INNER MITOCHONDRIAL-MEMBRANE}, url = {https://m2.mtmt.hu/api/publication/1060986}, author = {Sümegi, Balázs and Srere, P A}, journal-iso = {J BIOL CHEM}, journal = {JOURNAL OF BIOLOGICAL CHEMISTRY}, volume = {259}, unique-id = {1060986}, issn = {0021-9258}, year = {1984}, eissn = {1083-351X}, pages = {8748-8752} } @article{MTMT:1060984, title = {Complex I Binds Several Mitochondrial NAD-coupled Dehydrogenases}, url = {https://m2.mtmt.hu/api/publication/1060984}, author = {Sümegi, Balázs and Srere, P A}, journal-iso = {J BIOL CHEM}, journal = {JOURNAL OF BIOLOGICAL CHEMISTRY}, volume = {259}, unique-id = {1060984}, issn = {0021-9258}, keywords = {Oxygen Consumption; Animals; Humans; SWINE; KINETICS; Oxidoreductases/*metabolism; Protein Binding; Erythrocyte Membrane/metabolism; NAD; Malate Dehydrogenase/metabolism; Mitochondria, Heart/*enzymology; Intracellular Membranes/enzymology; Pyruvate Dehydrogenase Complex/metabolism; Ketoglutarate Dehydrogenase Complex/metabolism; NAD(P)H Dehydrogenase (Quinone); NADH, NADPH Oxidoreductases/*metabolism; 3-Hydroxyacyl CoA Dehydrogenases/metabolism; Quinone Reductases/*metabolism}, year = {1984}, eissn = {1083-351X}, pages = {15040-15045} } @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} }