D
Dieter Brdiczka
Researcher at University of Konstanz
Publications - 81
Citations - 9786
Dieter Brdiczka is an academic researcher from University of Konstanz. The author has contributed to research in topics: Mitochondrion & Hexokinase. The author has an hindex of 47, co-authored 81 publications receiving 9547 citations. Previous affiliations of Dieter Brdiczka include University of Rochester.
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Journal ArticleDOI
Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis.
Journal ArticleDOI
The permeability transition pore complex: a target for apoptosis regulation by caspases and bcl-2-related proteins.
Isabel Marzo,Catherine Brenner,Naoufal Zamzami,Santos A. Susin,Gisela Beutner,Dieter Brdiczka,René Rémy,Zhihua Xie,John C. Reed,Guido Kroemer +9 more
TL;DR: It is shown that PT pore complexes reconstituted in liposomes exhibit a functional behavior comparable with that of the naturalPT pore present in intact mitochondria.
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Metabolic Differentiation of Distinct Muscle Types at the Level of Enzymatic Organization
TL;DR: Nature of the fuel, type of metabolism and catabolic rate thus represent fundamental elements in metabolic differentiation.
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Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition
TL;DR: A fusion protein between cyclophilin-D and glutathione S-transferase (GST) was shown to bind to purified liver inner mitochondrial membranes (IMMs) in a cyclosporin A (CsA)-sensitive manner and was enhanced by diamide treatment of the IMMs.
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Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases.
TL;DR: The inhibitory effect of N-methylVal-4-cyclosporin on the hexokinase complex may be explained by direct interaction with the creatine kinase dimer that appeared to support octamer formation.