Mitochondrial ATP synthase disorders: molecular mechanisms and the quest for curative therapeutic approaches. Export

@article{citeulike:4460758, abstract = {In mammals, the majority of cellular ATP is produced by the mitochondrial F1F(O)-ATP synthase through an elaborate catalytic mechanism. While most subunits of this enzymatic complex are encoded by the nuclear genome, a few essential components are encoded in the mitochondrial genome. The biogenesis of this multi-subunit enzyme is a sophisticated multi-step process that is regulated on levels of transcription, translation and assembly. Defects that result in diminished abundance or functional impairment of the F1F(O)-ATP synthase can cause a variety of severe neuromuscular disorders. Underlying mutations have been identified in both the nuclear and the mitochondrial DNA. The pathogenic mechanisms are only partially understood. Currently, the therapeutic options are extremely limited. Alternative methods of treatment have however been proposed, but still encounter several technical difficulties. The application of novel scientific approaches promises to deepen our understanding of the molecular mechanisms of the ATP synthase, unravel novel therapeutic pathways and improve the unfortunate situation of the patients suffering from such diseases.}, author = {Kucharczyk, R. and Zick, M. and Bietenhader, M. and Rak, M. and Couplan, E. and Blondel, M. and Caubet, S. D. and di Rago, J. P.}, citeulike-article-id = {4460758}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.bbamcr.2008.06.012}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/18620007}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=18620007}, doi = {10.1016/j.bbamcr.2008.06.012}, issn = {0006-3002}, journal = {Biochimica et biophysica acta}, keywords = {allotopic, atp6, atp8, basis, disease, goodref, litrev, mitochondria, morphology, mtdna, narp, projmt, projnarp, respiration, review, ros, yeast}, month = {January}, number = {1}, pages = {186--199}, posted-at = {2009-05-04 16:51:10}, priority = {0}, title = {Mitochondrial ATP synthase disorders: molecular mechanisms and the quest for curative therapeutic approaches.}, url = {http://dx.doi.org/10.1016/j.bbamcr.2008.06.012}, volume = {1793}, year = {2009} }

TY - JOUR ID - citeulike:4460758 L3 - citeulike-article-id:4460758 N2 - In mammals, the majority of cellular ATP is produced by the mitochondrial F1F(O)-ATP synthase through an elaborate catalytic mechanism. While most subunits of this enzymatic complex are encoded by the nuclear genome, a few essential components are encoded in the mitochondrial genome. The biogenesis of this multi-subunit enzyme is a sophisticated multi-step process that is regulated on levels of transcription, translation and assembly. Defects that result in diminished abundance or functional impairment of the F1F(O)-ATP synthase can cause a variety of severe neuromuscular disorders. Underlying mutations have been identified in both the nuclear and the mitochondrial DNA. The pathogenic mechanisms are only partially understood. Currently, the therapeutic options are extremely limited. Alternative methods of treatment have however been proposed, but still encounter several technical difficulties. The application of novel scientific approaches promises to deepen our understanding of the molecular mechanisms of the ATP synthase, unravel novel therapeutic pathways and improve the unfortunate situation of the patients suffering from such diseases. IS - 1 JF - Biochimica et biophysica acta SN - 0006-3002 EP - 199 TI - Mitochondrial ATP synthase disorders: molecular mechanisms and the quest for curative therapeutic approaches. VL - 1793 SP - 186 KW - allotopic KW - atp6 KW - atp8 KW - basis KW - disease KW - goodref KW - litrev KW - mitochondria KW - morphology KW - mtdna KW - narp KW - projmt KW - projnarp KW - respiration KW - review KW - ros KW - yeast AU - Kucharczyk, R AU - Zick, M AU - Bietenhader, M AU - Rak, M AU - Couplan, E AU - Blondel, M AU - Caubet, SD AU - di Rago, JP PY - 2009/01// UR - http://dx.doi.org/10.1016/j.bbamcr.2008.06.012 ER -