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A list of all pages that have property "Has abstract" with value "10th Int. CeBiTec Research Conference, Bielefeld, Germany, 2021". Since there have been only a few results, also nearby values are displayed.

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  • Koenig 1969 Biochem J  + (1. The effects of succinate oxidation on p1. The effects of succinate oxidation on pyruvate and also isocitrate oxidation by rat liver mitochondria were studied. 2. Succinate oxidation was without effect on pyruvate and isocitrate oxidation when respiration was maximally activated with ADP. 3. When respiration was partially inhibited by atractylate, succinate oxidation severely inhibited the oxidation of pyruvate and isocitrate. 4. This inhibitory effect of succinate was associated with a two- to three-fold increase in the reduction of mitochondrial NAD(+) but no change in the reduction of cytochrome b. 5. It is concluded that, in the partially energy-controlled state, respiration is more severely inhibited at the first phosphorylating site than at the other two. 6. The effects of succinate oxidation are compared with those of palmitoylcarnitine oxidation. It is concluded that a rapid flow of electrons directly into the respiratory chain at the level of cytochrome b is in itself inadequate to inhibit the oxidation of intramitochondrial NADH. 7. The effects of succinate oxidation on pyruvate oxidation were similar in rat heart and liver mitochondria.milar in rat heart and liver mitochondria.)
  • Hoek 1970 Biochim Biophys Acta  + (1. The kinetics of the efflux of Pi and ma1. The kinetics of the efflux of Pi and malate as well as the relationship between Pi transport and intra- and extramitochondrial pH changes were studied in rat-liver mitochondria in the presence of rotenone and oligomycin at different pH's.</br></br>2. At high pH a fast efflux of Pi from the mitochondria occurs in the first few seconds, followed by a slow re-entry of Pi into the mitochondria. Under the same conditions the exit of malate shows a time lag of 2–4 sec. The exit of malate coincides with the re-entry of Pi.</br></br>3. In the presence of butylmalonate the exit of endogenous Pi is coupled with a concomitant alkalinization of the mitochondrial matrix space, as calculated from the distribution of 5,5-[14C]dimethyloxazolidine-2,4-dione.</br></br>4. The stoicheiometry of the Pi-hydroxyl exchange was found to be 1:1.</br></br>5. The kinetics of Pi transport are consistent with previous observations that there is a direct exchange between OH− and Pi, but not between OH− and malate. The equilibrium distribution of H2PO4− and OH− deviates from the Donnan distribution. This may be explained by assuming a pH-dependent binding of Pi in the mitochondria.pendent binding of Pi in the mitochondria.)
  • Claude 1945 J Exp Med  + (1. The present paper constitutes a prelimi1. The present paper constitutes a preliminary study of the morphology of mitochondria by means of electron microscopy.</br></br>2. The mitochondria that were the subject of this investigation were obtained from a lymphosarcoma of the rat. They were separated from the other components of the leukemic cells by a method of differential centrifugation, and thus made available for direct examination in the electron microscope.</br></br>3. In the purified form the mitochondria appeared as spherical bodies, the majority of them varying in size approximately from 0.6 to 1.3 µ in diameter.</br></br>4. Certain aspects of mitochondria in the electron microscope suggest that these elements are surrounded by a differentiated membrane. In some cases the limiting membrane seemed to be responsible for maintaining the general shape of the mitochondria, even when most of the mitochondrial substance had been lost.</br></br>5. By means of the electron microscope, it is possible to distinguish small elements, 80 to 100 mµ in diameter, within the body of certain mitochondria. Further work is suggested to establish whether these small granules are normal constituents of mitochondria, and what relation may exist between them and ordinary microsomes.</br></br>6. The nature of mitochondria as morphological units is discussed. Present evidence indicates that mitochondria constitute definite physical entities which can persist in the absence of the cytoplasm.n persist in the absence of the cytoplasm.)
  • Griffiths 1995 Biochem J  + (1. The yield of mitochondria isolated from1. The yield of mitochondria isolated from perfused hearts subjected to 30 min ischaemia followed by 15 min reperfusion was significantly less than that for control hearts, and this was associated with a decrease in the rates of ADP-stimulated respiration. 2. The presence of 0.2 microM cyclosporin A (CsA) in the perfusion medium during ischaemia and reperfusion caused mitochondrial recovery to return to control values, but did not reverse the inhibition of respiration. 3. A technique has been devised to investigate whether the Ca(2+)-induced non-specific pore of the mitochondrial inner membrane opens during ischaemia and/or reperfusion of the isolated rat heart. The protocol involved loading the heart with 2-deoxy[3H]glucose ([3H]DOG), which will only enter mitochondria when the pore opens. Subsequent isolation of mitochondria demonstrated that [3H]DOG did not enter mitochondria during global isothermic ischaemia, but did enter during the reperfusion period. 4. The amount of [3H]DOG that entered mitochondria increased with the time of ischaemia, and reached a maximal value after 30-40 min of ischaemia. 5. CsA at 0.2 microM did not prevent [3H]DOG becoming associated with the mitochondria, but rather increased it; this was despite CsA having a protective effect on heart function similar to that shown previously [Griffiths and Halestrap (1993) J. Mol. Cell. Cardiol. 25, 1461-1469]. 6. The non-immunosuppressive CsA analogue [MeAla6]cyclosporin was shown to have a similar Ki to CsA on purified mitochondrial peptidyl-prolyl cis-trans-isomerase and mitochondrial pore opening, and also to have a similar protective effect against reperfusion injury. 7. Using isolated heart mitochondria, it was demonstrated that pore opening could become CsA-insensitive under conditions of adenine nucleotide depletion and high matrix [Ca2+] such as may occur during the initial phase of reperfusion. The apparent increase in mitochondrial [3H]DOG in the CsA-perfused hearts is explained by the ability of the drug to stabilize pore closure and so decrease the loss of [3H]DOG from the mitochondria during their preparation.the mitochondria during their preparation.)
  • Kearney 1960 J Biol Chem  + (1. Unlike other known flavoproteins, in wh1. Unlike other known flavoproteins, in which the flavin is relatively loosely bound and is easily liberated by suitable methods of denaturation, in succinic dehydrogenase from beef heart the flavin component is so tightly held that neither treatment with strong acids nor thermal denaturation separates it from the protein.</br></br>2. Extensive digestion of the purified dehydrogenase with suitable proteolytic enzymes liberates the flavin in an acid-soluble form, which is not, however, identical with known derivatives of riboflavin. The flavin appears in the digest in several chromatographically distinct forms, which may be separated from each other by purification on ion exchange resins or by chromatography on filter paper.</br></br>3. The main flavin components have been extensively purified and degraded to the mononucleotide and dephosphorylated flavin levels. The dinucleotide contains 1 mole of 5’-adenylic acid, 2 atoms of phosphorus bound in pyrophosphate linkage and 1 mole of ribose. It differs from authentic flavin adenine dinucleotide (FAD) in numerous regards, including its inactivity in the n-amino acid oxidase test, shifted absorption spectrum, shifted pH-fluorescence curve, and in the presence of cationic group(s). After degradation to the mononucleotide and dephosphorylated flavin level, similar differences exist between the resulting compounds and authentic riboflavin 5’-phosphate and riboflavin, respectively. Irradiation in alkali degrades the flavin further, but the resulting compound is not identical with lumiflavin.</br></br>4. These differences and the greater water solubility of the unphosphorylated compound as compared with riboflavin are best explained by the hypothesis that the flavin in the dehydrogenase is held to a peptide chain by a covalent linkage which survives proteolytic digestion. The compounds in the digest, therefore, would be peptides of FAD, representing fragments of the original enzyme.</br></br>5. Evidence for the flavin peptide hypothesis has come from the finding that throughout very extensive purification by a variety of methods the flavin is always accompanied by peptide material. In the most purified fraction, believed to be free of contaminating peptides, alanine, serine, threonine, glutamic acid, and valine were present in molar ratio to the flavin and an additional mole of serine was present as N-terminal group. Similar amino acid compositions were found in 2 other samples, purified by different procedures.</br></br>6. Evidence pertaining to the flavin peptide hypothesis and the possible structure of the flavin is discussed.ible structure of the flavin is discussed.)
  • Gnaiger 2013 Abstract MiP2013  + (10 years ago the uncoupling hypothesis was10 years ago the uncoupling hypothesis was presented for mitochondrial haplogroups of arctic populations suggesting that lower coupling of mitochondrial respiration to ATP production was selected for in favor of higher heat dissipation as an adaptation to cold climates [1,2]. Up to date no actual tests have been published to compare mitochondrial coupling in tissues obtained from human populations with regional mtDNA variations. Analysis of oxidative phosphorylation (OXPHOS) is a major component of mitochondrial phenotyping [3]. We studied mitochondrial coupling in small biopsies of arm and leg muscle of Inuit of the Thule and Dorset haplogroups in northern Greenland compared to Danes from western Europe haplogroups. Inuit had a higher capacity to oxidize fat substrate in leg and arm muscle, yet mitochondrial respiration compensating for proton leak was proportionate with OXPHOS capacity. Biochemical coupling efficiency was preserved across variations in muscle fiber type and uncoupling protein-3 content. After 42 days of skiing on the sea ice in northern Greenland, Danes demonstrated adaptive substrate control through an increase in fatty acid oxidation approaching the level of the Inuit, yet coupling control of oxidative phosphorylation was conserved. Our findings reveal that coupled ATP production is of primary evolutionary significance for muscle tissue independent of adaptations to the cold.ue independent of adaptations to the cold.)
  • ASMRM 2013 Seoul KR  + (10<sup>th</sup> Conference of the Asian Society of Mitochondrial Research and Medicine - [http://asmrm2013.com/common_files/mess.asp ASMRM 2013], Seoul KR)
  • MiP2014  + (10<sup>th</sup> MiP''conference'': Joint IUBMB/MiP Symposium on Mitochondrial Physiology - a Point/Counterpoint Meeting, Obergurgl, Austria; with post-conference workshop '''[[MiPNet19.10 | 95th Oroboros O2k-Workshop]]'''.)
  • 10th Conference of the International Coenzyme Q10 Association 2022 Hamburg DE  + (10th Conference of the International Coenzyme Q10 Association, Hamburg, 2022)
  • 10th European Algae Industry Summit 2020 Reykjavik IS  + (10th European Algae Industry Summit, Reykjavik, Iceland, 2020)
  • 10th International Luebeck Conference on the Pathophysiology and Pharmacology of Erythropoietin and other Hemopoietic Growth Factors  + (10th International Luebeck Conference on the Pathophysiology and Pharmacology of Erythropoietin and other Hemopoietic Growth Factors, Lübeck, DE, [https://www.physio.uni-luebeck.de/index.php?id=162 10th International Luebeck Conference])
  • 10th Italian Meeting on Mitochondrial Disease 2020 IT  + (10th Italian Meeting on Mitochondrial Diseases , Virtual, 2020)
  • TriMAD Conference 2023 Pennsylvania US  + (10th Translational Research in Mitochondri10th Translational Research in Mitochondria/Metabolism, Aging, and Disease (TRiMAD) Conference, Pennsylvania, United States, 2023 </br></br></br></br>== General information ==</br>:::: TRiMAD is a collaborative venture between The Pennsylvania State University, University of Pittsburgh Medical Center, The Children’s Hospital of Philadelphia (CHoP) Research Institute, and The University of Pennsylvania Perelman School of Medicine ([https://www.huck.psu.edu/node/15830 Website])</br></br>== Venue == </br>:::: University of Pittsburgh</br>:::: Bridgeside Point 1, 5th Floor</br>:::: 100 Technology Drive</br>:::: Pittsburgh, PA 15219</br></br>== Organizers ==</br>:::: University of Pittsburgh</br>:::: Aging Institute</br>:::: Center for Metabolism & Mitochondrial Medicine</br></br>== Program ==</br>:::: Please find the programme [https://aging.pitt.edu/event/trimad-2023/ here]</br></br></br>== Registration ==</br>:::: [https://forms.office.com/pages/responsepage.aspx?id=ifT5nqDg606HzDpSYRL9DXg8U8hQ84RKssucFsBERrBURTU2T1lFR01DS0hYNlZGRjNDTzg2QVJRSC4u Register here]</br> </br>== Lecturers and tutors ==</br></br>:::: The list of speakers can be found [https://aging.pitt.edu/event/trimad-2023/ here]ttps://aging.pitt.edu/event/trimad-2023/ here])
  • Targeting Mitochondria World Congress 2019 Berlin DE  + (10th World Congress on Targeting Mitochond10th World Congress on Targeting Mitochondria, Berlin, Germany, 2019 </br></br></br>== General information == </br>:::: Flyer available for [http://wiki.oroboros.at/images/7/7f/Berlin_2019.pdf download]</br></br>== Venue == </br>:::: INTERCONINENTAL BERLIN HOTEL</br>:::: Budapester Str. 2, 10787</br>:::: Berlin, Germany</br>::::[https://targeting-mitochondria.com/venue Hotel and Travel]</br></br>== Programme ==</br>:::: [https://targeting-mitochondria.com/preliminary-program here]</br></br>== Speakers == </br>:::: List of speakers can be found [https://targeting-mitochondria.com/speakers-2019 here]</br></br>== Registration ==</br>:::: [https://targeting-mitochondria.com/registration Registration and more information]tration Registration and more information])
  • 115th International Titisee Conferences Titisee DE  + (115th ITC: Evolutionary mitochondrial biology: molecular, biochemical, and metabolic diversity, Titisee, Germany.)
  • 11th Annual Congress of Cardiology 2019 Suzhou CN  + (11th Annual Congress of Cardiology, Suzhou, China, 2019)
  • MiP2015  + (11th Conference on Mitochondrial Physiology, 2015 Sep 07-11, Luční Bouda, Czech Republic.)
  • Targeting Mitochondria World Congress 2020 Virtual  + (11th World Congress on Targeting Mitochond11th World Congress on Targeting Mitochondria, Virtual, 2020 </br></br></br>== General information == </br>:::: After a long and thorough discussion among the scientific and organizing committees, we have decided to organize our 11th Conference of Targeting Mitochondria, on October 29-30, 2020 as an ONLY Virtual Congress.</br></br>== Programme ==</br>:::: [https://targeting-mitochondria.com/preliminary-program here]</br></br>== Speakers == </br>:::: List of speakers can be found [https://targeting-mitochondria.com/speakers here]</br></br>== Registration ==</br>:::: [https://targeting-mitochondria.com/registration Registration and more information]tration Registration and more information])
  • 11th ÖGMBT Annual Meeting 2019 Salzburg AT  + (11th ÖGMBT Annual Meeting - Inside the world of biomolecules, Salzburg, Austria, 2019)
  • ASMRM 2015 Hangzhou CN  + (12<sup>th</sup> Conference of the Asian Society of Mitochondrial Research and Medicine - [http://www.ig.zju.edu.cn/ASMRM/EN/ ASMRM 2015], Hangzhou CN)