PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27129925-0 2016 Stimulation by pro-apoptotic valinomycin of cytosolic NADH/cytochrome c electron transport pathway-Effect of SH reagents. Valinomycin 29-40 cytochrome c, somatic Homo sapiens 59-71 27129925-6 2016 Valinomycin at 2nM stimulates both the energy-dependent reversible mitochondrial swelling and the NADH/cyto-c oxidation pathway. Valinomycin 0-11 cytochrome c, somatic Homo sapiens 103-109 27129925-7 2016 The pro-apoptotic activity of valinomycin, as well as to the dissipation of membrane potential, can be also ascribed to the increased activity of the NADH/cyto-c oxidation pathway useful as an additional source of energy for apoptosis. Valinomycin 30-41 cytochrome c, somatic Homo sapiens 155-161 27129925-8 2016 It can be speculated that the activation of the NADH/cyto-c system coupled to valinomycin-induced mitochondrial osmotic swelling may represent a strategy to activate apoptosis in confined solid tumours. Valinomycin 78-89 cytochrome c, somatic Homo sapiens 53-59 21739274-1 2011 In valinomycin induced stimulation of mitochondrial energy dependent reversible swelling, supported by succinate oxidation, cytochrome c (cyto-c) and sulfite oxidase (Sox) [both present in the mitochondrial intermembrane space (MIS)] are released outside. Valinomycin 3-14 cytochrome c, somatic Homo sapiens 124-136 23037694-5 2012 We previously showed that valinomycin, a potassium selective ionophore, also caused release of cytochrome c from mitochondria without inducing PT. Valinomycin 26-37 cytochrome c, somatic Homo sapiens 95-107 21739274-0 2011 Valinomycin induced energy-dependent mitochondrial swelling, cytochrome c release, cytosolic NADH/cytochrome c oxidation and apoptosis. Valinomycin 0-11 cytochrome c, somatic Homo sapiens 61-73 21739274-0 2011 Valinomycin induced energy-dependent mitochondrial swelling, cytochrome c release, cytosolic NADH/cytochrome c oxidation and apoptosis. Valinomycin 0-11 cytochrome c, somatic Homo sapiens 98-110 21739274-1 2011 In valinomycin induced stimulation of mitochondrial energy dependent reversible swelling, supported by succinate oxidation, cytochrome c (cyto-c) and sulfite oxidase (Sox) [both present in the mitochondrial intermembrane space (MIS)] are released outside. Valinomycin 3-14 cytochrome c, somatic Homo sapiens 138-144 21739274-8 2011 Rather than to the dissipation of membrane potential, the pro-apoptotic property of valinomycin can be ascribed to both the release of cyto-c from mitochondria to cytosol and the increased rate of cytosolic NADH coupled with an increased availability of energy in the form of glycolytic ATP, useful for the correct execution of apoptotic program. Valinomycin 84-95 cytochrome c, somatic Homo sapiens 135-141 19218587-2 2009 Our previous study showed that valinomycin also caused the release of cytochrome c from mitochondria but without inducing this PT (Shinohara, Y., Almofti, M. R., Yamamoto, T., Ishida, T., Kita, F., Kanzaki, H., Ohnishi, M., Yamashita, K., Shimizu, S., and Terada, H. (2002) Permeability transition-independent release of mitochondrial cytochrome c induced by valinomycin. Valinomycin 31-42 cytochrome c, somatic Homo sapiens 70-82 12841327-4 2002 CsA-sensitive mitochondrial swelling, depolarization, and the release of Ca2+ and Cyt.c were induced by low concentrations of arachidonic acid, triiodothyronine (T3), or 6-hydroxdopamine but not by valinomycin and high concentrations of the fatty acid or T3. Valinomycin 198-209 cytochrome c, somatic Homo sapiens 82-87 12392554-0 2002 Permeability transition-independent release of mitochondrial cytochrome c induced by valinomycin. Valinomycin 85-96 cytochrome c, somatic Homo sapiens 61-73 12392554-5 2002 However, valinomycin did induce a significant release of cytochrome c, and thus it may be a nice tool to study the processes of mitochondrial cytochrome c release. Valinomycin 9-20 cytochrome c, somatic Homo sapiens 57-69 12392554-5 2002 However, valinomycin did induce a significant release of cytochrome c, and thus it may be a nice tool to study the processes of mitochondrial cytochrome c release. Valinomycin 9-20 cytochrome c, somatic Homo sapiens 142-154 11641429-4 2001 In contrast, valinomycin-induced cytochrome c-EGFP release occurred slowly over several hours. Valinomycin 13-24 cytochrome c, somatic Homo sapiens 33-45 11641429-5 2001 Unlike staurosporine, the valinomycin-induced cytochrome c release was not associated with translocation of the proapoptotic Bax protein to the mitochondria, and was not accompanied by co-release of the proapoptotic Smac protein. Valinomycin 26-37 cytochrome c, somatic Homo sapiens 46-58 1665913-0 1991 Chlorophyll photosensitized electron transfer reactions in lipid vesicles: enhancement in yield of vectorial electron transfer across the bilayer from reduced cytochrome c to oxidized ferredoxin by addition of valinomycin plus potassium ion. Valinomycin 210-221 cytochrome c, somatic Homo sapiens 159-171 11426445-6 2001 Prolonged exposure to valinomycin induced significant matrix swelling, and per se also caused release of cytochrome c from mitochondria. Valinomycin 22-33 cytochrome c, somatic Homo sapiens 105-117 11426445-7 2001 In contrast to staurosporine, however, valinomycin-induced cytochrome c release and cell death were not associated with caspase-3 activation and insensitive to Bcl-xL overexpression. Valinomycin 39-50 cytochrome c, somatic Homo sapiens 59-71 1318017-2 1992 This appears as an inhibition of substrate oxidation (cytochrome c) or reduction (O2) rates which, in the first few turnovers, can be largely removed upon addition of valinomycin, a specific K+ carrier. Valinomycin 167-178 cytochrome c, somatic Homo sapiens 54-66 3032620-4 1987 The results obtained show that, whilst ferrocytochrome c pulses of the aerobic oxidase vesicles at neutral pH and in the presence of saturating concentrations of valinomycin and K+ to ensure charge compensation produced H+/e- ratios around 1 (as has been shown previously), oxygen pulses of reduced anaerobic vesicles supplemented with cytochrome c, gave H+/e- ratios around 0.3. Valinomycin 162-173 cytochrome c, somatic Homo sapiens 44-56 2158497-0 1990 The K(+)-ionophores nonactin and valinomycin interact differently with the protein of reconstituted cytochrome c oxidase. Valinomycin 33-44 cytochrome c, somatic Homo sapiens 100-112 2158497-1 1990 The K(+)-ionophores valinomycin and nonactin induce a qualitatively identical change of the visible spectrum of isolated oxidized cytochrome c oxidase (red shift), but the amplitude is half with nonactin. Valinomycin 20-31 cytochrome c, somatic Homo sapiens 130-142 2158497-2 1990 Valinomycin, in the presence or absence of a protonophore, stimulates the respiration of the reconstituted enzyme to a higher extent than nonactin and results in a higher Km for cytochrome c. Valinomycin 0-11 cytochrome c, somatic Homo sapiens 178-190 6305365-4 1983 The rates of both cytochrome c oxidation and proton uptake were stimulated by addition of ionophores such as trifluoromethoxy carbonyl cyanide phenylhydrazone (FCCP), nigericin and valinomycin. Valinomycin 181-192 cytochrome c, somatic Homo sapiens 18-30 2410909-2 1985 In the presence of valinomycin, the oxidation of cytochrome c is linked to proton ejection in the external medium, with an apparent stoichiometry (H+/e-) of 0.93 +/- 0.22, under conditions in which the enzyme is in the more active "pulsed" state (i.e., having undergone oxidation-reduction cycles). Valinomycin 19-30 cytochrome c, somatic Homo sapiens 49-61 2410570-2 1985 In the presence of valinomycin, proton pumping and cytochrome c oxidation by cytochrome oxidase are synchronous up to rate constants of approximately 9 sec-1. Valinomycin 19-30 cytochrome c, somatic Homo sapiens 51-63 207320-10 1978 The Km for cytochrome c in 67 mM, pH 7.4, phosphate buffer with ascorbate as substrate, was 9 micrometer in both absence and presence of valinomycin and FCCP. Valinomycin 137-148 cytochrome c, somatic Homo sapiens 11-23 40970-2 1979 In the presence of valinomycin, 2 K+ ions were taken up by the vesicles per electron transferred from cytochrome c to oxygen. Valinomycin 19-30 cytochrome c, somatic Homo sapiens 102-114 656407-7 1978 Azide acts non-competitively towards cytochrome c when the latter is oxidized by cytochrome aa3-containing proteoliposomes both in the energized and deenergized (plus p-trifluoromethoxy carbonyl cyanide phenylhydrazone and valinomycin) conditions. Valinomycin 223-234 cytochrome c, somatic Homo sapiens 37-49