oligomycin
Oligomycin is an antibiotic that inhibits ATP synthase by blocking its proton channel (F0 subunit), which is necessary for oxidative phosphorylation of ADP to ATP (energy production). The inhibition of ATP synthesis would also stop electron transport cha,The classical example is the antibiotic oligomycin which binds to a 23 kd polypeptide in the F0 baseplate subunit of the F0/F1 ATPase (ATP synthase) thereby preventing protons from passing back into the mitochondria and stopping the operation of the proto,Oligomycins are macrolides created by Streptomyces that can be poisonous to other organisms. Function[edit]. They have use as antibiotics. Oligomycin A is an inhibitor of ATP synthase. In oxidative phosphorylation research, it is used to prevent state 3 (,Oligomycin A ist ein von Streptomyces erzeugtes Antibiotikum aus der Gruppe der Makrolide, die für andere Organismen giftig sein können. Oligomycin A ist der bekannteste Vertreter der Oligomycine. Inhaltsverzeichnis. [Verbergen]. 1 Wirkung; 2 Oligomycine;,Sigma-Aldrich offers Sigma-75351, Oligomycin A for your research needs. Find product specific information including CAS, MSDS, protocols and references. ,Oligomycin is a natural antibiotic isolated from Streptomyces diastatochromogenes which inhibits mitochondrial H+-ATP synthase. It is primarily found to act as an inhibitor of mitochondrial respiration and swelling. This antibiotic is widely used as an in,Staurosporine-induced apoptosis is sensitive to Bcl-2 but insensitive to Cyclosporin A and oligomycin. The effect of oligomycin is not due to changes in mitochondrial membrane potential or to inhibition of ATP synthesis/hydrolysis since (a) uncouplers (CC,Oncogene. 2002 Nov 21;21(53):8149-57. Oligomycin, inhibitor of the F0 part of H+-ATP-synthase, suppresses the TNF-induced apoptosis. Shchepina LA(1), Pletjushkina OY, Avetisyan AV, Bakeeva LE, Fetisova EK, Izyumov DS, Saprunova VB, Vyssokikh MY, Chernyak
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 oligomycin 相關參考資料
7 Useful Tips for Oligomycin - AG Blog - AG Scientific
Oligomycin is an antibiotic that inhibits ATP synthase by blocking its proton channel (F0 subunit), which is necessary for oxidative phosphorylation of ADP to ATP (energy production). The inhibition ... http://agscientific.com Oligomycin - an overview | ScienceDirect Topics
The classical example is the antibiotic oligomycin which binds to a 23 kd polypeptide in the F0 baseplate subunit of the F0/F1 ATPase (ATP synthase) thereby preventing protons from passing back into t... https://www.sciencedirect.com Oligomycin - Wikipedia
Oligomycins are macrolides created by Streptomyces that can be poisonous to other organisms. Function[edit]. They have use as antibiotics. Oligomycin A is an inhibitor of ATP synthase. In oxidative ph... https://en.wikipedia.org Oligomycin A – Wikipedia
Oligomycin A ist ein von Streptomyces erzeugtes Antibiotikum aus der Gruppe der Makrolide, die für andere Organismen giftig sein können. Oligomycin A ist der bekannteste Vertreter der Oligomycine. Inh... https://de.wikipedia.org Oligomycin A ≥95% (HPLC) | Sigma-Aldrich
Sigma-Aldrich offers Sigma-75351, Oligomycin A for your research needs. Find product specific information including CAS, MSDS, protocols and references. https://www.sigmaaldrich.com Oligomycin | Alomone Labs
Oligomycin is a natural antibiotic isolated from Streptomyces diastatochromogenes which inhibits mitochondrial H+-ATP synthase. It is primarily found to act as an inhibitor of mitochondrial respiratio... https://www.alomone.com Oligomycin, inhibitor of the F0 part of H+-ATP-synthase ... - Nature
Staurosporine-induced apoptosis is sensitive to Bcl-2 but insensitive to Cyclosporin A and oligomycin. The effect of oligomycin is not due to changes in mitochondrial membrane potential or to inhibiti... http://www.nature.com Oligomycin, inhibitor of the F0 part of H+-ATP-synthase ... - NCBI
Oncogene. 2002 Nov 21;21(53):8149-57. Oligomycin, inhibitor of the F0 part of H+-ATP-synthase, suppresses the TNF-induced apoptosis. Shchepina LA(1), Pletjushkina OY, Avetisyan AV, Bakeeva LE, Fetisov... https://www.ncbi.nlm.nih.gov |