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Influence of quinacrine and chloroquine on the in vitro 3'-azido-3'-deoxythymidine antiretroviral effect.

AIDS research and therapy

Torres KJ, Reyes-Terán G, Sotelo J, Jung-Cook H, Aguirre-Cruz L.
PMID: 25788967
AIDS Res Ther. 2015 Mar 19;12:7. doi: 10.1186/s12981-015-0048-9. eCollection 2015.

BACKGROUND: Antimalarials quinacrine (Qc) and chloroquine (Cq) intercalate DNA, potentiate the activity of other drugs and have lysosomotropic, anti-inflammatory and antiviral activities that could increase the effect of the 3'-azido-3'-deoxythymidine (AZT) antiretroviral agent. The aim of the current study...

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Torres KJ, Reyes-Terán G, Sotelo J, et al. Influence of quinacrine and chloroquine on the in vitro 3'-azido-3'-deoxythymidine antiretroviral effect. AIDS Res Ther. 2015;12:7doi: 10.1186/s12981-015-0048-9.
Torres, K. J., Reyes-Terán, G., Sotelo, J., Jung-Cook, H., & Aguirre-Cruz, L. (2015). Influence of quinacrine and chloroquine on the in vitro 3'-azido-3'-deoxythymidine antiretroviral effect. AIDS research and therapy, 127. https://doi.org/10.1186/s12981-015-0048-9
Torres, Klintsy J, et al. "Influence of quinacrine and chloroquine on the in vitro 3'-azido-3'-deoxythymidine antiretroviral effect." AIDS research and therapy vol. 12 (2015): 7. doi: https://doi.org/10.1186/s12981-015-0048-9
Torres KJ, Reyes-Terán G, Sotelo J, Jung-Cook H, Aguirre-Cruz L. Influence of quinacrine and chloroquine on the in vitro 3'-azido-3'-deoxythymidine antiretroviral effect. AIDS Res Ther. 2015 Mar 19;12:7. doi: 10.1186/s12981-015-0048-9. eCollection 2015. PMID: 25788967; PMCID: PMC4364635.
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Machine learning models identify molecules active against the Ebola virus in vitro.

F1000Research

Ekins S, Freundlich JS, Clark AM, Anantpadma M, Davey RA, Madrid P.
PMID: 26834994
F1000Res. 2015 Oct 20;4:1091. doi: 10.12688/f1000research.7217.2. eCollection 2015.

The search for small molecule inhibitors of Ebola virus (EBOV) has led to several high throughput screens over the past 3 years. These have identified a range of FDA-approved active pharmaceutical ingredients (APIs) with anti-EBOV activity in vitro and...

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Ekins S, Freundlich JS, Clark AM, et al. Machine learning models identify molecules active against the Ebola virus in vitro. F1000Res. 2015;4:1091doi: 10.12688/f1000research.7217.2.
Ekins, S., Freundlich, J. S., Clark, A. M., Anantpadma, M., Davey, R. A., & Madrid, P. (2015). Machine learning models identify molecules active against the Ebola virus in vitro. F1000Research, 41091. https://doi.org/10.12688/f1000research.7217.2
Ekins, Sean, et al. "Machine learning models identify molecules active against the Ebola virus in vitro." F1000Research vol. 4 (2015): 1091. doi: https://doi.org/10.12688/f1000research.7217.2
Ekins S, Freundlich JS, Clark AM, Anantpadma M, Davey RA, Madrid P. Machine learning models identify molecules active against the Ebola virus in vitro. F1000Res. 2015 Oct 20;4:1091. doi: 10.12688/f1000research.7217.2. eCollection 2015. PMID: 26834994; PMCID: PMC4706063.
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Toxic Symptoms Associated with Quinacrine Treatment.

The Indian medical gazette

Nandi DK.
PMID: 29015266
Ind Med Gaz. 1947 May;82(5):273.

No abstract available.

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Nandi DK. Toxic Symptoms Associated with Quinacrine Treatment. Ind Med Gaz. 1947;82(5):273
Nandi, D. K. (1947). Toxic Symptoms Associated with Quinacrine Treatment. The Indian medical gazette, 82(5), 273.
Nandi, D K. "Toxic Symptoms Associated with Quinacrine Treatment." The Indian medical gazette vol. 82,5 (1947): 273.
Nandi DK. Toxic Symptoms Associated with Quinacrine Treatment. Ind Med Gaz. 1947 May;82(5):273. PMID: 29015266; PMCID: PMC5196395.
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The Chlorophyll Biosynthetic Enzyme Mg-Protoporphyrin IX Monomethyl Ester (Oxidative) Cyclase (Characterization and Partial Purification from Chlamydomonas reinhardtii and Synechocystis sp. PCC 6803).

Plant physiology

Bollivar DW, Beale SI.
PMID: 12226378
Plant Physiol. 1996 Sep;112(1):105-114. doi: 10.1104/pp.112.1.105.

A universal structural feature of chlorophyll molecules is the isocyclic ring. This ring is formed by the action of the enzyme Mg-protoporphyrin IX monomethyl ester (oxidative) cyclase, which catalyzes a complex reaction in which Mg-protoporphyrin IX monomethyl ester is...

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Bollivar DW, Beale SI. The Chlorophyll Biosynthetic Enzyme Mg-Protoporphyrin IX Monomethyl Ester (Oxidative) Cyclase (Characterization and Partial Purification from Chlamydomonas reinhardtii and Synechocystis sp. PCC 6803). Plant Physiol. 1996;112(1):105-114doi: 10.1104/pp.112.1.105.
Bollivar, D. W., & Beale, S. I. (1996). The Chlorophyll Biosynthetic Enzyme Mg-Protoporphyrin IX Monomethyl Ester (Oxidative) Cyclase (Characterization and Partial Purification from Chlamydomonas reinhardtii and Synechocystis sp. PCC 6803). Plant physiology, 112(1), 105-114. https://doi.org/10.1104/pp.112.1.105
Bollivar, D. W., and Beale, S. I.. "The Chlorophyll Biosynthetic Enzyme Mg-Protoporphyrin IX Monomethyl Ester (Oxidative) Cyclase (Characterization and Partial Purification from Chlamydomonas reinhardtii and Synechocystis sp. PCC 6803)." Plant physiology vol. 112,1 (1996): 105-114. doi: https://doi.org/10.1104/pp.112.1.105
Bollivar DW, Beale SI. The Chlorophyll Biosynthetic Enzyme Mg-Protoporphyrin IX Monomethyl Ester (Oxidative) Cyclase (Characterization and Partial Purification from Chlamydomonas reinhardtii and Synechocystis sp. PCC 6803). Plant Physiol. 1996 Sep;112(1):105-114. doi: 10.1104/pp.112.1.105. PMID: 12226378; PMCID: PMC157929.
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Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases.

Plant physiology

Van Gestelen P, Asard H, Caubergs RJ.
PMID: 12223822
Plant Physiol. 1997 Oct;115(2):543-550. doi: 10.1104/pp.115.2.543.

Solubilization and ion-exchange chromatography of plasma membrane proteins obtained from bean (Phaseolus vulgaris L.) seedlings resulted in a single NAD(P)H-O2--synthase protein peak. This enzyme showed a high preference toward NADPH as a substrate (reaction rate, 27.4 nmol O2- produced...

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Van Gestelen P, Asard H, Caubergs RJ. Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases. Plant Physiol. 1997;115(2):543-550doi: 10.1104/pp.115.2.543.
Van Gestelen, P., Asard, H., & Caubergs, R. J. (1997). Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases. Plant physiology, 115(2), 543-550. https://doi.org/10.1104/pp.115.2.543
Van Gestelen, P., et al. "Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases." Plant physiology vol. 115,2 (1997): 543-550. doi: https://doi.org/10.1104/pp.115.2.543
Van Gestelen P, Asard H, Caubergs RJ. Solubilization and Separation of a Plant Plasma Membrane NADPH-O2- Synthase from Other NAD(P)H Oxidoreductases. Plant Physiol. 1997 Oct;115(2):543-550. doi: 10.1104/pp.115.2.543. PMID: 12223822; PMCID: PMC158513.
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Evidence for a highly specific k/h antiporter in membrane vesicles from oil-seed rape hypocotyls.

Plant physiology

Cooper S, Lerner HR, Reinhold L.
PMID: 16668511
Plant Physiol. 1991 Nov;97(3):1212-20. doi: 10.1104/pp.97.3.1212.

We present evidence strongly suggesting that a proton gradient (acid inside) is used to drive an electroneutral, substrate-specific, K(+)/H(+) antiport in both tonoplast and plasma membrane-enriched vesicles obtained from oilseed rape (Brassica napus) hypocotyls. Proton fluxes into and out...

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Cooper S, Lerner HR, Reinhold L. Evidence for a highly specific k/h antiporter in membrane vesicles from oil-seed rape hypocotyls. Plant Physiol. 1991;97(3):1212-20doi: 10.1104/pp.97.3.1212.
Cooper, S., Lerner, H. R., & Reinhold, L. (1991). Evidence for a highly specific k/h antiporter in membrane vesicles from oil-seed rape hypocotyls. Plant physiology, 97(3), 1212-20. https://doi.org/10.1104/pp.97.3.1212
Cooper, S, et al. "Evidence for a highly specific k/h antiporter in membrane vesicles from oil-seed rape hypocotyls." Plant physiology vol. 97,3 (1991): 1212-20. doi: https://doi.org/10.1104/pp.97.3.1212
Cooper S, Lerner HR, Reinhold L. Evidence for a highly specific k/h antiporter in membrane vesicles from oil-seed rape hypocotyls. Plant Physiol. 1991 Nov;97(3):1212-20. doi: 10.1104/pp.97.3.1212. PMID: 16668511; PMCID: PMC1081144.
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Effect of Ca and Calmodulin on DeltapH Formation in Tonoplast Vesicles from Corn Roots.

Plant physiology

Ladror US, Zielinski RE.
PMID: 16667359
Plant Physiol. 1990 Mar;92(3):850-4. doi: 10.1104/pp.92.3.850.

The effects of calmodulin (CaM) on ATPase activity and ATP-dependent formation of a proton gradient (DeltapH) were studied in tonoplast membrane vesicles from corn (Zea mays L.) roots. At 0.6 micromolar, CaM stimulated ATPase activity by about 20% in...

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Ladror US, Zielinski RE. Effect of Ca and Calmodulin on DeltapH Formation in Tonoplast Vesicles from Corn Roots. Plant Physiol. 1990;92(3):850-4doi: 10.1104/pp.92.3.850.
Ladror, U. S., & Zielinski, R. E. (1990). Effect of Ca and Calmodulin on DeltapH Formation in Tonoplast Vesicles from Corn Roots. Plant physiology, 92(3), 850-4. https://doi.org/10.1104/pp.92.3.850
Ladror, U S, and Zielinski, R E. "Effect of Ca and Calmodulin on DeltapH Formation in Tonoplast Vesicles from Corn Roots." Plant physiology vol. 92,3 (1990): 850-4. doi: https://doi.org/10.1104/pp.92.3.850
Ladror US, Zielinski RE. Effect of Ca and Calmodulin on DeltapH Formation in Tonoplast Vesicles from Corn Roots. Plant Physiol. 1990 Mar;92(3):850-4. doi: 10.1104/pp.92.3.850. PMID: 16667359; PMCID: PMC1062379.
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Localization of a proton-translocating ATPase on sucrose gradients.

Plant physiology

Dupont FM, Bennett AB, Spanswick RM.
PMID: 16662623
Plant Physiol. 1982 Oct;70(4):1115-9. doi: 10.1104/pp.70.4.1115.

Ionophore-stimulated ATPase activity and ATP-dependent quinacrine quench were enriched in parallel when microsomal vesicles were prepared from corn (Crow Single Cross Hybrid WF9-Mo17) roots and collected on a cushion of 10% dextran. Activities were highest in the apical 1.5...

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Dupont FM, Bennett AB, Spanswick RM. Localization of a proton-translocating ATPase on sucrose gradients. Plant Physiol. 1982;70(4):1115-9doi: 10.1104/pp.70.4.1115.
Dupont, F. M., Bennett, A. B., & Spanswick, R. M. (1982). Localization of a proton-translocating ATPase on sucrose gradients. Plant physiology, 70(4), 1115-9. https://doi.org/10.1104/pp.70.4.1115
Dupont, F M, et al. "Localization of a proton-translocating ATPase on sucrose gradients." Plant physiology vol. 70,4 (1982): 1115-9. doi: https://doi.org/10.1104/pp.70.4.1115
Dupont FM, Bennett AB, Spanswick RM. Localization of a proton-translocating ATPase on sucrose gradients. Plant Physiol. 1982 Oct;70(4):1115-9. doi: 10.1104/pp.70.4.1115. PMID: 16662623; PMCID: PMC1065835.
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Anion-sensitive, h-pumping ATPase in membrane vesicles from oat roots.

Plant physiology

Churchill KA, Sze H.
PMID: 16662875
Plant Physiol. 1983 Mar;71(3):610-7. doi: 10.1104/pp.71.3.610.

H(+)-pumping ATPases were detected in microsomal vesicles of oat (Avena sativa L. var Lang) roots using [(14)C]methylamine distribution or quinacrine fluorescent quenching. Methylamine (MeA) accumulation into vesicles and quinacrine quench were specifically dependent on Mg,ATP. Both activities reflected formation...

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Churchill KA, Sze H. Anion-sensitive, h-pumping ATPase in membrane vesicles from oat roots. Plant Physiol. 1983;71(3):610-7doi: 10.1104/pp.71.3.610.
Churchill, K. A., & Sze, H. (1983). Anion-sensitive, h-pumping ATPase in membrane vesicles from oat roots. Plant physiology, 71(3), 610-7. https://doi.org/10.1104/pp.71.3.610
Churchill, K A, and Sze, H. "Anion-sensitive, h-pumping ATPase in membrane vesicles from oat roots." Plant physiology vol. 71,3 (1983): 610-7. doi: https://doi.org/10.1104/pp.71.3.610
Churchill KA, Sze H. Anion-sensitive, h-pumping ATPase in membrane vesicles from oat roots. Plant Physiol. 1983 Mar;71(3):610-7. doi: 10.1104/pp.71.3.610. PMID: 16662875; PMCID: PMC1066086.
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Separation of two types of electrogenic h-pumping ATPases from oat roots.

Plant physiology

Churchill KA, Holaway B, Sze H.
PMID: 16663344
Plant Physiol. 1983 Dec;73(4):921-8. doi: 10.1104/pp.73.4.921.

Microsomal vesicles of oat roots (Avena sativa var Lang) were separated with a linear dextran (0.5-10%, w/w) or sucrose (25-45%, w/w) gradient to determine the types and membrane identity of proton-pumping ATPases associated with plant membranes. ATPase activity stimulated...

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Churchill KA, Holaway B, Sze H. Separation of two types of electrogenic h-pumping ATPases from oat roots. Plant Physiol. 1983;73(4):921-8doi: 10.1104/pp.73.4.921.
Churchill, K. A., Holaway, B., & Sze, H. (1983). Separation of two types of electrogenic h-pumping ATPases from oat roots. Plant physiology, 73(4), 921-8. https://doi.org/10.1104/pp.73.4.921
Churchill, K A, et al. "Separation of two types of electrogenic h-pumping ATPases from oat roots." Plant physiology vol. 73,4 (1983): 921-8. doi: https://doi.org/10.1104/pp.73.4.921
Churchill KA, Holaway B, Sze H. Separation of two types of electrogenic h-pumping ATPases from oat roots. Plant Physiol. 1983 Dec;73(4):921-8. doi: 10.1104/pp.73.4.921. PMID: 16663344; PMCID: PMC1066581.
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Characterization of in vitro proton pumping by microsomal vesicles isolated from corn coleoptiles.

Plant physiology

Mettler IJ, Mandala S, Taiz L.
PMID: 16662754
Plant Physiol. 1982 Dec;70(6):1738-42. doi: 10.1104/pp.70.6.1738.

Corn (Zea mays L. cv Golden Cross Bantam) coleoptile microsomal vesicles have been isolated which are capable of ATP-driven H(+)-transport as measured by [(14)C]methylamine accumulation and quinacrine fluorescence quenching. Formation of the pH gradient in vitro shows a high...

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Mettler IJ, Mandala S, Taiz L. Characterization of in vitro proton pumping by microsomal vesicles isolated from corn coleoptiles. Plant Physiol. 1982;70(6):1738-42doi: 10.1104/pp.70.6.1738.
Mettler, I. J., Mandala, S., & Taiz, L. (1982). Characterization of in vitro proton pumping by microsomal vesicles isolated from corn coleoptiles. Plant physiology, 70(6), 1738-42. https://doi.org/10.1104/pp.70.6.1738
Mettler, I J, et al. "Characterization of in vitro proton pumping by microsomal vesicles isolated from corn coleoptiles." Plant physiology vol. 70,6 (1982): 1738-42. doi: https://doi.org/10.1104/pp.70.6.1738
Mettler IJ, Mandala S, Taiz L. Characterization of in vitro proton pumping by microsomal vesicles isolated from corn coleoptiles. Plant Physiol. 1982 Dec;70(6):1738-42. doi: 10.1104/pp.70.6.1738. PMID: 16662754; PMCID: PMC1065965.
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Studies on H-Translocating ATPases in Plants of Varying Resistance to Salinity : I. Salinity during Growth Modulates the Proton Pump in the Halophyte Atriplex nummularia.

Plant physiology

Braun Y, Hassidim M, Lerner HR, Reinhold L.
PMID: 16664942
Plant Physiol. 1986 Aug;81(4):1050-6. doi: 10.1104/pp.81.4.1050.

Membrane vesicles were isolated from the roots of the halophyte Atriplex nummularia Lindl. H(+)-translocating Mg(2+)-ATPase activity was manifested by the establishment of a positive membrane potential (measured as SCN(-) accumulation); and also by the establishment of a transmembrane pH...

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Braun Y, Hassidim M, Lerner HR, et al. Studies on H-Translocating ATPases in Plants of Varying Resistance to Salinity : I. Salinity during Growth Modulates the Proton Pump in the Halophyte Atriplex nummularia. Plant Physiol. 1986;81(4):1050-6doi: 10.1104/pp.81.4.1050.
Braun, Y., Hassidim, M., Lerner, H. R., & Reinhold, L. (1986). Studies on H-Translocating ATPases in Plants of Varying Resistance to Salinity : I. Salinity during Growth Modulates the Proton Pump in the Halophyte Atriplex nummularia. Plant physiology, 81(4), 1050-6. https://doi.org/10.1104/pp.81.4.1050
Braun, Y, et al. "Studies on H-Translocating ATPases in Plants of Varying Resistance to Salinity : I. Salinity during Growth Modulates the Proton Pump in the Halophyte Atriplex nummularia." Plant physiology vol. 81,4 (1986): 1050-6. doi: https://doi.org/10.1104/pp.81.4.1050
Braun Y, Hassidim M, Lerner HR, Reinhold L. Studies on H-Translocating ATPases in Plants of Varying Resistance to Salinity : I. Salinity during Growth Modulates the Proton Pump in the Halophyte Atriplex nummularia. Plant Physiol. 1986 Aug;81(4):1050-6. doi: 10.1104/pp.81.4.1050. PMID: 16664942; PMCID: PMC1075484.
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