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Showing 13 to 24 of 117 entries
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Drug modification of protein thiophosphorylation in permeabilized chromaffin cells.

Neurochemistry international

Brooks JC, Brooks M.
PMID: 20501188
Neurochem Int. 1987;11(4):407-15. doi: 10.1016/0197-0186(87)90030-1.

Treatment of permeabilized chromaffin cells with low concentrations of the ATP analog adenosine-5?-O-(3-thiotriphosphate)[(35)S] results in (35)S incorporation into a small number of cellular proteins. Of these proteins, a 47 kilodalton protein is most heavily thiophosphorylated. Permeabilized cells were treated...

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Brooks JC, Brooks M. Drug modification of protein thiophosphorylation in permeabilized chromaffin cells. Neurochem Int. 1987;11(4):407-15doi: 10.1016/0197-0186(87)90030-1.
Brooks, J. C., & Brooks, M. (1987). Drug modification of protein thiophosphorylation in permeabilized chromaffin cells. Neurochemistry international, 11(4), 407-15. https://doi.org/10.1016/0197-0186(87)90030-1
Brooks, J C, and Brooks, M. "Drug modification of protein thiophosphorylation in permeabilized chromaffin cells." Neurochemistry international vol. 11,4 (1987): 407-15. doi: https://doi.org/10.1016/0197-0186(87)90030-1
Brooks JC, Brooks M. Drug modification of protein thiophosphorylation in permeabilized chromaffin cells. Neurochem Int. 1987;11(4):407-15. doi: 10.1016/0197-0186(87)90030-1. PMID: 20501188.
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A drug utilization study of psychotropic drugs prescribed in the psychiatry outpatient department of a tertiary care hospital.

Journal of clinical and diagnostic research : JCDR

Thakkar KB, Jain MM, Billa G, Joshi A, Khobragade AA.
PMID: 24551631
J Clin Diagn Res. 2013 Dec;7(12):2759-64. doi: 10.7860/JCDR/2013/6760.3885. Epub 2013 Dec 15.

BACKGROUND: Psychiatric disorders are one of the major causes of morbidity. Development of newer drugs like SSRIs and atypical antipsychotics has altered the treatment paradigms. Various factors like cost of drugs, local paradigms, etc. play a role in the...

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Thakkar KB, Jain MM, Billa G, et al. A drug utilization study of psychotropic drugs prescribed in the psychiatry outpatient department of a tertiary care hospital. J Clin Diagn Res. 2013;7(12):2759-64doi: 10.7860/JCDR/2013/6760.3885.
Thakkar, K. B., Jain, M. M., Billa, G., Joshi, A., & Khobragade, A. A. (2013). A drug utilization study of psychotropic drugs prescribed in the psychiatry outpatient department of a tertiary care hospital. Journal of clinical and diagnostic research : JCDR, 7(12), 2759-64. https://doi.org/10.7860/JCDR/2013/6760.3885
Thakkar, Karan B, et al. "A drug utilization study of psychotropic drugs prescribed in the psychiatry outpatient department of a tertiary care hospital." Journal of clinical and diagnostic research : JCDR vol. 7,12 (2013): 2759-64. doi: https://doi.org/10.7860/JCDR/2013/6760.3885
Thakkar KB, Jain MM, Billa G, Joshi A, Khobragade AA. A drug utilization study of psychotropic drugs prescribed in the psychiatry outpatient department of a tertiary care hospital. J Clin Diagn Res. 2013 Dec;7(12):2759-64. doi: 10.7860/JCDR/2013/6760.3885. Epub 2013 Dec 15. PMID: 24551631; PMCID: PMC3919294.
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Calcium-dependent protein kinase from apple fruit membranes is calmodulin-independent but has calmodulin-like properties.

Planta

Battey NH, Venis MA.
PMID: 24220739
Planta. 1988 Nov;176(1):91-7. doi: 10.1007/BF00392484.

Crude Ca(2+)-activated protein kinase from membranes of apple (Malus domestica L. Borkh., Cox's Orange Pippin) fruit can be partially purified to yield a Ca(2+)-dependent protein kinase whose activity is apparently not regulated by calmodulin. The autophosphorylating catalytic subunit of...

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Battey NH, Venis MA. Calcium-dependent protein kinase from apple fruit membranes is calmodulin-independent but has calmodulin-like properties. Planta. 1988;176(1):91-7doi: 10.1007/BF00392484.
Battey, N. H., & Venis, M. A. (1988). Calcium-dependent protein kinase from apple fruit membranes is calmodulin-independent but has calmodulin-like properties. Planta, 176(1), 91-7. https://doi.org/10.1007/BF00392484
Battey, N H, and Venis, M A. "Calcium-dependent protein kinase from apple fruit membranes is calmodulin-independent but has calmodulin-like properties." Planta vol. 176,1 (1988): 91-7. doi: https://doi.org/10.1007/BF00392484
Battey NH, Venis MA. Calcium-dependent protein kinase from apple fruit membranes is calmodulin-independent but has calmodulin-like properties. Planta. 1988 Nov;176(1):91-7. doi: 10.1007/BF00392484. PMID: 24220739.
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Identification of calmodulin in the green alga Mougeotia and its possible function in chloroplast reorientational movement.

Planta

Wagner G, Valentin P, Dieter P, Marmé D.
PMID: 24253948
Planta. 1984 Sep;162(1):62-7. doi: 10.1007/BF00397422.

A soluble protein was isolated from Mougeotia by chloropromazine-sepharose 4 B affinity chromatography. The protein matches the properties of calmodulin in terms of heat stability, Ca(2+)-dependent electrophoretic mobility in sodium-dodecyl-sulfate polyacrylamide gels, and its ability to activate cyclic nucleotide...

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Wagner G, Valentin P, Dieter P, et al. Identification of calmodulin in the green alga Mougeotia and its possible function in chloroplast reorientational movement. Planta. 1984;162(1):62-7doi: 10.1007/BF00397422.
Wagner, G., Valentin, P., Dieter, P., & Marmé, D. (1984). Identification of calmodulin in the green alga Mougeotia and its possible function in chloroplast reorientational movement. Planta, 162(1), 62-7. https://doi.org/10.1007/BF00397422
Wagner, G, et al. "Identification of calmodulin in the green alga Mougeotia and its possible function in chloroplast reorientational movement." Planta vol. 162,1 (1984): 62-7. doi: https://doi.org/10.1007/BF00397422
Wagner G, Valentin P, Dieter P, Marmé D. Identification of calmodulin in the green alga Mougeotia and its possible function in chloroplast reorientational movement. Planta. 1984 Sep;162(1):62-7. doi: 10.1007/BF00397422. PMID: 24253948.
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The effects of ruthenium red, lanthanum, fluorescein isothiocyanate and trifluoperazine on vesicle transport, vesicle fusion and tip extension in pollen tubes.

Planta

Picton JM, Steer MW.
PMID: 24249263
Planta. 1985 Jan;163(1):20-6. doi: 10.1007/BF00395892.

The effects of ruthenium red, lanthanum, fluorescein isothiocyanate and trifluoperazine, all antagonists of Ca(2+) function in cells, have been studied in growing pollen tubes of Tradescantia virginiana. All four drugs inhibit pollen-tube growth but bring about different ultrastructural changes...

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Picton JM, Steer MW. The effects of ruthenium red, lanthanum, fluorescein isothiocyanate and trifluoperazine on vesicle transport, vesicle fusion and tip extension in pollen tubes. Planta. 1985;163(1):20-6doi: 10.1007/BF00395892.
Picton, J. M., & Steer, M. W. (1985). The effects of ruthenium red, lanthanum, fluorescein isothiocyanate and trifluoperazine on vesicle transport, vesicle fusion and tip extension in pollen tubes. Planta, 163(1), 20-6. https://doi.org/10.1007/BF00395892
Picton, J M, and Steer, M W. "The effects of ruthenium red, lanthanum, fluorescein isothiocyanate and trifluoperazine on vesicle transport, vesicle fusion and tip extension in pollen tubes." Planta vol. 163,1 (1985): 20-6. doi: https://doi.org/10.1007/BF00395892
Picton JM, Steer MW. The effects of ruthenium red, lanthanum, fluorescein isothiocyanate and trifluoperazine on vesicle transport, vesicle fusion and tip extension in pollen tubes. Planta. 1985 Jan;163(1):20-6. doi: 10.1007/BF00395892. PMID: 24249263.
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Design of Inhibitors of the Intrinsically Disordered Protein NUPR1: Balance between Drug Affinity and Target Function.

Biomolecules

Rizzuti B, Lan W, Santofimia-Castaño P, Zhou Z, Velázquez-Campoy A, Abián O, Peng L, Neira JL, Xia Y, Iovanna JL.
PMID: 34680086
Biomolecules. 2021 Oct 03;11(10). doi: 10.3390/biom11101453.

Intrinsically disordered proteins (IDPs) are emerging as attractive drug targets by virtue of their physiological ubiquity and their prevalence in various diseases, including cancer. NUPR1 is an IDP that localizes throughout the whole cell, and is involved in the...

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Rizzuti B, Lan W, Santofimia-Castaño P, et al. Design of Inhibitors of the Intrinsically Disordered Protein NUPR1: Balance between Drug Affinity and Target Function. Biomolecules. 2021;11(10)doi: 10.3390/biom11101453.
Rizzuti, B., Lan, W., Santofimia-Castaño, P., Zhou, Z., Velázquez-Campoy, A., Abián, O., Peng, L., Neira, J. L., Xia, Y., & Iovanna, J. L. (2021). Design of Inhibitors of the Intrinsically Disordered Protein NUPR1: Balance between Drug Affinity and Target Function. Biomolecules, 11(10), . https://doi.org/10.3390/biom11101453
Rizzuti, Bruno, et al. "Design of Inhibitors of the Intrinsically Disordered Protein NUPR1: Balance between Drug Affinity and Target Function." Biomolecules vol. 11,10 (2021). doi: https://doi.org/10.3390/biom11101453
Rizzuti B, Lan W, Santofimia-Castaño P, Zhou Z, Velázquez-Campoy A, Abián O, Peng L, Neira JL, Xia Y, Iovanna JL. Design of Inhibitors of the Intrinsically Disordered Protein NUPR1: Balance between Drug Affinity and Target Function. Biomolecules. 2021 Oct 03;11(10). doi: 10.3390/biom11101453. PMID: 34680086; PMCID: PMC8533202.
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Antimicrobial Properties on Non-Antibiotic Drugs in the Era of Increased Bacterial Resistance.

Antibiotics (Basel, Switzerland)

Lagadinou M, Onisor MO, Rigas A, Musetescu DV, Gkentzi D, Assimakopoulos SF, Panos G, Marangos M.
PMID: 32131427
Antibiotics (Basel). 2020 Mar 02;9(3). doi: 10.3390/antibiotics9030107.

In recent years, due to the dramatic increase in and global spread of bacterial resistance to a number of commonly used antibacterial agents, many studies have been directed at investigating drugs whose primary therapeutic purpose is not antimicrobial action....

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Lagadinou M, Onisor MO, Rigas A, et al. Antimicrobial Properties on Non-Antibiotic Drugs in the Era of Increased Bacterial Resistance. Antibiotics (Basel). 2020;9(3)doi: 10.3390/antibiotics9030107.
Lagadinou, M., Onisor, M. O., Rigas, A., Musetescu, D. V., Gkentzi, D., Assimakopoulos, S. F., Panos, G., & Marangos, M. (2020). Antimicrobial Properties on Non-Antibiotic Drugs in the Era of Increased Bacterial Resistance. Antibiotics (Basel, Switzerland), 9(3), . https://doi.org/10.3390/antibiotics9030107
Lagadinou, Maria, et al. "Antimicrobial Properties on Non-Antibiotic Drugs in the Era of Increased Bacterial Resistance." Antibiotics (Basel, Switzerland) vol. 9,3 (2020). doi: https://doi.org/10.3390/antibiotics9030107
Lagadinou M, Onisor MO, Rigas A, Musetescu DV, Gkentzi D, Assimakopoulos SF, Panos G, Marangos M. Antimicrobial Properties on Non-Antibiotic Drugs in the Era of Increased Bacterial Resistance. Antibiotics (Basel). 2020 Mar 02;9(3). doi: 10.3390/antibiotics9030107. PMID: 32131427; PMCID: PMC7175110.
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CONJUGATION WITH SILVER NANOPARTICLES ENHANCES ANTI-ACANTHAMOEBIC ACTIVITY OF KAPPAPHYCUS ALVAREZII.

The Journal of parasitology

Walvekar S, Anwar A, Anwar A, Lai NJY, Yow YY, Khalid M, Siddiqui R, Khan NA.
PMID: 34265050
J Parasitol. 2021 Jul 01;107(4):537-546. doi: 10.1645/21-41.

Nanomedicine has the potential in enhancing the efficacy and bioavailability of anti-infective agents. Here we determined whether conjugation of the Malaysian cultivated seaweed Kappaphycus alvarezii with silver-conjugated nanoparticles enhanced anti-acanthamoebic properties. Silver-conjugated K. alvarezii were successfully synthesized, followed by...

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Walvekar S, Anwar A, Anwar A, et al. CONJUGATION WITH SILVER NANOPARTICLES ENHANCES ANTI-ACANTHAMOEBIC ACTIVITY OF KAPPAPHYCUS ALVAREZII. J Parasitol. 2021;107(4):537-546doi: 10.1645/21-41.
Walvekar, S., Anwar, A., Anwar, A., Lai, N. J. Y., Yow, Y. Y., Khalid, M., Siddiqui, R., & Khan, N. A. (2021). CONJUGATION WITH SILVER NANOPARTICLES ENHANCES ANTI-ACANTHAMOEBIC ACTIVITY OF KAPPAPHYCUS ALVAREZII. The Journal of parasitology, 107(4), 537-546. https://doi.org/10.1645/21-41
Walvekar, Shweta, et al. "CONJUGATION WITH SILVER NANOPARTICLES ENHANCES ANTI-ACANTHAMOEBIC ACTIVITY OF KAPPAPHYCUS ALVAREZII." The Journal of parasitology vol. 107,4 (2021): 537-546. doi: https://doi.org/10.1645/21-41
Walvekar S, Anwar A, Anwar A, Lai NJY, Yow YY, Khalid M, Siddiqui R, Khan NA. CONJUGATION WITH SILVER NANOPARTICLES ENHANCES ANTI-ACANTHAMOEBIC ACTIVITY OF KAPPAPHYCUS ALVAREZII. J Parasitol. 2021 Jul 01;107(4):537-546. doi: 10.1645/21-41. PMID: 34265050.
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Ca2+ and Calmodulin Dynamics during Photopolarization in Fucus serratus Zygotes.

Plant physiology

Love J, Brownlee C, Trewavas AJ.
PMID: 12223805
Plant Physiol. 1997 Sep;115(1):249-261. doi: 10.1104/pp.115.1.249.

The role of Ca2+ in zygote polarization in fucoid algae (Fucus, Ascophyllum, and Pelvetia species) zygote polarization is controversial. Using a local source of Fucus serratus, we established that zygotes form a polar axis relative to unilateral light (photopolarization)...

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Love J, Brownlee C, Trewavas AJ. Ca2+ and Calmodulin Dynamics during Photopolarization in Fucus serratus Zygotes. Plant Physiol. 1997;115(1):249-261doi: 10.1104/pp.115.1.249.
Love, J., Brownlee, C., & Trewavas, A. J. (1997). Ca2+ and Calmodulin Dynamics during Photopolarization in Fucus serratus Zygotes. Plant physiology, 115(1), 249-261. https://doi.org/10.1104/pp.115.1.249
Love, J., et al. "Ca2+ and Calmodulin Dynamics during Photopolarization in Fucus serratus Zygotes." Plant physiology vol. 115,1 (1997): 249-261. doi: https://doi.org/10.1104/pp.115.1.249
Love J, Brownlee C, Trewavas AJ. Ca2+ and Calmodulin Dynamics during Photopolarization in Fucus serratus Zygotes. Plant Physiol. 1997 Sep;115(1):249-261. doi: 10.1104/pp.115.1.249. PMID: 12223805; PMCID: PMC158481.
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The regulation of N-Acetylglucosaminyl Transferase III by Protein Kinase C.

Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica

Ju TZ, Gu JX, Chen HL.
PMID: 12237684
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 1996;28(3):286-292.

The activity of N-acetylglucosaminyl transferase III (GnT III) in 7721 human heptocarcinoma cell was inhibited by two non-specific Ser/Thr protein kinase inhibitors, quercetin and trifluoperazine, and two PKC specific inhibitors, D-sphingosine and staurosporine. The change of GnT III activity...

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Ju TZ, Gu JX, Chen HL. The regulation of N-Acetylglucosaminyl Transferase III by Protein Kinase C. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 1996;28(3):286-292
Ju, T. Z., Gu, J. X., & Chen, H. L. (1996). The regulation of N-Acetylglucosaminyl Transferase III by Protein Kinase C. Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica, 28(3), 286-292.
Ju, Tong-Zhong, et al. "The regulation of N-Acetylglucosaminyl Transferase III by Protein Kinase C." Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica vol. 28,3 (1996): 286-292.
Ju TZ, Gu JX, Chen HL. The regulation of N-Acetylglucosaminyl Transferase III by Protein Kinase C. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 1996;28(3):286-292. PMID: 12237684.
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Antipsychotic Drug Trifluoperazine Suppresses Colorectal Cancer by Inducing G0/G1 Arrest and Apoptosis.

Frontiers in pharmacology

Xia Y, Jia C, Xue Q, Jiang J, Xie Y, Wang R, Ran Z, Xu F, Zhang Y, Ye T.
PMID: 31572198
Front Pharmacol. 2019 Sep 13;10:1029. doi: 10.3389/fphar.2019.01029. eCollection 2019.

Repurposing existing drugs for cancer treatment is an effective strategy. An approved antipsychotic drug, trifluoperazine (TFP), has been reported to have potential anticancer effects against several cancer types. Here, we investigated the effect and molecular mechanism of TFP in...

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Xia Y, Jia C, Xue Q, et al. Antipsychotic Drug Trifluoperazine Suppresses Colorectal Cancer by Inducing G0/G1 Arrest and Apoptosis. Front Pharmacol. 2019;10:1029doi: 10.3389/fphar.2019.01029.
Xia, Y., Jia, C., Xue, Q., Jiang, J., Xie, Y., Wang, R., Ran, Z., Xu, F., Zhang, Y., & Ye, T. (2019). Antipsychotic Drug Trifluoperazine Suppresses Colorectal Cancer by Inducing G0/G1 Arrest and Apoptosis. Frontiers in pharmacology, 101029. https://doi.org/10.3389/fphar.2019.01029
Xia, Yong, et al. "Antipsychotic Drug Trifluoperazine Suppresses Colorectal Cancer by Inducing G0/G1 Arrest and Apoptosis." Frontiers in pharmacology vol. 10 (2019): 1029. doi: https://doi.org/10.3389/fphar.2019.01029
Xia Y, Jia C, Xue Q, Jiang J, Xie Y, Wang R, Ran Z, Xu F, Zhang Y, Ye T. Antipsychotic Drug Trifluoperazine Suppresses Colorectal Cancer by Inducing G0/G1 Arrest and Apoptosis. Front Pharmacol. 2019 Sep 13;10:1029. doi: 10.3389/fphar.2019.01029. eCollection 2019. PMID: 31572198; PMCID: PMC6753363.
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Trifluoperazine prolongs the survival of experimental brain metastases by STAT3-dependent lysosomal membrane permeabilization.

American journal of cancer research

Zhang X, Ding K, Ji J, Parajuli H, Aasen SN, Espedal H, Huang B, Chen A, Wang J, Li X, Thorsen F.
PMID: 32195026
Am J Cancer Res. 2020 Feb 01;10(2):545-563. eCollection 2020.

Brain metastasis is a major cause of mortality in melanoma patients. The blood-brain barrier (BBB) prevents most anti-tumor compounds from entering the brain, which significantly limits their use in the treatment of brain metastasis. One strategy in the development...

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Zhang X, Ding K, Ji J, et al. Trifluoperazine prolongs the survival of experimental brain metastases by STAT3-dependent lysosomal membrane permeabilization. Am J Cancer Res. 2020;10(2):545-563
Zhang, X., Ding, K., Ji, J., Parajuli, H., Aasen, S. N., Espedal, H., Huang, B., Chen, A., Wang, J., Li, X., & Thorsen, F. (2020). Trifluoperazine prolongs the survival of experimental brain metastases by STAT3-dependent lysosomal membrane permeabilization. American journal of cancer research, 10(2), 545-563.
Zhang, Xin, et al. "Trifluoperazine prolongs the survival of experimental brain metastases by STAT3-dependent lysosomal membrane permeabilization." American journal of cancer research vol. 10,2 (2020): 545-563.
Zhang X, Ding K, Ji J, Parajuli H, Aasen SN, Espedal H, Huang B, Chen A, Wang J, Li X, Thorsen F. Trifluoperazine prolongs the survival of experimental brain metastases by STAT3-dependent lysosomal membrane permeabilization. Am J Cancer Res. 2020 Feb 01;10(2):545-563. eCollection 2020. PMID: 32195026; PMCID: PMC7061752.
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Showing 13 to 24 of 117 entries