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Showing 1 to 12 of 139 entries
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Bacterial Carriers for Glioblastoma Therapy.

Molecular therapy oncolytics

Mehta N, Lyon JG, Patil K, Mokarram N, Kim C, Bellamkonda RV.
PMID: 28345020
Mol Ther Oncolytics. 2016 Dec 14;4:1-17. doi: 10.1016/j.omto.2016.12.003. eCollection 2017 Mar 17.

Treatment of aggressive glioblastoma brain tumors is challenging, largely due to diffusion barriers preventing efficient drug dosing to tumors. To overcome these barriers, bacterial carriers that are actively motile and programmed to migrate and localize to tumor zones were...

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Mehta N, Lyon JG, Patil K, et al. Bacterial Carriers for Glioblastoma Therapy. Mol Ther Oncolytics. 2016;4:1-17doi: 10.1016/j.omto.2016.12.003.
Mehta, N., Lyon, J. G., Patil, K., Mokarram, N., Kim, C., & Bellamkonda, R. V. (2017). Bacterial Carriers for Glioblastoma Therapy. Molecular therapy oncolytics, 41-17. https://doi.org/10.1016/j.omto.2016.12.003
Mehta, Nalini, et al. "Bacterial Carriers for Glioblastoma Therapy." Molecular therapy oncolytics vol. 4 (2017): 1-17. doi: https://doi.org/10.1016/j.omto.2016.12.003
Mehta N, Lyon JG, Patil K, Mokarram N, Kim C, Bellamkonda RV. Bacterial Carriers for Glioblastoma Therapy. Mol Ther Oncolytics. 2016 Dec 14;4:1-17. doi: 10.1016/j.omto.2016.12.003. eCollection 2017 Mar 17. PMID: 28345020; PMCID: PMC5363759.
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Disruption of human papillomavirus 16 E6 gene by clustered regularly interspaced short palindromic repeat/Cas system in human cervical cancer cells.

OncoTargets and therapy

Yu L, Wang X, Zhu D, Ding W, Wang L, Zhang C, Jiang X, Shen H, Liao S, Ma D, Hu Z, Wang H.
PMID: 25565864
Onco Targets Ther. 2014 Dec 22;8:37-44. doi: 10.2147/OTT.S64092. eCollection 2015.

High-risk human papillomavirus (HPV), especially HPV16, is considered a main causative agent of cervical cancer. Upon HPV infection, the viral oncoprotein E6 disrupts the host tumor-suppressor protein p53, thus promoting malignant transformation of normal cervical cells. Here, we used...

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Yu L, Wang X, Zhu D, et al. Disruption of human papillomavirus 16 E6 gene by clustered regularly interspaced short palindromic repeat/Cas system in human cervical cancer cells. Onco Targets Ther. 2014;8:37-44doi: 10.2147/OTT.S64092.
Yu, L., Wang, X., Zhu, D., Ding, W., Wang, L., Zhang, C., Jiang, X., Shen, H., Liao, S., Ma, D., Hu, Z., & Wang, H. (2015). Disruption of human papillomavirus 16 E6 gene by clustered regularly interspaced short palindromic repeat/Cas system in human cervical cancer cells. OncoTargets and therapy, 837-44. https://doi.org/10.2147/OTT.S64092
Yu, Lan, et al. "Disruption of human papillomavirus 16 E6 gene by clustered regularly interspaced short palindromic repeat/Cas system in human cervical cancer cells." OncoTargets and therapy vol. 8 (2015): 37-44. doi: https://doi.org/10.2147/OTT.S64092
Yu L, Wang X, Zhu D, Ding W, Wang L, Zhang C, Jiang X, Shen H, Liao S, Ma D, Hu Z, Wang H. Disruption of human papillomavirus 16 E6 gene by clustered regularly interspaced short palindromic repeat/Cas system in human cervical cancer cells. Onco Targets Ther. 2014 Dec 22;8:37-44. doi: 10.2147/OTT.S64092. eCollection 2015. PMID: 25565864; PMCID: PMC4278796.
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Acute Endurance Exercise Induces Nuclear p53 Abundance in Human Skeletal Muscle.

Frontiers in physiology

Tachtsis B, Smiles WJ, Lane SC, Hawley JA, Camera DM.
PMID: 27199762
Front Physiol. 2016 Apr 26;7:144. doi: 10.3389/fphys.2016.00144. eCollection 2016.

PURPOSE: The tumor suppressor protein p53 may have regulatory roles in exercise response-adaptation processes such as mitochondrial biogenesis and autophagy, although its cellular location largely governs its biological role. We investigated the subcellular localization of p53 and selected signaling...

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Tachtsis B, Smiles WJ, Lane SC, et al. Acute Endurance Exercise Induces Nuclear p53 Abundance in Human Skeletal Muscle. Front Physiol. 2016;7:144doi: 10.3389/fphys.2016.00144.
Tachtsis, B., Smiles, W. J., Lane, S. C., Hawley, J. A., & Camera, D. M. (2016). Acute Endurance Exercise Induces Nuclear p53 Abundance in Human Skeletal Muscle. Frontiers in physiology, 7144. https://doi.org/10.3389/fphys.2016.00144
Tachtsis, Bill, et al. "Acute Endurance Exercise Induces Nuclear p53 Abundance in Human Skeletal Muscle." Frontiers in physiology vol. 7 (2016): 144. doi: https://doi.org/10.3389/fphys.2016.00144
Tachtsis B, Smiles WJ, Lane SC, Hawley JA, Camera DM. Acute Endurance Exercise Induces Nuclear p53 Abundance in Human Skeletal Muscle. Front Physiol. 2016 Apr 26;7:144. doi: 10.3389/fphys.2016.00144. eCollection 2016. PMID: 27199762; PMCID: PMC4845512.
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Antitumor cytotoxicity induced by bone-marrow-derived antigen-presenting cells is facilitated by the tumor suppressor protein p53 via regulation of IL-12.

Oncoimmunology

Slatter TL, Wilson M, Tang C, Campbell HG, Ward VK, Young VL, Van Ly D, Fleming NI, Braithwaite AW, Baird MA.
PMID: 27141366
Oncoimmunology. 2015 Dec 17;5(3):e1112941. doi: 10.1080/2162402X.2015.1112941. eCollection 2016 Mar.

Activated antigen-presenting cells (APC) deliver the three signals cytotoxic T cells require to differentiate into effector cells that destroy the tumor. These comprise antigen, co-stimulatory signals and cytokines. Once these cells have carried out their function, they apoptose. We...

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Slatter TL, Wilson M, Tang C, et al. Antitumor cytotoxicity induced by bone-marrow-derived antigen-presenting cells is facilitated by the tumor suppressor protein p53 via regulation of IL-12. Oncoimmunology. 2015;5(3):e1112941doi: 10.1080/2162402X.2015.1112941.
Slatter, T. L., Wilson, M., Tang, C., Campbell, H. G., Ward, V. K., Young, V. L., Van Ly, D., Fleming, N. I., Braithwaite, A. W., & Baird, M. A. (2016). Antitumor cytotoxicity induced by bone-marrow-derived antigen-presenting cells is facilitated by the tumor suppressor protein p53 via regulation of IL-12. Oncoimmunology, 5(3), e1112941. https://doi.org/10.1080/2162402X.2015.1112941
Slatter, Tania L, et al. "Antitumor cytotoxicity induced by bone-marrow-derived antigen-presenting cells is facilitated by the tumor suppressor protein p53 via regulation of IL-12." Oncoimmunology vol. 5,3 (2016): e1112941. doi: https://doi.org/10.1080/2162402X.2015.1112941
Slatter TL, Wilson M, Tang C, Campbell HG, Ward VK, Young VL, Van Ly D, Fleming NI, Braithwaite AW, Baird MA. Antitumor cytotoxicity induced by bone-marrow-derived antigen-presenting cells is facilitated by the tumor suppressor protein p53 via regulation of IL-12. Oncoimmunology. 2015 Dec 17;5(3):e1112941. doi: 10.1080/2162402X.2015.1112941. eCollection 2016 Mar. PMID: 27141366; PMCID: PMC4839352.
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p53 prevents immature escaping from cell cycle G2 checkpoint arrest through inhibiting cdk2-dependent NF-Y phosphorylation.

Cancer research and treatment

Yun UJ, Park HD, Shin DY.
PMID: 19771247
Cancer Res Treat. 2006 Dec;38(4):224-8. doi: 10.4143/crt.2006.38.4.224. Epub 2006 Dec 31.

PURPOSE: Recent studies have suggested that p53 regulates the G2 checkpoint in the cell cycle and this function is required for the maintenance of genomic integrity. In this study, we addressed a role of p53 in escaping from cell...

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Yun UJ, Park HD, Shin DY. p53 prevents immature escaping from cell cycle G2 checkpoint arrest through inhibiting cdk2-dependent NF-Y phosphorylation. Cancer Res Treat. 2006;38(4):224-8doi: 10.4143/crt.2006.38.4.224.
Yun, U. J., Park, H. D., & Shin, D. Y. (2006). p53 prevents immature escaping from cell cycle G2 checkpoint arrest through inhibiting cdk2-dependent NF-Y phosphorylation. Cancer research and treatment, 38(4), 224-8. https://doi.org/10.4143/crt.2006.38.4.224
Yun, Un-Jung, et al. "p53 prevents immature escaping from cell cycle G2 checkpoint arrest through inhibiting cdk2-dependent NF-Y phosphorylation." Cancer research and treatment vol. 38,4 (2006): 224-8. doi: https://doi.org/10.4143/crt.2006.38.4.224
Yun UJ, Park HD, Shin DY. p53 prevents immature escaping from cell cycle G2 checkpoint arrest through inhibiting cdk2-dependent NF-Y phosphorylation. Cancer Res Treat. 2006 Dec;38(4):224-8. doi: 10.4143/crt.2006.38.4.224. Epub 2006 Dec 31. PMID: 19771247; PMCID: PMC2741649.
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The tumor-suppressor protein p53 - relationship of structure to function (review).

Oncology reports

Sturzbecher H, Deppert W.
PMID: 21607355
Oncol Rep. 1994 Mar;1(2):301-7. doi: 10.3892/or.1.2.301.

Point mutations and/or rearrangements in the tumor suppressor gene p53 are the most common genetic alterations in human cancers. Recent observations indicate that the sum and substance of p53 protein function is the prevention of tumor formation by preservation...

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Sturzbecher H, Deppert W. The tumor-suppressor protein p53 - relationship of structure to function (review). Oncol Rep. 1994;1(2):301-7doi: 10.3892/or.1.2.301.
Sturzbecher, H., & Deppert, W. (1994). The tumor-suppressor protein p53 - relationship of structure to function (review). Oncology reports, 1(2), 301-7. https://doi.org/10.3892/or.1.2.301
Sturzbecher, H, and Deppert, W. "The tumor-suppressor protein p53 - relationship of structure to function (review)." Oncology reports vol. 1,2 (1994): 301-7. doi: https://doi.org/10.3892/or.1.2.301
Sturzbecher H, Deppert W. The tumor-suppressor protein p53 - relationship of structure to function (review). Oncol Rep. 1994 Mar;1(2):301-7. doi: 10.3892/or.1.2.301. PMID: 21607355.
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p53 and Cell Cycle Proteins Participate in Spinal Motor Neuron Cell Death in ALS.

The open pathology journal

Ranganathan S, Bowser R.
PMID: 21572928
Open Pathol J. 2010 Jan 01;4:11-22. doi: 10.2174/1874375701004010011.

Apoptosis has been implicated in many neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS). We previously demonstrated a role for G1 to S phase cell cycle regulators in ALS with increased levels of hyperphosphorylated retinoblastoma (ppRb) and E2F-1 in ALS...

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Ranganathan S, Bowser R. p53 and Cell Cycle Proteins Participate in Spinal Motor Neuron Cell Death in ALS. Open Pathol J. 2010;4:11-22doi: 10.2174/1874375701004010011.
Ranganathan, S., & Bowser, R. (2010). p53 and Cell Cycle Proteins Participate in Spinal Motor Neuron Cell Death in ALS. The open pathology journal, 411-22. https://doi.org/10.2174/1874375701004010011
Ranganathan, Srikanth, and Bowser, Robert. "p53 and Cell Cycle Proteins Participate in Spinal Motor Neuron Cell Death in ALS." The open pathology journal vol. 4 (2010): 11-22. doi: https://doi.org/10.2174/1874375701004010011
Ranganathan S, Bowser R. p53 and Cell Cycle Proteins Participate in Spinal Motor Neuron Cell Death in ALS. Open Pathol J. 2010 Jan 01;4:11-22. doi: 10.2174/1874375701004010011. PMID: 21572928; PMCID: PMC3092395.
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The Role of p53 in Marijuana Smoke Condensates-induced Genotoxicity and Apoptosis.

Environmental health and toxicology

Kim HR, Son BH, Lee SY, Chung KH, Oh SM.
PMID: 23106039
Environ Health Toxicol. 2012;27:e2012017. doi: 10.5620/eht.2012.27.e2012017. Epub 2012 Sep 30.

OBJECTIVES: Marijuana is one of the most frequently abused drug in Korea and its adverse health effects are controversial. p53 is known to be crucial in regulating the DNA damage responses, and adverse effects can occur when it is...

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Kim HR, Son BH, Lee SY, et al. The Role of p53 in Marijuana Smoke Condensates-induced Genotoxicity and Apoptosis. Environ Health Toxicol. 2012;27:e2012017doi: 10.5620/eht.2012.27.e2012017.
Kim, H. R., Son, B. H., Lee, S. Y., Chung, K. H., & Oh, S. M. (2012). The Role of p53 in Marijuana Smoke Condensates-induced Genotoxicity and Apoptosis. Environmental health and toxicology, 27e2012017. https://doi.org/10.5620/eht.2012.27.e2012017
Kim, Ha Ryong, et al. "The Role of p53 in Marijuana Smoke Condensates-induced Genotoxicity and Apoptosis." Environmental health and toxicology vol. 27 (2012): e2012017. doi: https://doi.org/10.5620/eht.2012.27.e2012017
Kim HR, Son BH, Lee SY, Chung KH, Oh SM. The Role of p53 in Marijuana Smoke Condensates-induced Genotoxicity and Apoptosis. Environ Health Toxicol. 2012;27:e2012017. doi: 10.5620/eht.2012.27.e2012017. Epub 2012 Sep 30. PMID: 23106039; PMCID: PMC3479268.
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Role of the N-terminal lid in regulating the interaction of phosphorylated MDMX with p53.

Oncotarget

Chan JV, Ping Koh DX, Liu Y, Joseph TL, Lane DP, Verma CS, Tan YS.
PMID: 29348869
Oncotarget. 2017 Dec 01;8(68):112825-112840. doi: 10.18632/oncotarget.22829. eCollection 2017 Dec 22.

Murine double minute 4 protein (MDMX) is crucial for the regulation of the tumor suppressor protein p53. Phosphorylation of the N-terminal domain of MDMX is thought to affect its binding with the transactivation domain of p53, thus playing a...

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Chan JV, Ping Koh DX, Liu Y, et al. Role of the N-terminal lid in regulating the interaction of phosphorylated MDMX with p53. Oncotarget. 2017;8(68):112825-112840doi: 10.18632/oncotarget.22829.
Chan, J. V., Ping Koh, D. X., Liu, Y., Joseph, T. L., Lane, D. P., Verma, C. S., & Tan, Y. S. (2017). Role of the N-terminal lid in regulating the interaction of phosphorylated MDMX with p53. Oncotarget, 8(68), 112825-112840. https://doi.org/10.18632/oncotarget.22829
Chan, Jane Vin, et al. "Role of the N-terminal lid in regulating the interaction of phosphorylated MDMX with p53." Oncotarget vol. 8,68 (2017): 112825-112840. doi: https://doi.org/10.18632/oncotarget.22829
Chan JV, Ping Koh DX, Liu Y, Joseph TL, Lane DP, Verma CS, Tan YS. Role of the N-terminal lid in regulating the interaction of phosphorylated MDMX with p53. Oncotarget. 2017 Dec 01;8(68):112825-112840. doi: 10.18632/oncotarget.22829. eCollection 2017 Dec 22. PMID: 29348869; PMCID: PMC5762554.
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Inhibitor of growth protein 4 interacts with Beclin 1 and represses autophagy.

Oncotarget

Sica V, Bravo-San Pedro JM, Chen G, Mariño G, Lachkar S, Izzo V, Maiuri MC, Niso-Santano M, Kroemer G.
PMID: 29163768
Oncotarget. 2017 Jul 06;8(52):89527-89538. doi: 10.18632/oncotarget.19033. eCollection 2017 Oct 27.

Beclin 1 (BECN1) is a multifunctional protein that activates the pro-autophagic class III phosphatidylinositol 3-kinase (PIK3C3, best known as VPS34), yet also interacts with multiple negative regulators. Here we report that BECN1 interacts with inhibitor of growth family member...

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Sica V, Bravo-San Pedro JM, Chen G, et al. Inhibitor of growth protein 4 interacts with Beclin 1 and represses autophagy. Oncotarget. 2017;8(52):89527-89538doi: 10.18632/oncotarget.19033.
Sica, V., Bravo-San Pedro, J. M., Chen, G., Mariño, G., Lachkar, S., Izzo, V., Maiuri, M. C., Niso-Santano, M., & Kroemer, G. (2017). Inhibitor of growth protein 4 interacts with Beclin 1 and represses autophagy. Oncotarget, 8(52), 89527-89538. https://doi.org/10.18632/oncotarget.19033
Sica, Valentina, et al. "Inhibitor of growth protein 4 interacts with Beclin 1 and represses autophagy." Oncotarget vol. 8,52 (2017): 89527-89538. doi: https://doi.org/10.18632/oncotarget.19033
Sica V, Bravo-San Pedro JM, Chen G, Mariño G, Lachkar S, Izzo V, Maiuri MC, Niso-Santano M, Kroemer G. Inhibitor of growth protein 4 interacts with Beclin 1 and represses autophagy. Oncotarget. 2017 Jul 06;8(52):89527-89538. doi: 10.18632/oncotarget.19033. eCollection 2017 Oct 27. PMID: 29163768; PMCID: PMC5685689.
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p53 Isoforms and Their Implications in Cancer.

Cancers

Vieler M, Sanyal S.
PMID: 30149602
Cancers (Basel). 2018 Aug 25;10(9). doi: 10.3390/cancers10090288.

In this review we focus on the major isoforms of the tumor-suppressor protein p53, dysfunction of which often leads to cancer. Mutations of the

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Vieler M, Sanyal S. p53 Isoforms and Their Implications in Cancer. Cancers (Basel). 2018;10(9)doi: 10.3390/cancers10090288.
Vieler, M., & Sanyal, S. (2018). p53 Isoforms and Their Implications in Cancer. Cancers, 10(9), . https://doi.org/10.3390/cancers10090288
Vieler, Maximilian, and Sanyal, Suparna. "p53 Isoforms and Their Implications in Cancer." Cancers vol. 10,9 (2018). doi: https://doi.org/10.3390/cancers10090288
Vieler M, Sanyal S. p53 Isoforms and Their Implications in Cancer. Cancers (Basel). 2018 Aug 25;10(9). doi: 10.3390/cancers10090288. PMID: 30149602; PMCID: PMC6162399.
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The regulation of tumor suppressor protein, p53, and estrogen receptor (ERα) by resveratrol in breast cancer cells.

Genes & cancer

Saluzzo J, Hallman KM, Aleck K, Dwyer B, Quigley M, Mladenovik V, Siebert AE, Dinda S.
PMID: 28191286
Genes Cancer. 2016 Nov;7(11):414-425. doi: 10.18632/genesandcancer.125.

Resveratrol (RES) is a natural antioxidant found abundantly in grapes, peanuts, and berries, and is known to possess anti-tumorigenic properties. However, there is a noticeable lack of studies on the mechanistic effects of Resveratrol on tumor suppressors. Previous studies...

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Saluzzo J, Hallman KM, Aleck K, et al. The regulation of tumor suppressor protein, p53, and estrogen receptor (ERα) by resveratrol in breast cancer cells. Genes Cancer. 2016;7(11):414-425doi: 10.18632/genesandcancer.125.
Saluzzo, J., Hallman, K. M., Aleck, K., Dwyer, B., Quigley, M., Mladenovik, V., Siebert, A. E., & Dinda, S. (2016). The regulation of tumor suppressor protein, p53, and estrogen receptor (ERα) by resveratrol in breast cancer cells. Genes & cancer, 7(11), 414-425. https://doi.org/10.18632/genesandcancer.125
Saluzzo, Julieta, et al. "The regulation of tumor suppressor protein, p53, and estrogen receptor (ERα) by resveratrol in breast cancer cells." Genes & cancer vol. 7,11 (2016): 414-425. doi: https://doi.org/10.18632/genesandcancer.125
Saluzzo J, Hallman KM, Aleck K, Dwyer B, Quigley M, Mladenovik V, Siebert AE, Dinda S. The regulation of tumor suppressor protein, p53, and estrogen receptor (ERα) by resveratrol in breast cancer cells. Genes Cancer. 2016 Nov;7(11):414-425. doi: 10.18632/genesandcancer.125. PMID: 28191286; PMCID: PMC5302041.
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Showing 1 to 12 of 139 entries