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Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets.

iScience

Park SK, Park S, Pentek C, Liebman SW.
PMID: 33490908
iScience. 2020 Dec 29;24(1):102000. doi: 10.1016/j.isci.2020.102000. eCollection 2021 Jan 22.

Mutations in the p53 tumor suppressor are frequent causes of cancer. Because p53 aggregates appear in some tumor cells, it has been suggested that p53 could also cause cancer by forming self-replicating protein aggregates (prions). Here, using yeast, we...

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Park SK, Park S, Pentek C, et al. Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets. iScience. 2020;24(1):102000doi: 10.1016/j.isci.2020.102000.
Park, S. K., Park, S., Pentek, C., & Liebman, S. W. (2021). Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets. iScience, 24(1), 102000. https://doi.org/10.1016/j.isci.2020.102000
Park, Sei-Kyoung, et al. "Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets." iScience vol. 24,1 (2021): 102000. doi: https://doi.org/10.1016/j.isci.2020.102000
Park SK, Park S, Pentek C, Liebman SW. Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets. iScience. 2020 Dec 29;24(1):102000. doi: 10.1016/j.isci.2020.102000. eCollection 2021 Jan 22. PMID: 33490908; PMCID: PMC7811139.
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P53 induces senescence in the unstable progeny of aneuploid cells.

Cell cycle (Georgetown, Tex.)

Giam M, Wong CK, Low JS, Sinelli M, Dreesen O, Rancati G.
PMID: 33305692
Cell Cycle. 2020 Dec;19(24):3508-3520. doi: 10.1080/15384101.2020.1850968. Epub 2020 Dec 11.

Aneuploidy is the condition of having an imbalanced karyotype, which is associated with tumor initiation, evolution, and acquisition of drug-resistant features, possibly by generating heterogeneous populations of cells with distinct genotypes and phenotypes. Multicellular eukaryotes have therefore evolved a...

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Giam M, Wong CK, Low JS, et al. P53 induces senescence in the unstable progeny of aneuploid cells. Cell Cycle. 2020;19(24):3508-3520doi: 10.1080/15384101.2020.1850968.
Giam, M., Wong, C. K., Low, J. S., Sinelli, M., Dreesen, O., & Rancati, G. (2020). P53 induces senescence in the unstable progeny of aneuploid cells. Cell cycle (Georgetown, Tex.), 19(24), 3508-3520. https://doi.org/10.1080/15384101.2020.1850968
Giam, Maybelline, et al. "P53 induces senescence in the unstable progeny of aneuploid cells." Cell cycle (Georgetown, Tex.) vol. 19,24 (2020): 3508-3520. doi: https://doi.org/10.1080/15384101.2020.1850968
Giam M, Wong CK, Low JS, Sinelli M, Dreesen O, Rancati G. P53 induces senescence in the unstable progeny of aneuploid cells. Cell Cycle. 2020 Dec;19(24):3508-3520. doi: 10.1080/15384101.2020.1850968. Epub 2020 Dec 11. PMID: 33305692; PMCID: PMC7781663.
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Low Dose Astaxanthin Treatments Trigger the Hormesis of Human Astroglioma Cells by Up-Regulating the Cyclin-Dependent Kinase and Down-Regulated the Tumor Suppressor Protein P53.

Biomedicines

Shin J, Saini RK, Oh JW.
PMID: 33086722
Biomedicines. 2020 Oct 19;8(10). doi: 10.3390/biomedicines8100434.

Astaxanthin (AXT) is a xanthophyll carotenoid known to have potent anti-cancer effects via upregulation of the intracellular reactive oxygen species (ROS) levels, which triggers apoptosis of cancer cells. While several studies have shown that AXT has potential as an...

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Shin J, Saini RK, Oh JW. Low Dose Astaxanthin Treatments Trigger the Hormesis of Human Astroglioma Cells by Up-Regulating the Cyclin-Dependent Kinase and Down-Regulated the Tumor Suppressor Protein P53. Biomedicines. 2020;8(10)doi: 10.3390/biomedicines8100434.
Shin, J., Saini, R. K., & Oh, J. W. (2020). Low Dose Astaxanthin Treatments Trigger the Hormesis of Human Astroglioma Cells by Up-Regulating the Cyclin-Dependent Kinase and Down-Regulated the Tumor Suppressor Protein P53. Biomedicines, 8(10), . https://doi.org/10.3390/biomedicines8100434
Shin, Juhyun, et al. "Low Dose Astaxanthin Treatments Trigger the Hormesis of Human Astroglioma Cells by Up-Regulating the Cyclin-Dependent Kinase and Down-Regulated the Tumor Suppressor Protein P53." Biomedicines vol. 8,10 (2020). doi: https://doi.org/10.3390/biomedicines8100434
Shin J, Saini RK, Oh JW. Low Dose Astaxanthin Treatments Trigger the Hormesis of Human Astroglioma Cells by Up-Regulating the Cyclin-Dependent Kinase and Down-Regulated the Tumor Suppressor Protein P53. Biomedicines. 2020 Oct 19;8(10). doi: 10.3390/biomedicines8100434. PMID: 33086722; PMCID: PMC7590133.
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Clinical Significance of p53 Protein Expression, Beta-catenin Expression and HER2 Expression for Epstein-Barr Virus-associated Gastric Cancer.

Chonnam medical journal

Baek DW, Kang BW, Hwang S, Kim JG, Seo AN, Bae HI, Kwon OK, Lee SS, Chung HY, Yu W.
PMID: 28584793
Chonnam Med J. 2017 May;53(2):140-146. doi: 10.4068/cmj.2017.53.2.140. Epub 2017 May 25.

This study assessed the expression of the p53 protein, beta-catenin, and HER2 and their prognostic implications in patients with EBV-associated gastric cancer (EBVaGC). After reviewing 1318 consecutive cases of surgically resected or endoscopic submucosal dissected gastric cancers, 117 patients...

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Baek DW, Kang BW, Hwang S, et al. Clinical Significance of p53 Protein Expression, Beta-catenin Expression and HER2 Expression for Epstein-Barr Virus-associated Gastric Cancer. Chonnam Med J. 2017;53(2):140-146doi: 10.4068/cmj.2017.53.2.140.
Baek, D. W., Kang, B. W., Hwang, S., Kim, J. G., Seo, A. N., Bae, H. I., Kwon, O. K., Lee, S. S., Chung, H. Y., & Yu, W. (2017). Clinical Significance of p53 Protein Expression, Beta-catenin Expression and HER2 Expression for Epstein-Barr Virus-associated Gastric Cancer. Chonnam medical journal, 53(2), 140-146. https://doi.org/10.4068/cmj.2017.53.2.140
Baek, Dong Won, et al. "Clinical Significance of p53 Protein Expression, Beta-catenin Expression and HER2 Expression for Epstein-Barr Virus-associated Gastric Cancer." Chonnam medical journal vol. 53,2 (2017): 140-146. doi: https://doi.org/10.4068/cmj.2017.53.2.140
Baek DW, Kang BW, Hwang S, Kim JG, Seo AN, Bae HI, Kwon OK, Lee SS, Chung HY, Yu W. Clinical Significance of p53 Protein Expression, Beta-catenin Expression and HER2 Expression for Epstein-Barr Virus-associated Gastric Cancer. Chonnam Med J. 2017 May;53(2):140-146. doi: 10.4068/cmj.2017.53.2.140. Epub 2017 May 25. PMID: 28584793; PMCID: PMC5457949.
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Characterization of brain tumor initiating cells isolated from an animal model of CNS primitive neuroectodermal tumors.

Oncotarget

Malchenko S, Sredni ST, Boyineni J, Bi Y, Margaryan NV, Guda MR, Kostenko Y, Tomita T, Davuluri RV, Velpula K, Hendrix MJC, Soares MB.
PMID: 29568390
Oncotarget. 2018 Feb 09;9(17):13733-13747. doi: 10.18632/oncotarget.24460. eCollection 2018 Mar 02.

CNS Primitive Neuroectodermal tumors (CNS-PNETs) are members of the embryonal family of malignant childhood brain tumors, which remain refractory to current therapeutic treatments. Current paradigm of brain tumorigenesis implicates brain tumor-initiating cells (BTIC) in the onset of tumorigenesis and...

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Malchenko S, Sredni ST, Boyineni J, et al. Characterization of brain tumor initiating cells isolated from an animal model of CNS primitive neuroectodermal tumors. Oncotarget. 2018;9(17):13733-13747doi: 10.18632/oncotarget.24460.
Malchenko, S., Sredni, S. T., Boyineni, J., Bi, Y., Margaryan, N. V., Guda, M. R., Kostenko, Y., Tomita, T., Davuluri, R. V., Velpula, K., Hendrix, M. J. C., & Soares, M. B. (2018). Characterization of brain tumor initiating cells isolated from an animal model of CNS primitive neuroectodermal tumors. Oncotarget, 9(17), 13733-13747. https://doi.org/10.18632/oncotarget.24460
Malchenko, Sergey, et al. "Characterization of brain tumor initiating cells isolated from an animal model of CNS primitive neuroectodermal tumors." Oncotarget vol. 9,17 (2018): 13733-13747. doi: https://doi.org/10.18632/oncotarget.24460
Malchenko S, Sredni ST, Boyineni J, Bi Y, Margaryan NV, Guda MR, Kostenko Y, Tomita T, Davuluri RV, Velpula K, Hendrix MJC, Soares MB. Characterization of brain tumor initiating cells isolated from an animal model of CNS primitive neuroectodermal tumors. Oncotarget. 2018 Feb 09;9(17):13733-13747. doi: 10.18632/oncotarget.24460. eCollection 2018 Mar 02. PMID: 29568390; PMCID: PMC5862611.
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Structure-based analysis of curcumin and conventionaldrugs targeting tumor-inducing protein PHF20.

Bioinformation

Agrawal V, Mishra A, Tiwari S, Akhileshwar KS.
PMID: 31223206
Bioinformation. 2018 Nov 03;14(9):477-481. doi: 10.6026/97320630014477. eCollection 2018.

Recently, the PHF20 has been reported as tumor inducer protein by suppressing the activity of tumor suppressor protein p53. Conventional drugs (albendazole, doxazosin, and propranolol) are used for treatment of cancer causing side effect. The secondary metabolite curcumin is...

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Agrawal V, Mishra A, Tiwari S, et al. Structure-based analysis of curcumin and conventionaldrugs targeting tumor-inducing protein PHF20. Bioinformation. 2018;14(9):477-481doi: 10.6026/97320630014477.
Agrawal, V., Mishra, A., Tiwari, S., & Akhileshwar, K. S. (2018). Structure-based analysis of curcumin and conventionaldrugs targeting tumor-inducing protein PHF20. Bioinformation, 14(9), 477-481. https://doi.org/10.6026/97320630014477
Agrawal, Vibha, et al. "Structure-based analysis of curcumin and conventionaldrugs targeting tumor-inducing protein PHF20." Bioinformation vol. 14,9 (2018): 477-481. doi: https://doi.org/10.6026/97320630014477
Agrawal V, Mishra A, Tiwari S, Akhileshwar KS. Structure-based analysis of curcumin and conventionaldrugs targeting tumor-inducing protein PHF20. Bioinformation. 2018 Nov 03;14(9):477-481. doi: 10.6026/97320630014477. eCollection 2018. PMID: 31223206; PMCID: PMC6563658.
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Regulation of Skeletal Muscle Plasticity by Protein Arginine Methyltransferases and Their Potential Roles in Neuromuscular Disorders.

Frontiers in physiology

Stouth DW, vanLieshout TL, Shen NY, Ljubicic V.
PMID: 29163212
Front Physiol. 2017 Nov 01;8:870. doi: 10.3389/fphys.2017.00870. eCollection 2017.

Protein arginine methyltransferases (PRMTs) are a family of enzymes that catalyze the methylation of arginine residues on target proteins, thereby mediating a diverse set of intracellular functions that are indispensable for survival. Indeed, full-body knockouts of specific PRMTs are...

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Stouth DW, vanLieshout TL, Shen NY, et al. Regulation of Skeletal Muscle Plasticity by Protein Arginine Methyltransferases and Their Potential Roles in Neuromuscular Disorders. Front Physiol. 2017;8:870doi: 10.3389/fphys.2017.00870.
Stouth, D. W., vanLieshout, T. L., Shen, N. Y., & Ljubicic, V. (2017). Regulation of Skeletal Muscle Plasticity by Protein Arginine Methyltransferases and Their Potential Roles in Neuromuscular Disorders. Frontiers in physiology, 8870. https://doi.org/10.3389/fphys.2017.00870
Stouth, Derek W, et al. "Regulation of Skeletal Muscle Plasticity by Protein Arginine Methyltransferases and Their Potential Roles in Neuromuscular Disorders." Frontiers in physiology vol. 8 (2017): 870. doi: https://doi.org/10.3389/fphys.2017.00870
Stouth DW, vanLieshout TL, Shen NY, Ljubicic V. Regulation of Skeletal Muscle Plasticity by Protein Arginine Methyltransferases and Their Potential Roles in Neuromuscular Disorders. Front Physiol. 2017 Nov 01;8:870. doi: 10.3389/fphys.2017.00870. eCollection 2017. PMID: 29163212; PMCID: PMC5674940.
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Successful development of squamous cell carcinoma and hyperplasia in RGEN-mediated p27 KO mice after the treatment of DMBA and TPA.

Laboratory animal research

Choi JY, Yun WB, Kim JE, Lee MR, Park JJ, Song BR, Kim HR, Park JW, Kang MJ, Kang BC, Lee HW, Hwang DY.
PMID: 30310408
Lab Anim Res. 2018 Sep;34(3):118-125. doi: 10.5625/lar.2018.34.3.118. Epub 2018 Sep 27.

To evaluate the carcinogenicity of p27 knockout (KO) mice with RNA-guided endonuclease (RGENs)-mediated p27 mutant exon I gene (IΔ), alterations in the carcinogenic phenotypes including tumor spectrum, tumor suppressor proteins, apoptotic proteins and cell cycle regulators were observed in...

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Choi JY, Yun WB, Kim JE, et al. Successful development of squamous cell carcinoma and hyperplasia in RGEN-mediated p27 KO mice after the treatment of DMBA and TPA. Lab Anim Res. 2018;34(3):118-125doi: 10.5625/lar.2018.34.3.118.
Choi, J. Y., Yun, W. B., Kim, J. E., Lee, M. R., Park, J. J., Song, B. R., Kim, H. R., Park, J. W., Kang, M. J., Kang, B. C., Lee, H. W., & Hwang, D. Y. (2018). Successful development of squamous cell carcinoma and hyperplasia in RGEN-mediated p27 KO mice after the treatment of DMBA and TPA. Laboratory animal research, 34(3), 118-125. https://doi.org/10.5625/lar.2018.34.3.118
Choi, Jun Young, et al. "Successful development of squamous cell carcinoma and hyperplasia in RGEN-mediated p27 KO mice after the treatment of DMBA and TPA." Laboratory animal research vol. 34,3 (2018): 118-125. doi: https://doi.org/10.5625/lar.2018.34.3.118
Choi JY, Yun WB, Kim JE, Lee MR, Park JJ, Song BR, Kim HR, Park JW, Kang MJ, Kang BC, Lee HW, Hwang DY. Successful development of squamous cell carcinoma and hyperplasia in RGEN-mediated p27 KO mice after the treatment of DMBA and TPA. Lab Anim Res. 2018 Sep;34(3):118-125. doi: 10.5625/lar.2018.34.3.118. Epub 2018 Sep 27. PMID: 30310408; PMCID: PMC6170220.
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p53 and Ceramide as Collaborators in the Stress Response.

International journal of molecular sciences

Hage-Sleiman R, Esmerian MO, Kobeissy H, Dbaibo G.
PMID: 23455468
Int J Mol Sci. 2013 Mar 01;14(3):4982-5012. doi: 10.3390/ijms14034982.

The sphingolipid ceramide mediates various cellular processes in response to several extracellular stimuli. Some genotoxic stresses are able to induce p53-dependent ceramide accumulation leading to cell death. However, in other cases, in the absence of the tumor suppressor protein...

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Hage-Sleiman R, Esmerian MO, Kobeissy H, et al. p53 and Ceramide as Collaborators in the Stress Response. Int J Mol Sci. 2013;14(3):4982-5012doi: 10.3390/ijms14034982.
Hage-Sleiman, R., Esmerian, M. O., Kobeissy, H., & Dbaibo, G. (2013). p53 and Ceramide as Collaborators in the Stress Response. International journal of molecular sciences, 14(3), 4982-5012. https://doi.org/10.3390/ijms14034982
Hage-Sleiman, Rouba, et al. "p53 and Ceramide as Collaborators in the Stress Response." International journal of molecular sciences vol. 14,3 (2013): 4982-5012. doi: https://doi.org/10.3390/ijms14034982
Hage-Sleiman R, Esmerian MO, Kobeissy H, Dbaibo G. p53 and Ceramide as Collaborators in the Stress Response. Int J Mol Sci. 2013 Mar 01;14(3):4982-5012. doi: 10.3390/ijms14034982. PMID: 23455468; PMCID: PMC3634419.
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Tumor suppressor protein Pdcd4 interacts with Daxx and modulates the stability of Daxx and the Hipk2-dependent phosphorylation of p53 at serine 46.

Oncogenesis

Kumar N, Wethkamp N, Waters LC, Carr MD, Klempnauer KH.
PMID: 23536002
Oncogenesis. 2013 Jan 14;2:e37. doi: 10.1038/oncsis.2012.37.

The tumor suppressor protein Pdcd4 is a nuclear/cytoplasmic shuttling protein that has been implicated in the development of several types of human cancer. In the nucleus, Pdcd4 affects the transcription of specific genes by modulating the activity of several...

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Kumar N, Wethkamp N, Waters LC, et al. Tumor suppressor protein Pdcd4 interacts with Daxx and modulates the stability of Daxx and the Hipk2-dependent phosphorylation of p53 at serine 46. Oncogenesis. 2013;2:e37doi: 10.1038/oncsis.2012.37.
Kumar, N., Wethkamp, N., Waters, L. C., Carr, M. D., & Klempnauer, K. H. (2013). Tumor suppressor protein Pdcd4 interacts with Daxx and modulates the stability of Daxx and the Hipk2-dependent phosphorylation of p53 at serine 46. Oncogenesis, 2e37. https://doi.org/10.1038/oncsis.2012.37
Kumar, N, et al. "Tumor suppressor protein Pdcd4 interacts with Daxx and modulates the stability of Daxx and the Hipk2-dependent phosphorylation of p53 at serine 46." Oncogenesis vol. 2 (2013): e37. doi: https://doi.org/10.1038/oncsis.2012.37
Kumar N, Wethkamp N, Waters LC, Carr MD, Klempnauer KH. Tumor suppressor protein Pdcd4 interacts with Daxx and modulates the stability of Daxx and the Hipk2-dependent phosphorylation of p53 at serine 46. Oncogenesis. 2013 Jan 14;2:e37. doi: 10.1038/oncsis.2012.37. PMID: 23536002; PMCID: PMC3564021.
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Activation of Raf kinase by phorbol ester does not correlate with enhanced phosphorylation or transactivation activity of tumor suppressor protein p53.

International journal of oncology

Jaitner B, Lohrum M, Scheidtmann K.
PMID: 21533428
Int J Oncol. 1997 Mar;10(3):649-57. doi: 10.3892/ijo.10.3.649.

The tumor suppressor protein p53 appears to be regulated by various means including phosphorylation. We investigated a possible influence of the raf kinase on phosphorylation and transactivation of p53. The phosphorylation pattern of p53 was analysed in normal or...

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Jaitner B, Lohrum M, Scheidtmann K. Activation of Raf kinase by phorbol ester does not correlate with enhanced phosphorylation or transactivation activity of tumor suppressor protein p53. Int J Oncol. 1997;10(3):649-57doi: 10.3892/ijo.10.3.649.
Jaitner, B., Lohrum, M., & Scheidtmann, K. (1997). Activation of Raf kinase by phorbol ester does not correlate with enhanced phosphorylation or transactivation activity of tumor suppressor protein p53. International journal of oncology, 10(3), 649-57. https://doi.org/10.3892/ijo.10.3.649
Jaitner, B, et al. "Activation of Raf kinase by phorbol ester does not correlate with enhanced phosphorylation or transactivation activity of tumor suppressor protein p53." International journal of oncology vol. 10,3 (1997): 649-57. doi: https://doi.org/10.3892/ijo.10.3.649
Jaitner B, Lohrum M, Scheidtmann K. Activation of Raf kinase by phorbol ester does not correlate with enhanced phosphorylation or transactivation activity of tumor suppressor protein p53. Int J Oncol. 1997 Mar;10(3):649-57. doi: 10.3892/ijo.10.3.649. PMID: 21533428.
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The Blocking of c-Met Signaling Induces Apoptosis through the Increase of p53 Protein in Lung Cancer.

Cancer research and treatment

Jung HY, Joo HJ, Park JK, Kim YH.
PMID: 23341789
Cancer Res Treat. 2012 Dec;44(4):251-61. doi: 10.4143/crt.2012.44.4.251. Epub 2012 Dec 31.

PURPOSE: c-Met is an attractive potential target for novel therapeutic inhibition of human cancer, and c-Met tyrosine kinase inhibitors (TKIs) are effective growth inhibitors of various malignancies. However, their mechanisms in anticancer effects are not clear. In the present...

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Jung HY, Joo HJ, Park JK, et al. The Blocking of c-Met Signaling Induces Apoptosis through the Increase of p53 Protein in Lung Cancer. Cancer Res Treat. 2012;44(4):251-61doi: 10.4143/crt.2012.44.4.251.
Jung, H. Y., Joo, H. J., Park, J. K., & Kim, Y. H. (2012). The Blocking of c-Met Signaling Induces Apoptosis through the Increase of p53 Protein in Lung Cancer. Cancer research and treatment, 44(4), 251-61. https://doi.org/10.4143/crt.2012.44.4.251
Jung, Hae-Yun, et al. "The Blocking of c-Met Signaling Induces Apoptosis through the Increase of p53 Protein in Lung Cancer." Cancer research and treatment vol. 44,4 (2012): 251-61. doi: https://doi.org/10.4143/crt.2012.44.4.251
Jung HY, Joo HJ, Park JK, Kim YH. The Blocking of c-Met Signaling Induces Apoptosis through the Increase of p53 Protein in Lung Cancer. Cancer Res Treat. 2012 Dec;44(4):251-61. doi: 10.4143/crt.2012.44.4.251. Epub 2012 Dec 31. PMID: 23341789; PMCID: PMC3546272.
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Showing 25 to 36 of 139 entries