SILAC-based quantitative MS approach reveals Withaferin A regulated proteins in prostate cancer
Abstract
Withaferin A (WA) is a steroidal lactone extracted from Withania somnifera, commonly known as Ashwagandha. WA has several therapeutic benefits. The current study aims to identify proteins that are potentially regulated by WA in prostate cancer (PCA) cells. We used a SILAC-based proteomic approach to analyze the expression of proteins in response to WA treatment at 4 h and 24 h time points in three PCA cell lines: 22Rv1, DU-145, and LNCaP. Ontology analysis suggested that prolonged treatment with WA upregulated the expression of proteins involved in stress-response pathways. Treatment with WA increased oxidative stress, reduced global mRNA translation, and elevated the expression of cytoprotective stress granule (SG) protein G3BP1. WA treatment also enhanced the formation of SGs. The elevated expression of G3BP1 and the formation of SGs might constitute a mechanism of cytoprotection in PCA cells. Knockdown of G3BP1 blocked SG formation and enhanced the efficacy of WA to reduce PCA cell survival. SIGNIFICANCE: Withaferin A, a steroidal lactone, extracted from Withania somnifera is a promising anti-cancer drug. Using a SILAC-based quantitative proteomic approach, we identified proteins changed by WA-treatment at 4 h and 24 h in three prostate cancer (PCA) cell lines. WA-treatment induced the expression of proteins involved in apoptosis and reduced the expression of proteins involved in cell growth at 4 h. WA-treatment for 24 h enhanced the expression of proteins involved in stress response pathways. WA-treated cells exhibited increased oxidative stress, reduced mRNA translation and enhanced SG formation. PCA is characterized by higher metabolic rate and increased oxidative stress. PCA with a higher stress tolerance can effectively adapt to anti-cancer treatment stress, leading to drug resistance and cellular protection. Enhancing the level of oxidative stress along with inhibition of corresponding cytoprotective stress response pathways is a feasible option to prevent PCA from getting adapted to treatment stress. WA-treatment induced oxidative stress, in combination with blocking SGs by G3BP1 targeting, offers a therapeutic strategy to reduce PCA cell survival.
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Withanolides and sitoindosides (VII-X) escalate the activities of catalase and glutathione peroxidase.
“Later, further studies have validated the potential of withanolides and sitoindosides (VII-X) to escalate the activities of catalase and glutathione peroxidase [176].”
From Withania somnifera (L.) Dunal (Ashwagandha): A comprehensive review on ethnopharmacology, pharmacotherapeutics, biomedicinal and toxicological aspects (2021) · cites this paper as [176]
Withanolides and sitoindosides increase GPx in mice.
“| Withanolides and sitoindosides | Neuroprotective activity | Mice | Increase in catalase, GPx | [176] |”
From Withania somnifera (L.) Dunal (Ashwagandha): A comprehensive review on ethnopharmacology, pharmacotherapeutics, biomedicinal and toxicological aspects (2021) · cites this paper as [176]
Withanolides and sitoindosides increase catalase in mice.
“| Withanolides and sitoindosides | Neuroprotective activity | Mice | Increase in catalase, GPx | [176] |”
From Withania somnifera (L.) Dunal (Ashwagandha): A comprehensive review on ethnopharmacology, pharmacotherapeutics, biomedicinal and toxicological aspects (2021) · cites this paper as [176]
Glycowithanolides decrease lipid peroxidation in mice.
“| Glycowithanolides | Neuroprotective activity | Mice | Decrease in lipid peroxidation | [176] |”
From Withania somnifera (L.) Dunal (Ashwagandha): A comprehensive review on ethnopharmacology, pharmacotherapeutics, biomedicinal and toxicological aspects (2021) · cites this paper as [176]
Withanolides and sitoindosides have neuroprotective activity in mice.
“| Withanolides and sitoindosides | Neuroprotective activity | Mice | Increase in catalase, GPx | [176] |”
From Withania somnifera (L.) Dunal (Ashwagandha): A comprehensive review on ethnopharmacology, pharmacotherapeutics, biomedicinal and toxicological aspects (2021) · cites this paper as [176]
Glycowithanolides have neuroprotective activity in mice.
“| Glycowithanolides | Neuroprotective activity | Mice | Decrease in lipid peroxidation | [176] |”
From Withania somnifera (L.) Dunal (Ashwagandha): A comprehensive review on ethnopharmacology, pharmacotherapeutics, biomedicinal and toxicological aspects (2021) · cites this paper as [176]
Cites
1 retracted
RETRACTED: The RasGAP-associated endoribonuclease G3BP assembles stress granules
Tourrière, H., Chébli, K., Zekri, L., Courselaud, B., Blanchard, J. M., Bertrand, É., & Tazi, J. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200212128 · Cited by 834 · see citing works
RetractedBray, F., Ferlay, J., Soerjomataram, I., Siegel, R. L., Torre, L. A., & Jemal, A. (2018) · CA: A Cancer Journal for Clinicians · doi:10.3322/caac.21492 · Cited by 84,109 · see citing works
Pérez-Riverol, Y., Csordas, A., Bai, J.-W., Bernal-Llinares, M., Hewapathirana, S., Kundu, D. J., Inuganti, A., Griss, J., Mayer, G., Eisenacher, M., et al. (2018) · Nucleic Acids Res. · doi:10.1093/nar/gky1106 · Cited by 6,216 · see citing works
Rappsilber, J., Mann, M., & Ishihama, Y. (2007) · Nature Protocols · doi:10.1038/nprot.2007.261 · Cited by 4,641 · see citing works
10-Year Outcomes after Monitoring, Surgery, or Radiotherapy for Localized Prostate Cancer
Hamdy, F. C., Donovan, J., Lane, J. A., Mason, M. D., Metcalfe, C. D., Holding, P., Davis, M., Peters, T. J., Turner, E. L., Martin, R. M., et al. (2016) · New England Journal of Medicine · doi:10.1056/nejmoa1606220 · Cited by 2,642 · see citing works
Drug resistance in cancer: An overview
Housman, G., Byler, S., Heerboth, S., Lapinska, K., Longacre, M., Snyder, N., & Sarkar, S. (2014) · Cancers · doi:10.3390/cancers6031769 · Cited by 2,463 · see citing works
Blue silver: A very sensitive colloidal Coomassie G‐250 staining for proteome analysis
Candiano, G., Bruschi, M., Musante, L., Santucci, L., Ghiggeri, G. M., Carnemolla, B., Orecchia, P., Zardi, L., & Righetti, P. G. (2004) · Electrophoresis · doi:10.1002/elps.200305844 · Cited by 1,927 · see citing works
Rowinsky, E. K., & Donehower, R. C. (1995) · New England Journal of Medicine · doi:10.1056/nejm199504133321507 · Cited by 1,924 · see citing works
Eukaryotic stress granules: the ins and outs of translation.
Buchan, J., & Parker, R. (2009) · Molecules and Cells · doi:10.1016/j.molcel.2009.11.020 · Cited by 1,517 · see citing works
Scientific basis for the therapeutic use of Withania somnifera (ashwagandha): a review.
Mishra, L. C., Singh, B. B., & Dagenais, S. (2000) · PubMed · Cited by 776 · see citing works
Molecular characterization of human prostate carcinoma cell lines
van Bokhoven, A., Varella‐Garcia, M., Korch, C. T., Johannes, W. U., Smith, E. E., Miller, H. L., Nordeen, S. K., Miller, G. J., & Lucia, M. S. (2003) · The Prostate · doi:10.1002/pros.10290 · Cited by 635 · see citing works
Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways
有本, 京., Fukuda, H., Imajoh‐Ohmi, S., Saito, H., & Takekawa, M. (2008) · Nature Cell Biology · doi:10.1038/ncb1791 · Cited by 607 · see citing works
Kwon, S., Zhang, Y., & Matthias, P. (2007) · Genes & Development · doi:10.1101/gad.461107 · Cited by 402 · see citing works
Pharmacologic overview of Withania somnifera, the Indian Ginseng
Dar, N. J., Hamid, A., & Ahmad, M. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2012-1 · Cited by 391 · see citing works
The discovery of the vinca alkaloids—chemotherapeutic agents against cancer
NOBLE, R. L. (1990) · Biochemistry and Cell Biology · doi:10.1139/o90-197 · Cited by 388 · see citing works
Taipale, M., Tucker, G., Peng, J., Krykbaeva, I., Lin, Z., Larsen, B. G., Choi, H., Berger, B., Gingras, A., & Lindquist, S. L. (2014) · Cell · doi:10.1016/j.cell.2014.05.039 · Cited by 388 · see citing works
Withaferin A is a potent inhibitor of angiogenesis
Mohan, R., Hammers, H. J., Bargagna‐Mohan, P., Zhan, X. H., Herbstritt, C. J., Ruiz, A. R. L., Li, Z., Hanson, A., Conner, B., Rougas, J., et al. (2004) · Angiogenesis · doi:10.1007/s10456-004-1026-3 · Cited by 384 · see citing works
p53 oncogene mutations in three human prostate cancer cell lines
Carroll, A. G., Voeller, H. J., Sugars, L. V. Y., & Gelmann, E. P. (1993) · The Prostate · doi:10.1002/pros.2990230206 · Cited by 303 · see citing works
Both G 3 BP 1 and G 3 BP 2 contribute to stress granule formation
Matsuki, H., Takahashi, M., Higuchi, M., Makokha, G. N., Oie, M., & Fujii, M. (2012) · Genes to Cells · doi:10.1111/gtc.12023 · Cited by 300 · see citing works
Thaiparambil, J. T., Bender, L., Ganesh, T., Kline, E. R., Patel, P., Liu, Y., Tighiouart, M., Vertino, P. M., Harvey, R. D., García, A., et al. (2011) · International Journal of Cancer · doi:10.1002/ijc.25938 · Cited by 289 · see citing works
YB-1 regulates stress granule formation and tumor progression by translationally activating G3BP1
Somasekharan, S. P., El-Naggar, A. M., Leprivier, G., Cheng, H., Hajee, S., Grünewald, T. G. P., Zhang, F., Ng, T., Delattre, O., Evdokimova, V. E., et al. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201411047 · Cited by 279 · see citing works
Self-citationEndoplasmic reticulum stress signaling and chemotherapy resistance in solid cancers
Avril, T., Vauléon, É., & Chevet, É. (2017) · Oncogenesis · doi:10.1038/oncsis.2017.72 · Cited by 274 · see citing works
Alimirah, F., Chen, J., Basrawala, Z. K., Xin, H., & Choubey, D. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.03.041 · Cited by 264 · see citing works
Translational reprogramming in cellular stress response
Liu, B., & Qian, S. (2013) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1212 · Cited by 249 · see citing works
Withaferin A-Induced Apoptosis in Human Breast Cancer Cells Is Mediated by Reactive Oxygen Species
Hahm, E., de Moura, M. B., Kelley, E. E., Houten, B. V., Shiva, S., & Singh, S. V. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023354 · Cited by 247 · see citing works
Reprogramming mRNA translation during stress
Yamasaki, S., & Anderson, P. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.01.013 · Cited by 230 · see citing works
Arginine Demethylation of G3BP1 Promotes Stress Granule Assembly
Tsai, W.-C., Gayatri, S., Reineke, L. C., Sbardella, G., Bedford, M. T., & Lloyd, R. E. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.739573 · Cited by 195 · see citing works
Hu, T., RamachandraRao, S., Siva, S., Valancius, C., Zhu, Y., Mahadev, K., Toh, I., Goldstein, B. J., Woolkalís, M. J., & Sharma, K. (2005) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00024.2005 · Cited by 166 · see citing works
Withaferin-A—A Natural Anticancer Agent with Pleitropic Mechanisms of Action
Lee, I., & Choi, B. Y. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17030290 · Cited by 165 · see citing works
Cleaning up the masses: Exclusion lists to reduce contamination with HPLC-MS/MS
Hodge, K., ten Have, S., Hutton, L., & Lamond, A. I. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.02.023 · Cited by 152 · see citing works
Clark, D. J., Fondrie, W. E., Yang, A. J., & Mao, L. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.12.023 · Cited by 142 · see citing works
G3BP1 promotes stress-induced RNA granule interactions to preserve polyadenylated mRNA
Aulas, A., Caron, G., Gkogkas, C. G., Mohamed, N., Destroismaisons, L., Sonenberg, N., Leclerc, N. M., Parker, J. A., & Velde, C. V. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201408092 · Cited by 131 · see citing works
Large G3BP-induced granules trigger eIF2α phosphorylation
Reineke, L. C., Dougherty, J. D., Pierre, P., & Lloyd, R. E. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-05-0385 · Cited by 130 · see citing works
Androgen‐deprivation therapy as primary treatment for localized prostate cancer
Kawakami, J., Cowan, J. E., Elkin, E. P., Latini, D. M., DuChane, J., & Carroll, P. R. (2006) · Cancer · doi:10.1002/cncr.21799 · Cited by 107 · see citing works
Szic, K. S. V., de Beeck, K. O., Ratman, D., Wouters, A., Beck, I. M. E., Declerck, K., Heyninck, K., Fransén, E., Bracke, M., Bosscher, K. D., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087850 · Cited by 103 · see citing works
Wang, Y., Fu, D., Chen, Y., Su, J., Wang, Y., Li, X., Zhai, W., Niu, Y., Yue, D., & Geng, H. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0504-2 · Cited by 99 · see citing works
Cronauer, M. V., Schulz, W. A., Burchardt, T., Ackermann, R., & Burchardt, M. (2004) · Oncogene · doi:10.1038/sj.onc.1207346 · Cited by 95 · see citing works
Li, X., Zhu, F., Jiang, J., Sun, C., Zhong, Q., Shen, M., Wang, X., Tian, R., Shi, C., Xu, M., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1191722 · Cited by 91 · see citing works
Withaferin A Induces Oxidative Stress-Mediated Apoptosis and DNA Damage in Oral Cancer Cells
Chang, H., Li, R.-N., Wang, H.-R., Liu, J.-R., Tang, J., Huang, H., Chan, Y., & Yen, C.-Y. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00634 · Cited by 91 · see citing works
Lavut, A., & Raveh, D. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002527 · Cited by 90 · see citing works
Endoplasmic reticulum stress mediates withaferin A-induced apoptosis in human renal carcinoma cells
Choi, M. J., Park, E., Min, K. J., Park, J., & Kwon, T. K. (2011) · Toxicology in Vitro · doi:10.1016/j.tiv.2011.01.010 · Cited by 84 · see citing works
Chronic starvation induces non-canonical pro-death stress granules
Reineke, L. C., Cheema, S. A., Dubrulle, J., & Neilson, J. R. (2018) · Journal of Cell Science · doi:10.1242/jcs.220244 · Cited by 77 · see citing works
Oi, N., Yuan, J., Malakhova, M. L., Luo, K., Li, Y., Ryu, J., Zhang, L., Bode, A. M., Xu, Z., Li, Y., et al. (2014) · Oncogene · doi:10.1038/onc.2014.194 · Cited by 73 · see citing works
Evolving standards in the treatment of docetaxel-refractory castration-resistant prostate cancer
Antonarakis, E. S., & Armstrong, A. J. (2011) · Prostate Cancer and Prostatic Diseases · doi:10.1038/pcan.2011.23 · Cited by 71 · see citing works
Adaptive stress signaling in targeted cancer therapy resistance
Pazarentzos, E., & Bivona, T. G. (2015) · Oncogene · doi:10.1038/onc.2015.26 · Cited by 71 · see citing works
The roles and mechanisms of G3BP1 in tumour promotion
Zhang, C.-H., Wang, J., Cai, M., Shao, R., Liu, H., & Zhao, W. (2018) · Journal of drug targeting · doi:10.1080/1061186x.2018.1523415 · Cited by 71 · see citing works
Nishikawa, Y., Okuzaki, D., Fukushima, K., Mukai, S., Ohno, S., Ozaki, Y., Yabuta, N., & Nojima, H. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134137 · Cited by 70 · see citing works
Bale, S., Pooladanda, V., Sunkoju, M., & Godugu, C. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00248 · Cited by 70 · see citing works
Whole-Genome Sequence of the Metastatic PC3 and LNCaP Human Prostate Cancer Cell Lines
Seim, I., Jeffery, P. L., Thomas, P. B., Nelson, C. C., & Chopin, L. K. (2017) · G3 Genes Genomes Genetics · doi:10.1534/g3.117.039909 · Cited by 63 · see citing works
Synergistic antileukemic therapies in NOTCH1 -induced T-ALL
Sánchez-Martín, M., Ambesi‐Impiombato, A., Qin, Y., Herranz, D., Bansal, M., Girardi, T., Paietta, E. M., Tallman, M. S., Rowe, J. M., Keersmaecker, K. D., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1611831114 · Cited by 61 · see citing works
Lohiya, V., Aragon‐Ching, J. B., & Sonpavde, G. (2016) · Clinical Medicine Insights Oncology · doi:10.4137/cmo.s34535 · Cited by 59 · see citing works
Ghosh, K., De, S., Mukherjee, S., Das, S., Ghosh, A. N., & Sengupta, S. (2017) · Toxicology in Vitro · doi:10.1016/j.tiv.2017.07.025 · Cited by 55 · see citing works
G3BP1-linked mRNA partitioning supports selective protein synthesis in response to oxidative stress
Somasekharan, S., Zhang, F., Saxena, N., Huang, J.-N., Kuo, I.-C., Low, C., Bell, R., Adomat, H., Stoynov, N., Foster, L., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa376 · Cited by 55 · see citing works
Self-citationSkjøth, I. H. E., & Issinger, O. (2006) · International Journal of Oncology · doi:10.3892/ijo.28.1.217 · Cited by 52 · see citing works
UVC-Induced Stress Granules in Mammalian Cells
Moutaoufik, M. T., Fatimy, R. E., Nassour, H., Gareau, C., Lang, J., Tanguay, R. M., Mazrouï, R., & Khandjian, É. W. (2014) · PLoS ONE · doi:10.1371/journal.pone.0112742 · Cited by 50 · see citing works
Stress Granule Formation Attenuates RACK1-Mediated Apoptotic Cell Death Induced by Morusin
Park, Y., Choi, D. W., Cho, S. W., Han, J., Yang, S., & Choi, C. Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155360 · Cited by 50 · see citing works
Characterization of a novel RP2–OSTF1 interaction and its implication for actin remodelling
Lyraki, R., Lokaj, M., Soares, D. C., Little, A., Vermeren, M., Marsh, J. A., Wittinghofer, A., & Hurd, T. W. (2018) · Journal of Cell Science · doi:10.1242/jcs.211748 · Cited by 47 · see citing works
Somasekharan, S. P., Stoynov, N., Rotblat, B., Leprivier, G., Galpin, J. D., Ahern, C. A., Foster, L. J., & Sorensen, P. H. B. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.08.019 · Cited by 46 · see citing works
Self-citationG3BP1 activates the TGF-β/Smad signaling pathway to promote gastric cancer
Xiong, R., Gao, J., & Yin, T. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s213728 · Cited by 45 · see citing works
Khan, S. M., Rammeloo, A. W., & Heikkila, J. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050547 · Cited by 41 · see citing works
Chemotherapy in Prostate Cancer
Hurwitz, M. E. (2015) · Current Oncology Reports · doi:10.1007/s11912-015-0468-7 · Cited by 40 · see citing works
Allkinꝉ, R. (2017) · Cited by 39 · see citing works
Yu, T., Tang, J., Ou‐Yang, F., Wang, Y., Yuan, S. F., Tseng, K., Lin, L., & Chang, H. (2020) · Biomolecules · doi:10.3390/biom10050777 · Cited by 38 · see citing works
Palangi, F., Samuel, S. M., Thompson, I. R., Triggle, C. R., & Emara, M. M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0182059 · Cited by 35 · see citing works
Khalilpourfarshbafi, M., Murugan, D. D., Sattar, M. Z. A., Sucedaram, Y., & Abdullah, N. A. (2019) · PLoS ONE · doi:10.1371/journal.pone.0218792 · Cited by 33 · see citing works
Withaferin A protects against spinal cord injury by inhibiting apoptosis and inflammation in mice
Yan, X., Huang, G., Liu, Q., Zheng, J., Chen, H., Huang, Q., Chen, J., & Huang, H. (2017) · Pharmaceutical Biology · doi:10.1080/13880209.2017.1288262 · Cited by 31 · see citing works
Liu, X., Chen, L., Liang, T., Tian, X., Liu, Y., & Zhang, T. (2017) · PubMed · Cited by 30 · see citing works
Broad-spectrum antitumor properties of Withaferin A: a proteomic perspective
Dom, M. P., Berghe, W. V., & Ostade, X. V. (2019) · RSC Medicinal Chemistry · doi:10.1039/c9md00296k · Cited by 29 · see citing works
mRNA cycles through hypoxia-induced stress granules in live Drosophila embryonic muscles
van der Laan, A. M. A., Vangemert, A. M. C., Dirks, R. W., Noordermeer, J. N., Fradkin, L. G., Tanke, H. J., & Jost, C. R. (2012) · The International Journal of Developmental Biology · doi:10.1387/ijdb.103172al · Cited by 28 · see citing works
Bittencourt, L. F. F., Negreiros-Lima, G. L., Sousa, L. P., Silva, A. G., de Souza, I. B. S., Ribeiro, R. I. M. D. A., Dutra, M. F., Silva, R. F., Dias, A. C. F., Soriani, F. M., et al. (2019) · Journal of Neuro-Oncology · doi:10.1007/s11060-019-03252-6 · Cited by 28 · see citing works
Gonçalves, A. C., Towers, E. R., Haq, N., Porco, J. A. J., Pelletier, J., Dawson, S. J., & Gale, J. E. (2019) · Scientific Reports · doi:10.1038/s41598-019-48393-w · Cited by 26 · see citing works
Zhang, X., Timmermann, B. N., Samadi, A. K., & Cohen, M. S. (2012) · ISRN Biochemistry · doi:10.5402/2012/707586 · Cited by 25 · see citing works
G3BP1 Depletion Increases Radiosensitisation by Inducing Oxidative Stress in Response to DNA Damage
Cho, E., Than, T. T., Kim, S.-H., Park, E., Kim, M., Lee, K. H., & SHIN, H. J. (2019) · Anticancer Research · doi:10.21873/anticanres.13816 · Cited by 24 · see citing works
Li, Y., Wang, J., Zhong, S., Li, J., & Du, W. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11527 · Cited by 19 · see citing works
Kinetic Measurement of Apoptosis and Immune Cell Killing Using Live-Cell Imaging and Analysis
Granger, J. E., & Appledorn, D. M. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-1162-3_17 · Cited by 10 · see citing works
Flagged first, then by citations
1 of the 76 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Paul, S., Chakraborty, S., Anand, U., Dey, S., Nandy, S., Ghorai, M., Saha, S. C., Patil, M. T., Kandimalla, R., Proćków, J., et al. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112175 · Cited by 306 · see citing works
Evaluating anticancer properties of Withaferin A—a potent phytochemical
Atteeq, M. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.975320 · Cited by 93 · see citing works
Xing, Z., Su, A., Li, M., Zhang, Y., He, T., Qiu, Y., Wei, T., Li, Z., Zhu, J., & Wu, W. (2023) · Drug Design Development and Therapy · doi:10.2147/dddt.s422512 · Cited by 55 · see citing works
The roles of G3BP1 in human diseases (review)
Ge, Y., Jin, J., Li, J., Meng, Y., & Jin, X. (2022) · Gene · doi:10.1016/j.gene.2022.146294 · Cited by 50 · see citing works
Somasekharan, S. P., & Gleave, M. E. (2021) · FEBS Letters · doi:10.1002/1873-3468.14229 · Cited by 41 · see citing works
Self-citationPotential clinical applications of Ashwagandha (Withania somnifera) in medicine and neuropsychiatry
Dcruz, M. M., & Andrade, C. (2022) · Expert Review of Clinical Pharmacology · doi:10.1080/17512433.2022.2121699 · Cited by 38 · see citing works
Application of stress granule core element G3BP1 in various diseases: A review
Guo, J., Huang, R., Mei, Y., Lu, S., Gong, J., Wang, L., Ding, L., Wu, H., Pan, D., & Liu, W. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.137254 · Cited by 16 · see citing works
Fan, H., Wang, C., Liu, S., Li, Y., & Xu, Z. (2025) · Current Pharmaceutical Analysis · doi:10.1016/j.cpan.2025.01.004 · Cited by 15 · see citing works
Kumar, P., Banik, S. P., Goel, A., Chakraborty, S., Bagchi, M., & Bagchi, D. (2023) · Journal of the American Nutrition Association · doi:10.1080/27697061.2023.2228863 · Cited by 14 · see citing works
Gopalaiah, S. B., & Jayaseelan, K. (2024) · Critical Reviews in Analytical Chemistry · doi:10.1080/10408347.2024.2307887 · Cited by 12 · see citing works
Withaferin A and Celastrol Overwhelm Proteostasis
Vilaboa, N. E., & Voellmy, R. W. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010367 · Cited by 9 · see citing works
Withanolides as Prospective Drug Candidates: Production and Therapeutic Applications–A Review
Gupta, A., & Vasundhara, M. (2025) · Planta Medica · doi:10.1055/a-2659-7263 · Cited by 4 · see citing works
LC-MS-based proteomics: insights into natural product-directed cellular targeting
Ranapangu, B., Sandhu, M., & Paul, A. T. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104534 · Cited by 2 · see citing works
Molecular insights into withaferin A: A holistic approach to cancer therapy
Islam, M. R., Rauf, A., Rakesh, M. M., Akash, S., Fakir, M. N. H., Islam, M. S., Naba, A. F., Al-Imran, M. I. K., Alomar, T. S., Ogaly, H. A., et al. (2024) · Inorganic Chemistry Communications · doi:10.1016/j.inoche.2024.113316 · Cited by 1 · see citing works
Withanolides as anti-prostate cancer agents of promise
Shukla, A., Bisht, R., Maurya, R., & Dev, K. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-21842-2.00003-6 · Cited by 1 · see citing works
Xu, Z., You, H., Gu, J., Jiang, J., Yan, Z., & Jin, X. (2025) · Gene · doi:10.1016/j.gene.2025.149776 · Cited by 1 · see citing works
Chronic stress disrupts the network among stress granules, processing bodies and motor proteins
Adachi, Y., Masuda, M., Taketani, Y., Anderson, P. J., & Ivanov, P. V. (2026) · Journal of Cell Science · doi:10.1242/jcs.264801 · Cited by 1 · see citing works
Clinical Proteomics: Liquid Chromatography-Mass Spectrometry (LC-MS) Purification Systems
Henry, M. A., & Meleady, P. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3362-5_14
Analysis of androgen modulation by natural products
Sharma, K., Yakubu, J., & Pandey, A. V. (2026) · Pharmacological Research · doi:10.1016/j.phrs.2026.108377
- Authors
- Kumar, R., Nayak, D., & Somasekharan, S. P.
- Affiliations
- Indian Institute of Technology Indore (IN)
- Vancouver Prostate Centre (CA)
- Corresponding author
- Somasekharan, Syam Prakash
- Venue
- Journal of Proteomics
- Publisher
- Elsevier BV
- Published
- 2021-09
- Volume
- 247
- Pages
- 104334
- ISSN
- 1874-3919 (ISSN-L)
- OpenAlex
- W3185321016
- Cited by
- 19
- References
- 76
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 3 · 2023: 4 · 2022: 3 · 2021: 2
- FWCI
- 3.38
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Journal of Proteomics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Department of Biotechnology, Ministry of Science and Technology, India
- Topics
- Health Sciences › Medicine › Complementary and alternative medicine › Phytochemicals and Medicinal Plants
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Prostate Cancer Treatment and Research
- Keywords
- withaferin A, prostate cancer, Withania somnifera, steroidal lactones, G3BP1, stress granules, oxidative stress, mRNA translation, cytoprotection, apoptosis, drug resistance, LNCaP cells, DU145 cells, 22Rv1 cells
- MeSH terms
- RNA Recognition Motif Proteins, Poly-ADP-Ribose Binding Proteins, DNA Helicases, Humans, Male, Prostatic Neoplasms, RNA Helicases, Proteomics, Withanolides
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