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Journal articles on the topic 'SMAR1'

Author: Grafiati

Published: 6 September 2023

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1

Bhattacharya, Apoorva, Shravanti Mukherjee, Poulami Khan, Shruti Banerjee, Apratim Dutta, Nilanjan Banerjee, Debomita Sengupta, et al. "SMAR1 repression by pluripotency factors and consequent chemoresistance in breast cancer stem-like cells is reversed by aspirin." Science Signaling 13, no. 654 (October 20, 2020): eaay6077. http://dx.doi.org/10.1126/scisignal.aay6077.

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The high abundance of drug efflux pumps in cancer stem cells (CSCs) contributes to chemotherapy resistance. The transcriptional regulator SMAR1 suppresses CSC expansion in colorectal cancer, and increased abundance of SMAR1 is associated with better prognosis. Here, we found in breast tumors that the expression of SMAR1 was decreased in CSCs through the cooperative interaction of the pluripotency factors Oct4 and Sox2 with the histone deacetylase HDAC1. Overexpressing SMAR1 sensitized CSCs to chemotherapy through SMAR1-dependent recruitment of HDAC2 to the promoter of the gene encoding the drug efflux pump ABCG2. Treating cultured CSCs or 4T1 tumor-bearing mice with the nonsteroidal anti-inflammatory drug aspirin restored SMAR1 expression and ABCG2 repression and enhanced tumor sensitivity to doxorubicin. Our findings reveal transcriptional mechanisms regulating SMAR1 that also regulate cancer stemness and chemoresistance and suggest that, by restoring SMAR1 expression, aspirin might enhance chemotherapeutic efficacy in patients with stem-like tumors.

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2

Rampalli, Shravanti, L. Pavithra, Altaf Bhatt, Tapas K. Kundu, and Samit Chattopadhyay. "Tumor Suppressor SMAR1 Mediates Cyclin D1 Repression by Recruitment of the SIN3/Histone Deacetylase 1 Complex." Molecular and Cellular Biology 25, no. 19 (October 1, 2005): 8415–29. http://dx.doi.org/10.1128/mcb.25.19.8415-8429.2005.

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ABSTRACT Matrix attachment region binding proteins have been shown to play an important role in gene regulation by altering chromatin in a stage- and tissue-specific manner. Our previous studies report that SMAR1, a matrix-associated protein, regresses B16-F1-induced tumors in mice. Here we show SMAR1 targets the cyclin D1 promoter, a gene product whose dysregulation is attributed to breast malignancies. Our studies reveal that SMAR1 represses cyclin D1 gene expression, which can be reversed by small interfering RNA specific to SMAR1. We demonstrate that SMAR1 interacts with histone deacetylation complex 1, SIN3, and pocket retinoblastomas to form a multiprotein repressor complex. This interaction is mediated by the SMAR1(160-350) domain. Our data suggest SMAR1 recruits a repressor complex to the cyclin D1 promoter that results in deacetylation of chromatin at that locus, which spreads to a distance of at least the 5 kb studied upstream of the cyclin D1 promoter. Interestingly, we find that the high induction of cyclin D1 in breast cancer cell lines can be correlated to the decreased levels of SMAR1 in these lines. Our results establish the molecular mechanism exhibited by SMAR1 to regulate cyclin D1 by modification of chromatin.

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3

Nakka, Kiran Kumar, Nidhi Chaudhary, Shruti Joshi, Jyotsna Bhat, Kulwant Singh, Subhrangsu Chatterjee, Renu Malhotra, et al. "Nuclear matrix-associated protein SMAR1 regulates alternative splicing via HDAC6-mediated deacetylation of Sam68." Proceedings of the National Academy of Sciences 112, no. 26 (June 15, 2015): E3374—E3383. http://dx.doi.org/10.1073/pnas.1418603112.

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Pre-mRNA splicing is a complex regulatory nexus modulated by various trans-factors and their posttranslational modifications to create a dynamic transcriptome through alternative splicing. Signal-induced phosphorylation and dephosphorylation of trans-factors are known to regulate alternative splicing. However, the role of other posttranslational modifications, such as deacetylation/acetylation, methylation, and ubiquitination, that could modulate alternative splicing in either a signal-dependent or -independent manner remain enigmatic. Here, we demonstrate that Scaffold/matrix-associated region-binding protein 1 (SMAR1) negatively regulates alternative splicing through histone deacetylase 6 (HDAC6)-mediated deacetylation of RNA-binding protein Sam68 (Src-associated substrate during mitosis of 68 kDa). SMAR1 is enriched in nuclear splicing speckles and associates with the snRNAs that are involved in splice site recognition. ERK–MAPK pathway that regulates alternative splicing facilitates ERK-1/2–mediated phosphorylation of SMAR1 at threonines 345 and 360 and localizes SMAR1 to the cytoplasm, preventing its interaction with Sam68. We showed that endogenously, SMAR1 through HDAC6 maintains Sam68 in a deacetylated state. However, knockdown or ERK-mediated phosphorylation of SMAR1 releases the inhibitory SMAR1–HDAC6–Sam68 complex, facilitating Sam68 acetylation and alternative splicing. Furthermore, loss of heterozygosity at the Chr.16q24.3 locus in breast cancer cells, wherein the human homolog of SMAR1 (BANP) has been mapped, enhances Sam68 acetylation and CD44 variant exon inclusion. In addition, tail-vein injections in mice with human breast cancer MCF-7 cells depleted for SMAR1 showed increased CD44 variant exon inclusion and concomitant metastatic propensity, confirming the functional role of SMAR1 in regulation of alternative splicing. Thus, our results reveal the complex molecular mechanism underlying SMAR1-mediated signal-dependent and -independent regulation of alternative splicing via Sam68 deacetylation.

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4

Jalota, Archana, Kamini Singh, Lakshminarasimhan Pavithra, Ruchika Kaul-Ghanekar, Shahid Jameel, and Samit Chattopadhyay. "Tumor Suppressor SMAR1 Activates and Stabilizes p53 through Its Arginine-Serine-rich Motif." Journal of Biological Chemistry 280, no. 16 (February 8, 2005): 16019–29. http://dx.doi.org/10.1074/jbc.m413200200.

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Various stresses and DNA-damaging agents trigger transcriptional activity of p53 by post-translational modifications, making it a global regulatory switch that controls cell proliferation and apoptosis. Earlier we have shown that the novel MAR-associated protein SMAR1 interacts with p53. Here we delineate the minimal domain of SMAR1 (the arginine-serine-rich domain) that is phosphorylated by protein kinase C family proteins and is responsible for p53 interaction, activation, and stabilization within the nucleus. SMAR1-mediated stabilization of p53 is brought about by inhibiting Mdm2-mediated degradation of p53. We also demonstrate that this arginine-serine (RS)-rich domain triggers the various cell cycle modulating proteins that decide cell fate. Furthermore, phenotypic knock-down experiments using small interfering RNA showed that SMAR1 is required for activation and nuclear retention of p53. The level of phosphorylated p53 was significantly increased in the thymus of SMAR1 transgenic mice, showingin vivosignificance of SMAR1 expression. This is the first report that demonstrates the mechanism of action of the MAR-binding protein SMAR1 in modulating the activity of p53, often referred to as the “guardian of the genome.”

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5

Malik, Md Zubbair, Md Jahoor Alam, Romana Ishrat, Subhash M. Agarwal, and R. K. Brojen Singh. "Control of apoptosis by SMAR1." Molecular BioSystems 13, no. 2 (2017): 350–62. http://dx.doi.org/10.1039/c6mb00525j.

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6

Zhou, L. "How smart can it be: transcriptional regulation of T helper cells by SMAR1." Mucosal Immunology 8, no. 6 (July 29, 2015): 1181–83. http://dx.doi.org/10.1038/mi.2015.71.

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7

Faucher, Frédérick, and Zongchao Jia. "High-resolution structure of AKR1a4 in the apo form and its interaction with ligands." Acta Crystallographica Section F Structural Biology and Crystallization Communications 68, no. 11 (October 26, 2012): 1271–74. http://dx.doi.org/10.1107/s1744309112037128.

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Aldo-keto reductase 1a4 (AKR1a4; EC 1.1.1.2) is the mouse orthologue of human aldehyde reductase (AKR1a1), the founding member of the AKR family. As an NADPH-dependent enzyme, AKR1a4 catalyses the conversion of D-glucuronate to L-gulonate. AKR1a4 is involved in ascorbate biosynthesis in mice, but has also recently been found to interact with SMAR1, providing a novel mechanism of ROS regulation by ATM. Here, the crystal structure of AKR1a4 in its apo form at 1.64 Å resolution as well as the characterization of the binding of AKR1a4 to NADPH and P44, a peptide derived from SMAR1, is presented.

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8

Mittal, Smriti P. K., Jinumary Mathai, Abhijeet P. Kulkarni, Jayanta K. Pal, and Samit Chattopadhyay. "miR-320a regulates erythroid differentiation through MAR binding protein SMAR1." International Journal of Biochemistry & Cell Biology 45, no. 11 (November 2013): 2519–29. http://dx.doi.org/10.1016/j.biocel.2013.07.006.

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9

Malonia, Sunil Kumar, Surajit Sinha, Pavithra Lakshminarasimhan, Kamini Singh, Archana Jalota-Badhwar, Shravanti Rampalli, Ruchika Kaul-Ghanekar, and Samit Chattopadhyay. "Gene regulation by SMAR1: Role in cellular homeostasis and cancer." Biochimica et Biophysica Acta (BBA) - Reviews on Cancer 1815, no. 1 (January 2011): 1–12. http://dx.doi.org/10.1016/j.bbcan.2010.08.003.

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10

Taye, Nandaraj, Aftab Alam, Suvankar Ghorai, Deya Ghosh Chatterji, Apoorva Parulekar, Devraj Mogare, Snahlata Singh, et al. "SMAR1 inhibits Wnt/β-catenin signaling and prevents colorectal cancer progression." Oncotarget 9, no. 30 (April 20, 2018): 21322–36. http://dx.doi.org/10.18632/oncotarget.25093.

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11

Singh, Kamini, Surajit Sinha, Sunil Kumar Malonia, and Samit Chattopadhyay. "Tumor Necrosis Factor alpha (TNFα) regulates CD40 expression through SMAR1 phosphorylation." Biochemical and Biophysical Research Communications 391, no. 2 (January 2010): 1255–61. http://dx.doi.org/10.1016/j.bbrc.2009.12.055.

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12

Singh, Sandeep, Kadreppa Sreenath, Lakshminarasimhan Pavithra, Siddhartha Roy, and Samit Chattopadhyay. "SMAR1 regulates free radical stress through modulation of AKR1a4 enzyme activity." International Journal of Biochemistry & Cell Biology 42, no. 7 (July 2010): 1105–14. http://dx.doi.org/10.1016/j.biocel.2010.01.022.

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13

Pant, Richa, Aftab Alam, Arpankumar Choksi, Vibhuti Kumar Shah, Priyanka Firmal, and Samit Chattopadhyay. "Chromatin remodeling protein SMAR1 regulates adipogenesis by modulating the expression of PPARγ." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1866, no. 12 (December 2021): 159045. http://dx.doi.org/10.1016/j.bbalip.2021.159045.

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14

Nakka, Kiran K., and Samit Chattopadhyay. "Modulation of chromatin by MARs and MAR binding oncogenic transcription factor SMAR1." Molecular and Cellular Biochemistry 336, no. 1-2 (October 3, 2009): 75–84. http://dx.doi.org/10.1007/s11010-009-0262-7.

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15

Xu, Hongyu, Ting Liu, Wenjie Li, and Qi Yao. "SMAR1 attenuates the stemness of osteosarcoma cells via through suppressing ABCG2 transcriptional activity." Environmental Toxicology 36, no. 6 (February 5, 2021): 1090–98. http://dx.doi.org/10.1002/tox.23108.

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16

Chattopadhyay, Samit, Bhalchandra Mirlekar, Subeer Majumdar, and Madhukar Khetmalas. "Regulation of T cell lineage commitment by SMAR1 during inflammatory & autoimmune diseases." Indian Journal of Medical Research 142, no. 4 (2015): 405. http://dx.doi.org/10.4103/0971-5916.169198.

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17

Chaudhary, N., K. K. Nakka, P. L. Chavali, J. Bhat, S. Chatterjee, and S. Chattopadhyay. "SMAR1 coordinates HDAC6-induced deacetylation of Ku70 and dictates cell fate upon irradiation." Cell Death & Disease 5, no. 10 (October 2014): e1447-e1447. http://dx.doi.org/10.1038/cddis.2014.397.

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18

Jalota-Badhwar, Archana, Ruchika Kaul-Ghanekar, Devraj Mogare, Ramanamurthy Boppana, Kishore M. Paknikar, and Samit Chattopadhyay. "SMAR1-derived P44 Peptide Retains Its Tumor Suppressor Function through Modulation of p53." Journal of Biological Chemistry 282, no. 13 (January 17, 2007): 9902–13. http://dx.doi.org/10.1074/jbc.m608434200.

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19

Alam, Aftab, Nandaraj Taye, Sonal Patel, Milind Thube, Jayati Mullick, Vibhuti Kumar Shah, Richa Pant, et al. "SMAR1 favors immunosurveillance of cancer cells by modulating calnexin and MHC I expression." Neoplasia 21, no. 10 (October 2019): 945–62. http://dx.doi.org/10.1016/j.neo.2019.07.002.

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20

Sreenath, Kadreppa, Lakshminarasimhan Pavithra, Sandeep Singh, Surajit Sinha, Prasanta K. Dash, Nagadenahalli B. Siddappa, Udaykumar Ranga, Debashis Mitra, and Samit Chattopadhyay. "Nuclear Matrix protein SMAR1 represses HIV-1 LTR mediated transcription through chromatin remodeling." Virology 400, no. 1 (April 2010): 76–85. http://dx.doi.org/10.1016/j.virol.2010.01.017.

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21

Chemmannur, S. V., A. J. Badhwar, B. Mirlekar, S. K. Malonia, M. Gupta, N. Wadhwa, R. Bopanna, et al. "Nuclear matrix binding protein SMAR1 regulates T-cell differentiation and allergic airway disease." Mucosal Immunology 8, no. 6 (March 4, 2015): 1201–11. http://dx.doi.org/10.1038/mi.2015.11.

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22

Singh, Kamini, Surajit Sinha, Sunil Kumar Malonia, Pradeep Bist, Vinay Tergaonkar, and Samit Chattopadhyay. "Tumor Suppressor SMAR1 RepressesIκBα Expression and Inhibits p65 Transactivation through Matrix Attachment Regions." Journal of Biological Chemistry 284, no. 2 (November 3, 2008): 1267–78. http://dx.doi.org/10.1074/jbc.m801088200.

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23

Sinha, Surajit, Sunil Kumar Malonia, Smriti P. K. Mittal, Jinumary Mathai, Jayanta K. Pal, and Samit Chattopadhyay. "Chromatin remodelling protein SMAR1 inhibits p53 dependent transactivation by regulating acetyl transferase p300." International Journal of Biochemistry & Cell Biology 44, no. 1 (January 2012): 46–52. http://dx.doi.org/10.1016/j.biocel.2011.10.020.

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24

Ma, Feiyu, Hu Wang, Bin Chen, Feng Wang, and Haixiong Xu. "Metallothionein 3 attenuated the apoptosis of neurons in the CA1 region of the hippocampus in the senescence-accelerated mouse/PRONE8 (SAMP8)." Arquivos de Neuro-Psiquiatria 69, no. 1 (February 2011): 105–11. http://dx.doi.org/10.1590/s0004-282x2011000100020.

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OBJECTIVE: Metallothionein 3 (MT-3) has been shown to protect against apoptotic neuronal death in the brains of patients with Alzheimer's disease. Zinc is a potent inhibitor of caspase-3 and its deficiency was found to promote apoptosis. Here, we measured the zinc and copper content in the brains of senescence-accelerated mouse/PRONE8 (SAMP8) and sought to investigate the effect of MT-3 on the apoptosis of neurons in the hippocampal CA1 region of these mice. METHOD: The zinc and copper content in the brain samples of SAMP8 and normal control SAMR1 mice were determined using an atomic absorption spectrophotometer. The mice were administered intraperitoneally for four weeks with MT-3 or MT1 and thereafter apoptosis was measured using the TUNEL method and the expression of anti-apoptotic protein Bcl-2 and proapoptotic protein Bax was examined by immunohistochemistry. RESULTS: Compared with that in SMAR1 mice, the content of zinc in the brains of SAMP8 mice was significantly reduced (P<0.05). Moreover, significant levels of apoptosis of neurons were observed in the hippocampus of SAMP8 mice, which, compared with those in SMAR1 mice, also showed significantly lower levels of Bcl-2 and higher levels of Bax (P<0.05). MT-3 increased zinc concentration in the hippocampus of SAMP8 mice and also significantly decreased apoptosis in these neurons dose-dependently and increased the levels of Bcl-2 and decreased the levels of Bax. CONCLUSION: MT-3 could attenuate apoptotic neuron death in the hippocampus of SAMP8, suggesting that the protein may lessen the development of neurodegeneration.

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25

Malonia, Sunil K., Bhawna Yadav, Surajit Sinha, Gwendel Lazennec, and Samit Chattopadhyay. "Chromatin remodeling protein SMAR1 regulates NF-κB dependent Interleukin-8 transcription in breast cancer." International Journal of Biochemistry & Cell Biology 55 (October 2014): 220–26. http://dx.doi.org/10.1016/j.biocel.2014.09.008.

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26

Jalota, Archana, Kamini Singh, Lakshminarasimhan Pavithra, Ruchika Kaul-Ghanekar, Shahid Jameel, and Samit Chattopadhyay. "Withdrawal: Tumor suppressor SMAR1 activates and stabilizes p53 through its arginine-serine-rich motif." Journal of Biological Chemistry 295, no. 10 (March 6, 2020): 3390. http://dx.doi.org/10.1074/jbc.w120.012894.

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27

Mirlekar, B., S. Ghorai, M. Khetmalas, R. Bopanna, and S. Chattopadhyay. "Nuclear matrix protein SMAR1 control regulatory T-cell fate during inflammatory bowel disease (IBD)." Mucosal Immunology 8, no. 6 (May 20, 2015): 1184–200. http://dx.doi.org/10.1038/mi.2015.42.

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28

Pavithra, Lakshminarasimhan, Sandeep Singh, Kadreppa Sreenath, and Samit Chattopadhyay. "Tumor suppressor SMAR1 downregulates Cytokeratin 8 expression by displacing p53 from its cognate site." International Journal of Biochemistry & Cell Biology 41, no. 4 (April 2009): 862–71. http://dx.doi.org/10.1016/j.biocel.2008.08.038.

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29

Pavithra, Lakshminarasimhan, Srijata Mukherjee, Kadreppa Sreenath, Sanchari Kar, Kazuyasu Sakaguchi, Siddhartha Roy, and Samit Chattopadhyay. "SMAR1 Forms a Ternary Complex with p53-MDM2 and Negatively Regulates p53-mediated Transcription." Journal of Molecular Biology 388, no. 4 (May 2009): 691–702. http://dx.doi.org/10.1016/j.jmb.2009.03.033.

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30

Chattopadhyay, Samit, Bhawna Yadav, SunilK Malonia, SubeerS Majumdar, Pushpa Gupta, Neerja Wadhwa, Archana Badhwar, UmeshD Gupta, and VishwaM Katoch. "Constitutive expression of SMAR1 confers susceptibility to Mycobacterium tuberculosis infection in a transgenic mouse model." Indian Journal of Medical Research 142, no. 6 (2015): 732. http://dx.doi.org/10.4103/0971-5916.174566.

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31

Kaul-Ghanekar, Ruchika, Subeer Majumdar, Archana Jalota, Neerja Gulati, Neetu Dubey, Bhaskar Saha, and Samit Chattopadhyay. "Abnormal V(D)J Recombination of T Cell Receptor β Locus in SMAR1 Transgenic Mice." Journal of Biological Chemistry 280, no. 10 (March 2005): 9450–59. http://dx.doi.org/10.1074/jbc.m412206200.

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32

Pavithra, Lakshminarasimhan, Shravanti Rampalli, Surajit Sinha, Kadreppa Sreenath, Richard G. Pestell, and Samit Chattopadhyay. "Stabilization of SMAR1 mRNA by PGA2 involves a stem–loop structure in the 5′ UTR." Nucleic Acids Research 35, no. 18 (August 28, 2007): 6004–16. http://dx.doi.org/10.1093/nar/gkm649.

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33

Mirlekar, Bhalchandra, Sachin Patil, Ramanamurthy Bopanna, and Samit Chattopadhyay. "MAR binding protein SMAR1 favors IL-10 mediated regulatory T cell function in acute colitis." Biochemical and Biophysical Research Communications 464, no. 2 (August 2015): 647–53. http://dx.doi.org/10.1016/j.bbrc.2015.07.028.

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34

Sinha, Surajit, Sunil Kumar Malonia, Smriti P. K. Mittal, Kamini Singh, Sreenath Kadreppa, Rohan Kamat, Robin Mukhopadhyaya, Jayanta K. Pal, and Samit Chattopadhyay. "Coordinated regulation of p53 apoptotic targets BAX and PUMA by SMAR1 through an identical MAR element." EMBO Journal 29, no. 4 (January 14, 2010): 830–42. http://dx.doi.org/10.1038/emboj.2009.395.

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35

Kaul-Ghanekar, R. "SMAR1 and Cux/CDP modulate chromatin and act as negative regulators of the TCR enhancer (E )." Nucleic Acids Research 32, no. 16 (September 7, 2004): 4862–75. http://dx.doi.org/10.1093/nar/gkh807.

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36

Bhagat, Prasad N., Sachin H. Jadhav, Samit Chattopadhyay, and Kishore M. Paknikar. "Carbon nanospheres mediated nuclear delivery of SMAR1 protein (DNA binding domain) controls breast tumor in mice model." Nanomedicine 13, no. 4 (February 2018): 353–72. http://dx.doi.org/10.2217/nnm-2017-0298.

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37

Chakraborty, Samik, Kaushik Das, Shilpi Saha, Minakshi Mazumdar, Argha Manna, Sreeparna Chakraborty, Shravanti Mukherjee, et al. "Nuclear Matrix Protein SMAR1 Represses c-Fos-mediated HPV18 E6 Transcription through Alteration of Chromatin Histone Deacetylation." Journal of Biological Chemistry 289, no. 42 (August 25, 2014): 29074–85. http://dx.doi.org/10.1074/jbc.m114.564872.

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38

Singh, Kamini, Devraj Mogare, Ramprasad Obula Giridharagopalan, Rajinikanth Gogiraju, Gopal Pande, and Samit Chattopadhyay. "p53 Target Gene SMAR1 Is Dysregulated in Breast Cancer: Its Role in Cancer Cell Migration and Invasion." PLoS ONE 2, no. 8 (August 1, 2007): e660. http://dx.doi.org/10.1371/journal.pone.0000660.

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39

Liu, Heng-chao, Fang Ma, Yong Shen, Yong-quan Hu, and Shaojun Pan. "Overexpression of SMAR1 Enhances Radiosensitivity in Human Breast Cancer Cell Line MCF7 via Activation of p53 Signaling Pathway." Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics 22, no. 5 (November 25, 2015): 293–300. http://dx.doi.org/10.3727/096504015x14424348426035.

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40

Xiaohua, Wang, Xu Hongxia, Deng Rong, Wu Pingping, Huang Xing, Zhu Yichao, and Chen Cheng. "SMAR1 promotes immune escape of Tri-negative Breast Cancer through a mechanism involving T-bet/PD-1 Axis." Cellular and Molecular Biology 64, no. 12 (September 30, 2018): 70. http://dx.doi.org/10.14715/cmb/2018.64.12.14.

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41

Trivedi, Jay, Aftab Alam, Shruti Joshi, Togapur Pavan Kumar, Venkatraju Chippala, Prathama S. Mainkar, Srivari Chandrasekhar, Samit Chattopadhyay, and Debashis Mitra. "A novel isothiocyanate derivative inhibits HIV-1 gene expression and replication by modulating the nuclear matrix associated protein SMAR1." Antiviral Research 173 (January 2020): 104648. http://dx.doi.org/10.1016/j.antiviral.2019.104648.

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42

Paul, Debasish, Suvankar Ghorai, U. S. Dinesh, Praveenkumar Shetty, Samit Chattopadhyay, and Manas Kumar Santra. "Cdc20 directs proteasome-mediated degradation of the tumor suppressor SMAR1 in higher grades of cancer through the anaphase promoting complex." Cell Death & Disease 8, no. 6 (June 2017): e2882-e2882. http://dx.doi.org/10.1038/cddis.2017.270.

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43

Chattopadhyay, Samit, Ruchika Kaul, Alan Charest, David Housman, and Jianzhu Chen. "SMAR1, a Novel, Alternatively Spliced Gene Product, Binds the Scaffold/Matrix-Associated Region at the T Cell Receptor β Locus." Genomics 68, no. 1 (August 2000): 93–96. http://dx.doi.org/10.1006/geno.2000.6279.

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44

Firmal, Priyanka, Vibhuti Kumar Shah, Richa Pant, and Samit Chattopadhyay. "RING finger protein TOPORS modulates the expression of tumor suppressor SMAR1 in colorectal cancer via the TLR4‐TRIF pathway." Molecular Oncology 16, no. 7 (February 5, 2022): 1523–40. http://dx.doi.org/10.1002/1878-0261.13126.

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45

Chakraborty, Samik, Arghya Adhikary, Minakshi Mazumdar, Shravanti Mukherjee, Pushpak Bhattacharjee, Deblina Guha, Tathagata Choudhuri, et al. "Capsaicin-Induced Activation of p53-SMAR1 Auto-Regulatory Loop Down-Regulates VEGF in Non-Small Cell Lung Cancer to Restrain Angiogenesis." PLoS ONE 9, no. 6 (June 13, 2014): e99743. http://dx.doi.org/10.1371/journal.pone.0099743.

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46

Kaul, Ruchika, Sujoy Mukherjee, Farid Ahmed, Manoj Kumar Bhat, Rishiraj Chhipa, Sanjeev Galande, and Samit Chattopadhyay. "Direct interaction with and activation of p53 by SMAR1 retards cell-cycle progression at G2/M phase and delays tumor growth in mice." International Journal of Cancer 103, no. 5 (December 19, 2002): 606–15. http://dx.doi.org/10.1002/ijc.10881.

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47

Pavithra, Lakshminarasimhan, Kadreppa Sreenath, Sandeep Singh, and Samit Chattopadhyay. "Heat-shock protein 70 binds to a novel sequence in 5′ UTR of tumor suppressor SMAR1 and regulates its mRNA stability upon Prostaglandin A2 treatment." FEBS Letters 584, no. 6 (February 11, 2010): 1187–92. http://dx.doi.org/10.1016/j.febslet.2010.02.025.

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Henderson, L. J., S. D. Narasipura, V. Adarichev, F. Kashanchi, and L. Al-Harthi. "Identification of Novel T Cell Factor 4 (TCF-4) Binding Sites on the HIV Long Terminal Repeat Which Associate with TCF-4, -Catenin, and SMAR1 To Repress HIV Transcription." Journal of Virology 86, no. 17 (June 6, 2012): 9495–503. http://dx.doi.org/10.1128/jvi.00486-12.

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Li, Tongtao, Kwok Hoe Chan, Tianpeng Ding, Xiao-Qiao Wang, Yin Cheng, Chen Zhang, Wanheng Lu, Gamze Yilmaz, Cheng-Wei Qiu, and Ghim Wei Ho. "Dynamic thermal trapping enables cross-species smart nanoparticle swarms." Science Advances 7, no. 2 (January 2021): eabe3184. http://dx.doi.org/10.1126/sciadv.abe3184.

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Abstract:

Bioinspired nano/microswarm enables fascinating collective controllability beyond the abilities of the constituent individuals, yet almost invariably, the composed units are of single species. Advancing such swarm technologies poses a grand challenge in synchronous mass manipulation of multimaterials that hold different physiochemical identities. Here, we present a dynamic thermal trapping strategy using thermoresponsive-based magnetic smart nanoparticles as host species to reversibly trap and couple given nonmagnetic entities in aqueous surroundings, enabling cross-species smart nanoparticle swarms (SMARS). Such trapping process endows unaddressable nonmagnetic species with efficient thermo-switchable magnetic response, which determines SMARS’ cross-species synchronized maneuverability. Benefiting from collective merits of hybrid components, SMARS can be configured into specific smart modules spanning from chain, vesicle, droplet, to ionic module, which can implement localized or distributed functions that are single-species unachievable. Our methodology allows dynamic multimaterials integration despite the odds of their intrinsic identities to conceive distinctive structures and functions.

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Atin, Sufa, Hanhan Maulana, Irawan Afrianto, Dedeng Hirawan, Richi Dwi Agustia, Alif Finandhita, and Irfan Dwiguna Saputra. "Pelatihan dan Penerapan IoT Smart Farming Hidroponik Guna Mendukung Mata Pelajaran Prakarya dan Kewirausahaan (PKWU) di SMAN 1 Majalaya." Dinamisia : Jurnal Pengabdian Kepada Masyarakat 7, no. 2 (April 29, 2023): 342–53. http://dx.doi.org/10.31849/dinamisia.v7i2.12570.

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Abstract:

Pengembangan bahan ajar dengan bantuan TIK merupakan hal yang menjadi kebutuhan saat ini. Hal ini disebabkan TIK mampu memberikan konten yang lebih kaya, serta mampu menarik minat dan motivasi siswa dalam mengikuti mata pelajaran tersebut. Tujuan dari kegiatan pengabdian ini adalah untuk meningkatkan softskill dan hardskill dari para guru di SMAN1 Majalaya agar dapat mengembangkan bahan ajar mata pelajaran PKWU dengan menerapan teknologi IoT smart farming didalamnya. IoT smart farming dipilih menjadi tema pengabdian dikarenakan sesuai dengan kebutuhan dan permasalahan yang ada di SMAN 1 Majalaya, dimana mekanisme kebun hidroponik yang digunakan saat ini masih bersifat konvesional dan ingin dikembangkan dengan bantuan IoT smart farming guna meningkatkan efektivitas dan efisiensi pengelolaannya. Tahapan kegiatan pengabdian ini mencakup pemberian materi konsep IoT, kunjungan ke laboratorium IoT Unikom, memberikan pelatihan perakitan kit IoT smart farming serta mengkonfigurasi aplikasi monitoring tanaman hidroponik, serta melakuan evaluasi berdasar kuesioner yang dibagikan kepada peserta pelatihan guna mendapat respon kegiatan. Berdasarkan hasil kuesioner, diperoleh kesimpulan bahwa kegiatan ini telah berhasil dengan sangat baik dalam memberikan peningkatan softskill dan hardskill guru-guru SMAN1 Majalaya guna mengembangkan sistem IoT smart farming yang dapat diterapkan pada mata pelajaran PKWU.

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