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44 results on '"Venkateswaran, Niranjan"'

1. Tryptophan fuels MYC-dependent liver tumorigenesis through indole 3-pyruvate synthesis

Author

Venkateswaran, Niranjan, Garcia, Roy, Lafita-Navarro, M. Carmen, Hao, Yi-Heng, Perez-Castro, Lizbeth, Nogueira, Pedro A. S., Solmonson, Ashley, Mender, Ilgen, Kilgore, Jessica A., Fang, Shun, Brown, Isabella N., Li, Li, Parks, Emily, Lopes dos Santos, Igor, Bhaskar, Mahima, Kim, Jiwoong, Jia, Yuemeng, Lemoff, Andrew, Grishin, Nick V., Kinch, Lisa, Xu, Lin, Williams, Noelle S., Shay, Jerry W., DeBerardinis, Ralph J., Zhu, Hao, and Conacci-Sorrell, Maralice

Published
2024
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2. ZNF692 organizes a hub specialized in 40S ribosomal subunit maturation enhancing translation in rapidly proliferating cells

Author

Lafita-Navarro, M. Carmen, Hao, Yi-Heng, Jiang, Chunhui, Jang, Seoyeon, Chang, Tsung-Cheng, Brown, Isabella N., Venkateswaran, Niranjan, Maurais, Elizabeth, Stachera, Weronika, Zhang, Yanfeng, Mundy, Dorothy, Han, Jungsoo, Tran, Vanna M., Mettlen, Marcel, Xu, Lin, Woodruff, Jeffrey B., Grishin, Nick V., Kinch, Lisa, Mendell, Joshua T., Buszczak, Michael, and Conacci-Sorrell, Maralice

Published
2023
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3. Supplementary Table1 from Activating an Adaptive Immune Response with a Telomerase-Mediated Telomere Targeting Therapeutic in Hepatocellular Carcinoma

Author

Mender, Ilgen, primary, Siteni, Silvia, primary, Barron, Summer, primary, Flusche, Ann Marie, primary, Kubota, Naoto, primary, Yu, Chunhua, primary, Cornelius, Crystal, primary, Tedone, Enzo, primary, Maziveyi, Mazvita, primary, Grichuk, Anthony, primary, Venkateswaran, Niranjan, primary, Conacci-Sorrell, Maralice, primary, Hoshida, Yujin, primary, Kang, Rui, primary, Tang, Daolin, primary, Gryaznov, Sergei, primary, and Shay, Jerry W., primary

Published
2023
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4. Figure S1-S5 and Table S1 from Activating an Adaptive Immune Response with a Telomerase-Mediated Telomere Targeting Therapeutic in Hepatocellular Carcinoma

Author

Mender, Ilgen, primary, Siteni, Silvia, primary, Barron, Summer, primary, Flusche, Ann Marie, primary, Kubota, Naoto, primary, Yu, Chunhua, primary, Cornelius, Crystal, primary, Tedone, Enzo, primary, Maziveyi, Mazvita, primary, Grichuk, Anthony, primary, Venkateswaran, Niranjan, primary, Conacci-Sorrell, Maralice, primary, Hoshida, Yujin, primary, Kang, Rui, primary, Tang, Daolin, primary, Gryaznov, Sergei, primary, and Shay, Jerry W., primary

Published
2023
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5. Data from Activating an Adaptive Immune Response with a Telomerase-Mediated Telomere Targeting Therapeutic in Hepatocellular Carcinoma

Author

Mender, Ilgen, primary, Siteni, Silvia, primary, Barron, Summer, primary, Flusche, Ann Marie, primary, Kubota, Naoto, primary, Yu, Chunhua, primary, Cornelius, Crystal, primary, Tedone, Enzo, primary, Maziveyi, Mazvita, primary, Grichuk, Anthony, primary, Venkateswaran, Niranjan, primary, Conacci-Sorrell, Maralice, primary, Hoshida, Yujin, primary, Kang, Rui, primary, Tang, Daolin, primary, Gryaznov, Sergei, primary, and Shay, Jerry W., primary

Published
2023
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6. Figure S1-S5 from Activating an Adaptive Immune Response with a Telomerase-Mediated Telomere Targeting Therapeutic in Hepatocellular Carcinoma

Author

Mender, Ilgen, primary, Siteni, Silvia, primary, Barron, Summer, primary, Flusche, Ann Marie, primary, Kubota, Naoto, primary, Yu, Chunhua, primary, Cornelius, Crystal, primary, Tedone, Enzo, primary, Maziveyi, Mazvita, primary, Grichuk, Anthony, primary, Venkateswaran, Niranjan, primary, Conacci-Sorrell, Maralice, primary, Hoshida, Yujin, primary, Kang, Rui, primary, Tang, Daolin, primary, Gryaznov, Sergei, primary, and Shay, Jerry W., primary

Published
2023
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7. Supplementary Table 1 from Activating an Adaptive Immune Response with a Telomerase-Mediated Telomere Targeting Therapeutic in Hepatocellular Carcinoma

Author

Mender, Ilgen, primary, Siteni, Silvia, primary, Barron, Summer, primary, Flusche, Ann Marie, primary, Kubota, Naoto, primary, Yu, Chunhua, primary, Cornelius, Crystal, primary, Tedone, Enzo, primary, Maziveyi, Mazvita, primary, Grichuk, Anthony, primary, Venkateswaran, Niranjan, primary, Conacci-Sorrell, Maralice, primary, Hoshida, Yujin, primary, Kang, Rui, primary, Tang, Daolin, primary, Gryaznov, Sergei, primary, and Shay, Jerry W., primary

Published
2023
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8. Fatty Acid Oxidation Mediated by Acyl-CoA Synthetase Long Chain 3 Is Required for Mutant KRAS Lung Tumorigenesis

Author

Padanad, Mahesh S., Konstantinidou, Georgia, Venkateswaran, Niranjan, Melegari, Margherita, Rindhe, Smita, Mitsche, Matthew, Yang, Chendong, Batten, Kimberly, Huffman, Kenneth E., Liu, Jingwen, Tang, Ximing, Rodriguez-Canales, Jaime, Kalhor, Neda, Shay, Jerry W., Minna, John D., McDonald, Jeffrey, Wistuba, Ignacio I., DeBerardinis, Ralph J., and Scaglioni, Pier Paolo

Published
2016
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9. Activating an Adaptive Immune Response with a Telomerase-mediated Telomere Targeting Therapeutic in Hepatocellular Carcinoma

Author

Mender, Ilgen, primary, Siteni, Silvia, additional, Barron, Summer, additional, Flusche, Ann Marie, additional, Kubota, Naoto, additional, Yu, Chunhua, additional, Cornelius, Crystal, additional, Tedone, Enzo, additional, Maziveyi, Mazvita, additional, Grichuk, Anthony, additional, Venkateswaran, Niranjan, additional, Conacci Sorrell, Maralice, additional, Hoshida, Yujin, additional, Kang, Rui, additional, Tang, Daolin, additional, Gryaznov, Sergei, additional, and Shay, Jerry W., additional

Published
2023
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23. Supplementary Table 2 and 3 from Focal Adhesion Kinase Regulates the DNA Damage Response and Its Inhibition Radiosensitizes Mutant KRAS Lung Cancer

Author

Tang, Ke-Jing, primary, Constanzo, Jerfiz D., primary, Venkateswaran, Niranjan, primary, Melegari, Margherita, primary, Ilcheva, Mariya, primary, Morales, Julio C., primary, Skoulidis, Ferdinandos, primary, Heymach, John V., primary, Boothman, David A., primary, and Scaglioni, Pier Paolo, primary

Published
2023
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27. The AHR target gene scinderin activates the WNT pathway by facilitating the nuclear translocation of β-catenin

Author

Perez-Castro, Lizbeth, primary, Venkateswaran, Niranjan, additional, Garcia, Roy, additional, Hao, Yi-Heng, additional, Lafita-Navarro, M. C., additional, Kim, Jiwoong, additional, Segal, Dagan, additional, Saponzik, Etai, additional, Chang, Bo-Jui, additional, Fiolka, Reto, additional, Danuser, Gaudenz, additional, Xu, Lin, additional, Brabletz, Thomas, additional, and Conacci-Sorrell, Maralice, additional

Published
2022
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29. Tryptophan and its metabolites in normal physiology and cancer etiology.

Author

Perez‐Castro, Lizbeth, Garcia, Roy, Venkateswaran, Niranjan, Barnes, Spencer, and Conacci‐Sorrell, Maralice

Subjects
ETIOLOGY of cancer, METABOLITES, ARYL hydrocarbon receptors, TRYPTOPHAN, TRP channels, PHYSIOLOGY, AMINO acid metabolism
Abstract

Within the growing field of amino acid metabolism, tryptophan (Trp) catabolism is an area of increasing interest. Trp is essential for protein synthesis, and its metabolism gives rise to biologically active catabolites including serotonin and numerous metabolites in the kynurenine (Kyn) pathway. In normal tissues, the production of Trp metabolites is directly regulated by the tissue‐specific expression of Trp‐metabolizing enzymes. Alterations of these enzymes in cancers can shift the balance and lead to an increased production of specific byproducts that can function as oncometabolites. For example, increased expression of the enzyme indoleamine 2,3‐dioxygenase, which converts Trp into Kyn, leads to an increase in Kyn levels in numerous cancers. Kyn functions as an oncometabolite in cancer cells by promoting the activity of the transcription factor aryl hydrocarbon receptor, which regulates progrowth genes. Moreover, Kyn also inhibits T‐cell activity and thus allows cancer cells to evade clearance by the immune system. Therefore, targeting the Kyn pathway has become a therapeutic focus as a novel means to abrogate tumor growth and immune resistance. This review summarizes the biological role and regulation of Trp metabolism and its catabolites with an emphasis on tumor cell growth and immune evasion and outlines areas for future research focus. [ABSTRACT FROM AUTHOR]

Published
2023
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30. The AHR target gene scinderin activates the WNT pathway by facilitating the nuclear translocation of _-catenin.

Author

Perez-Castro, Lizbeth, Venkateswaran, Niranjan, Garcia, Roy, Yi-Heng Hao, Lafita-Navarro, M. C., Jiwoong Kim, Dagan Segal, Saponzik, Etai, Bo-Jui Chang, Fiolka, Reto, Danuser, Gaudenz, Lin Xu, Brabletz, Thomas, and Conacci-Sorrell, Maralice

Subjects
*ARYL hydrocarbon receptors, *WNT signal transduction, *COLON cancer, *TRANSCRIPTION factors, *CYTOSKELETON, *CELL proliferation
Abstract

The ligand-activated transcription factor aryl hydrocarbon receptor (AHR) regulates cellular detoxification, proliferation and immune evasion in a range of cell types and tissues, including cancer cells. In this study, we used RNA-sequencing to identify the signature of the AHR target genes regulated by the pollutant 2,3,7,8-tetrachlorodibenzodioxin (TCDD) and the endogenous ligand kynurenine (Kyn), a tryptophan-derived metabolite. This approach identified a signature of six genes (CYP1A1, ALDH1A3, ABCG2, ADGRF1 and SCIN) as commonly activated by endogenous or exogenous ligands of AHR in multiple colon cancer cell lines. Among these, the actin-severing protein scinderin (SCIN) was necessary for cell proliferation; SCIN downregulation limited cell proliferation and its expression increased it. SCIN expression was elevated in a subset of colon cancer patient samples, which also contained elevated ß-catenin levels. Remarkably, SCIN expression promoted nuclear translocation of ß-catenin and activates the WNT pathway. Our study identifies a new mechanism for adhesion-mediated signaling in which SCIN, likely via its ability to alter the actin cytoskeleton, facilitates the nuclear translocation of ß-catenin. [ABSTRACT FROM AUTHOR]

Published
2022
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31. Inhibition of the de novo pyrimidine biosynthesis pathway limits ribosomal RNA transcription causing nucleolar stress in glioblastoma cells

Author

Lafita-Navarro, M. Carmen, primary, Venkateswaran, Niranjan, additional, Kilgore, Jessica A., additional, Kanji, Suman, additional, Han, Jungsoo, additional, Barnes, Spencer, additional, Williams, Noelle S., additional, Buszczak, Michael, additional, Burma, Sandeep, additional, and Conacci-Sorrell, Maralice, additional

Published
2020
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32. XPO1-dependent nuclear export is a druggable vulnerability in KRAS-mutant lung cancer

Author

Kim, Jimi, McMillan, Elizabeth, Kim, Hyun Seok, Venkateswaran, Niranjan, Makkar, Gurbani, Rodriguez-Canales, Jaime, Villalobos, Pamela, Neggers, Jasper Edgar, Mendiratta, Saurabh, Wei, Shuguang, Landesman, Yosef, Senapedis, William, Baloglu, Erkan, Chow, Chi-Wan B., Frink, Robin E., Gao, Boning, Roth, Michael, Minna, John D., Daelemans, Dirk, Wistuba, Ignacio I., Posner, Bruce A., Scaglioni, Pier Paolo, and White, Michael A.

Subjects
Lung cancer -- Care and treatment -- Genetic aspects, Gene mutation -- Health aspects, GTPases -- Health aspects -- Genetic aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): Jimi Kim [1]; Elizabeth McMillan [1]; Hyun Seok Kim [2]; Niranjan Venkateswaran [3]; Gurbani Makkar [1]; Jaime Rodriguez-Canales [4]; Pamela Villalobos [4]; Jasper Edgar Neggers [5]; Saurabh Mendiratta [1]; [...]

Published
2016
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34. MYC promotes tryptophan uptake and metabolism by the kynurenine pathway in colon cancer

Author

Venkateswaran, Niranjan, primary, Lafita-Navarro, M. Carmen, additional, Hao, Yi-Heng, additional, Kilgore, Jessica A., additional, Perez-Castro, Lizbeth, additional, Braverman, Jonathan, additional, Borenstein-Auerbach, Nofit, additional, Kim, Min, additional, Lesner, Nicholas P., additional, Mishra, Prashant, additional, Brabletz, Thomas, additional, Shay, Jerry W., additional, DeBerardinis, Ralph J., additional, Williams, Noelle S., additional, Yilmaz, Omer H., additional, and Conacci-Sorrell, Maralice, additional

Published
2019
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35. MYC leads the way.

Author

Venkateswaran, Niranjan and Conacci-Sorrell, Maralice

Subjects
*MYC oncogenes, *MYC proteins, *CANCER invasiveness, *CELL proliferation, *TRANSCRIPTION factors, *ONCOGENES
Abstract

Members of the MYC family of proto-oncogenes are the most commonly deregulated genes in all human cancers. MYC proteins drive an increase in cellular proliferation and facilitate multiple aspects of tumor initiation and progression, thereby controlling all hallmarks of cancer. MYC's ability to drive metabolic reprogramming of tumor cells leading to biomass accumulation and cellular proliferation is the most studied function of these oncogenes. MYC also regulates tumor progression and is often implicated in resistance to chemotherapy and in metastasis. While most oncogenic functions of MYC are attributed to its role as a transcription factor, more recently, new roles of MYC as a pro-survival factor in the cytoplasm suggest a previously unappreciated diversity in MYC's roles in cancer progression. This review will focus on the role of MYC in invasion and will discuss the canonical functions of MYC in Epithelial to Mesenchymal Transition and the cytoplasmic functions of MYC-nick in collective migration [ABSTRACT FROM AUTHOR]

Published
2020
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40. Abstract B22: Acyl-CoA synthetase long-chain family member 3 dependent lipid homeostasis is required for mutant KRAS driven lung cancer

Author

Padanad, Mahesh S., primary, Konstantinidou, Georgia, additional, Yang, Chendong, additional, Melegari, Margherita, additional, Venkateswaran, Niranjan, additional, Batten, Kimberly, additional, Huffman, Kenneth E., additional, Shay, Jerry W., additional, Minna, John D., additional, DeBerardinis, Ralph J., additional, and Scaglioni, Pier P., additional

Published
2016
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42. Fatty Acid Oxidation Mediated by Acyl-CoA Synthetase Long Chain 3 Is Required for Mutant KRASLung Tumorigenesis

Author

Padanad, Mahesh S., Konstantinidou, Georgia, Venkateswaran, Niranjan, Melegari, Margherita, Rindhe, Smita, Mitsche, Matthew, Yang, Chendong, Batten, Kimberly, Huffman, Kenneth E., Liu, Jingwen, Tang, Ximing, Rodriguez-Canales, Jaime, Kalhor, Neda, Shay, Jerry W., Minna, John D., McDonald, Jeffrey, Wistuba, Ignacio I., DeBerardinis, Ralph J., and Scaglioni, Pier Paolo

Abstract

KRASis one of the most commonly mutated oncogenes in human cancer. Mutant KRASaberrantly regulates metabolic networks. However, the contribution of cellular metabolism to mutant KRAS tumorigenesis is not completely understood. We report that mutant KRASregulates intracellular fatty acid metabolism through Acyl-coenzyme A(CoA) synthetase long-chain family member 3(ACSL3), which converts fatty acids into fatty Acyl-CoA esters, the substrates for lipid synthesis and β-oxidation. ACSL3suppression is associated with depletion of cellular ATP and causes the death of lung cancer cells. Furthermore, mutant KRAS promotes the cellular uptake, retention, accumulation, and β-oxidation of fatty acids in lung cancer cells in an ACSL3-dependent manner. Finally, ACSL3is essential for mutant KRASlung cancer tumorigenesis in vivo and is highly expressed in human lung cancer. Our data demonstrate that mutant KRAS reprograms lipid homeostasis, establishing a metabolic requirement that could be exploited for therapeutic gain.

Published
2016
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43. Diet-Induced Unresolved ER Stress Hinders KRAS-Driven Lung Tumorigenesis

Author

Biscotti, Tommasina, Luchetti, Michele, Ramadori, Giorgio, Konstantinidou, Georgia, Venkateswaran, Niranjan, Santinelli, Alfredo, Galié, Mirco, Williams, Noelle S., Coppari, Roberto, Scaglioni, Pier Paolo, and Morlock, Lorraine

Subjects
610 Medicine & health, 3. Good health

44. Anchorage-independent cell proliferation promoted by fascin's F-actin bundling.

Author

Isogai T, Murali VS, Zhou F, Wang X, Rajendran D, Perez-Castro L, Venkateswaran N, Conacci-Sorrell M, and Danuser G

Abstract

The actin filament (F-actin) bundling protein fascin-1 is highly enriched in many metastatic cancers. Fascin's contribution to metastasis have been ascribed to its enhancement of cell migration and invasion. However, mouse genetic studies clearly point to functions also in tumorigenesis, yet without mechanistic underpinnings. Here, we show that fascin expression promotes the formation of a non-canonical signaling complex that enables anchorage-independent proliferation. This complex shares similarities to focal adhesions and we refer to them as pseudo-adhesion signaling scaffolds (PASS). PASS are enriched with tyrosine phosphorylated proteins and require fascin's F-actin-bundling activity for its assembly. PASS serve as hubs for the Rac1/PAK/JNK proliferation signaling axis, driven by PASS-associated Rac-specific GEFs. Experimental disruption of either fascin or RacGEF function abrogates sustained proliferation of aggressive cancers in vitro and in vivo . These results add a new molecular element to the growing arsenal of metabolic and oncogenic signaling programs regulated by the cytoskeleton architecture.

Published
2024
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