{"id":363,"date":"2020-07-09T16:51:59","date_gmt":"2020-07-09T16:51:59","guid":{"rendered":"http:\/\/sites.rutgers.edu\/jacinto-lab\/?page_id=363"},"modified":"2025-06-27T15:15:51","modified_gmt":"2025-06-27T15:15:51","slug":"publications","status":"publish","type":"page","link":"https:\/\/sites.rutgers.edu\/jacinto-lab\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"<p>&nbsp;<\/p>\n<p>Jacinto, E. Making sense of fat in cancer, <b>Science 2025<\/b>; 387(6739): 1147-1148. PMID: 40080596.<\/p>\n<p>Werlen, G., Hernandez, T. and <strong>Jacinto, E.<\/strong> Food for thought: Nutrient metabolism controlling early T cell development. <a href=\"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/bies.202400179\"><strong>Bioessays 2024<\/strong><\/a> PMID: 39504233<\/p>\n<p>Chi, O.Z., Liu, X., Fortus, H., Werlen, G.,<b>Jacinto, E<\/b>., and Weiss, H.R. Inhibition of p70 ribosomal S6 kinase (S6K1) reduces cortical blood flow in a rat model of autism-tuberous sclerosis.<a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/pmid\/38570425\/\"><b>Neuromol. Med. 2024<\/b>, 4:26(1):10<\/a>, PMID: 3857042<\/p>\n<div><\/div>\n<p>Ragupathi, A., Kim, C., and <strong>Jacinto, E<\/strong>. The mTORC2 signaling network: targets and cross-talks, <a href=\"https:\/\/portlandpress.com\/biochemj\/article\/481\/2\/45\/233987\/The-mTORC2-signaling-network-targets-and-cross\"><strong>Biochem. J.<\/strong> 2024, 481: 45-91<\/a>. PMID: 38270460<\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E.<\/strong> mTOR takes charge: Relaying uncharged tRNA levels by mTOR ubiquitination, <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1550413123004175?via%3Dihub\"><strong>Cell Metab<\/strong> 2023, 35(12):2097-2099. PMID: 38056426<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Patel, N. and <strong>Jacinto, E<\/strong>. The mTOR complexes: Coordinating metabolism and translation, <a href=\"https:\/\/www.worldscientific.com\/doi\/10.1142\/9789811248665_0008\"><strong>RNA-based Mechanisms in Cancer<\/strong>, pp243-302 (2023<\/a>), World Scientific<\/p>\n<p>&nbsp;<\/p>\n<p>Paneque, A., Fortus, H., Zheng, J., Werlen, G., and <strong>Jacinto, E<\/strong>. The hexosamine biosynthesis pathway: regulation and function, <a href=\"https:\/\/www.mdpi.com\/2073-4425\/14\/4\/933\"><strong>Genes<\/strong> 2023, 14(4),933<\/a>.<\/p>\n<p>&nbsp;<\/p>\n<p>Werlen, G., Li, M.L., Tottone, L., da Silva-Diz, V., Su, X., Herranz, D., and <strong>Jacinto, E<\/strong>. Dietary glucosamine overcomes the defects in alpha\/beta-T cell ontogeny caused by the loss of de novo hexosamine biosynthesis, <a href=\"https:\/\/www.nature.com\/articles\/s41467-022-35014-w\"><strong>Nature Comm<\/strong>. 2022, 13, 7404<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Li, M.L., Ragupathi, A., Patel, N., Hernandez, T., Magsino, J., Werlen, G., Brewer, G. and <strong>Jacinto, E<\/strong>. The RNA-binding protein AUF1 facilitates Akt phosphorylation at the membrane. <a href=\"https:\/\/www.jbc.org\/article\/S0021-9258(22)00880-8\/fulltext\"><strong>J. Biol. Chem. 2022<\/strong> 298(10):102437. PMID: 36041631<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Werlen, G., Jain, R. and <strong>Jacinto, E<\/strong>. mTOR signaling and metabolism in early T cell development. <a href=\"https:\/\/www.mdpi.com\/2073-4425\/12\/5\/728\"><strong>Genes 2021<\/strong>, 12, 728<\/a>.<\/p>\n<p>&nbsp;<\/p>\n<p>Szwed, A., Kim, E. and <strong>Jacinto, E<\/strong>. Regulation and metabolic functions of mTORC1 and mTORC2.,<a href=\"https:\/\/journals.physiology.org\/doi\/full\/10.1152\/physrev.00026.2020?rfr_dat=cr_pub++0pubmed&amp;url_ver=Z39.88-2003&amp;rfr_id=ori%3Arid%3Acrossref.org\"> <strong>Physiol. Rev. 2021<\/strong>, 101(3):1371-1426 PMID: 33599151<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Chi, O.Z., Chiricolo, A. Liu, X., Patel, N., <strong>Jacinto E<\/strong>., and Weiss, H.R. Inhibition of serum and glucocorticoid regulated kinases by GSK650394 reduced infarct size in early cerebral ischemia-reperfusion with decreased BBB disruption. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/abs\/pii\/S0304394021005218?via%3Dihub\"><strong>Neurosci. Lett 2021<\/strong>, 762:136143, PMID: 34332027<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Chi, O.Z., Liu, X., Cofano, S., Patel, N., <strong>Jacinto, E.<\/strong>, and Weiss, H.R. Rapalink-1 increased infarct size in early cerebral ischemia-reperfusion with increased blood-brain barrier disruption. <a href=\"https:\/\/www.frontiersin.org\/articles\/10.3389\/fphys.2021.706528\/full\"><strong>Front. Phys. 2021<\/strong>, 12:706528, doi: 10.3389\/fphys.2021.706528.<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Ye, C., Liu, B., Lu, H., Liu, J., Rabson, A.B., <strong>Jacinto, E<\/strong>., Pestov, D.G., and Shen, Z. BCCIP is required for nucleolar recruitment of eIF6 and 12s pre-rRNA production during 60S ribosome biogenesis. <a href=\"https:\/\/academic.oup.com\/nar\/article\/48\/22\/12817\/6007667?login=false\"><strong>Nucleic Acids Res. 2020<\/strong>, 48(22):12817-12832 PMID: 33245766<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Chi, O.Z., Mellender, S.J., Kiss, G.K., Chiricolo, A., Liu, X., Patel, N., <strong>Jacinto, E<\/strong>., and Weiss, H.R. Lysophosphatidic acid increased infarct size in the early stage of cerebral ischemia-reperfusion with increased BBB permeability. <a href=\"https:\/\/www.strokejournal.org\/article\/S1052-3057(20)30447-X\/fulltext\"><strong>J. Stroke Cerebrovasc Dis. 2020<\/strong>, 29(10):105029 PMID: 32912542<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Chou, P.C., Rajput, S., Zhao, X., Patel, C., Albaciete, D., Oh, W.J., Daguplo, H.Q., Patel, N., Su,, B., Werlen, G., and <strong>Jacinto, E<\/strong>. mTORC2 is involved in the induction of RSK phosphorylation by serum or nutrient starvation. <a href=\"https:\/\/www.mdpi.com\/2073-4409\/9\/7\/1567\"><strong>Cells 2020<\/strong>, 9(7):E1567, PMID:32605013<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>La Manna, F., De Menna, M., Patel, N., Karkampouna, S., De Filippo, M., Klima, I., Kloen, P., Beimers, L., Thalmann, G.N., Pelger, R.C.M., <strong>Jacinto, E.,<\/strong> and Kruithof-de Julio, M. Dual mTOR inhibitor Rapalink-1 reduces prostate cancer patient-derived xenograft growth and alters tumor heterogeneity. <a href=\"https:\/\/www.frontiersin.org\/articles\/10.3389\/fonc.2020.01012\/full\"><strong>Front. Onc. 2020<\/strong>, 10:1012. PMID:32656088<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Cordover, E., Wei, J., Patel, C., Shen, N.L., Gionco, J., Sargsyan, D., Wu, R., Cai, L., Kong, A.T., <strong>Jacinto, E<\/strong>, and Minden, A. KPT_9274, an inhibitor of PAK4 and NAMPT, leads to downregulation of mTORC2 in triple negative breast cancer cells. <a href=\"https:\/\/pubs.acs.org\/doi\/10.1021\/acs.chemrestox.9b00376\"><strong>Chem. Res. Toxicol. 2019<\/strong>, PMID: 31876149<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Magaway, C., Kim, E., and <strong>Jacinto, E.<\/strong> Targeting mTOR and metabolism in cancer:\u00a0 Lessons and Innovations<strong>. \u00a0<a href=\"https:\/\/www.mdpi.com\/2073-4409\/8\/12\/1584\">Cells<\/a><\/strong> <strong>2019<\/strong>, 8(12). Pii:E1584. PMID: 31817676<\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E.<\/strong>\u00a0 The young and the restless: Isolating the dynamic mammalian pre-ribosomes, <a href=\"https:\/\/www.jbc.org\/article\/S0021-9258(20)30180-0\/fulltext\"><strong>J. Biol. Chem<\/strong>., <strong>2019<\/strong>, 294(28): 10758-10759. PMID 31300590.<\/a><\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E<\/strong>.\u00a0 Amplifying mTORC2 signals through AMPK during energy stress., <a href=\"https:\/\/www.science.org\/doi\/10.1126\/scisignal.aax5855?url_ver=Z39.88-2003&amp;rfr_id=ori:rid:crossref.org&amp;rfr_dat=cr_pub%20%200pubmed\"><strong>Science Sig<\/strong>. <strong>2019<\/strong>, 12(585). PMID 31186374<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Chi, O.Z., Kiss, G.K., Mellender, S.J., Liu, X., Liu, S., <strong>Jacinto, E<\/strong>., and Weiss, H. Inhibition of p70 ribosomal S6 kinase (S6K1) by PF-4708671 decreased infarct size in early cerebral ischemia-reperfusion with decreased BBB permeability. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/abs\/pii\/S0014299919303140?via%3Dihub\"><strong>Eur. J. Pharmacol. 2019<\/strong>, 855:202-207. PMID:31063769<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Moloughney, J.G., Vega-Cotto, N.M., Liu, S., Patel, C., Kim, P.K., Wu, C., Albaciete, D., Magaway, C., Chang, A., Rajput, S., Su, X., Werlen, G., and <strong>Jacinto, E<\/strong>. mTORC2 modulates the amplitude and duration of GFAT1 Ser243 phosphorylation to maintain flux through the hexosamine pathway during starvation.\u00a0 <a href=\"https:\/\/www.jbc.org\/article\/S0021-9258(20)35111-5\/fulltext\"><strong>J. Biol Chem. 2018<\/strong>, 293(42): 16464-16478, PMID 30201609<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Weiss, H.R., Chi, O.Z., Kiss, G.K., Liu, X., Damito, S., and <strong>Jacinto E<\/strong>., Akt activation improves microregional oxygen supply\/consumption balance after cerebral ischemia-reperfusion. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/abs\/pii\/S0006899318300337?via%3Dihub\"><strong>Brain Res. 2018<\/strong> 1683:48-54. PMID 29371097<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Moloughney, J.G.*, Kim, P.K.*, Vega-Cotto, N.M.*, Wu, C., Zhang, S., Adlam, M., Lynch, T., Chou, P.C., Rabinowitz, J.D., Werlen, G. and <strong>Jacinto, E<\/strong>. mTORC2 responds to glutamine catabolite levels to modulate the hexosamine biosynthesis enzyme GFAT1. <a href=\"https:\/\/www.cell.com\/molecular-cell\/fulltext\/S1097-2765(16)30368-9?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS1097276516303689%3Fshowall%3Dtrue\"><strong>Molecular Cell 2016, <\/strong>63, 811-826. PMID:27570073<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Chi, O.Z., Barsoum, S., Vega-Cotto, N.M., <strong>Jacinto, E<\/strong>., Liu X., Mellender, S.J., and Weiss, H.R. Effects of rapamycin on cerebral oxygen supply and consumption during reperfusion after cerebral ischemia, <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC4881736\/\"><strong>Neuroscience 2016<\/strong> 316:321-7. PMID 26742793<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Tobias, I., Kaulich, M., Kim, P.K., Simon, N., <strong>Jacinto, E<\/strong>., Dowdy, S., King, C.C., and Newton, AC. Protein kinase C z exhibits constitutive phosphorylation and phosphatidylinositol-3,4,5-triphosphate-independent regulation, <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC4888060\/\"><strong>Biochem J 2016<\/strong>, 473(4):509-23.\u00a0 PMID: 26635352<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Lynch, T., Moloughney, J., and <strong>Jacinto, E<\/strong>. The mTOR complexes in cancer cell metabolism., in <a href=\"https:\/\/link.springer.com\/chapter\/10.1007\/978-3-319-34211-5_2\"><strong>PI3K-mTOR in cancer and cancer therapy 2016<\/strong>, Springer,\u00a0 p. 29-63, ed. B. Leyland Jones, P. De, N. Dey,.<\/a><\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E<\/strong>. and Werlen, G. mTOR: The mTOR complexes in T cell development and immunity, in <a href=\"https:\/\/link.springer.com\/referenceworkentry\/10.1007\/978-3-0348-0620-6_135-1\"><strong>Encyclopedia of Inflammatory Diseases 2015<\/strong>, ed. M.J. Parnham, Springer.<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Chi, O.Z., Wu, C.C., Liu, X., Rah, K.H., <strong>Jacinto, E<\/strong>., and Weiss, H.R., Restoration of cerebral oxygen consumption with rapamycin treatment in a rat model of autism-tuberous sclerosis, <a href=\"https:\/\/link.springer.com\/article\/10.1007\/s12017-015-8359-5\"><strong>Neuromolecular Medicine 2015<\/strong>, 17(3):305-13. PMID: 26048361<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Chou, P.C., Moloughney, J., Oh, W.J., Wu, C.C., Chen, P.H., Ruegg, M., Hall, M.N., <strong>Jacinto, E.*<\/strong> and Werlen, G.* mTORC2 modulates alpha\/beta T cell receptor processing and surface expression during thymocyte development., <a href=\"https:\/\/journals.aai.org\/jimmunol\/article\/193\/3\/1162\/108995\/Mammalian-Target-of-Rapamycin-Complex-2-Modulates\"><strong>J. Immunol. 2014<\/strong>,\u00a0 193, 1162-1170.\u00a0 PMID: 24981454<\/a> *co-corresponding authors<\/p>\n<p>&nbsp;<\/p>\n<p>DeStefano, M.A. and <strong>Jacinto, E<\/strong>. Regulation of insulin receptor substrate-1 by mTORC2. <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC4881742\/\"><strong>Biochem. Soc. Trans<\/strong>. <strong>2013<\/strong>;\u00a0 41, 896-901. PMID: 23142081<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Kim, S.J*., DeStefano, M.A.*, Oh, W.J., Wu, C., Vega-Cotto, N.M., Finlan, M., Liu, D., Su, B., and <strong>Jacinto, E<\/strong>. mTOR complex 2 regulates proper turnover of insulin receptor substrate-1 via the ubiquitin ligase Fbw8.\u00a0 <a href=\"https:\/\/www.cell.com\/molecular-cell\/fulltext\/S1097-2765(12)00852-0?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS1097276512008520%3Fshowall%3Dtrue\"><strong>Molecular Cell 2012; <\/strong>48, 875-887<strong>.\u00a0 <\/strong>PMID: 23142081<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Wu, C., Chou, P., and <strong>Jacinto, E<\/strong>.\u00a0 The target of rapamycin; structure and functions, in <a href=\"https:\/\/www.rwjms.rutgers.edu\/documents\/labs\/jacinto-lab\/InTechBookChapter2012.pdf\"><strong>Protein Kinases 2012<\/strong>, Intech Publishing, p1-40, ed. Xavier, G.<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Su, B., and <strong>Jacinto, E<\/strong>.\u00a0 mTOR signaling to the AGC kinases.\u00a0 <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC3223267\/\"><strong>Crit. Rev. in Biochem. and Molec. Biol. 2011<\/strong>, 46, 527-547.<\/a><\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E<\/strong>.\u00a0 TFEBulous control of traffic by mTOR.\u00a0 <a href=\"https:\/\/www.embopress.org\/doi\/full\/10.1038\/emboj.2011.258\"><strong>EMBO J<\/strong>. <strong>2011<\/strong>, 30, 3215-3216<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Oh, W., and <strong>Jacinto, E<\/strong>.\u00a0 mTOR complex 2 signaling and functions.\u00a0 <a href=\"https:\/\/www.tandfonline.com\/doi\/full\/10.4161\/cc.10.14.16586\"><strong>Cell Cycle 2011<\/strong>; 10, 1-12. PMID: 21670596<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Oh, W*., Wu, C.*, Kim, S.J., Facchinetti, V., Julien, L.A., Finlan, M., Roux, P.P., Su, B., and <strong>Jacinto, E<\/strong>. mTORC2 associates with ribosomes to promote cotranslational phosphorylation and stability of nascent Akt polypeptide. <a href=\"https:\/\/www.embopress.org\/doi\/full\/10.1038\/emboj.2010.271\"><strong>EMBO J. 2010<em>; <\/em><\/strong>29, 3939-3951. PMID: 21045808<\/a><\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E.<\/strong>\u00a0 AGC kinases in mTOR signaling.\u00a0 Ed. M. Hall and F. Tamanoi: <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1874604710270075?casa_token=8xKakE3Cm9oAAAAA:tLvAVCTAOBHiSCeOujrNRbXIWAjCkYLv1Uyd5NO777eUe7mQ1bIQ_5v2OyMy_0prDkN2NVkiAQ\"><strong>The Enzymes 2010<\/strong>; 27, 101-128. Burlington: Academic Press.\u00a0 PMID: 18215152<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Facchinetti, V., Ouyang, W., Wei, H., Soto, N., Lazorchak, A., Gould, C., Lowry, C., Newton, A.C., Mao, Y., Miao, R.Q., Sessa, W.C., Qin, J., Zhang, P., Su, B., and <strong>Jacinto, E.<\/strong> The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C. <a href=\"https:\/\/www.embopress.org\/doi\/full\/10.1038\/emboj.2008.120\"><strong>EMBO J 2008; <\/strong>27, 1932-1943. PMID: 18566586<\/a><\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E.<\/strong>, and Lorberg, A.\u00a0 TOR regulation of AGC kinases in yeast and mammals.\u00a0\u00a0<a href=\"https:\/\/www.rwjms.rutgers.edu\/documents\/labs\/jacinto-lab\/JacintoLorberg2008.pdf\"> <strong>Biochem. J. 2008;<\/strong> 410, 19-37.\u00a0 PMID:18215152<\/a><\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E.<\/strong>\u00a0 What controls TOR?\u00a0 <a href=\"https:\/\/iubmb.onlinelibrary.wiley.com\/doi\/10.1002\/iub.56\"><strong>IUBMB Life 2008;<\/strong> 60, 483-96.\u00a0 PMID: 18493947<\/a><\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E.<\/strong> *, Facchinetti*, V., Liu, D., Soto, N., Wei, S., Jung, S.Y., Huang, Q., Qin, J., and Su, B. SIN1\/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity. <a href=\"https:\/\/www.cell.com\/cell\/fulltext\/S0092-8674(06)01147-0?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS0092867406011470%3Fshowall%3Dtrue\"><strong>Cell 2006<\/strong>; 127, 125-137. PMID: 16962653<\/a><\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E.<\/strong> Phosphatase targets in TOR signaling.\u00a0 Ed. G. Moorhead, <a href=\"https:\/\/web.archive.org\/web\/20200321064031id_\/http:\/\/rwjms.rutgers.edu\/departments_institutes\/molecular_biochemistry\/faculty\/jacinto\/documents\/24_Jaci_323_334.pdf\"><strong>Methods Mol. Biol 2006;<\/strong> 365, 323-334.\u00a0 Humana Press Inc., Totowa, NJ.\u00a0 PMID: 17200572<\/a><\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E.*<\/strong>, Loewith, R.*, Schmidt, A., Lin, S., Ruegg, M., Hall, A., and Hall, M.N. Mammalian TOR complex 2 (mTORC2) controls the actin cytoskeleton and is rapamycin insensitive. <a href=\"https:\/\/www.nature.com\/articles\/ncb1183\"><strong>Nature Cell Biology 2004;<\/strong> 6, 1122-1128. \u00a0PMID: 15467718<\/a> *equal contribution<\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E.<\/strong>, and Hall, M.N.\u00a0 TOR signaling in bugs, brain, and brawn.\u00a0 <a href=\"https:\/\/www.nature.com\/articles\/nrm1018\"><strong>Nature Reviews (Mol. Cell. Biol.) 2003;<\/strong> 4, 117-126. PMID: 12563289<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Bonenfant, D., Schmelzle, T., <strong>Jacinto, E.<\/strong>, Crespo, J.L., Mini, T., Hall, M.N., and Jenoe, P. Quantitation of changes in site specific phosphorylation: a simple method based on stable isotope labelling and mass spectrometry.<a href=\"https:\/\/www.pnas.org\/doi\/10.1073\/pnas.232735599?url_ver=Z39.88-2003&amp;rfr_id=ori%3Arid%3Acrossref.org&amp;rfr_dat=cr_pub++0pubmed\"> <strong>Proc. Natl. Acad. Sci. 2003; <\/strong>100, 880-885. PMID: 12540831<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Loewith, R., <strong>Jacinto, E.<\/strong>, Wullschleger, S., Lorberg, A., Crespo, J.L., Bonenfant, D., Oppliger, W., Jenoe, P., and Hall, M.N. Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control. <a href=\"https:\/\/www.cell.com\/molecular-cell\/fulltext\/S1097-2765(02)00636-6?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS1097276502006366%3Fshowall%3Dtrue\"><strong>Molecular Cell 2002<\/strong>; 10, 457-468. PMID:12408816<\/a><\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E.<\/strong>, Guo, B., Arndt, K.T., Schmelzle, T., and Hall, M.N. TIP41 interacts with TAP42 and negatively regulates the TOR signaling pathway. <a href=\"https:\/\/www.cell.com\/molecular-cell\/fulltext\/S1097-2765(01)00386-0?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS1097276501003860%3Fshowall%3Dtrue\"><strong>Molecular Cell 2001; <\/strong>\u00a08, 1017-1026. PMID: 11741537<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Werlen, G., <strong>Jacinto, E.<\/strong>, Xia, Y., and Karin, M. Calcineurin preferentially synergizes with PKC-theta to activate JNK in T lymphocytes. <a href=\"https:\/\/www.embopress.org\/doi\/full\/10.1093\/emboj\/17.11.3101\"><strong>EMBO J 1998;<\/strong> 17, 3101-3111. PMID: 9606192<\/a><\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E.<\/strong>, Werlen, G., and Karin, M. Cooperation between Syk and Rac1 leads to synergistic JNK activation in T lymphocytes. <a href=\"https:\/\/www.cell.com\/immunity\/fulltext\/S1074-7613(00)80456-2?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS1074761300804562%3Fshowall%3Dtrue\"><strong>Immunity 1998; <\/strong>\u00a08, 31-41. PMID: 9462509<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Wu, Z., Wu, J., <strong>Jacinto, E.<\/strong>, and Karin, M. Molecular cloning and characterization of human JNKK2, a novel Jun N-terminal kinase (JNK)-specific kinase. <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC232596\/\"><strong>Mol. Cell. Biol 1997; <\/strong>\u00a017, 7407-7416. PMID: 9372971<\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Su, B., <strong>Jacinto, E.<\/strong>, Hibi, M., Kallunki, T., Karin, M., and Ben-Neriah, Y. JNK is involved in signal integration during costimulation of T lymphocytes. <a href=\"https:\/\/www.cell.com\/cell\/pdf\/0092-8674(94)90056-6.pdf?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2F0092867494900566%3Fshowall%3Dtrue\"><strong>Cell 1994;<\/strong> 77, 727-736. PMID: 8205621<\/a><\/p>\n<p>&nbsp;<\/p>\n<p><strong>Jacinto, E<\/strong>. Signal integration in T lymphocytes: The role of JNK and ERK. <a href=\"https:\/\/www.proquest.com\/docview\/304329304?pq-origsite=gscholar&amp;fromopenview=true\">Dissertation (UCSD) 1997<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"<p>&nbsp; Jacinto, E. Making sense of fat in cancer, Science 2025; 387(6739): 1147-1148. PMID: 40080596. Werlen, G., Hernandez, T. and Jacinto, E. Food for thought: Nutrient metabolism controlling early T &hellip; <a href=\"https:\/\/sites.rutgers.edu\/jacinto-lab\/publications\/\" class=\"\">Read More<\/a><\/p>\n","protected":false},"author":21,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"template-custom.php","meta":{"_acf_changed":false,"footnotes":""},"class_list":["post-363","page","type-page","status-publish","hentry"],"acf":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v23.5 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>Publications - Jacinto Lab<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/sites.rutgers.edu\/jacinto-lab\/publications\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Publications - Jacinto Lab\" \/>\n<meta property=\"og:description\" content=\"&nbsp; Jacinto, E. 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