Van de Velde, S., Yu, J., Garrett Evensen, K., Pakhlevanyan, E., Williams, A.E., Shaw, R.J., Montminy, M. Med14 phosphorylation shapes genomic response to GLP-1 agonists. (2026) Proceedings of the National Academy of Sciences of the United States of America. 123(10):e2536772123. DOI: 10.1073/pnas.2536772123

Layng, F.I.A.L., Ren, H., Bakas, N.A., Panickar, D.R., Lambert, L.J., Celeridad, M., Wu, J., De Backer, L., Chandrachud, P., Limpert, A.S., Vamos, M., Chaikuad, A., Verdugo, B.B., Hagan, P.M., Brun, S.N., Tautz, L., Knapp, S., Shaw, R.J., Salvesen, G.S., Sheffler, D.J., Cosford, N.D.P. Synthesis and Characterization of ULK1/2 Kinase Inhibitors That Inhibit Autophagy and Upregulate Expression of Major Histocompatibility Complex I for the Treatment of Non-Small Cell Lung Cancer. (2026) ACS Chemical Biology. DOI: 10.1021/acschembio.5c00711

Wessendorf-Rodriguez, K., Ruchhoeft, M.L., Murray, C.W., Huang, Y., Ashley, E.L., Galvez, H.M., McGregor, G.H., Kambhampati, S., Shaw, R.J., Metallo, C.M. Modeling lipid homeostasis using stable isotope tracing and flux analysis. (2026) Zellstoffwechsel. DOI: 10.1016/j.cmet.2026.01.020

Malik, N., Shaw, R.J. The AMPK Pathway: Molecular Rejuvenation of Metabolism and Mitochondria. (2025) Annual Review of Cell and Developmental Biology. DOI: 10.1146/annurev-cellbio-120420-094431

Dufresne, S., Kuna, R.S., Wong, K., Komarla, A., Rock, A., Rosada-Encarnación, J., Shen, C., Mondal, P., Parham, L.R., Layng, F.I., Peck, K.L., Fowler, A., Lowy, A.M., Engle, D., Tiriac, H., Shaw, R., Cosford, N., Metallo, C., Towers, C. Leveraging autophagy and pyrimidine metabolism to target pancreatic cancer. (2025) bioRxiv. DOI: 10.1101/2025.05.29.656904

Van de Velde, S., Yu, J., Evensen, K.G., Pakhlevanyan, E., Williams, A.E., Shaw, R.J., Montminy, M. Med14 phosphorylation shapes genomic response to GLP-1 Agonist. (2025) bioRxiv. DOI: 10.1101/2025.06.17.660196

Sainz, A.G., Rojas, G.R., Moyzis, A.G., Donnelly, M.P., Mangalhara, K.C., Johnson, M.A., Esparza-Moltó, P.B., Grae, K.J., Shaw, R.J., Shadel, G.S. FAM43A coordinates mtDNA replication and mitochondrial biogenesis in response to mtDNA depletion. (2025) Journal of Cell Biology. 224(3). DOI: 10.1083/jcb.202311082

McGuire, C.K., Meehan, A.S., Couser, E., Bull, L., Minor, A.C., Kuhlmann-Hogan, A., Kaech, S.M., Shaw, R.J., Eichner, L.J. Transcriptional repression by HDAC3 mediates T cell exclusion from mutant lung tumors. (2024) Proceedings of the National Academy of Sciences of the United States of America. 121(42):e2317694121. DOI: 10.1073/pnas.2317694121

Wessendorf-Rodriguez, K., Ruchhoeft, M.L., Ashley, E.L., Galvez, H.M., Murray, C.W., McGregor, G., Kambhampati, S., Shaw, R.J., Metallo, C.M. Modeling compound lipid homeostasis using stable isotope tracing. (2024) bioRxiv. DOI: 10.1101/2024.10.16.618599

Kuhlmann-Hogan, A., Cordes, T., Xu, Z., Kuna, R.S., Traina, K.A., Robles-Oteiza, C., Ayeni, D., Kwong, E.M., Levy, S., Globig, A.M., Nobari, M.M., Cheng, G.Z., Leibel, S.L., Homer, R.J., Shaw, R.J., Metallo, C.M., Politi, K., Kaech, S.M. EGFR-driven lung adenocarcinomas coopt alveolar macrophage metabolism and function to support EGFR signaling and growth. (2024) Cancer Discovery.:OF1-OF22 DOI: 10.1158/2159-8290.CD-23-0434

Zhang, T., Xu, D., Trefts, E., Lv, M., Inuzuka, H., Song, G., Liu, M., Lu, J., Liu, J., Chu, C., Wang, M., Wang, H., Meng, H., Liu, H., Zhuang, Y., Xie, X., Dang, F., Guan, D., Men, Y., Jiang, S., Jiang, C., Dai, X., Liu, J., Wang, Z., Yan, P., Wang, J., Tu, Z., Babuta, M., Erickson, E., Hillis, A.L., Dibble, C.C., Asara, J.M., Szabo, G., Sicinski, P., Miao, J., Lee, Y.R., Pan, L., Shaw, R.J., Yuan, J., Wei, W. Metabolic orchestration of cell death by AMPK-mediated phosphorylation of RIPK1. (2023) Wissenschaft. 380(6652):1372-1380. DOI: 10.1126/science.abn1725

Kuna, R.S., Kumar, A., Wessendorf-Rodriguez, K.A., Galvez, H., Green, C.R., McGregor, G.H., Cordes, T., Shaw, R.J., Svensson, R.U., Metallo, C.M. Inter-organelle cross-talk supports acetyl-coenzyme A homeostasis and lipogenesis under metabolic stress. (2023) Science Advances. 9(18):eadf0138. DOI: 10.1126/sciadv.adf0138

Malik, N., Ferreira, B.I., Hollstein, P.E., Curtis, S.D., Trefts, E., Weiser Novak, S., Yu, J., Gilson, R., Hellberg, K., Fang, L., Sheridan, A., Hah, N., Shadel, G.S., Manor, U., Shaw, R.J. Induction of lysosomal and mitochondrial biogenesis by AMPK phosphorylation of FNIP1. (2023) Wissenschaft. 380(6642):eabj5559. DOI: 10.1126/science.abj5559

Kuhlmann-Hogan, A., Cordes, T., Xu, Z., Traina, K.A., Robles-Oteíza, C., Ayeni, D., Kwong, E.M., Levy, S.R., Nobari, M., Cheng, G.Z., Shaw, R., Leibel, S.L., Metallo, C.M., Politi, K., Kaech, S.M. EGFR lung adenocarcinomas coopt alveolar macrophage metabolism and function to support EGFR signaling and growth. (2023) bioRxiv. DOI: 10.1101/2023.04.15.536974

Eichner, L.J., Curtis, S.D., Brun, S.N., McGuire, C.K., Gushterova, I., Baumgart, J.T., Trefts, E., Ross, D.S., Rymoff, T.J., Shaw, R.J. HDAC3 is critical in tumor development and therapeutic resistance in -mutant non-small cell lung cancer. (2023) Science Advances. 9(11):eadd3243. DOI: 10.1126/sciadv.add3243

Stein, B.D., Ferrarone, J.R., Gardner, E.E., Chang, J.W., Wu, D., Hollstein, P.E., Liang, R.J., Yuan, M., Chen, Q., Coukos, J.S., Sindelar, M., Ngo, B., Gross, S.S., Shaw, R.J., Zhang, C., Asara, J.M., Moellering, R.E., Varmus, H., Cantley, L.C. LKB1-dependent regulation of TPI1 creates a divergent metabolic liability between human and mouse lung adenocarcinoma. (2023) Cancer Discovery. DOI: 10.1158/2159-8290.CD-22-0805

Pariollaud, M., Ibrahim, L.H., Irizarry, E., Mello, R.M., Chan, A.B., Altman, B.J., Shaw, R.J., Bollong, M.J., Wiseman, R.L., Lamia, K.A. Circadian disruption enhances HSF1 signaling and tumorigenesis in -driven lung cancer. (2022) Science Advances. 8(39):eabo1123. DOI: 10.1126/sciadv.abo1123

Lee, A., Kondapalli, C., Virga, D.M., Lewis, T.L., Koo, S.Y., Ashok, A., Mairet-Coello, G., Herzig, S., Foretz, M., Viollet, B., Shaw, R., Sproul, A., Polleux, F. Aβ42 oligomers trigger synaptic loss through CAMKK2-AMPK-dependent effectors coordinating mitochondrial fission and mitophagy. (2022) Nature Communications. 13(1):4444. DOI: 10.1038/s41467-022-32130-5

Schmitt, D.L., Curtis, S.D., Lyons, A.C., Zhang, J.F., Chen, M., He, C.Y., Mehta, S., Shaw, R.J., Zhang, J. Spatial regulation of AMPK signaling revealed by a sensitive kinase activity reporter. (2022) Nature Communications. 13(1):3856. DOI: 10.1038/s41467-022-31190-x

Lerman, C., Hughes-Halbert, C., Falcone, M., Gosky, D.M., Jensen, R.A., Lee, K.P., Mitchell, E., Odunsi, K., Pegher, J.W., Rodriguez, E., Sanchez, Y., Shaw, R., Weiner, G., Willman, C.L. Leadership Diversity and Development in the Nation's Cancer Centers. (2022) J Natl Cancer Inst. DOI: 10.1093/jnci/djac121

Lim, E.W., Handzlik, M.K., Trefts, E., Gengatharan, J.M., Pondevida, C.M., Shaw, R.J., Metallo, C.M. Progressive alterations in amino acid and lipid metabolism correlate with peripheral neuropathy in mice. (2021) Science Advances. 7(42):eabj4077. DOI: 10.1126/sciadv.abj4077

Trefts, E., Shaw, R.J. AMPK: restoring metabolic homeostasis over space and time. (2021) Molecular Cell. 81(18):3677-3690. DOI: 10.1016/j.molcel.2021.08.015

Hung, C.M., Lombardo, P.S., Malik, N., Brun, S.N., Hellberg, K., Van Nostrand, J.L., Garcia, D., Baumgart, J., Diffenderfer, K., Asara, J.M., Shaw, R.J. AMPK/ULK1-mediated phosphorylation of Parkin ACT domain mediates an early step in mitophagy. (2021) Science Advances. 7(15). DOI: 10.1126/sciadv.abg4544

Lin, C., Blessing, A.M., Pulliam, T.L., Shi, Y., Wilkenfeld, S.R., Han, J.J., Murray, M.M., Pham, A.H., Duong, K., Brun, S.N., Shaw, R.J., Ittmann, M.M., Frigo, D.E. Inhibition of CAMKK2 impairs autophagy and castration-resistant prostate cancer via suppression of AMPK-ULK1 signaling. (2021) Oncogene. DOI: 10.1038/s41388-021-01658-z

Ren, H., Bakas, N.A., Vamos, M., Chaikuad, A., Limpert, A.S., Wimer, C.D., Brun, S.N., Lambert, L.J., Tautz, L., Celeridad, M., Sheffler, D.J., Knapp, S., Shaw, R.J., Cosford, N.D.P. Design, Synthesis, and Characterization of an Orally Active Dual-Specific ULK1/2 Autophagy Inhibitor that Synergizes with the PARP Inhibitor Olaparib for the Treatment of Triple-Negative Breast Cancer (2020) Journal of Medicinal Chemistry. DOI: 10.1021/acs.jmedchem.0c00873

Van Nostrand, J.L., Hellberg, K., Luo, E.C., Van Nostrand, E.L., Dayn, A., Yu, J., Shokhirev, M.N., Dayn, Y., Yeo, G.W., Shaw, R.J. AMPK regulation of Raptor and TSC2 mediate metformin effects on transcriptional control of anabolism and inflammation. (2020) Genes & Development. DOI: 10.1101/gad.339895.120

Yoon, H., Spinelli, J.B., Zaganjor, E., Wong, S.J., German, N.J., Randall, E.C., Dean, A., Clermont, A., Paulo, J.A., Garcia, D., Li, H., Rombold, O., Agar, N.Y.R., Goodyear, L.J., Shaw, R.J., Gygi, S.P., Auwerx, J., Haigis, M.C. PHD3 Loss Promotes Exercise Capacity and Fat Oxidation in Skeletal Muscle. (2020) Zellstoffwechsel. DOI: 10.1016/j.cmet.2020.06.017

Stein, B.D., Calzolari, D., Hellberg, K., Hu, Y.S., He, L., Hung, C.M., Toyama, E.Q., Ross, D.S., Lillemeier, B.F., Cantley, L.C., Yates, J.R., Shaw, R.J. Quantitative In Vivo Proteomics of Metformin Response in Liver Reveals AMPK-Dependent and -Independent Signaling Networks. (2019) Cell Reports. 29(10):3331-3348.e7. DOI: 10.1016/j.celrep.2019.10.117

Stein, B.D., Herzig, S., Martínez-Bartolomé, S., Lavallée-Adam, M., Shaw, R.J., Yates, J.R. Comparison of CRISPR Genomic Tagging for Affinity Purification and Endogenous Immunoprecipitation Coupled with Quantitative Mass Spectrometry To Identify the Dynamic AMPKα2 Interactome. (2019) Journal of Proteome Research. 18(10):3703-3714. DOI: 10.1021/acs.jproteome.9b00378

Hollstein, P.E., Eichner, L.J., Brun, S.N., Kamireddy, A., Svensson, R.U., Vera, L.I., Ross, D.S., Rymoff, T.J., Hutchins, A., Galvez, H.M., Williams, A.E., Shokhirev, M.N., Screaton, R.A., Berdeaux, R., Shaw, R.J. The AMPK-related kinases SIK1 and SIK3 mediate key tumor suppressive effects of LKB1 in NSCLC. (2019) Cancer Discovery. DOI: 10.1158/2159-8290.CD-18-1261

Rodón, L., Svensson, R.U., Wiater, E., Chun, M.G.H., Tsai, W.W., Eichner, L.J., Shaw, R.J., Montminy, M. The CREB coactivator CRTC2 promotes oncogenesis in LKB1-mutant non-small cell lung cancer. (2019) Science Advances. 5(7):eaaw6455. DOI: 10.1126/sciadv.aaw6455

Hishida, T., Vazquez-Ferrer, E., Hishida-Nozaki, Y., Sancho-Martinez, I., Takahashi, Y., Hatanaka, F., Wu, J., Ocampo, A., Reddy, P., Wu, M.Z., Gerken, L., Shaw, R.J., Rodriguez Esteban, C., Benner, C., Nakagawa, H., Guillen Garcia, P., Nuñez Delicado, E., Castells, A., Campistol, J.M., Liu, G.H., Izpisua Belmonte, J.C. Mutations in foregut SOX2 cells induce efficient proliferation via CXCR2 pathway. (2019) Protein & Cell. 10(7):485-495. DOI: 10.1007/s13238-019-0630-3

Nassour, J., Radford, R., Correia, A., Fusté, J.M., Schoell, B., Jauch, A., Shaw, R.J., Karlseder, J. Autophagic cell death restricts chromosomal instability during replicative crisis. (2019) Natur. 565(7741):659-663. DOI: 10.1038/s41586-019-0885-0

Garcia, D., Hellberg, K., Chaix, A., Wallace, M., Herzig, S., Badur, M.G., Lin, T., Shokhirev, M.N., Pinto, A.F.M., Ross, D.S., Saghatelian, A., Panda, S., Dow, L.E., Metallo, C.M., Shaw, R.J. Genetic Liver-Specific AMPK Activation Protects against Diet-Induced Obesity and NAFLD. (2019) Cell Reports. 26(1):192-208.e6. DOI: 10.1016/j.celrep.2018.12.036

Limpert, A.S., Lambert, L.J., Bakas, N.A., Bata, N., Brun, S.N., Shaw, R.J., Cosford, N.D.P. Autophagy in Cancer: Regulation by Small Molecules. (2018) Trends in Pharmacological Sciences. 39(12):1021-1032. DOI: 10.1016/j.tips.2018.10.004

Eichner, L.J., Brun, S.N., Herzig, S., Young, N.P., Curtis, S.D., Shackelford, D.B., Shokhirev, M.N., Leblanc, M., Vera, L.I., Hutchins, A., Ross, D.S., Shaw, R.J., Svensson, R.U. Genetic Analysis Reveals AMPK Is Required to Support Tumor Growth in Murine Kras-Dependent Lung Cancer Models. (2018) Zellstoffwechsel. 29(2):285-302. DOI: 10.1016/j.cmet.2018.10.005

Lewis, T.L., Kwon, S.K., Lee, A., Shaw, R., Polleux, F. MFF-dependent mitochondrial fission regulates presynaptic release and axon branching by limiting axonal mitochondria size. (2018) Nature Communications. 9(1):5008. DOI: 10.1038/s41467-018-07416-2

Fiedler, E.C., Shaw, R.J. AMPK Regulates the Epigenome through Phosphorylation of TET2. (2018) Zellstoffwechsel. 28(4):534-536. DOI: 10.1016/j.cmet.2018.09.015

Hollstein, P.E., Shaw, R.J. Inflamed T cells and stroma drive gut tumors. (2018) Wissenschaft. 361(6400):332-333. DOI: 10.1126/science.aau4804

Hollstein, P.E., Shaw, R.J. GNAS shifts metabolism in pancreatic cancer. (2018) Nature Cell Biology. 20(7):740-741. DOI: 10.1038/s41556-018-0120-5

Herzig, S., Shaw, R.J. AMPK: guardian of metabolism and mitochondrial homeostasis. (2017) Nature Reviews Molecular Cell Biology. 19(2):121-135. DOI: 10.1038/nrm.2017.95

Parker, S.J., Svensson, R.U., Divakaruni, A.S., Lefebvre, A.E., Murphy, A.N., Shaw, R.J., Metallo, C.M. LKB1 promotes metabolic flexibility in response to energy stress. (2017) Metab Eng. 43(Pt B):208-217. DOI: 10.1016/j.ymben.2016.12.010

Bar-Peled, L., Kemper, E.K., Suciu, R.M., Vinogradova, E.V., Backus, K.M., Horning, B.D., Paul, T.A., Ichu, T.A., Svensson, R.U., Olucha, J., Chang, M.W., Kok, B.P., Zhu, Z., Ihle, N.T., Dix, M.M., Jiang, P., Hayward, M.M., Saez, E., Shaw, R.J., Cravatt, B.F. Chemical Proteomics Identifies Druggable Vulnerabilities in a Genetically Defined Cancer. (2017) Cell. 171(3):696-709. DOI: 10.1016/j.cell.2017.08.051

Garcia, D., Shaw, R.J. AMPK: Mechanisms of Cellular Energy Sensing and Restoration of Metabolic Balance. (2017) Molecular Cell. 66(6):789-800. DOI: 10.1016/j.molcel.2017.05.032

Ruggero, D., Shaw, R.J. Editorial overview: Cell regulation: 1000 Flavors including chocolate and chili peppers. (2017) Current Opinion in Cell Biology. 45:iv-vi. DOI: 10.1016/j.ceb.2017.05.008

Howell, J.J., Hellberg, K., Turner, M., Talbott, G., Kolar, M.J., Ross, D.S., Hoxhaj, G., Saghatelian, A., Shaw, R.J., Manning, B.D. Metformin Inhibits Hepatic mTORC1 Signaling via Dose-Dependent Mechanisms Involving AMPK and the TSC Complex. (2017) Zellstoffwechsel. 25(2):463-471. DOI: 10.1016/j.cmet.2016.12.009

Svensson, R.U., Shaw, R.J. Lipid Synthesis Is a Metabolic Liability of Non-Small Cell Lung Cancer. (2016) Cold Spring Harbor Symposia on Quantitative Biology. 81:93-103. DOI: 10.1101/sqb.2016.81.030874

Svensson, R.U., Parker, S.J., Eichner, L.J., Kolar, M.J., Wallace, M., Brun, S.N., Lombardo, P.S., Van Nostrand, J.L., Hutchins, A., Vera, L., Gerken, L., Greenwood, J., Bhat, S., Harriman, G., Westlin, W.F., Harwood, H.J., Saghatelian, A., Kapeller, R., Metallo, C.M., Shaw, R.J. Inhibition of acetyl-CoA carboxylase suppresses fatty acid synthesis and tumor growth of non-small-cell lung cancer in preclinical models. (2016) Nature Medicine. 22(10):1108-1119. DOI: 10.1038/nm.4181

Merkwirth, C., Jovaisaite, V., Durieux, J., Matilainen, O., Jordan, S.D., Quiros, P.M., Steffen, K.K., Williams, E.G., Mouchiroud, L., Tronnes, S.U., Murillo, V., Wolff, S.C., Shaw, R.J., Auwerx, J., Dillin, A. Two Conserved Histone Demethylases Regulate Mitochondrial Stress-Induced Longevity. (2016) Cell. 165(5):1209-23. DOI: 10.1016/j.cell.2016.04.012

Young, N.P., Kamireddy, A., Van Nostrand, J.L., Eichner, L.J., Shokhirev, M.N., Dayn, Y., Shaw, R.J. AMPK governs lineage specification through Tfeb-dependent regulation of lysosomes. (2016) Genes & Development. 30(5):535-52. DOI: 10.1101/gad.274142.115

Toyama, E.Q., Herzig, S., Courchet, J., Lewis, T.L., Losón, O.C., Hellberg, K., Young, N.P., Chen, H., Polleux, F., Chan, D.C., Shaw, R.J. Metabolism. AMP-activated protein kinase mediates mitochondrial fission in response to energy stress. (2016) Wissenschaft. 351(6270):275-281. DOI: 10.1126/science.aab4138

Shaw, R.J. AMPK Keeps Tumor Cells from Starving to Death. (2015) Cell Stem Cell. 17(5):503-4. DOI: 10.1016/j.stem.2015.10.007

Schaffer, B.E., Levin, R.S., Hertz, N.T., Maures, T.J., Schoof, M.L., Hollstein, P.E., Benayoun, B.A., Banko, M.R., Shaw, R.J., Shokat, K.M., Brunet, A. Identification of AMPK Phosphorylation Sites Reveals a Network of Proteins Involved in Cell Invasion and Facilitates Large-Scale Substrate Prediction. (2015) Zellstoffwechsel. 22(5):907-21. DOI: 10.1016/j.cmet.2015.09.009

McClatchy, D.B., Ma, Y., Liu, C., Stein, B.D., Martínez-Bartolomé, S., Vasquez, D., Hellberg, K., Shaw, R.J., Yates, J.R. Pulsed Azidohomoalanine Labeling in Mammals (PALM) Detects Changes in Liver-Specific LKB1 Knockout Mice. (2015) Journal of Proteome Research. 14(11):4815-22. DOI: 10.1021/acs.jproteome.5b00653

Egan, D.F., Chun, M.G., Vamos, M., Zou, H., Rong, J., Miller, C.J., Lou, H.J., Raveendra-Panickar, D., Yang, C.C., Sheffler, D.J., Teriete, P., Asara, J.M., Turk, B.E., Cosford, N.D., Shaw, R.J. Small Molecule Inhibition of the Autophagy Kinase ULK1 and Identification of ULK1 Substrates. (2015) Molecular Cell. 59(2):285-97. DOI: 10.1016/j.molcel.2015.05.031

Shaw, R.J. Tumor Metabolism: MAGE-A Proteins Help TRIM Turn Over AMPK. (2015) Current Biology. 25(10):R418-20. DOI: 10.1016/j.cub.2015.03.019

Xia, Y., Yeddula, N., Leblanc, M., Ke, E., Zhang, Y., Oldfield, E., Shaw, R.J., Verma, I.M. Reduced cell proliferation by IKK2 depletion in a mouse lung-cancer model. (2015) Nature Cell Biology. 17(4):532. DOI: 10.1038/ncb3145

Goodwin, J.M., Svensson, R.U., Lou, H.J., Winslow, M.M., Turk, B.E., Shaw, R.J. An AMPK-independent signaling pathway downstream of the LKB1 tumor suppressor controls Snail1 and metastatic potential. (2014) Molecular Cell. 55(3):436-50. DOI: 10.1016/j.molcel.2014.06.021

Mouchiroud, L., Eichner, L.J., Shaw, R.J., Auwerx, J. Transcriptional coregulators: fine-tuning metabolism. (2014) Zellstoffwechsel. 20(1):26-40. DOI: 10.1016/j.cmet.2014.03.027

Luan, B., Goodarzi, M.O., Phillips, N.G., Guo, X., Chen, Y.D., Yao, J., Allison, M., Rotter, J.I., Shaw, R., Montminy, M. Leptin-mediated increases in catecholamine signaling reduce adipose tissue inflammation via activation of macrophage HDAC4. (2014) Zellstoffwechsel. 19(6):1058-65. DOI: 10.1016/j.cmet.2014.03.024

Faubert, B., Vincent, E.E., Griss, T., Samborska, B., Izreig, S., Svensson, R.U., Mamer, O.A., Avizonis, D., Shackelford, D.B., Shaw, R.J., Jones, R.G. Loss of the tumor suppressor LKB1 promotes metabolic reprogramming of cancer cells via HIF-1α. (2014) Proceedings of the National Academy of Sciences of the United States of America. 111(7):2554-9. DOI: 10.1073/pnas.1312570111

Shaw, R.J. Metformin trims fats to restore insulin sensitivity. (2013) Nature Medicine. 19(12):1570-2. DOI: 10.1038/nm.3414

Masui, K., Tanaka, K., Akhavan, D., Babic, I., Gini, B., Matsutani, T., Iwanami, A., Liu, F., Villa, G.R., Gu, Y., Campos, C., Zhu, S., Yang, H., Yong, W.H., Cloughesy, T.F., Mellinghoff, I.K., Cavenee, W.K., Shaw, R.J., Mischel, P.S. mTOR complex 2 controls glycolytic metabolism in glioblastoma through FoxO acetylation and upregulation of c-Myc. (2013) Zellstoffwechsel. 18(5):726-39. DOI: 10.1016/j.cmet.2013.09.013

Liu, Y., Marks, K., Cowley, G.S., Carretero, J., Liu, Q., Nieland, T.J., Xu, C., Cohoon, T.J., Gao, P., Zhang, Y., Chen, Z., Altabef, A.B., Tchaicha, J.H., Wang, X., Choe, S., Driggers, E.M., Zhang, J., Bailey, S.T., Sharpless, N.E., Hayes, D.N., Patel, N.M., Janne, P.A., Bardeesy, N., Engelman, J.A., Manning, B.D., Shaw, R.J., Asara, J.M., Scully, R., Kimmelman, A., Byers, L.A., Gibbons, D.L., Wistuba, I.I., Heymach, J.V., Kwiatkowski, D.J., Kim, W.Y., Kung, A.L., Gray, N.S., Root, D.E., Cantley, L.C., Wong, K.K. Metabolic and functional genomic studies identify deoxythymidylate kinase as a target in LKB1-mutant lung cancer. (2013) Cancer Discovery. 3(8):870-9. DOI: 10.1158/2159-8290.CD-13-0015

Chun, M.G., Shaw, R.J. Cancer metabolism in breadth and depth. (2013) Nature Biotechnology. 31(6):505-7. DOI: 10.1038/nbt.2611

Shaw, R.J. Cell biology. GATORs take a bite out of mTOR. (2013) Wissenschaft. 340(6136):1056-7. DOI: 10.1126/science.1240315

Shackelford, D.B., Abt, E., Gerken, L., Vasquez, D.S., Seki, A., Leblanc, M., Wei, L., Fishbein, M.C., Czernin, J., Mischel, P.S., Shaw, R.J. LKB1 inactivation dictates therapeutic response of non-small cell lung cancer to the metabolism drug phenformin. (2013) Cancer Cell. 23(2):143-58. DOI: 10.1016/j.ccr.2012.12.008

Mihaylova, M.M., Shaw, R.J. Metabolic reprogramming by class I and II histone deacetylases. (2013) Trends in Endocrinology and Metabolism. 24(1):48-57. DOI: 10.1016/j.tem.2012.09.003

Shaw, R.J., Cantley, L.C. Cell biology. Ancient sensor for ancient drug. (2012) Wissenschaft. 336(6083):813-4. DOI: 10.1126/science.1223140

Svensson, R.U., Shaw, R.J. Cancer metabolism: Tumour friend or foe. (2012) Natur. 485(7400):590-1. DOI: 10.1038/485590a

Klionsky, D.J., Abdalla, F.C., Abeliovich, H., Abraham, R.T., Acevedo-Arozena, A., Adeli, K., Agholme, L., Agnello, M., Agostinis, P., Aguirre-Ghiso, J.A., Ahn, H.J., Ait-Mohamed, O., Ait-Si-Ali, S., Akematsu, T., Akira, S., Al-Younes, H.M., Al-Zeer, M.A., Albert, M.L., Albin, R.L., Alegre-Abarrategui, J., Aleo, M.F., Alirezaei, M., Almasan, A., Almonte-Becerril, M., Amano, A., Amaravadi, R., Amarnath, S., Amer, A.O., Andrieu-Abadie, N., Anantharam, V., Ann, D.K., Anoopkumar-Dukie, S., Aoki, H., Apostolova, N., Arancia, G., Aris, J.P., Asanuma, K., Asare, N.Y., Ashida, H., Askanas, V., Askew, D.S., Auberger, P., Baba, M., Backues, S.K., Baehrecke, E.H., Bahr, B.A., Bai, X.Y., Bailly, Y., Baiocchi, R., Baldini, G., Balduini, W., Ballabio, A., Bamber, B.A., Bampton, E.T., Bánhegyi, G., Bartholomew, C.R., Bassham, D.C., Bast, R.C., Batoko, H., Bay, B.H., Beau, I., Béchet, D.M., Begley, T.J., Behl, C., Behrends, C., Bekri, S., Bellaire, B., Bendall, L.J., Benetti, L., Berliocchi, L., Bernardi, H., Bernassola, F., Besteiro, S., Bhatia-Kissova, I., Bi, X., Biard-Piechaczyk, M., Blum, J.S., Boise, L.H., Bonaldo, P., Boone, D.L., Bornhauser, B.C., Bortoluci, K.R., Bossis, I., Bost, F., Bourquin, J.P., Boya, P., Boyer-Guittaut, M., Bozhkov, P.V., Brady, N.R., Brancolini, C., Brech, A., Brenman, J.E., Brennand, A., Bresnick, E.H., Brest, P., Bridges, D., Bristol, M.L., Brookes, P.S., Brown, E.J., Brumell, J.H., Brunetti-Pierri, N., Brunk, U.T., Bulman, D.E., Bultman, S.J., Bultynck, G., Burbulla, L.F., Bursch, W., Butchar, J.P., Buzgariu, W., Bydlowski, S.P., Cadwell, K., Cahová, M., Cai, D., Cai, J., Cai, Q., Calabretta, B., Calvo-Garrido, J., Camougrand, N., Campanella, M., Campos-Salinas, J., Candi, E., Cao, L., Caplan, A.B., Carding, S.R., Cardoso, S.M., Carew, J.S., Carlin, C.R., Carmignac, V., Carneiro, L.A., Carra, S., Caruso, R.A., Casari, G., Casas, C., Castino, R., Cebollero, E., Cecconi, F., Celli, J., Chaachouay, H., Chae, H.J., Chai, C.Y., Chan, D.C., Chan, E.Y., Chang, R.C., Che, C.M., Chen, C.C., Chen, G.C., Chen, G.Q., Chen, M., Chen, Q., Chen, S.S., Chen, W., Chen, X., Chen, X., Chen, X., Chen, Y.G., Chen, Y., Chen, Y., Chen, Y.J., Chen, Z., Cheng, A., Cheng, C.H., Cheng, Y., Cheong, H., Cheong, J.H., Cherry, S., Chess-Williams, R., Cheung, Z.H., Chevet, E., Chiang, H.L., Chiarelli, R., Chiba, T., Chin, L.S., Chiou, S.H., Chisari, F.V., Cho, C.H., Cho, D.H., Choi, A.M., Choi, D., Choi, K.S., Choi, M.E., Chouaib, S., Choubey, D., Choubey, V., Chu, C.T., Chuang, T.H., Chueh, S.H., Chun, T., Chwae, Y.J., Chye, M.L., Ciarcia, R., Ciriolo, M.R., Clague, M.J., Clark, R.S., Clarke, P.G., Clarke, R., Codogno, P., Coller, H.A., Colombo, M.I., Comincini, S., Condello, M., Condorelli, F., Cookson, M.R., Coombs, G.H., Coppens, I., Corbalan, R., Cossart, P., Costelli, P., Costes, S., Coto-Montes, A., Couve, E., Coxon, F.P., Cregg, J.M., Crespo, J.L., Cronjé, M.J., Cuervo, A.M., Cullen, J.J., Czaja, M.J., D'Amelio, M., Darfeuille-Michaud, A., Davids, L.M., Davies, F.E., De Felici, M., de Groot, J.F., de Haan, C.A., De Martino, L., De Milito, A., De Tata, V., Debnath, J., Degterev, A., Dehay, B., Delbridge, L.M., Demarchi, F., Deng, Y.Z., Dengjel, J., Dent, P., Denton, D., Deretic, V., Desai, S.D., Devenish, R.J., Di Gioacchino, M., Di Paolo, G., Di Pietro, C., Díaz-Araya, G., Díaz-Laviada, I., Diaz-Meco, M.T., Diaz-Nido, J., Dikic, I., Dinesh-Kumar, S.P., Ding, W.X., Distelhorst, C.W., Diwan, A., Djavaheri-Mergny, M., Dokudovskaya, S., Dong, Z., Dorsey, F.C., Dosenko, V., Dowling, J.J., Doxsey, S., Dreux, M., Drew, M.E., Duan, Q., Duchosal, M.A., Duff, K., Dugail, I., Durbeej, M., Duszenko, M., Edelstein, C.L., Edinger, A.L., Egea, G., Eichinger, L., Eissa, N.T., Ekmekcioglu, S., El-Deiry, W.S., Elazar, Z., Elgendy, M., Ellerby, L.M., Eng, K.E., Engelbrecht, A.M., Engelender, S., Erenpreisa, J., Escalante, R., Esclatine, A., Eskelinen, E.L., Espert, L., Espina, V., Fan, H., Fan, J., Fan, Q.W., Fan, Z., Fang, S., Fang, Y., Fanto, M., Fanzani, A., Farkas, T., Farré, J.C., Faure, M., Fechheimer, M., Feng, C.G., Feng, J., Feng, Q., Feng, Y., Fésüs, L., Feuer, R., Figueiredo-Pereira, M.E., Fimia, G.M., Fingar, D.C., Finkbeiner, S., Finkel, T., Finley, K.D., Fiorito, F., Fisher, E.A., Fisher, P.B., Flajolet, M., Florez-McClure, M.L., Florio, S., Fon, E.A., Fornai, F., Fortunato, F., Fotedar, R., Fowler, D.H., Fox, H.S., Franco, R., Frankel, L.B., Fransen, M., Fuentes, J.M., Fueyo, J., Fujii, J., Fujisaki, K., Fujita, E., Fukuda, M., Furukawa, R.H., Gaestel, M., Gailly, P., Gajewska, M., Galliot, B., Galy, V., Ganesh, S., Ganetzky, B., Ganley, I.G., Gao, F.B., Gao, G.F., Gao, J., Garcia, L., Garcia-Manero, G., Garcia-Marcos, M., Garmyn, M., Gartel, A.L., Gatti, E., Gautel, M., Gawriluk, T.R., Gegg, M.E., Geng, J., Germain, M., Gestwicki, J.E., Gewirtz, D.A., Ghavami, S., Ghosh, P., Giammarioli, A.M., Giatromanolaki, A.N., Gibson, S.B., Gilkerson, R.W., Ginger, M.L., Ginsberg, H.N., Golab, J., Goligorsky, M.S., Golstein, P., Gomez-Manzano, C., Goncu, E., Gongora, C., Gonzalez, C.D., Gonzalez, R., González-Estévez, C., González-Polo, R.A., Gonzalez-Rey, E., Gorbunov, N.V., Gorski, S., Goruppi, S., Gottlieb, R.A., Gozuacik, D., Granato, G.E., Grant, G.D., Green, K.N., Gregorc, A., Gros, F., Grose, C., Grunt, T.W., Gual, P., Guan, J.L., Guan, K.L., Guichard, S.M., Gukovskaya, A.S., Gukovsky, I., Gunst, J., Gustafsson, A.B., Halayko, A.J., Hale, A.N., Halonen, S.K., Hamasaki, M., Han, F., Han, T., Hancock, M.K., Hansen, M., Harada, H., Harada, M., Hardt, S.E., Harper, J.W., Harris, A.L., Harris, J., Harris, S.D., Hashimoto, M., Haspel, J.A., Hayashi, S., Hazelhurst, L.A., He, C., He, Y.W., Hébert, M.J., Heidenreich, K.A., Helfrich, M.H., Helgason, G.V., Henske, E.P., Herman, B., Herman, P.K., Hetz, C., Hilfiker, S., Hill, J.A., Hocking, L.J., Hofman, P., Hofmann, T.G., Höhfeld, J., Holyoake, T.L., Hong, M.H., Hood, D.A., Hotamisligil, G.S., Houwerzijl, E.J., Høyer-Hansen, M., Hu, B., Hu, C.A., Hu, H.M., Hua, Y., Huang, C., Huang, J., Huang, S., Huang, W.P., Huber, T.B., Huh, W.K., Hung, T.H., Hupp, T.R., Hur, G.M., Hurley, J.B., Hussain, S.N., Hussey, P.J., Hwang, J.J., Hwang, S., Ichihara, A., Ilkhanizadeh, S., Inoki, K., Into, T., Iovane, V., Iovanna, J.L., Ip, N.Y., Isaka, Y., Ishida, H., Isidoro, C., Isobe, K., Iwasaki, A., Izquierdo, M., Izumi, Y., Jaakkola, P.M., Jäättelä, M., Jackson, G.R., Jackson, W.T., Janji, B., Jendrach, M., Jeon, J.H., Jeung, E.B., Jiang, H., Jiang, H., Jiang, J.X., Jiang, M., Jiang, Q., Jiang, X., Jiang, X., Jiménez, A., Jin, M., Jin, S., Joe, C.O., Johansen, T., Johnson, D.E., Johnson, G.V., Jones, N.L., Joseph, B., Joseph, S.K., Joubert, A.M., Juhász, G., Juillerat-Jeanneret, L., Jung, C.H., Jung, Y.K., Kaarniranta, K., Kaasik, A., Kabuta, T., Kadowaki, M., Kagedal, K., Kamada, Y., Kaminskyy, V.O., Kampinga, H.H., Kanamori, H., Kang, C., Kang, K.B., Kang, K.I., Kang, R., Kang, Y.A., Kanki, T., Kanneganti, T.D., Kanno, H., Kanthasamy, A.G., Kanthasamy, A., Karantza, V., Kaushal, G.P., Kaushik, S., Kawazoe, Y., Ke, P.Y., Kehrl, J.H., Kelekar, A., Kerkhoff, C., Kessel, D.H., Khalil, H., Kiel, J.A., Kiger, A.A., Kihara, A., Kim, D.R., Kim, D.H., Kim, D.H., Kim, E.K., Kim, H.R., Kim, J.S., Kim, J.H., Kim, J.C., Kim, J.K., Kim, P.K., Kim, S.W., Kim, Y.S., Kim, Y., Kimchi, A., Kimmelman, A.C., King, J.S., Kinsella, T.J., Kirkin, V., Kirshenbaum, L.A., Kitamoto, K., Kitazato, K., Klein, L., Klimecki, W.T., Klucken, J., Knecht, E., Ko, B.C., Koch, J.C., Koga, H., Koh, J.Y., Koh, Y.H., Koike, M., Komatsu, M., Kominami, E., Kong, H.J., Kong, W.J., Korolchuk, V.I., Kotake, Y., Koukourakis, M.I., Kouri Flores, J.B., Kovács, A.L., Kraft, C., Krainc, D., Krämer, H., Kretz-Remy, C., Krichevsky, A.M., Kroemer, G., Krüger, R., Krut, O., Ktistakis, N.T., Kuan, C.Y., Kucharczyk, R., Kumar, A., Kumar, R., Kumar, S., Kundu, M., Kung, H.J., Kurz, T., Kwon, H.J., La Spada, A.R., Lafont, F., Lamark, T., Landry, J., Lane, J.D., Lapaquette, P., Laporte, J.F., László, L., Lavandero, S., Lavoie, J.N., Layfield, R., Lazo, P.A., Le, W., Le Cam, L., Ledbetter, D.J., Lee, A.J., Lee, B.W., Lee, G.M., Lee, J., Lee, J.H., Lee, M., Lee, M.S., Lee, S.H., Leeuwenburgh, C., Legembre, P., Legouis, R., Lehmann, M., Lei, H.Y., Lei, Q.Y., Leib, D.A., Leiro, J., Lemasters, J.J., Lemoine, A., Lesniak, M.S., Lev, D., Levenson, V.V., Levine, B., Levy, E., Li, F., Li, J.L., Li, L., Li, S., Li, W., Li, X.J., Li, Y.B., Li, Y.P., Liang, C., Liang, Q., Liao, Y.F., Liberski, P.P., Lieberman, A., Lim, H.J., Lim, K.L., Lim, K., Lin, C.F., Lin, F.C., Lin, J., Lin, J.D., Lin, K., Lin, W.W., Lin, W.C., Lin, Y.L., Linden, R., Lingor, P., Lippincott-Schwartz, J., Lisanti, M.P., Liton, P.B., Liu, B., Liu, C.F., Liu, K., Liu, L., Liu, Q.A., Liu, W., Liu, Y.C., Liu, Y., Lockshin, R.A., Lok, C.N., Lonial, S., Loos, B., Lopez-Berestein, G., López-Otín, C., Lossi, L., Lotze, M.T., Lőw, P., Lu, B., Lu, B., Lu, B., Lu, Z., Luciano, F., Lukacs, N.W., Lund, A.H., Lynch-Day, M.A., Ma, Y., Macian, F., MacKeigan, J.P., Macleod, K.F., Madeo, F., Maiuri, L., Maiuri, M.C., Malagoli, D., Malicdan, M.C., Malorni, W., Man, N., Mandelkow, E.M., Manon, S., Manov, I., Mao, K., Mao, X., Mao, Z., Marambaud, P., Marazziti, D., Marcel, Y.L., Marchbank, K., Marchetti, P., Marciniak, S.J., Marcondes, M., Mardi, M., Marfe, G., Mariño, G., Markaki, M., Marten, M.R., Martin, S.J., Martinand-Mari, C., Martinet, W., Martinez-Vicente, M., Masini, M., Matarrese, P., Matsuo, S., Matteoni, R., Mayer, A., Mazure, N.M., McConkey, D.J., McConnell, M.J., McDermott, C., McDonald, C., McInerney, G.M., McKenna, S.L., McLaughlin, B., McLean, P.J., McMaster, C.R., McQuibban, G.A., Meijer, A.J., Meisler, M.H., Meléndez, A., Melia, T.J., Melino, G., Mena, M.A., Menendez, J.A., Menna-Barreto, R.F., Menon, M.B., Menzies, F.M., Mercer, C.A., Merighi, A., Merry, D.E., Meschini, S., Meyer, C.G., Meyer, T.F., Miao, C.Y., Miao, J.Y., Michels, P.A., Michiels, C., Mijaljica, D., Milojkovic, A., Minucci, S., Miracco, C., Miranti, C.K., Mitroulis, I., Miyazawa, K., Mizushima, N., Mograbi, B., Mohseni, S., Molero, X., Mollereau, B., Mollinedo, F., Momoi, T., Monastyrska, I., Monick, M.M., Monteiro, M.J., Moore, M.N., Mora, R., Moreau, K., Moreira, P.I., Moriyasu, Y., Moscat, J., Mostowy, S., Mottram, J.C., Motyl, T., Moussa, C.E., Müller, S., Muller, S., Münger, K., Münz, C., Murphy, L.O., Murphy, M.E., Musarò, A., Mysorekar, I., Nagata, E., Nagata, K., Nahimana, A., Nair, U., Nakagawa, T., Nakahira, K., Nakano, H., Nakatogawa, H., Nanjundan, M., Naqvi, N.I., Narendra, D.P., Narita, M., Navarro, M., Nawrocki, S.T., Nazarko, T.Y., Nemchenko, A., Netea, M.G., Neufeld, T.P., Ney, P.A., Nezis, I.P., Nguyen, H.P., Nie, D., Nishino, I., Nislow, C., Nixon, R.A., Noda, T., Noegel, A.A., Nogalska, A., Noguchi, S., Notterpek, L., Novak, I., Nozaki, T., Nukina, N., Nürnberger, T., Nyfeler, B., Obara, K., Oberley, T.D., Oddo, S., Ogawa, M., Ohashi, T., Okamoto, K., Oleinick, N.L., Oliver, F.J., Olsen, L.J., Olsson, S., Opota, O., Osborne, T.F., Ostrander, G.K., Otsu, K., Ou, J.H., Ouimet, M., Overholtzer, M., Ozpolat, B., Paganetti, P., Pagnini, U., Pallet, N., Palmer, G.E., Palumbo, C., Pan, T., Panaretakis, T., Pandey, U.B., Papackova, Z., Papassideri, I., Paris, I., Park, J., Park, O.K., Parys, J.B., Parzych, K.R., Patschan, S., Patterson, C., Pattingre, S., Pawelek, J.M., Peng, J., Perlmutter, D.H., Perrotta, I., Perry, G., Pervaiz, S., Peter, M., Peters, G.J., Petersen, M., Petrovski, G., Phang, J.M., Piacentini, M., Pierre, P., Pierrefite-Carle, V., Pierron, G., Pinkas-Kramarski, R., Piras, A., Piri, N., Platanias, L.C., Pöggeler, S., Poirot, M., Poletti, A., Poüs, C., Pozuelo-Rubio, M., Prætorius-Ibba, M., Prasad, A., Prescott, M., Priault, M., Produit-Zengaffinen, N., Progulske-Fox, A., Proikas-Cezanne, T., Przedborski, S., Przyklenk, K., Puertollano, R., Puyal, J., Qian, S.B., Qin, L., Qin, Z.H., Quaggin, S.E., Raben, N., Rabinowich, H., Rabkin, S.W., Rahman, I., Rami, A., Ramm, G., Randall, G., Randow, F., Rao, V.A., Rathmell, J.C., Ravikumar, B., Ray, S.K., Reed, B.H., Reed, J.C., Reggiori, F., Régnier-Vigouroux, A., Reichert, A.S., Reiners, J.J., Reiter, R.J., Ren, J., Revuelta, J.L., Rhodes, C.J., Ritis, K., Rizzo, E., Robbins, J., Roberge, M., Roca, H., Roccheri, M.C., Rocchi, S., Rodemann, H.P., Rodríguez de Córdoba, S., Rohrer, B., Roninson, I.B., Rosen, K., Rost-Roszkowska, M.M., Rouis, M., Rouschop, K.M., Rovetta, F., Rubin, B.P., Rubinsztein, D.C., Ruckdeschel, K., Rucker, E.B., Rudich, A., Rudolf, E., Ruiz-Opazo, N., Russo, R., Rusten, T.E., Ryan, K.M., Ryter, S.W., Sabatini, D.M., Sadoshima, J., Saha, T., Saitoh, T., Sakagami, H., Sakai, Y., Salekdeh, G.H., Salomoni, P., Salvaterra, P.M., Salvesen, G., Salvioli, R., Sanchez, A.M., Sánchez-Alcázar, J.A., Sánchez-Prieto, R., Sandri, M., Sankar, U., Sansanwal, P., Santambrogio, L., Saran, S., Sarkar, S., Sarwal, M., Sasakawa, C., Sasnauskiene, A., Sass, M., Sato, K., Sato, M., Schapira, A.H., Scharl, M., Schätzl, H.M., Scheper, W., Schiaffino, S., Schneider, C., Schneider, M.E., Schneider-Stock, R., Schoenlein, P.V., Schorderet, D.F., Schüller, C., Schwartz, G.K., Scorrano, L., Sealy, L., Seglen, P.O., Segura-Aguilar, J., Seiliez, I., Seleverstov, O., Sell, C., Seo, J.B., Separovic, D., Setaluri, V., Setoguchi, T., Settembre, C., Shacka, J.J., Shanmugam, M., Shapiro, I.M., Shaulian, E., Shaw, R.J., Shelhamer, J.H., Shen, H.M., Shen, W.C., Sheng, Z.H., Shi, Y., Shibuya, K., Shidoji, Y., Shieh, J.J., Shih, C.M., Shimada, Y., Shimizu, S., Shintani, T., Shirihai, O.S., Shore, G.C., Sibirny, A.A., Sidhu, S.B., Sikorska, B., Silva-Zacarin, E.C., Simmons, A., Simon, A.K., Simon, H.U., Simone, C., Simonsen, A., Sinclair, D.A., Singh, R., Sinha, D., Sinicrope, F.A., Sirko, A., Siu, P.M., Sivridis, E., Skop, V., Skulachev, V.P., Slack, R.S., Smaili, S.S., Smith, D.R., Soengas, M.S., Soldati, T., Song, X., Sood, A.K., Soong, T.W., Sotgia, F., Spector, S.A., Spies, C.D., Springer, W., Srinivasula, S.M., Stefanis, L., Steffan, J.S., Stendel, R., Stenmark, H., Stephanou, A., Stern, S.T., Sternberg, C., Stork, B., Strålfors, P., Subauste, C.S., Sui, X., Sulzer, D., Sun, J., Sun, S.Y., Sun, Z.J., Sung, J.J., Suzuki, K., Suzuki, T., Swanson, M.S., Swanton, C., Sweeney, S.T., Sy, L.K., Szabadkai, G., Tabas, I., Taegtmeyer, H., Tafani, M., Takács-Vellai, K., Takano, Y., Takegawa, K., Takemura, G., Takeshita, F., Talbot, N.J., Tan, K.S., Tanaka, K., Tanaka, K., Tang, D., Tang, D., Tanida, I., Tannous, B.A., Tavernarakis, N., Taylor, G.S., Taylor, G.A., Taylor, J.P., Terada, L.S., Terman, A., Tettamanti, G., Thevissen, K., Thompson, C.B., Thorburn, A., Thumm, M., Tian, F., Tian, Y., Tocchini-Valentini, G., Tolkovsky, A.M., Tomino, Y., Tönges, L., Tooze, S.A., Tournier, C., Tower, J., Towns, R., Trajkovic, V., Travassos, L.H., Tsai, T.F., Tschan, M.P., Tsubata, T., Tsung, A., Turk, B., Turner, L.S., Tyagi, S.C., Uchiyama, Y., Ueno, T., Umekawa, M., Umemiya-Shirafuji, R., Unni, V.K., Vaccaro, M.I., Valente, E.M., Van den Berghe, G., van der Klei, I.J., van Doorn, W., van Dyk, L.F., van Egmond, M., van Grunsven, L.A., Vandenabeele, P., Vandenberghe, W.P., Vanhorebeek, I., Vaquero, E.C., Velasco, G., Vellai, T., Vicencio, J.M., Vierstra, R.D., Vila, M., Vindis, C., Viola, G., Viscomi, M.T., Voitsekhovskaja, O.V., von Haefen, C., Votruba, M., Wada, K., Wade-Martins, R., Walker, C.L., Walsh, C.M., Walter, J., Wan, X.B., Wang, A., Wang, C., Wang, D., Wang, F., Wang, F., Wang, G., Wang, H., Wang, H.G., Wang, H.D., Wang, J., Wang, K., Wang, M., Wang, R.C., Wang, X., Wang, X., Wang, Y.J., Wang, Y., Wang, Z., Wang, Z.C., Wang, Z., Wansink, D.G., Ward, D.M., Watada, H., Waters, S.L., Webster, P., Wei, L., Weihl, C.C., Weiss, W.A., Welford, S.M., Wen, L.P., Whitehouse, C.A., Whitton, J.L., Whitworth, A.J., Wileman, T., Wiley, J.W., Wilkinson, S., Willbold, D., Williams, R.L., Williamson, P.R., Wouters, B.G., Wu, C., Wu, D.C., Wu, W.K., Wyttenbach, A., Xavier, R.J., Xi, Z., Xia, P., Xiao, G., Xie, Z., Xie, Z., Xu, D.Z., Xu, J., Xu, L., Xu, X., Yamamoto, A., Yamamoto, A., Yamashina, S., Yamashita, M., Yan, X., Yanagida, M., Yang, D.S., Yang, E., Yang, J.M., Yang, S.Y., Yang, W., Yang, W.Y., Yang, Z., Yao, M.C., Yao, T.P., Yeganeh, B., Yen, W.L., Yin, J.J., Yin, X.M., Yoo, O.J., Yoon, G., Yoon, S.Y., Yorimitsu, T., Yoshikawa, Y., Yoshimori, T., Yoshimoto, K., You, H.J., Youle, R.J., Younes, A., Yu, L., Yu, L., Yu, S.W., Yu, W.H., Yuan, Z.M., Yue, Z., Yun, C.H., Yuzaki, M., Zabirnyk, O., Silva-Zacarin, E., Zacks, D., Zacksenhaus, E., Zaffaroni, N., Zakeri, Z., Zeh, H.J., Zeitlin, S.O., Zhang, H., Zhang, H.L., Zhang, J., Zhang, J.P., Zhang, L., Zhang, L., Zhang, M.Y., Zhang, X.D., Zhao, M., Zhao, Y.F., Zhao, Y., Zhao, Z.J., Zheng, X., Zhivotovsky, B., Zhong, Q., Zhou, C.Z., Zhu, C., Zhu, W.G., Zhu, X.F., Zhu, X., Zhu, Y., Zoladek, T., Zong, W.X., Zorzano, A., Zschocke, J., Zuckerbraun, B. Guidelines for the use and interpretation of assays for monitoring autophagy. (2012) Autophagy. 8(4):445-544.

Xia, Y., Yeddula, N., Leblanc, M., Ke, E., Zhang, Y., Oldfield, E., Shaw, R.J., Verma, I.M. Reduced cell proliferation by IKK2 depletion in a mouse lung-cancer model. (2012) Nature Cell Biology. 14(3):257-65. DOI: 10.1038/ncb2428

Auricchio, N., Malinowska, I., Shaw, R., Manning, B.D., Kwiatkowski, D.J. Therapeutic trial of metformin and bortezomib in a mouse model of tuberous sclerosis complex (TSC). (2012) PLOS One. 7(2):e31900. DOI: 10.1371/journal.pone.0031900

Shaw, R.J., Cantley, L.C. Decoding key nodes in the metabolism of cancer cells: sugar & spice and all things nice. (2012) F1000 Biology Reports. 4:2. DOI: 10.3410/B4-2

Mihaylova, M.M., Shaw, R.J. The AMPK signalling pathway coordinates cell growth, autophagy and metabolism. (2011) Nature Cell Biology. 13(9):1016-23. DOI: 10.1038/ncb2329

Akhtar, A., Fuchs, E., Mitchison, T., Shaw, R.J., St Johnston, D., Strasser, A., Taylor, S., Walczak, C., Zerial, M. A decade of molecular cell biology: achievements and challenges. (2011) Nature Reviews Molecular Cell Biology. 12(10):669-74. DOI: 10.1038/nrm3187

Egan, D., Kim, J., Shaw, R.J., Guan, K.L. The autophagy initiating kinase ULK1 is regulated via opposing phosphorylation by AMPK and mTOR. (2011) Autophagy. 7(6):643-4.

Mihaylova, M.M., Vasquez, D.S., Ravnskjaer, K., Denechaud, P.D., Yu, R.T., Alvarez, J.G., Downes, M., Evans, R.M., Montminy, M., Shaw, R.J. Class IIa histone deacetylases are hormone-activated regulators of FOXO and mammalian glucose homeostasis. (2011) Cell. 145(4):607-21. DOI: 10.1016/j.cell.2011.03.043

Wang, B., Moya, N., Niessen, S., Hoover, H., Mihaylova, M.M., Shaw, R.J., Yates, J.R., Fischer, W.H., Thomas, J.B., Montminy, M. A hormone-dependent module regulating energy balance. (2011) Cell. 145(4):596-606. DOI: 10.1016/j.cell.2011.04.013

Li, Y., Xu, S., Mihaylova, M.M., Zheng, B., Hou, X., Jiang, B., Park, O., Luo, Z., Lefai, E., Shyy, J.Y., Gao, B., Wierzbicki, M., Verbeuren, T.J., Shaw, R.J., Cohen, R.A., Zang, M. AMPK phosphorylates and inhibits SREBP activity to attenuate hepatic steatosis and atherosclerosis in diet-induced insulin-resistant mice. (2011) Zellstoffwechsel. 13(4):376-388. DOI: 10.1016/j.cmet.2011.03.009

Mair, W., Morantte, I., Rodrigues, A.P., Manning, G., Montminy, M., Shaw, R.J., Dillin, A. Lifespan extension induced by AMPK and calcineurin is mediated by CRTC-1 and CREB. (2011) Natur. 470(7334):404-8. DOI: 10.1038/nature09706

Birnbaum, M.J., Shaw, R.J. Genomics: Drugs, diabetes and cancer. (2011) Natur. 470(7334):338-9. DOI: 10.1038/470338a

Egan, D.F., Shackelford, D.B., Mihaylova, M.M., Gelino, S., Kohnz, R.A., Mair, W., Vasquez, D.S., Joshi, A., Gwinn, D.M., Taylor, R., Asara, J.M., Fitzpatrick, J., Dillin, A., Viollet, B., Kundu, M., Hansen, M., Shaw, R.J. Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy. (2011) Wissenschaft. 331(6016):456-61. DOI: 10.1126/science.1196371

Ohashi, K., Ouchi, N., Higuchi, A., Shaw, R.J., Walsh, K. LKB1 deficiency in Tie2-Cre-expressing cells impairs ischemia-induced angiogenesis. (2010) Journal of Biological Chemistry. 285(29):22291-8. DOI: 10.1074/jbc.M110.123794

Shaw, R.J., Evans, R.M., Simon, M.C. Metabolism and cancer in La Jolla. (2010) Cancer Research. 70(10):3864-9. DOI: 10.1158/0008-5472.CAN-09-4529

Shaw, R.J. Metabolism and cancer mix in Madrid. (2010) EMBO Reports. 11(4):249-51. DOI: 10.1038/embor.2010.40

Gwinn, D.M., Asara, J.M., Shaw, R.J. Raptor is phosphorylated by cdc2 during mitosis. (2010) PLOS One. 5(2):e9197. DOI: 10.1371/journal.pone.0009197

Shaw, R. Journal club. A cancer researcher ponders a fundamental connection between nutrients and gene expression. (2009) Natur. 462(7275):829. DOI: 10.1038/462829f

Ikeda, Y., Sato, K., Pimentel, D.R., Sam, F., Shaw, R.J., Dyck, J.R., Walsh, K. Cardiac-specific deletion of LKB1 leads to hypertrophy and dysfunction. (2009) Journal of Biological Chemistry. 284(51):35839-49. DOI: 10.1074/jbc.M109.057273

Lamia, K.A., Sachdeva, U.M., DiTacchio, L., Williams, E.C., Alvarez, J.G., Egan, D.F., Vasquez, D.S., Juguilon, H., Panda, S., Shaw, R.J., Thompson, C.B., Evans, R.M. AMPK regulates the circadian clock by cryptochrome phosphorylation and degradation. (2009) Wissenschaft. 326(5951):437-40. DOI: 10.1126/science.1172156

Shaw, R.J. Tumor suppression by LKB1: SIK-ness prevents metastasis. (2009) Science Signaling. 2(86):pe55. DOI: 10.1126/scisignal.286pe55

Shackelford, D.B., Shaw, R.J. The LKB1-AMPK pathway: metabolism and growth control in tumour suppression. (2009) Nature Reviews Cancer. 9(8):563-75. DOI: 10.1038/nrc2676

Shackelford, D.B., Vasquez, D.S., Corbeil, J., Wu, S., Leblanc, M., Wu, C.L., Vera, D.R., Shaw, R.J. mTOR and HIF-1alpha-mediated tumor metabolism in an LKB1 mouse model of Peutz-Jeghers syndrome. (2009) Proceedings of the National Academy of Sciences of the United States of America. 106(27):11137-42. DOI: 10.1073/pnas.0900465106

Shaw, R.J. LKB1 and AMP-activated protein kinase control of mTOR signalling and growth. (2009) Acta Physiologica. 196(1):65-80. DOI: 10.1111/j.1748-1716.2009.01972.x

Shaw, R., Dillin, A. PPTR-1 counterAkts insulin signaling. (2009) Cell. 136(5):816-8. DOI: 10.1016/j.cell.2009.02.029

Mair, W., Panowski, S.H., Shaw, R.J., Dillin, A. Optimizing dietary restriction for genetic epistasis analysis and gene discovery in C. elegans. (2009) PLOS One. 4(2):e4535. DOI: 10.1371/journal.pone.0004535

Shaw, R.J. mTOR signaling: RAG GTPases transmit the amino acid signal. (2008) Trends in Biochemical Sciences. 33(12):565-8. DOI: 10.1016/j.tibs.2008.09.005

Shaw, R.J. Raptor swoops in on metabolism. (2008) Zellstoffwechsel. 8(5):343-4. DOI: 10.1016/j.cmet.2008.10.007

Shaw, R.J. LKB1: cancer, polarity, metabolism, and now fertility. (2008) Biochemical Journal. 416(1):e1-3. DOI: 10.1042/BJ20082023

Narkar, V.A., Downes, M., Yu, R.T., Embler, E., Wang, Y.X., Banayo, E., Mihaylova, M.M., Nelson, M.C., Zou, Y., Juguilon, H., Kang, H., Shaw, R.J., Evans, R.M. AMPK and PPARdelta agonists are exercise mimetics. (2008) Cell. 134(3):405-15. DOI: 10.1016/j.cell.2008.06.051

Gwinn, D.M., Shackelford, D.B., Egan, D.F., Mihaylova, M.M., Mery, A., Vasquez, D.S., Turk, B.E., Shaw, R.J. AMPK phosphorylation of raptor mediates a metabolic checkpoint. (2008) Molecular Cell. 30(2):214-26. DOI: 10.1016/j.molcel.2008.03.003

Shaw, R.J. Glucose metabolism and cancer. (2006) Current Opinion in Cell Biology. 18(6):598-608. DOI: 10.1016/j.ceb.2006.10.005

Baur, J.A., Pearson, K.J., Price, N.L., Jamieson, H.A., Lerin, C., Kalra, A., Prabhu, V.V., Allard, J.S., Lopez-Lluch, G., Lewis, K., Pistell, P.J., Poosala, S., Becker, K.G., Boss, O., Gwinn, D., Wang, M., Ramaswamy, S., Fishbein, K.W., Spencer, R.G., Lakatta, E.G., Le Couteur, D., Shaw, R.J., Navas, P., Puigserver, P., Ingram, D.K., de Cabo, R., Sinclair, D.A. Resveratrol improves health and survival of mice on a high-calorie diet. (2006) Natur. 444(7117):337-42. DOI: 10.1038/nature05354

Shaw, R.J., Cantley, L.C. Ras, PI(3)K and mTOR signalling controls tumour cell growth. (2006) Natur. 441(7092):424-30. DOI: 10.1038/nature04869

Shaw, R.J., Lamia, K.A., Vasquez, D., Koo, S.H., Bardeesy, N., Depinho, R.A., Montminy, M., Cantley, L.C. The kinase LKB1 mediates glucose homeostasis in liver and therapeutic effects of metformin. (2005) Wissenschaft. 310(5754):1642-6. DOI: 10.1126/science.1120781

Fernandes, N., Sun, Y., Chen, S., Paul, P., Shaw, R.J., Cantley, L.C., Price, B.D. DNA damage-induced association of ATM with its target proteins requires a protein interaction domain in the N terminus of ATM. (2005) Journal of Biological Chemistry. 280(15):15158-64. DOI: 10.1074/jbc.M412065200

Shaw, R.J., Bardeesy, N., Manning, B.D., Lopez, L., Kosmatka, M., DePinho, R.A., Cantley, L.C. The LKB1 tumor suppressor negatively regulates mTOR signaling. (2004) Cancer Cell. 6(1):91-9. DOI: 10.1016/j.ccr.2004.06.007

Shaw, R.J., Kosmatka, M., Bardeesy, N., Hurley, R.L., Witters, L.A., DePinho, R.A., Cantley, L.C. The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress. (2004) Proceedings of the National Academy of Sciences of the United States of America. 101(10):3329-35. DOI: 10.1073/pnas.0308061100

Shaw, R.J., Paez, J.G., Curto, M., Yaktine, A., Pruitt, W.M., Saotome, I., O'Bryan, J.P., Gupta, V., Ratner, N., Der, C.J., Jacks, T., McClatchey, A.I. The Nf2 tumor suppressor, merlin, functions in Rac-dependent signaling. (2001) Developmental Cell. 1(1):63-72.

Karuman, P., Gozani, O., Odze, R.D., Zhou, X.C., Zhu, H., Shaw, R., Brien, T.P., Bozzuto, C.D., Ooi, D., Cantley, L.C., Yuan, J. The Peutz-Jegher gene product LKB1 is a mediator of p53-dependent cell death. (2001) Molecular Cell. 7(6):1307-19.

Shaw, R.J., McClatchey, A.I., Jacks, T. Localization and functional domains of the neurofibromatosis type II tumor suppressor, merlin. (1998) Cell Growth & Differentiation. 9(4):287-96.

Shaw, R.J., McClatchey, A.I., Jacks, T. Regulation of the neurofibromatosis type 2 tumor suppressor protein, merlin, by adhesion and growth arrest stimuli. (1998) Journal of Biological Chemistry. 273(13):7757-64.

Shaw, R.J., Henry, M., Solomon, F., Jacks, T. RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts. (1998) Molecular Biology of the Cell. 9(2):403-19.

Platko, J.V., Leonard, D.A., Adra, C.N., Shaw, R.J., Cerione, R.A., Lim, B. A single residue can modify target-binding affinity and activity of the functional domain of the Rho-subfamily GDP dissociation inhibitors. (1995) Proceedings of the National Academy of Sciences of the United States of America. 92(7):2974-8.