The Stress-inducted Proteins RTP801 and RTP801L Are Negative Regulators of the Mammalian Target of Rapamycin Pathway

Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action

Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652

Upstream and downstream of mTOR

Hay, N., & Sonenberg, N. (2004) · Genes & Development · doi:10.1101/gad.1212704 · Cited by 4,181

TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival

Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914

TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling

Inoki, K., Li, Y., Zhu, T., Wu, J., & Guan, K.-L. (2002) · Nature Cell Biology · doi:10.1038/ncb839 · Cited by 3,083

Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling

Inoki, K., Li, Y., Xu, T., & Guan, K.-L. (2003) · Genes & Development · doi:10.1101/gad.1110003 · Cited by 1,911

Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway

Manning, B. D., Tee, A. R., Logsdon, M. N., Blenis, J., & Cantley, L. C. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00568-3 · Cited by 1,555

Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex

Brugarolas, J., Lei, K., Hurley, R. L., Manning, B. D., Reiling, J. H., Hafen, E., Witters, L. A., Ellisen, L. W., & Kaelin, W. G. (2004) · Genes & Development · doi:10.1101/gad.1256804 · Cited by 1,384

Target of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression

Fingar, D. C., & Blenis, J. (2004) · Oncogene · doi:10.1038/sj.onc.1207542 · Cited by 1,264

The AMP-activated protein kinase pathway – new players upstream and downstream

Hardie, D. G. (2004) · Journal of Cell Science · doi:10.1242/jcs.01540 · Cited by 1,163

Dysregulation of the TSC-mTOR pathway in human disease

Inoki, K., Corradetti, M. N., & Guan, K. (2004) · Nature Genetics · doi:10.1038/ng1494 · Cited by 980

Progress on ocular siRNA gene‐silencing therapy and drug delivery systems

Jiang, J., Zhang, X., Tang, Y., Li, S., & Chen, J. (2020) · Fundamental and Clinical Pharmacology · doi:10.1111/fcp.12561 · Cited by 58

Transcriptional regulation of gene expression during osmotic stress responses by the mammalian target of rapamycin

Ortells, M. C., Morancho, B., Drews‐Elger, K., Viollet, B., Laderoute, K. R., López‐Rodríguez, C., & Aramburu, J. F. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks038 · Cited by 56

The Mammalian Target of Rapamycin Pathway as a Potential Target for Cancer Chemoprevention

Kopelovich, L., Fay, J. R., Sigman, C. C., & Crowell, J. A. (2007) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-07-0045 · Cited by 54

Immunometabolic Signatures Predict Risk of Progression to Active Tuberculosis and Disease Outcome

Duffy, F. J., Weiner, J. M., Hansen, S. G., Tabb, D. L., Suliman, S., Thompson, E. G., Maertzdorf, J., Shankar, S., Tromp, G., Parida, S. K., et al. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00527 · Cited by 57

Pulmonary lymphangioleiomyomatosis (LAM): Progress and current challenges

Goncharova, E. A., & Krymskaya, V. P. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21419 · Cited by 53

Induction of Endoplasmic Reticulum Stress Response by the Indole-3-Carbinol Cyclic Tetrameric Derivative CTet in Human Breast Cancer Cell Lines

Galluzzi, L., Santi, M. D., Crinelli, R., Marco, C. D., Zaffaroni, N., Duranti, A., Brandi, G., & Magnani, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043249 · Cited by 55

Oocyte-dependent activation of MTOR in cumulus cells controls the development and survival of cumulus-oocyte complexes

Guo, J., Shi, L., Gong, X., Jiang, M., Yin, Y., Zhang, X., Yin, H. X., Li, H., Emori, C., Sugiura, K., et al. (2016) · Journal of Cell Science · doi:10.1242/jcs.182642 · Cited by 51

Nuclear protein 1 induced by ATF4 in response to various stressors acts as a positive regulator on the transcriptional activation of ATF4

Jin, H., Seo, S., Woo, S., Choe, T., Hong, S., Kim, J., & Park, I. (2009) · IUBMB Life · doi:10.1002/iub.271 · Cited by 50

Rheb and mammalian target of rapamycin in mitochondrial homoeostasis

Groenewoud, M. J., & Zwartkruis, F. J. T. (2013) · Open Biology · doi:10.1098/rsob.130185 · Cited by 51

Gene expression alterations in activated human T-cells induced by modeled microgravity

Ward, N. E., Pellis, N. R., Risin, S. A., & Risin, D. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20988 · Cited by 47

Immune- and stress-related transcriptomic responses of Solea senegalensis stimulated with lipopolysaccharide and copper sulphate using heterologous cDNA microarrays

Osuna-Jiménez, I., Williams, T., Prieto‐Álamo, M., Abril, N., Chipman, J. K., & Pueyo, C. (2009) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2009.02.020 · Cited by 48

PKR, the double stranded RNA‐dependent protein kinase as a critical target in Alzheimer's disease

Morel, M., Couturier, J., Lafay‐Chebassier, C., Paccalin, M., & Page, G. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00849.x · Cited by 47

Feedback Control of p53 Translation by REDD1 and mTORC1 Limits the p53-Dependent DNA Damage Response

Vadysirisack, D. D., Baenke, F., Ory, B., Lei, K., & Ellisen, L. W. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05541-11 · Cited by 51

Emerging role for regulated in development and DNA damage 1 (REDD1) in the regulation of skeletal muscle metabolism

Gordon, B. S., Steiner, J. L., Williamson, D. L., Lang, C. H., & Kimball, S. R. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00059.2016 · Cited by 49

Multifaceted Role of Insulin-Like Growth Factors and Mammalian Target of Rapamycin in Skeletal Muscle

Frost, R. A., & Lang, C. H. (2012) · Endocrinology and Metabolism Clinics of North America · doi:10.1016/j.ecl.2012.04.012 · Cited by 47

Reduced REDD1 expression contributes to activation of mTORC1 following electrically induced muscle contraction

Gordon, B. S., Steiner, J. L., Lang, C. H., Jefferson, L. S., & Kimball, S. R. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00250.2014 · Cited by 47

Inhibition of mammalian target of rapamycin signaling potentiates the effects of all‐trans retinoic acid to induce growth arrest and differentiation of human acute myelogenous leukemia cells

Nishioka, C., Ikezoe, T., Yang, J., Gery, S., Koeffler, H. P., & Yokoyama, A. (2009) · International Journal of Cancer · doi:10.1002/ijc.24472 · Cited by 44

Gene expression deregulation by KRAS G12D and G12V in a BRAF V600E context

Monticone, M., Biollo, E., Maffei, M., Donadini, A., Romeo, F., Storlazzi, C. T., Giaretti, W., & Castagnola, P. (2008) · Molecular Cancer · doi:10.1186/1476-4598-7-92 · Cited by 43

Induction of HSP27 and HSP70 by constitutive overexpression of Redd1 confers resistance of lung cancer cells to ionizing radiation

Jin, H., Hong, S., Kim, J., Kim, M., Chang, Y. H., Hong, Y. J., Lee, J., & Park, I. (2019) · Oncology Reports · doi:10.3892/or.2019.7036 · Cited by 42

Regulation of REDD1 by insulin‐like growth factor‐I in skeletal muscle and myotubes

Frost, R. A., Huber, D. S., Pruznak, A. M., & Lang, C. H. (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22349 · Cited by 42

Translation termination efficiency modulates ATF4 response by regulating ATF4 mRNA translation at 5′ short ORFs

Ghezala, H. A., Jollès, B., Salhi, S., Castrillo, K., Carpentier, W., Cagnard, N., Bruhat, A., Fafournoux, P., & Jean‐Jean, O. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks762 · Cited by 43

Cellular metabolism constrains innate immune responses in early human ontogeny

Kan, B., Michalski, C., Fu, H., Au, H. H. T., Lee, K., Marchant, E. A., Cheng, M. F., Anderson‐Baucum, E. K., Aharoni-Simon, M., Tilley, P. A. G., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07215-9 · Cited by 43

Mammalian target of rapamycin (mTOR) signaling pathway and traumatic brain injury: A novel insight into targeted therapy

Movahedpour, A., Vakili, O., Khalifeh, M., Mousavi, P., Mahmoodzadeh, A., Taheri‐Anganeh, M., Razmeh, S., Shabaninejad, Z., Yousefi, F., Behrouj, H., et al. (2022) · Cell Biochemistry and Function · doi:10.1002/cbf.3692 · Cited by 43

siRNA-Mediated Knockdown of the mTOR Inhibitor RTP801 Promotes Retinal Ganglion Cell Survival and Axon Elongation by Direct and Indirect Mechanisms

Morgan-Warren, P. J., O'Neill, J., de Cogan, F., Spivak, I., Ashush, H., Kalinski, H., Ahmed, Z., Berry, M., Feinstein, E., Scott, R. A. H., et al. (2016) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.15-17511 · Cited by 40

Epithelial X-Box Binding Protein 1 Coordinates Tumor Protein p53-Driven DNA Damage Responses and Suppression of Intestinal Carcinogenesis

Welz, L., Kakavand, N., Hang, X., Laue, G., Ito, G., Silva, M. G., Plattner, C., Mishra, N., Tengen, F., Ogris, C., et al. (2021) · Gastroenterology · doi:10.1053/j.gastro.2021.09.057 · Cited by 40

Acute Alcohol Intoxication Increases REDD1 in Skeletal Muscle

Lang, C. H., Frost, R. A., & Vary, T. C. (2008) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2008.00637.x · Cited by 40

Targeting tissue-specific metabolic signaling pathways in aging: the promise and limitations

Hu, F., & Liu, F. (2013) · Protein & Cell · doi:10.1007/s13238-013-0002-3 · Cited by 39

Overexpression of the recently identified oncogene REDD1 correlates with tumor progression and is an independent unfavorable prognostic factor for ovarian carcinoma

Chang, B., Meng, J., Zhu, H., Du, X., Sun, L., Wang, L., Li, S., & Yang, G. S. (2018) · Diagnostic Pathology · doi:10.1186/s13000-018-0754-4 · Cited by 37

REDD1 and p-AKT over-expression may predict poor prognosis in ovarian cancer.

Jia, W., Chang, B., Sun, L., Zhu, H., Pang, L., Lin, T., Zou, H., Du, J.-Z., Dong, Y., Yan, Q., et al. (2014) · PubMed Central · Cited by 36

Plasma membrane translocation of REDD1 governed by GPCRs contributes to mTORC1 activation

Michel, G., Matthes, H. W. D., Hachet‐Haas, M., Baghdadi, K. E., Mey, J. D., Pepperkok, R., Simpson, J. C., Galzi, J., & Lecat, S. (2013) · Journal of Cell Science · doi:10.1242/jcs.136432 · Cited by 36

SP600125 negatively regulates the mammalian target of rapamycin via ATF4‐induced Redd1 expression

Jin, H.-O., Seo, S.-K., Woo, S., Kim, E.-S., Lee, H.-C., Yoo, D.-H., Choe, T.-B., Hong, S.-I., Kim, J.-I., & Park, I. (2009) · FEBS Letters · doi:10.1016/j.febslet.2008.11.035 · Cited by 39

Control of HIF-1α and vascular signaling in fetal lung involves cross talk between mTORC1 and the FGF-10/FGFR2b/Spry2 airway branching periodicity clock

Scott, C. L., Walker, D. J., Cwiklinski, E., Tait, C., Tee, A. R., & Land, S. C. (2010) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00348.2009 · Cited by 36

REDD2 expression in rat skeletal muscle correlates with nutrient-induced activation of mTORC1: responses to aging, immobilization, and remobilization

Kelleher, A. R., Pereira, S. L., Jefferson, L. S., & Kimball, S. R. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00341.2014 · Cited by 37

Role of the TSC1-TSC2 Complex in the Integration of Insulin and Glucose Signaling Involved in Pancreatic β-Cell Proliferation

Bartolomé, A., Guillén, C., & Benito, M. (2010) · Endocrinology · doi:10.1210/en.2010-0048 · Cited by 35

The stress response protein REDD1 as a causal factor for oxidative stress in diabetic retinopathy

Miller, W. P., Sunilkumar, S., & Dennis, M. D. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.01.041 · Cited by 35

Evidence of molecular links between PKR and mTOR signalling pathways in Aβ neurotoxicity: Role of p53, Redd1 and TSC2

Morel, M., Couturier, J., Pontcharraud, R., Gil, R., Fauconneau, B., Paccalin, M., & Page, G. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.07.004 · Cited by 36

The Mammalian Target of Rapamycin Kinase and Tumor Growth Inhibition

Boulay, A., & Lane, H. A. (2007) · Springer eBooks · doi:10.1007/978-3-540-31209-3_7 · Cited by 34

RTP801 is a novel retinoic acid–responsive gene associated with myeloid differentiation

Gery, S., Park, D. J., Vuong, P. T., Virk, R. K., Müller, C. I., Hofmann, W., & Koeffler, H. P. (2007) · Experimental Hematology · doi:10.1016/j.exphem.2007.01.049 · Cited by 33

REDD1 Is Essential for Optimal T Cell Proliferation and Survival

Reuschel, E. L., Wang, J., Shivers, D. K., Muthumani, K., Weiner, D. B., Ma, Z., & Finkel, T. H. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136323 · Cited by 31

PKR, a cognitive decline biomarker, can regulate translation via two consecutive molecular targets p53 and Redd1 in lymphocytes of AD patients

Damjanac, M., Page, G., Ragot, S., Laborie, G., Gil, R., Hugon, J., & Paccalin, M. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00688.x · Cited by 31

RTP801 Gene Expression Is Differentially Upregulated in Retinopathy and Is Silenced by PF-04523655, a 19-Mer siRNA Directed Against RTP801

Rittenhouse, K. D., Johnson, T. R., Vicini, P., Hirakawa, B. P., Kalabat, D. Y., Yang, A. H., Huang, W., & Basile, A. S. (2014) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.13-13449 · Cited by 30

Advances in pharmacotherapy for wet age-related macular degeneration

Santarelli, M., Diplotti, L., Samassa, F., Veritti, D., Kuppermann, B. D., & Lanzetta, P. (2015) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.2015.1067679 · Cited by 29

Molecular and Epigenetic Mechanisms for the Complex Effects of Stress on Synaptic Physiology and Cognitive Functions

Yuen, E. Y., Wei, J., & Yan, Z. (2017) · The International Journal of Neuropsychopharmacology · doi:10.1093/ijnp/pyx052 · Cited by 31

REDD1/DDIT4-Independent mTORC1 Inhibition and Apoptosis by Glucocorticoids in Thymocytes

Wolff, N. C., McKay, R. M., & Brugarolas, J. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0625 · Cited by 30

Bile acid-induced inflammatory signaling in mice lacking Foxa2 in the liver leads to activation of mTOR and age-onset obesity

Bochkis, I. M., Shin, S., & Kaestner, K. H. (2013) · Molecular Metabolism · doi:10.1016/j.molmet.2013.08.005 · Cited by 28

Loss of REDD1 augments the rate of the overload-induced increase in muscle mass

Gordon, B. S., Liu, C., Steiner, J. L., Nader, G. A., Jefferson, L. S., & Kimball, S. R. (2016) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00159.2016 · Cited by 28

PC12 Cells as a model for parkinson's disease research

Malagelada, C., & Greene, L. A. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-374028-1.00029-4 · Cited by 28

Multiple Changes of Gene Expression and Function Reveal Genomic and Phenotypic Complexity in SLE-like Disease

Wilbe, M., Kozyrev, S. V., Farias, F., Bremer, H., Hedlund, A., Pielberg, G., Seppälä, E. H., Gustafson, U., Lohi, H., Carlborg, Ö., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005248 · Cited by 27

RTP801 immunoreactivity in retinal ganglion cells and its down-regulation in cultured cells protect them from light and cobalt chloride

del Olmo‐Aguado, S., Núñez‐Álvarez, C., Ji, D., Manso, A. G., & Osborne, N. N. (2013) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2013.08.002 · Cited by 26

Methylseleninic acid elevates REDD1 and inhibits prostate cancer cell growth despite AKT activation and mTOR dysregulation in hypoxia

Sinha, I., Allen, J. E., Pinto, J. T., & Sinha, R. (2014) · Cancer Medicine · doi:10.1002/cam4.198 · Cited by 25

Steroid and Oxygen Effects on eIF4F Complex, mTOR, and ENaC Translation in Fetal Lung Epithelia

Otulakowski, G., Duan, W., Gandhi, S. G., & O'Brodovich, H. M. (2007) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2007-0055oc · Cited by 25

Microarray analyses in bladder cancer cells: Inhibition of hTERT expression down‐regulates EGFR

Kraemer, K., Schmidt, U., Fuessel, S., Herr, A., Wirth, M. P., & Meye, A. (2006) · International Journal of Cancer · doi:10.1002/ijc.21975 · Cited by 25

Transcriptome comparison identifies potential biomarkers of spine and skull base chordomas

Bell, A., DeMonte, F., Raza, S. M., Rhines, L. D., Tatsui, C. E., Prieto, V. G., Fuller, G. N., & Bell, D. (2017) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/s00428-017-2224-x · Cited by 24

REDD1 deletion attenuates cancer cachexia in mice

Hain, B. A., Xu, H., VanCleave, A. M., Gordon, B. S., Kimball, S. R., & Waning, D. L. (2021) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00536.2021 · Cited by 24

Regulation of mammalian target of rapamycin complex 1 (mTORC1) by hypoxia: causes and consequences

Çam, H., & Houghton, P. J. (2011) · Targeted Oncology · doi:10.1007/s11523-011-0173-x · Cited by 25

Depot Dependent Effects of Dexamethasone on Gene Expression in Human Omental and Abdominal Subcutaneous Adipose Tissues from Obese Women

Pickering, R. T., Lee, M., Karastergiou, K., Gower, A. C., & Fried, S. K. (2016) · PLoS ONE · doi:10.1371/journal.pone.0167337 · Cited by 24

Differential alterations in gene expression profiles contribute to time-dependent effects of nandrolone to prevent denervation atrophy

Qin, W., Pan, J., Bauman, W. A., & Cardozo, C. P. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-596 · Cited by 23

Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase.

Moreno, D., Viana, R., & Sanz, P. (2009) · International Journal of Biochemistry and Cell Biology · doi:10.1016/j.biocel.2009.07.002 · Cited by 28

Protein Phosphorylation as a Key Mechanism of mTORC1/2 Signaling Pathways

Tchevkina, E. M., & Komelkov, A. V. (2012) · InTech eBooks · doi:10.5772/48274 · Cited by 26

Rapamycin Induces Apoptosis When Autophagy is Inhibited in T-47D Mammary Cells and Both Processes are Regulated by Phlda1

Moad, A. I. H., Muhammad, T. S. T., Oon, C. E., & Tan, M. (2013) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-012-9504-5 · Cited by 22

Redd1 inhibits the invasiveness of non-small cell lung cancer cells

Jin, H., Seo, S., Woo, S., Kim, Y., Hong, S., Yi, J.-Y., Noh, W.-C., Kim, E., Lee, J., Hong, S., et al. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.03.047 · Cited by 23

Familial Mediterranean fever: the molecular pathways from stress exposure to attacks

Korkmaz, C., Cansu, D. Ü., & Cansu, G. B. (2020) · Rheumatology · doi:10.1093/rheumatology/keaa450 · Cited by 23

In vivo inducible reverse genetics in patients’ tumors to identify individual therapeutic targets

Carlet, M., Völse, K., Vergalli, J., Becker, M., Herold, T., Arner, A., Senft, D., Jurinović, V., Liu, W., Gao, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25963-z · Cited by 19

Novel Ser/Thr Protein Phosphatase 5 (PP5) Regulated Targets during DNA Damage Identified by Proteomics Analysis

Ham, B. M., Jayachandran, H., Yang, F., Jaitly, N., Polpitiya, A. D., Monroe, M. E., Wang, L., Zhao, R., Purvine, S. O., Livesay, E. A., et al. (2009) · Journal of Proteome Research · doi:10.1021/pr9008207 · Cited by 20

Nuclear factor of activated T-cell c3 inhibition of mammalian target of rapamycin signaling through induction of regulated in development and DNA damage response 1 in human intestinal cells

Zhou, Y., Wang, Q., Guo, Z., Weiss, H. L., & Evers, B. M. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-01-0037 · Cited by 22

Nuclear factor of activated T-cells 5 increases intestinal goblet cell differentiation through an mTOR/Notch signaling pathway

Zhou, Y., Wang, Q., Weiss, H. L., & Evers, B. M. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-05-0998 · Cited by 20

REDD1 overexpression in oral squamous cell carcinoma may predict poor prognosis and correlates with high microvessel density

Feng, Y., Song, K., Shang, W., Chen, L., Wang, C., Pang, B., & Wang, N. (2019) · Oncology Letters · doi:10.3892/ol.2019.11070 · Cited by 20

In silico discovery of small molecules for efficient stem cell differentiation into definitive endoderm

Novakovsky, G., Sasaki, S., Fornés, O., Omur, M. E., Huang, H., Bayly, C. L., Zhang, D., Lim, N., Cherkasov, A. R., Pavlidis, P., et al. (2023) · Stem Cell Reports · doi:10.1016/j.stemcr.2023.01.008 · Cited by 21

Comparative Meta-Analysis of Transcriptomics Data during Cellular Senescence andIn VivoTissue Ageing

Voutetakis, K., Chatziioannou, A. A., Gonos, E. S., & Trougakos, I. P. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/732914 · Cited by 17

Expression profiling reveals heightened apoptosis and supports fiber size economy in the murine muscles of mastication

Evans, M., Morine, K., Kulkarni, C., & Barton, E. R. (2008) · Physiological Genomics · doi:10.1152/physiolgenomics.00232.2007 · Cited by 17

Testing an Aflatoxin B1 Gene Signature in Rat Archival Tissues

Merrick, B. A., Auerbach, S. S., Stockton, P. S., Foley, J. F., Malarkey, D. E., Sills, R. C., Irwin, R. D., & Tice, R. R. (2012) · Chemical Research in Toxicology · doi:10.1021/tx3000945 · Cited by 17

Inhibition of mTORC1 activity by REDD1 induction in myeloma cells resistant to bortezomib cytotoxicity

Decaux, O., Clément, M., Magrangeas, F., Gouraud, W., Guérin‐Charbonnel, C., Campion, L., Avet‐Loiseau, H., & Minvielle, S. (2009) · Cancer Science · doi:10.1111/j.1349-7006.2009.01467.x · Cited by 22

Dendrite pathology and neurodegeneration: focus on mTOR

Polo, A. (2015) · Neural Regeneration Research · doi:10.4103/1673-5374.155421 · Cited by 16

mTORC1 senses glutamine and other amino acids through GCN2

Figlia, G., Müller, S., Cortizo, F. G., Neff, M., Klinke, G., Poschet, G., & Teleman, A. A. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00505-1 · Cited by 16

The regulated in development and DNA damage response 2 (REDD2) gene mediates human monocyte cell death through a reduction in thioredoxin-1 expression

Jguirim-Souissi, I., Billiet, L., Cuaz‐Pérolin, C., Michaud, N., & Rouis, M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.02.020 · Cited by 14

Nitrate increases cisplatin chemosensitivity of oral squamous cell carcinoma via REDD1/AKT signaling pathway

Feng, Y., Cao, X., Zhao, B., Song, C., Pang, B., Hu, L., Zhang, C., Wang, J., He, J., & Wang, S. (2021) · Science China Life Sciences · doi:10.1007/s11427-020-1978-4 · Cited by 13

Transcript profiles in longissimus dorsi muscle and subcutaneous adipose tissue: A comparison of pigs with different postweaning growth rates1

Pilcher, C. M., Jones, C. K., Schroyen, M., Severin, A. J., Patience, J. F., Tuggle, C. K., & Koltes, J. E. (2015) · Journal of Animal Science · doi:10.2527/jas.2014-8593 · Cited by 13

Kinase Inhibitors and Interferons as Other Myeloid Differentiation Inducers in Leukemia Therapy

Takahashi, S. (2021) · Acta Haematologica · doi:10.1159/000519769 · Cited by 13

DDIT4L regulates mitochondrial and innate immune activities in early life

Michalski, C., Cheung, C., Oh, J., Ackermann, E., Popescu, C. R., Archambault, A., Prusinkiewicz, M. A., Silva, R. D., Majdoubi, A., Paramo, M. V., et al. (2024) · JCI Insight · doi:10.1172/jci.insight.172312 · Cited by 13

Targeting of hyperactivated mTOR signaling in high-risk acute lymphoblastic leukemia in a pre-clinical model

Hasan, M. N., Queudeville, M., Trentin, L., Eckhoff, S. M., Bronzini, I., Palmi, C., Barth, T. E. F., Cazzaniga, G., Kronnie, G. T., Debatin, K., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.2842 · Cited by 11

Impact of Pyrrolidine Dithiocarbamate and Interleukin-6 on Mammalian Target of Rapamycin Complex 1 Regulation and Global Protein Translation

Song, S., Abdelmohsen, K., Zhang, Y., Becker, K. G., Gorospe, M., & Bernier, M. (2011) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.111.185678 · Cited by 11

Impaired Transcriptional Response of the Murine Heart to Cigarette Smoke in the Setting of High Fat Diet and Obesity

Tilton, S. C., Karin, N. J., Webb‐Robertson, B., Waters, K. M., Mikheev, V. B., Lee, K. M., CORLEY, R. A., Pounds, J. G., & Bigelow, D. J. (2013) · Chemical Research in Toxicology · doi:10.1021/tx400078b · Cited by 11

Glucocorticoid-Mediated Repression of REDD1 mRNA Expression in Rat Fetal Distal Lung Epithelial Cells

Otulakowski, G., Duan, W., Sarangapani, A., Gandhi, S. G., & O'Brodovich, H. M. (2009) · Pediatric Research · doi:10.1203/pdr.0b013e3181998db6 · Cited by 13

Pooled genome-wide CRISPR activation screening for rapamycin resistance genes in Drosophila cells

Xia, B., Viswanatha, R., Hu, Y., Mohr, S. E., & Perrimon, N. (2023) · eLife · doi:10.7554/elife.85542 · Cited by 14

Regulation of mTOR signaling in skeletal muscle hypertrophy.

Esser, K. A. (2008) · PubMed · Cited by 10

Interferon regulatory factor-1 (IRF-1) interacts with regulated in development and DNA damage response 2 (REDD2) in the cytoplasm of mouse bone marrow cells

Gupta, M. K., & Rath, P. C. (2014) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2014.01.005 · Cited by 9

siRNA Knockdown of REDD1 Facilitates Aspirin-Mediated Dephosphorylation of mTORC1 Target 4E-BP1 in MDA-MB-468 Human Breast Cancer Cell Line

Savukaitytė, A., Gudoitytė, G., Bartnykaitė, A., Ugenskienė, R., & Juozaitytė, E. (2021) · Cancer Management and Research · doi:10.2147/cmar.s264414 · Cited by 9

Regulation of hypoxia-inducible factor-1α, regulated in development and DNA damage response-1 and mammalian target of rapamycin in human placental BeWo cells under hypoxia

Zhou, F., Guan, L., Yu, P., Wang, X. D., & Hu, Y. (2016) · Placenta · doi:10.1016/j.placenta.2016.07.003 · Cited by 9

Dysregulation of the leukotriene pathway in Parkinson's disease: The potential role of montelukast

Alshahrani, S. M., Al-Kuraishy, H. M., Al-Gareeb, A. I., Shokr, M. M., Alexiou, A. T., Papadakis, M., & Batiha, G. E. (2025) · Cytokine · doi:10.1016/j.cyto.2025.157010 · Cited by 8

APEX2-Mediated Proximity Labeling Resolves the DDIT4-Interacting Proteome

Naki, M., Gourdomichali, O., Zonke, K., Kattan, F.-G., Makridakis, M., Kontostathi, G., Vlahou, A., & Doxakis, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23095189 · Cited by 7

Research Translation and Personalized Medicine

Brugarolas, J. (2012) · Springer eBooks · doi:10.1007/978-1-4614-2400-0_8 · Cited by 7

REDD1 Expression in Placenta During Human Gestation

Hu, Y. Y., Liu, J. C., Xing, A., You, Y., & Wang, X. D. (2012) · Reproductive Sciences · doi:10.1177/1933719112440054 · Cited by 7

The dual role of the TSC complex in cancer

Hartung, J., Müller, C., & Calkhoven, C. F. (2024) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2024.10.009 · Cited by 8

Comprehensive Analysis of Programmed Cell Death-Related Genes in Diagnosis and Synovitis During Osteoarthritis Development: Based on Bulk and Single-Cell RNA Sequencing Data

Zhou, J., Jiao, S., Huang, J., Dai, T., Xu, Y., Xia, D., Feng, Z., Chen, J., Li, Z., Hu, L., et al. (2025) · Journal of Inflammation Research · doi:10.2147/jir.s491203 · Cited by 5

Vhl Dependent Expression of REDD1 and PDK3 Proteins in Clear-Cell Renal Cell Carcinoma

Ilic, B. B., Antic, J. A., Bankovic, J. Z., Milicevic, I., Rodic, G., Ilic, D. S., Tulić, C., Todorovic, V. N., & Damjanovic, S. S. (2017) · Journal of Medical Biochemistry · doi:10.1515/jomb-2017-0030 · Cited by 5

Redd1 Is a Novel Marker of Testis Development but Is Not Required for Normal Male Reproduction

Notini, A. J., McClive, P. J., Meachem, S. J., van den Bergen, J. A., Western, P. S., Gustin, S. E., Harley, V. R., Koopman, P. A., & Sinclair, A. H. (2012) · Sexual Development · doi:10.1159/000339723 · Cited by 5

mTORC1 Signaling and Hypoxia

Brugarolas, J. (2009) · Humana Press eBooks · doi:10.1007/978-1-60327-271-1_4 · Cited by 4

Early Life Stress Induces Brain Mitochondrial Dynamics Changes and Sex‐Specific Adverse Effects in Adulthood

Vlaikou, A., Nußbaumer, M., Iliou, A., Papageorgiou, M. P., Komini, C., Theodoridou, D., Benaki, D. C., Mikros, E., Gikas, E. E., Syrrou, M., et al. (2025) · Journal of Neuroscience Research · doi:10.1002/jnr.70023 · Cited by 4

Identification and validation of three potential biomarkers and immune microenvironment for in severe asthma in microarray and single-cell datasets

Zhang, F., Weng, X., Zhu, J., Tang, Q., Lei, M., & Zhou, W. (2024) · Journal of Asthma · doi:10.1080/02770903.2024.2335562 · Cited by 3

RNASET2 silencing affects miRNAs and target gene expression pattern in a human ovarian cancer cell model

Turconi, G., Scaldaferri, D., Fabbri, M., Monti, L., Lualdi, M., Pedrini, E., Gribaldo, L., Taramelli, R., & Acquati, F. (2016) · International Journal of Oncology · doi:10.3892/ijo.2016.3763 · Cited by 3

Regulation of mTOR and Cell Growth in Response to Energy Stress by REDD1

Sofer, A., Lei, K., Johannessen, C. M., & Ellisen, L. W. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.14.5834-5845.2005 · Cited by 449

RTP801/REDD1: a stress coping regulator that turns into a troublemaker in neurodegenerative disorders

Canal, M., Romaní-Aumedes, J., Martín‐Flores, N., Pérez-Fernández, V., & Malagelada, C. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00313 · Cited by 65

Regulation of the Mechanistic Target of Rapamycin by Cellular Stress.

Magnuson, B. (2013) · Deep Blue (University of Michigan)

Transcriptional regulation of the stress response by mTOR

Aramburu, J. F., Ortells, M. C., Vaquero, S. T., Buxadé, M., & López‐Rodríguez, C. (2014) · Science Signaling · doi:10.1126/scisignal.2005326 · Cited by 100

TOR Signaling

Harris, T. E., & Lawrence, J. C. (2003) · Science s STKE · doi:10.1126/stke.2122003re15 · Cited by 239