Last updated September 2023 - Biochemistry and Molecular Biology
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Li F, Fang Y, Zhuang Q, Cheng M, Moronge D, Jue H, et al. Blocking ribosomal protein S6 phosphorylation inhibits podocyte hypertrophy and focal segmental glomerulosclerosis. Kidney International [Internet]. 2022;102(1):121–35. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85129976617&doi=10.1016%252fj.kint.2022.02.037&partnerID=40&md5=5d7957e86485fc96b83db5b65cc6d4ec
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Puighermanal E, Biever A, Pascoli V, Melser S, Pratlong M, Cutando L, et al. Ribosomal protein s6 phosphorylation is involved in novelty-induced locomotion, synaptic plasticity and mRNA translation. Frontiers in Molecular Neuroscience [Internet]. 2017;10. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85041804049&doi=10.3389%252ffnmol.2017.00419&partnerID=40&md5=72c282e93a0ee515504f398ab23c6ce3
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Wittenberg AD, Azar S, Klochendler A, Stolovich-Rain M, Avraham S, Birnbaum L, et al. Phosphorylated ribosomal protein S6 is required for Akt-driven hyperplasia and malignant transformation, but not for hypertrophy, aneuploidy and hyperfunction of pancreatic β-cells. PLoS ONE [Internet]. 2016;11(2). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84960459861&doi=10.1371%252fjournal.pone.0149995&partnerID=40&md5=14ccaab5cb050da260364f4a5e6f1434
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Wu H, Chen J, Xu J, Dong Z, Meyuhas O, Chen JK. Blocking rpS6 phosphorylation exacerbates Tsc1 deletion–induced kidney growth. Journal of the American Society of Nephrology [Internet]. 2016;27(4):1145–58. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85017044204&doi=10.1681%252fASN.2014121264&partnerID=40&md5=3591d43e6061401009ef53b510bc5309
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Volovelsky O, Cohen G, Kenig A, Wasserman G, Dreazen A, Meyuhas O, et al. Phosphorylation of ribosomal protein S6 mediates mammalian target of rapamycin complex 1-induced parathyroid cell proliferation in secondary hyperparathyroidism. Journal of the American Society of Nephrology [Internet]. 2016;27(4):1091–101. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84981263305&doi=10.1681%252fASN.2015040339&partnerID=40&md5=087a78db9e468dcf465faad1284c1082
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Salmond RJ, Brownlie RJ, Meyuhas O, Zamoyska R. Mechanistic target of rapamycin complex 1/S6 kinase 1 signals influence T cell activation independently of ribosomal protein S6 phosphorylation. Journal of Immunology [Internet]. 2015;195(10):4615–22. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84958641630&doi=10.4049%252fjimmunol.1501473&partnerID=40&md5=344853a1cce1ed36bb184de0f980468a
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Meyuhas O, Kahan T. The race to decipher the top secrets of TOP mRNAs. Biochimica et Biophysica Acta - Gene Regulatory Mechanisms [Internet]. 2015;1849(7):801–11. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84930959981&doi=10.1016%252fj.bbagrm.2014.08.015&partnerID=40&md5=47dd725902efa86ca6d3a3fb2f9ae83e
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Xu J, Chen J, Dong Z, Meyuhas O, Chen JK. Phosphorylation of ribosomal protein S6 mediates compensatory renal hypertrophy. Kidney International [Internet]. 2015;87(3):543–56. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84930406310&doi=10.1038%252fki.2014.302&partnerID=40&md5=4d87aeb1f2ce5dd2b1c617b0e92bc0b4
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Faller WJ, Jackson TJ, Knight JRP, Ridgway RA, Jamieson T, Karim SA, et al. MTORC1-mediated translational elongation limits intestinal tumour initiation and growth. Nature [Internet]. 2015;517(7535):497–500. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84925491509&doi=10.1038%252fnature13896&partnerID=40&md5=954796b8e0fe1308c8d0d2921fd2c33a
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Meyuhas O. Ribosomal Protein S6 Phosphorylation: Four Decades of Research. International Review of Cell and Molecular Biology [Internet]. 2015;320:41–73. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84938629848&doi=10.1016%252fbs.ircmb.2015.07.006&partnerID=40&md5=297899a4d22c9700ac51a251b6391445
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Biever A, Puighermanal E, Nishi A, David A, Panciatici C, Longueville S, et al. PKA-dependent phosphorylation of ribosomal protein S6 does not correlate with translation efficiency in striatonigral and striatopallidal medium-sized spiny neurons. Journal of Neuroscience [Internet]. 2015;35(10):4113–30. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84924439941&doi=10.1523%252fJNEUROSCI.3288-14.2015&partnerID=40&md5=c6139a991c400023e0ae2c7f6be09881
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Patursky-Polischuk I, Kasir J, Miloslavski R, Hayouka Z, Hausner-Hanochi M, Stolovich-Rain M, et al. Reassessment of the Role of TSC, mTORC1 and MicroRNAs in Amino Acids-Meditated Translational Control of TOP mRNAs. PLoS ONE [Internet]. 2014;9(10). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84908610762&doi=10.1371%252fjournal.pone.0109410&partnerID=40&md5=b2d0c926781ea2eb9ea1e17bccd8be90
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Chauvin C, Koka V, Nouschi A, Mieulet V, Hoareau-Aveilla C, Dreazen A, et al. Ribosomal protein S6 kinase activity controls the ribosome biogenesis transcriptional program. Oncogene [Internet]. 2014;33(4):474–83. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84896629473&doi=10.1038%252fonc.2012.606&partnerID=40&md5=66cee6b5752b2116f8d0587f6c613dbf
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Miloslavski R, Cohen E, Avraham A, Iluz Y, Hayouka Z, Kasir J, et al. Oxygen sufficiency controls TOP mRNA translation via the TSC-Rheb-mTOR pathway in a 4E-BP-independent manner. Journal of Molecular Cell Biology [Internet]. 2014;6(3):255–66. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84901700198&doi=10.1093%252fjmcb%252fmju008&partnerID=40&md5=8b0c478746f07913388e87346d94e9f9
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Han K, Jaimovich A, Dey G, Ruggero D, Meyuhas O, Sonenberg N, et al. Parallel measurement of dynamic changes in translation rates in single cells. Nature Methods [Internet]. 2014;11(1):86–93. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84894628550&doi=10.1038%252fnmeth.2729&partnerID=40&md5=f578168e9b3702d13bfab10bec522fe9
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Khalaileh A, Dreazen A, Khatib A, Apel R, Swisa A, Kidess-Bassir N, et al. Phosphorylation of ribosomal protein S6 attenuates DNA damage and tumor suppression during development of pancreatic cancer. Cancer Research [Internet]. 2013;73(6):1811–20. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84875448111&doi=10.1158%252f0008-5472.CAN-12-2014&partnerID=40&md5=d5b45d28016e8dd7b1f0a7c2e0a64d21
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Hsieh AC, Costa M, Zollo O, Davis C, Feldman ME, Testa JR, et al. Genetic Dissection of the Oncogenic mTOR Pathway Reveals Druggable Addiction to Translational Control via 4EBP-eIF4E. Cancer Cell [Internet]. 2010;17(3):249–61. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-77649286736&doi=10.1016%252fj.ccr.2010.01.021&partnerID=40&md5=17de9d4b1c78ba2fb1ce1698273252f2
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Meyuhas O, Dreazen A. Chapter 3 Ribosomal Protein S6 Kinase. From TOP mRNAs to Cell Size. Progress in Molecular Biology and Translational Science [Internet]. 2009;90(C):109–53. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-77957075353&doi=10.1016%2fS1877-1173%2809%2990003-5&partnerID=40&md5=1174cbcf5d4ef36d5c848642c72d9fbe
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Ruvinsky I, Katz M, Dreazen A, Gielchinsky Y, Saada A, Freedman N, et al. Mice deficient in ribosomal protein S6 phosphorylation suffer from muscle weakness that reflects a growth defect and energy deficit. PLoS ONE [Internet]. 2009;4(5). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-66049157014&doi=10.1371%252fjournal.pone.0005618&partnerID=40&md5=5d260ebe9c88d4324d77c77a6852bf54
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Patursky-Polischuk I, Stolovich-Rain M, Hausner-Hanochi M, Kasir J, Cybulski N, Avruch J, et al. The TSC-mTOR pathway mediates translational activation of TOP mRNAs by insulin largely in a raptor- or rictor-independent manner. Molecular and Cellular Biology [Internet]. 2009;29(6):1670. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-62849087835&doi=10.1128%252fMCB.00104-09&partnerID=40&md5=6f0bbf05cc09855f892cdf50dc8e72dd
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Patursky-Polischuk I, Stolovich-Rain M, Hausner-Hanochi M, Kasir J, Cybulski N, Avruch J, et al. The TSC-mTOR pathway mediates translational activation of TOP mRNAs by insulin largely in a raptor- or rictor-independent manner. Molecular and Cellular Biology [Internet]. 2009;29(3):640–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-59249097362&doi=10.1128%252fMCB.00980-08&partnerID=40&md5=694fcb163942ecb71f946d77f97a0206
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Meyuhas O. Chapter 1 Physiological Roles of Ribosomal Protein S6: One of Its Kind. International Review of Cell and Molecular Biology [Internet]. 2008;268:1–37. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-52049103675&doi=10.1016%2fS1937-6448%2808%2900801-0&partnerID=40&md5=a41433a67648373d5eb4ba804af955b1
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Jeon YJ, Kim IK, Hong SH, Nan H, Kim HJ, Lee HJ, et al. Ribosomal protein S6 is a selective mediator of TRAIL-apoptotic signaling. Oncogene [Internet]. 2008;27(31):4344–52. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-47549095202&doi=10.1038%252fonc.2008.73&partnerID=40&md5=54770f363391b978f844ce1e8137e264
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Markert A, Grimm M, Martinez J, Wiesner J, Meyerhans A, Meyuhas O, et al. The La-related protein LARP7 is a component of the 7SK ribonucleoprotein and affects transcription of cellular and viral polymerase II genes. EMBO Reports [Internet]. 2008;9(6):569–75. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-44649135099&doi=10.1038%252fembor.2008.72&partnerID=40&md5=5469efc184ac76cd1a20232919abd47d
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Ruvinsky I, Meyuhas O. Ribosomal protein S6 phosphorylation: from protein synthesis to cell size. Trends in Biochemical Sciences [Internet]. 2006;31(6):342–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33745150462&doi=10.1016%252fj.tibs.2006.04.003&partnerID=40&md5=c973a1220bf9b660657b236778f11c9f
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Ruvinsky I, Sharon N, Lerer T, Cohen H, Stolovich-Rain M, Nir T, et al. Ribosomal protein S6 phosphorylation is a determinant of cell size and glucose homeostasis. Genes and Development [Internet]. 2005;19(18):2199–211. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-24944464482&doi=10.1101%252fgad.351605&partnerID=40&md5=1c405cc4acf80f81e74a46dda5684a2b
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Karni R, Gus Y, Dor Y, Meyuhas O, Levitzki A. Active Src elevates the expression of β-catenin by enhancement of cap-dependent translation. Molecular and Cellular Biology [Internet]. 2005;25(12):5031–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-20344387465&doi=10.1128%252fMCB.25.12.5031-5039.2005&partnerID=40&md5=a74f99d02621db5e0e59953d7a83365f
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Stolovich M, Lerer T, Bolkier Y, Cohen H, Meyuhas O. Lithium can relieve translational repression of TOP mRNAs elicited by various blocks along the cell cycle in a glycogen synthase kinase-3- and S6-kinase-independent manner. Journal of Biological Chemistry [Internet]. 2005;280(7):5336–42. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-14044276306&doi=10.1074%252fjbc.M412434200&partnerID=40&md5=25c05beaf438e53d1b7cb0df814331b5
31.
Stolovich M, Tang H, Hornstein E, Levy G, Cohen R, Bae SS, et al. Transduction of growth or mitogenic signals into translational activation of TOP mRNAs is fully reliant on the phosphatidylinositol 3-kinase-mediated pathway but requires neither S6K1 nor rpS6 phosphorylation. Molecular and Cellular Biology [Internet]. 2002;22(23):8101–13. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036889291&doi=10.1128%252fMCB.22.23.8101-8113.2002&partnerID=40&md5=ae1a164b73a4f4b45559c993fe4ec2c7
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Karni R, Dor Y, Keshet E, Meyuhas O, Levitzki A. Activated pp60c-Src leads to elevated hypoxia-inducible factor (HIF)-1α expression under normoxia. Journal of Biological Chemistry [Internet]. 2002;277(45):42919–25. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037044578&doi=10.1074%252fjbc.M206141200&partnerID=40&md5=fa991aa0ae0207d62c4d9af87e705661
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Barth-Baus D, Stratton CA, Parrott L, Myerson H, Meyuhas O, Templeton DJ, et al. S6 phosphorylation-independent pathways regulate translation of 5′-terminal oligopyrimidine tract-containing mRNAs in differentiating hematopoietic cells. Nucleic Acids Research [Internet]. 2002;30(9):1919–28. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0036566786&doi=10.1093%252fnar%252f30.9.1919&partnerID=40&md5=35e4ef326e1406b2f11870aa842194d6
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Tang H, Hornstein E, Stolovich M, Levy G, Livingstone M, Templeton D, et al. Amino acid-induced translation of TOP mRNAs is fully dependent on phosphatidylinositol 3-kinase-mediated signaling, is partially inhibited by rapamycin, and is independent of S6K1 and rpS6 phosphorylation. Molecular and Cellular Biology [Internet]. 2001;21(24):8671–83. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035200856&doi=10.1128%252fMCB.21.24.8671-8683.2001&partnerID=40&md5=0ff197e7900932d88daae2b2867b32a3
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Kerner M, Meyuhas O, Hirsch-Lerner D, Rosen LJ, Min Z, Barenholz Y. Interplay in lipoplexes between type of pDNA promoter and lipid composition determines transfection efficiency of human growth hormone in NIH3T3 cells in culture. Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids [Internet]. 2001;1532(1–2):128–36. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035978433&doi=10.1016%2fS1388-1981%2801%2900118-4&partnerID=40&md5=f3679eef5cfa2e2db9a04ea5a27fce49
36.
Hornstein E, Tang H, Meyuhas O. Mitogenic and nutritional signals are transduced into translational efficiency of TOP mRNAs. Cold Spring Harbor Symposia on Quantitative Biology [Internet]. 2001;66:477–84. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035787712&doi=10.1101%252fsqb.2001.66.477&partnerID=40&md5=29f942cda7b95b41fb1f568bf8cb7693
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Meyuhas O. Synthesis of the translational apparatus is regulated at the translational level. European Journal of Biochemistry [Internet]. 2000;267(21):6321–30. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033761629&doi=10.1046%252fj.1432-1327.2000.01719.x&partnerID=40&md5=26dc51cd0e8406e55d0cdba3c4d15a68
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Hornstein E, Harel H, Levy G, Meyuhas O. Overexpression of poly(A)-binding protein down-regulates the translation or the abundance of its own mRNA. FEBS Letters [Internet]. 1999;457(2):209–13. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032772533&doi=10.1016%2fS0014-5793%2899%2901039-X&partnerID=40&md5=2427e336e488dc466a9cbc6a5afe07b1
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Biberman Y, Meyuhas O. TOP mRNAs are translationally inhibited by a titratable repressor in both wheat germ extract and reticulocyte lysate. FEBS Letters [Internet]. 1999;456(3):357–60. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032866822&doi=10.1016%2fS0014-5793%2899%2900983-7&partnerID=40&md5=89fc38c193246ef6a41ccc3100a31a5c
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Hornstein E, Git A, Braunstein I, Avni D, Meyuhas O. The expression of poly(A)-binding protein gene is translationally regulated in a growth-dependent fashion through a 5’-terminal oligopyrimidine tract motif. Journal of Biological Chemistry [Internet]. 1999;274(3):1708–14. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033556419&doi=10.1074%252fjbc.274.3.1708&partnerID=40&md5=278bf7c7cdcf52f9630ed05780d7e418
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Zhang ZC, Nechushtan H, Jacob-Hirsch J, Avni D, Meyuhas O, Razin E. Growth-dependent and PKC-mediated translational regulation of the upstream stimulating factor-2 (USF2) mRNA in hematopoietic cells. Oncogene [Internet]. 1998;16(6):763–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0000500599&doi=10.1038%252fsj.onc.1201584&partnerID=40&md5=5342488f60e4a959f695e7e9937d27fc
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Meyuhas O, Avni D, Bibermant Y, Shama S, Ostareck B, Ostareck-Lederer A, et al. Growth-dependent translational control of top mRNAS. FASEB Journal [Internet]. 1997;11(9):A1283. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33750231671&partnerID=40&md5=01a875aed141cef192a511d6b8d690f1
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Biberman Y, Meyuhas O. Substitution of just five nucleotides at and around the transcription start site of rat β-actin promoter is sufficient to render the resulting transcript a subject for translational control. FEBS Letters [Internet]. 1997;405(3):333–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030929822&doi=10.1016%2fS0014-5793%2897%2900234-2&partnerID=40&md5=fa1217ffe9e150f04f19e1d409ddb41e
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Avni D, Biberman Y, Meyuhas O. The 5′ Terminal Oligopyrimidine Tract Confers Translational Control on Top Mrnas in a Cell Type-and Sequence Context-Dependent Manner. Nucleic Acids Research [Internet]. 1996;25(5):995–1001. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030838872&doi=10.1093%252fnar%252f25.5.995&partnerID=40&md5=9f5d4f33af8ffbf4dba854536510640d
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Shama S, Meyuhas O. The translational cis-regulatory element of mammalian ribosomal protein mRNAs is recognized by the plant translational apparatus. European Journal of Biochemistry [Internet]. 1996;236(2):383–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029875022&doi=10.1111%252fj.1432-1033.1996.00383.x&partnerID=40&md5=b8b4394c84ff9d3b1d7d5f03ec99cc6b
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Shama S, Avni D, Frederickson RM, Sonenberg N, Meyuhas O. Overexpression of initiation factor eIF-4E does not relieve the translational repression of ribosomal protein mRNAs in quiescent cells. Gene Expression [Internet]. 1995;4(4–5):241–52. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029168362&partnerID=40&md5=71b4bb499865eded3c3f85ec4304aad9
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Avni D, Shama S, Loreni F, Meyuhas O. Vertebrate mRNAs with a 5’-terminal pyrimidine tract are candidates for translational repression in quiescent cells: Characterization of the translational cis-regulatory element. Molecular and Cellular Biology [Internet]. 1994;14(6):3822–33. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028356914&doi=10.1128%252fMCB.14.6.3822&partnerID=40&md5=2eb1e901e5fc4a8c4f049c6562c90518
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Aloni R, Peleg D, Meyuhas O. Selective translational control and nonspecific posttranscriptional regulation of ribosomal protein gene expression during development and regeneration of rat liver. Molecular and Cellular Biology [Internet]. 1992;12(5):2203–12. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026719232&doi=10.1128%252fMCB.12.5.2203&partnerID=40&md5=aeb48739fbafb2b1388de86302615beb
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Levy S, Avni D, Hariharan N, Perry RP, Meyuhas O. Oligopyrimidine tract at the 5’ end of mammalian ribosomal protein mRNAs is required for their translational control. Proceedings of the National Academy of Sciences of the United States of America [Internet]. 1991;88(8):3319–23. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026323221&doi=10.1073%252fpnas.88.8.3319&partnerID=40&md5=894ebfd9b8c6318bfdcc67b2391c80e3
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Shiran A, Flusser G, Aloni R, Meyuhas O. The mammalian genome contains a high proportion of processed pseudogenes corresponding to ribosomal protein L19. Biochemistry International [Internet]. 1990;22(5):921–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025614735&partnerID=40&md5=6c2a178f433244e5a0b9e55430b2a36c
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Meyuhas O, Klein A. The mouse ribosomal protein L7 gene. Its primary structure and functional analysis of the promoter region. Journal of Biological Chemistry [Internet]. 1990;265(20):11465–73. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025368830&partnerID=40&md5=ccc3fbf13d99898be3b0abdce51d78aa
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Meyuhas O, Baldin V, Bouche G, Amalric F. Glucocorticoids repress ribosome biosynthesis in lymphosarcoma cells by affecting gene expression at the level of transcription, posttranscription and translation. BBA - Gene Structure and Expression [Internet]. 1990;1049(1):38–44. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025285836&doi=10.1016%2f0167-4781%2890%2990082-D&partnerID=40&md5=5491bf60f69ca01af13322181ea5ce0f
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Perry RP, Meyuhas O. Translational control of ribosomal protein production in mammalian cells. Enzyme [Internet]. 1990;44(1–4):83–92. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025679961&doi=10.1159%252f000468749&partnerID=40&md5=5e123550670fb2d8acb3dc1396e3ac5f
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Aoyama Y, Chan YL, Meyuhas O, Wool IG. The primary structure of rat ribosomal protein L18a. FEBS Letters [Internet]. 1989;247(2):242–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0024593501&doi=10.1016%2f0014-5793%2889%2981344-4&partnerID=40&md5=35e1e01ee56b134d627edde67d037a61
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Atchison ML, Meyuhas O, Perry RP. Localization of transcriptional regulatory elements and nuclear factor binding sites in mouse ribosomal protein gene rpL32. Molecular and Cellular Biology [Internet]. 1989;9(5):2067–74. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0024514078&doi=10.1128%252fMCB.9.5.2067&partnerID=40&md5=e3a4a285f62e82929b7d10b989ddfc17
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Flusser G, Ginzburg V, Meyuhas O. Glucocorticoids induce transcription of ribosomal protein genes in rat liver. Molecular and Cellular Endocrinology [Internet]. 1989;64(2):213–22. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0024378001&doi=10.1016%2f0303-7207%2889%2990148-2&partnerID=40&md5=5e5f53e8e65c46ad5d4439c94f6ee204
57.
Lin A, Chan YL, McNally J, Peleg D, Meyuhas O, Wool IG. The primary structure of rat ribosomal protein L7. The presence near the amino terminus of L7 of five tandem repeats of a sequence of 12 amino acids. Journal of Biological Chemistry [Internet]. 1987;262(26):12665–71. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023656165&partnerID=40&md5=2dd39f4f9dcbeda88722bfdcc75fa5ad
58.
Chan YL, Lin A, McNally J, Peleg D, Meyuhas O, Wool IG. The primary structure of rat ribosomal protein L19. A determination from the sequence of nucleotides in a cDNA and from the sequence of amino acids in the protein. Journal of Biological Chemistry [Internet]. 1987;262(3):1111–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023102943&partnerID=40&md5=8fad7113d47915dd08c2050dd22bd477
59.
Theodor L, Peleg D, Meyuhas O. P31, a mammalian housekeeping protein encoded by a multigene family containing a high proportion of pseudogenes. BBA - Gene Structure and Expression [Internet]. 1985;826(2–3):137–46. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0022374394&doi=10.1016%2f0167-4781%2885%2990119-8&partnerID=40&md5=2d362e2d4ac90fd1ca1f759ed44e6ab8
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Meyuhas O. Evolutionary conservation of ribosomal protein mRNA sequences: application for expansion of corresponding cDNA and gene libraries. BBA - Gene Structure and Expression [Internet]. 1985;825(4):393–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021858530&doi=10.1016%2f0167-4781%2885%2990066-1&partnerID=40&md5=bdbcb6d374835949d2b1c4de3438c4fa
61.
Benvenisty N, Mencher D, Meyuhas O, Razin A, Reshef L. Sequential changes in DNA methylation patterns of the rat phosphoenolpyruvate carboxykinase gene during development. Proceedings of the National Academy of Sciences of the United States of America [Internet]. 1985;82(2):267–71. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021906662&doi=10.1073%252fpnas.82.2.267&partnerID=40&md5=f53194dd177a48994708591b27e23b04
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Cohen H, Gidoni B, Shouval D, Benvenisty N, Mencher D, Meyuhas O, et al. Conservation from rat to human of cytosolic phosphoenolpyruvate carboxykinase and the control of its gene expression. FEBS Letters [Internet]. 1985;180(2):175–80. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0022005422&doi=10.1016%2f0014-5793%2885%2981066-8&partnerID=40&md5=b14b66c3704b2ea55204ba53a574202c
63.
Peled-Yalif E, Cohen-Binder l., Meyuhas O. Isolation and characterization of four mouse ribosomal-protein-L18 genes that appear to be processed pseudogenes. Gene [Internet]. 1984;29(1–2):157–66. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021181733&doi=10.1016%2f0378-1119%2884%2990176-8&partnerID=40&md5=53a80f731d5440d7c8de69b2fc28bac9
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BENVENISTY N, SIMCHON EB, COHEN H, MENCHER D, MEYUHAS O, RESHEF L. Control of the Activity of Phosphoertolpyruvate Carboxykinase and the Level of ItsmRNA in Livers of Newborn Rats: Effect of Diabetes, Glucose Load and Glucocorticoids. European Journal of Biochemistry [Internet]. 1983;132(3):663–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0020598290&doi=10.1111%252fj.1432-1033.1983.tb07416.x&partnerID=40&md5=1c373471d74fffa4f97446a1b69c0108
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Faliks D, Meyuhas O. Coordinate regulation of ribosomal protein mRNA level in regenerating rat liver. Study with the corresponding mouse cloned cDNAs. Nucleic Acids Research [Internet]. 1982;10(3):789–801. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0020480134&doi=10.1093%252fnar%252f10.3.789&partnerID=40&md5=f099ab091d638e6d70d6e7f42cd5052d
66.
Geyer PK, Meyuhas O, Perry RP, Johnson LF. Regulation of ribosomal protein mRNA content and translation in growth-stimulated mouse fibroblasts. Molecular and Cellular Biology [Internet]. 1982;2(6):685–93. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0020320668&doi=10.1128%252fMCB.2.6.685&partnerID=40&md5=5ac76158e191fe1437fb031d3757617a
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D’Eustachio P, Meyuhas O, Ruddle F, Perry RP. Chromosomal distribution of ribosomal protein genes in the mouse. Cell [Internet]. 1981;24(2):307–12. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0019522010&doi=10.1016%2f0092-8674%2881%2990320-2&partnerID=40&md5=9e94d09842700c9263ce5c0a14e8a3d6
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Monk RJ, Meyuhas O, Perry RP. Mammals have multiple genes for individual ribosomal proteins. Cell [Internet]. 1981;24(2):301–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0019395010&doi=10.1016%2f0092-8674%2881%2990319-6&partnerID=40&md5=bde3605690582909756a416e25d0c160
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Meyuhas O, Perry RP. Construction and identification of cDNA clones for mouse ribosomal proteins: Application for the study of r-protein gene expression. Gene [Internet]. 1980;10(2):113–29. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0018961141&doi=10.1016%2f0378-1119%2880%2990129-8&partnerID=40&md5=940aee6309a418b2d0b7f0897f8338b9
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Meyuhas O, Perry RP. Relationship between size, stability and abundance of the messenger RNA of mouse L cells. Cell [Internet]. 1979;16(1):139–48. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0018352605&doi=10.1016%2f0092-8674%2879%2990195-8&partnerID=40&md5=60d2fd0e3e41ad1f13e888cdc91836db
71.
Meyuhas O, Reshef L, Gunn JM, Hanson RW, Ballard FJ. Regulation of phosphoenolpyruvate carboxykinase (GTP) in adipose tissue in vivo by glucocorticoids and insulin. The Biochemical journal [Internet]. 1976;158(1):1–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0017307606&doi=10.1042%252fbj1580001&partnerID=40&md5=7deeaf52791c99662059939b795f8c93
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Meyuhas O, Reshef L, Ballard FJ, Hanson RW. The effect of insulin and glucocorticoids on the synthesis and degradation of phosphoenolpyruvate carboxykinase (GTP) in rat adipose tissue cultured in vitro. Biochemical Journal [Internet]. 1976;158(1):9–16. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0017185748&doi=10.1042%252fbj1580009&partnerID=40&md5=03492f86911388e41a9a198376c2bd31
73.
Potash S, Meyuhas O, Reshef L. Proceedings: Increased metabolism of glucose in adipose tissue organ culture. Israel Journal of Medical Sciences [Internet]. 1975;11(11):1181–2. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0016576460&partnerID=40&md5=c04110ab67aac4472cbe6f1d194dff2c
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Meyuhas O, Reshef L. Proceedings: Repression by insulin and corticosteroids of phosphoenolpyruvate carboxykinase synthesis, in rat adipose tissue organ culture. Israel Journal of Medical Sciences [Internet]. 1975;11(11):1181. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0016571218&partnerID=40&md5=2b20ecaf4c2873469ca4a4f5a14f0409
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Gunn JM, Hanson RW, Meyuhas O. Glucorticoids and the regulation of phosphoenolpyruvate carboxykinase (guanosine triphosphate) in the rat. Biochemical Journal [Internet]. 1975;150(2):195–203. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0016594745&doi=10.1042%252fbj1500195&partnerID=40&md5=c372f7870780b2a7cafa3146e639fea8
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Reshef L, Meyuhas O, Boshwitz C, Hanson RW, Ballard FJ. Physiological role and regulation of glyceroneogenesis in rat adipose tissue. Israel Journal of Medical Sciences [Internet]. 1972;8(3):372–81. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0015314679&partnerID=40&md5=f59273219a4d852f94a43230862b754c
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Meyuhas O, Boshwitz Ch, Reshef L. Phosphoenolpyruvate carboxylase decarboxylation catalyzed reaction in cytosol of rat adipose tissue. BBA - Enzymology [Internet]. 1971;250(1):224–37. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0015138433&doi=10.1016%2f0005-2744%2871%2990138-0&partnerID=40&md5=fb91b0f6e8960797f5f34352ff133ec6