Difference between revisions of "Ribosomal Proteins"
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+ | =Minute Loci= | ||
+ | Farnsworth, M. W. (1970). Uptake and incorporation of amino acids in minute mutants of Drosophila. Journal of Experimental Zoology, 175(3), 375-381. | ||
+ | |||
+ | Ferrús, A., & García-Bellido, A. (1977). Minute mosaics caused by early chromosome loss. Wilhelm Roux's archives of developmental biology, 183(4), 337-349. | ||
+ | |||
+ | Lambertsson, A. (1998). The Minute Genes in Drosophila and Their Molecular Functions. In Advances in genetics (Vol. 38, pp. 69-134). Academic Press. | ||
+ | |||
+ | Marygold, S. J., Roote, J., Reuter, G., Lambertsson, A., Ashburner, M., Millburn, G. H., ... & Leevers, S. J. (2007). The ribosomal protein genes and Minute loci of Drosophila melanogaster. Genome biology, 8(10), R216. | ||
+ | |||
+ | Morata, G., & Ripoll, P. (1975). Minutes: mutants of Drosophila autonomously affecting cell division rate. Developmental biology, 42(2), 211-221. | ||
+ | |||
+ | Oliver, E. R., Saunders, T. L., Tarlé, S. A., & Glaser, T. (2004). Ribosomal protein L24 defect in belly spot and tail (Bst), a mouse Minute. Development, 131(16), 3907-3920. | ||
+ | |||
+ | Schultz, J. (1929). The Minute reaction in the development of Drosophila melanogaster. Genetics, 14(4), 366. | ||
+ | |||
+ | Sæbøe-Larssen, S., Lyamouri, M., Merriam, J., Oksvold, M. P., & Lambertsson, A. (1998). Ribosomal protein insufficiency and the minute syndrome in Drosophila: a dose-response relationship. Genetics, 148(3), 1215-1224. | ||
+ | |||
+ | Weijers, D., Franke-van Dijk, M., Vencken, R. J., Quint, A., Hooykaas, P., & Offringa, R. (2001). An Arabidopsis Minute-like phenotype caused by a semi-dominant mutation in a RIBOSOMAL PROTEIN S5 gene. Development, 128(21), 4289-4299. | ||
=Ribosomal Proteins and Cancer= | =Ribosomal Proteins and Cancer= | ||
Line 8: | Line 26: | ||
Artero-Castro, A., Castellvi, J., García, A., Hernández, J., y Cajal, S. R., & LLeonart, M. E. (2011). Expression of the ribosomal proteins Rplp0, Rplp1, and Rplp2 in gynecologic tumors. Human pathology, 42(2), 194-203. | Artero-Castro, A., Castellvi, J., García, A., Hernández, J., y Cajal, S. R., & LLeonart, M. E. (2011). Expression of the ribosomal proteins Rplp0, Rplp1, and Rplp2 in gynecologic tumors. Human pathology, 42(2), 194-203. | ||
+ | |||
+ | Barkić, M., Crnomarković, S., Grabušić, K., Bogetić, I., Panić, L., Tamarut, S., ... & Volarević, S. (2009). The p53 tumor suppressor causes congenital malformations in Rpl24-deficient mice and promotes their survival. Molecular and cellular biology, 29(10), 2489-2504. | ||
+ | |||
+ | Barna, M., Pusic, A., Zollo, O., Costa, M., Kondrashov, N., Rego, E., ... & Ruggero, D. (2008). Suppression of Myc oncogenic activity by ribosomal protein haploinsufficiency. Nature, 456(7224), 971. | ||
Bee, A., Ke, Y., Forootan, S., Lin, K., Beesley, C., Forrest, S. E., & Foster, C. S. (2006). Ribosomal protein l19 is a prognostic marker for human prostate cancer. Clinical Cancer Research, 12(7), 2061-2065. | Bee, A., Ke, Y., Forootan, S., Lin, K., Beesley, C., Forrest, S. E., & Foster, C. S. (2006). Ribosomal protein l19 is a prognostic marker for human prostate cancer. Clinical Cancer Research, 12(7), 2061-2065. | ||
Line 46: | Line 68: | ||
Russo, A., & Russo, G. (2017). Ribosomal proteins control or bypass p53 during nucleolar stress. International journal of molecular sciences, 18(1), 140. | Russo, A., & Russo, G. (2017). Ribosomal proteins control or bypass p53 during nucleolar stress. International journal of molecular sciences, 18(1), 140. | ||
+ | |||
+ | Russo, A., Pagliara, V., Albano, F., Esposito, D., Sagar, V., Loreni, F., ... & Russo, G. (2016). Regulatory role of rpL3 in cell response to nucleolar stress induced by Act D in tumor cells lacking functional p53. Cell Cycle, 15(1), 41-51. | ||
+ | |||
+ | Teng, T., Mercer, C. A., Hexley, P., Thomas, G., & Fumagalli, S. (2013). Loss of tumor suppressor RPL5/RPL11 does not induce cell-cycle arrest, but impedes proliferation due to reduced ribosome content and translation capacity. Molecular and Cellular Biology, MCB-01174. | ||
Warner, J. R., & McIntosh, K. B. (2009). How common are extraribosomal functions of ribosomal proteins?. Molecular cell, 34(1), 3-11. | Warner, J. R., & McIntosh, K. B. (2009). How common are extraribosomal functions of ribosomal proteins?. Molecular cell, 34(1), 3-11. | ||
Line 58: | Line 84: | ||
Zhao, Y., Tan, M., Liu, X., Xiong, X., & Sun, Y. (2018). Inactivation of ribosomal protein S27-like confers radiosensitivity via the Mdm2-p53 and Mdm2–MRN–ATM axes. Cell death & disease, 9(2), 145. | Zhao, Y., Tan, M., Liu, X., Xiong, X., & Sun, Y. (2018). Inactivation of ribosomal protein S27-like confers radiosensitivity via the Mdm2-p53 and Mdm2–MRN–ATM axes. Cell death & disease, 9(2), 145. | ||
+ | |||
+ | ZHENG, S. E., LIN, F., SHEN, Z., TANG, L. N., & YAO, Y. (2009). Expression of ribosomal protein L7a (RPL7A) in human osteosarcoma and its clinical significance [J]. China Oncology, 2, 008. | ||
=Ribosomal Protein Structure= | =Ribosomal Protein Structure= | ||
Line 70: | Line 98: | ||
Byrne, M. E. (2009). A role for the ribosome in development. Trends in plant science, 14(9), 512-519. | Byrne, M. E. (2009). A role for the ribosome in development. Trends in plant science, 14(9), 512-519. | ||
+ | |||
+ | Choesmel, V., Bacqueville, D., Rouquette, J., Noaillac-Depeyre, J., Fribourg, S., Crétien, A., ... & Gleizes, P. E. (2007). Impaired ribosome biogenesis in Diamond-Blackfan anemia. Blood, 109(3), 1275-1283. | ||
Cole, J. R., Chai, B., Marsh, T. L., Farris, R. J., Wang, Q., Kulam, S. A., ... & Tiedje, J. M. (2003). The Ribosomal Database Project (RDP-II): previewing a new autoaligner that allows regular updates and the new prokaryotic taxonomy. Nucleic acids research, 31(1), 442-443. | Cole, J. R., Chai, B., Marsh, T. L., Farris, R. J., Wang, Q., Kulam, S. A., ... & Tiedje, J. M. (2003). The Ribosomal Database Project (RDP-II): previewing a new autoaligner that allows regular updates and the new prokaryotic taxonomy. Nucleic acids research, 31(1), 442-443. |
Latest revision as of 21:58, 10 August 2018
Minute Loci
Farnsworth, M. W. (1970). Uptake and incorporation of amino acids in minute mutants of Drosophila. Journal of Experimental Zoology, 175(3), 375-381.
Ferrús, A., & García-Bellido, A. (1977). Minute mosaics caused by early chromosome loss. Wilhelm Roux's archives of developmental biology, 183(4), 337-349.
Lambertsson, A. (1998). The Minute Genes in Drosophila and Their Molecular Functions. In Advances in genetics (Vol. 38, pp. 69-134). Academic Press.
Marygold, S. J., Roote, J., Reuter, G., Lambertsson, A., Ashburner, M., Millburn, G. H., ... & Leevers, S. J. (2007). The ribosomal protein genes and Minute loci of Drosophila melanogaster. Genome biology, 8(10), R216.
Morata, G., & Ripoll, P. (1975). Minutes: mutants of Drosophila autonomously affecting cell division rate. Developmental biology, 42(2), 211-221.
Oliver, E. R., Saunders, T. L., Tarlé, S. A., & Glaser, T. (2004). Ribosomal protein L24 defect in belly spot and tail (Bst), a mouse Minute. Development, 131(16), 3907-3920.
Schultz, J. (1929). The Minute reaction in the development of Drosophila melanogaster. Genetics, 14(4), 366.
Sæbøe-Larssen, S., Lyamouri, M., Merriam, J., Oksvold, M. P., & Lambertsson, A. (1998). Ribosomal protein insufficiency and the minute syndrome in Drosophila: a dose-response relationship. Genetics, 148(3), 1215-1224.
Weijers, D., Franke-van Dijk, M., Vencken, R. J., Quint, A., Hooykaas, P., & Offringa, R. (2001). An Arabidopsis Minute-like phenotype caused by a semi-dominant mutation in a RIBOSOMAL PROTEIN S5 gene. Development, 128(21), 4289-4299.
Ribosomal Proteins and Cancer
Amsterdam, A., Sadler, K. C., Lai, K., Farrington, S., Bronson, R. T., Lees, J. A., & Hopkins, N. (2004). Many ribosomal protein genes are cancer genes in zebrafish. PLoS biology, 2(5), e139.
Ajore, R., Raiser, D., McConkey, M., Jöud, M., Boidol, B., Mar, B., ... & Ebert, B. L. (2017). Deletion of ribosomal protein genes is a common vulnerability in human cancer, especially in concert with TP53 mutations. EMBO molecular medicine, 9(4), 498-507.
Artero-Castro, A., Castellvi, J., García, A., Hernández, J., y Cajal, S. R., & LLeonart, M. E. (2011). Expression of the ribosomal proteins Rplp0, Rplp1, and Rplp2 in gynecologic tumors. Human pathology, 42(2), 194-203.
Barkić, M., Crnomarković, S., Grabušić, K., Bogetić, I., Panić, L., Tamarut, S., ... & Volarević, S. (2009). The p53 tumor suppressor causes congenital malformations in Rpl24-deficient mice and promotes their survival. Molecular and cellular biology, 29(10), 2489-2504.
Barna, M., Pusic, A., Zollo, O., Costa, M., Kondrashov, N., Rego, E., ... & Ruggero, D. (2008). Suppression of Myc oncogenic activity by ribosomal protein haploinsufficiency. Nature, 456(7224), 971.
Bee, A., Ke, Y., Forootan, S., Lin, K., Beesley, C., Forrest, S. E., & Foster, C. S. (2006). Ribosomal protein l19 is a prognostic marker for human prostate cancer. Clinical Cancer Research, 12(7), 2061-2065.
Bhattacharya, A., McIntosh, K. B., Willis, I. M., & Warner, J. R. (2010). Why Dom34 stimulates growth of cells with defects of 40S ribosomal subunit biosynthesis. Molecular and cellular biology, 30(23), 5562-5571.
Caldarola, S., De Stefano, M. C., Amaldi, F., & Loreni, F. (2009). Synthesis and function of ribosomal proteins–fading models and new perspectives. The FEBS journal, 276(12), 3199-3210.
Deisenroth, C., & Zhang, Y. (2010). Ribosome biogenesis surveillance: probing the ribosomal protein-Mdm2-p53 pathway. Oncogene, 29(30), 4253.
Derenzini, M., Montanaro, L., & Trere, D. (2017). Ribosome biogenesis and cancer. Acta histochemica, 119(3), 190-197.
Dolezal, J. M., Dash, A. P., & Prochownik, E. V. (2018). Diagnostic and prognostic implications of ribosomal protein transcript expression patterns in human cancers. BMC cancer, 18(1), 275.
Donati, G., Bertoni, S., Brighenti, E., Vici, M., Trere, D., Volarevic, S., ... & Derenzini, M. (2011). The balance between rRNA and ribosomal protein synthesis up-and downregulates the tumour suppressor p53 in mammalian cells. Oncogene, 30(29), 3274.
Fancello, L., Kampen, K. R., Hofman, I. J., Verbeeck, J., & De Keersmaecker, K. (2017). The ribosomal protein gene RPL5 is a haploinsufficient tumor suppressor in multiple cancer types. Oncotarget, 8(9), 14462.
Han, S. H., Chung, J. H., Kim, J., Kim, K. S., & Han, Y. S. (2017). New role of human ribosomal protein S3: Regulation of cell cycle via phosphorylation by cyclin‑dependent kinase 2. Oncology letters, 13(5), 3681-3687.
Hannan, K. M., Sanij, E., Hein, N., Hannan, R. D., & Pearson, R. B. (2011). Signaling to the ribosome in cancer—It is more than just mTORC1. IUBMB life, 63(2), 79-85.
Jin, A., Itahana, K., O'Keefe, K., & Zhang, Y. (2004). Inhibition of HDM2 and activation of p53 by ribosomal protein L23. Molecular and cellular biology, 24(17), 7669-7680.
Kuang, J., Li, Q. Y., Fan, F., Shen, N. J., Zhan, Y. J., Tang, Z. H., & Yu, W. L. (2017). Overexpression of the X-linked ribosomal protein S4 predicts poor prognosis in patients with intrahepatic cholangiocarcinoma. Oncology letters, 14(1), 41-46.
Lai, K., Amsterdam, A., Farrington, S., Bronson, R. T., Hopkins, N., & Lees, J. A. (2009). Many ribosomal protein mutations are associated with growth impairment and tumor predisposition in zebrafish. Developmental dynamics: an official publication of the American Association of Anatomists, 238(1), 76-85.
Lee, C. H., Kiparaki, M., Blanco, J., Folgado, V., Ji, Z., Kumar, A., ... & Baker, N. E. (2018). A Regulatory Response to Ribosomal Protein Mutations Controls Translation, Growth, and Cell Competition. Developmental Cell.
Macias, E., Jin, A., Deisenroth, C., Bhat, K., Mao, H., Lindström, M. S., & Zhang, Y. (2010). An ARF-independent c-MYC-activated tumor suppression pathway mediated by ribosomal protein-Mdm2 Interaction. Cancer cell, 18(3), 231-243.
Markiewski, M. M., Vadrevu, S. K., Sharma, S. K., Chintala, N. K., Ghouse, S., Cho, J. H., ... & Karbowniczek, M. (2017). The ribosomal protein S19 suppresses antitumor immune responses via the complement C5a receptor 1. The Journal of Immunology, 1602057.
Naora, H., & Naora, H. (1999). Involvement of ribosomal proteins in regulating cell growth and apoptosis: translational modulation or recruitment for extraribosomal activity?. Immunology and cell biology, 77(3), 197-205.
Qi, Y., Li, X., Chang, C., Xu, F., He, Q., Zhao, Y., & Wu, L. (2017). Ribosomal protein L23 negatively regulates cellular apoptosis via the RPL23/Miz-1/c-Myc circuit in higher-risk myelodysplastic syndrome. Scientific reports, 7(1), 2323.
Russo, A., & Russo, G. (2017). Ribosomal proteins control or bypass p53 during nucleolar stress. International journal of molecular sciences, 18(1), 140.
Russo, A., Pagliara, V., Albano, F., Esposito, D., Sagar, V., Loreni, F., ... & Russo, G. (2016). Regulatory role of rpL3 in cell response to nucleolar stress induced by Act D in tumor cells lacking functional p53. Cell Cycle, 15(1), 41-51.
Teng, T., Mercer, C. A., Hexley, P., Thomas, G., & Fumagalli, S. (2013). Loss of tumor suppressor RPL5/RPL11 does not induce cell-cycle arrest, but impedes proliferation due to reduced ribosome content and translation capacity. Molecular and Cellular Biology, MCB-01174.
Warner, J. R., & McIntosh, K. B. (2009). How common are extraribosomal functions of ribosomal proteins?. Molecular cell, 34(1), 3-11.
Wool, I. G. (1996). Extraribosomal functions of ribosomal proteins. Trends in biochemical sciences, 21(5), 164-165.
Xie, X., & Guan, K. L. (2011). The ribosome and TORC2: collaborators for cell growth. Cell, 144(5), 640-642.
Xie, X., Guo, P., Yu, H., Wang, Y., & Chen, G. (2018). Ribosomal proteins: insight into molecular roles and functions in hepatocellular carcinoma. Oncogene, 37(3), 277. [1]
Zhang, Y., & Lu, H. (2009). Signaling to p53: ribosomal proteins find their way. Cancer cell, 16(5), 369-377.
Zhao, Y., Tan, M., Liu, X., Xiong, X., & Sun, Y. (2018). Inactivation of ribosomal protein S27-like confers radiosensitivity via the Mdm2-p53 and Mdm2–MRN–ATM axes. Cell death & disease, 9(2), 145.
ZHENG, S. E., LIN, F., SHEN, Z., TANG, L. N., & YAO, Y. (2009). Expression of ribosomal protein L7a (RPL7A) in human osteosarcoma and its clinical significance [J]. China Oncology, 2, 008.
Ribosomal Protein Structure
Chan, Y. L., Lin, A., McNally, J., Peleg, D., Meyuhas, O., & Wool, I. G. (1987). 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, 262(3), 1111-1115.
Edmondson, S. P., Turri, J., Smith, K., Clark, A., & Shriver, J. W. (2009). Structure, stability, and flexibility of ribosomal protein L14e from Sulfolobus solfataricus. Biochemistry, 48(24), 5553-5562.
Unclassified
Barakat, A., Szick-Miranda, K., Chang, F., Guyot, R., Blanc, G., Cooke, R., ... & Bailey-Serres, J. (2001). The organization of cytoplasmic ribosomal protein genes in the Arabidopsis genome. Plant physiology, 127(2), 398-415.
Byrne, M. E. (2009). A role for the ribosome in development. Trends in plant science, 14(9), 512-519.
Choesmel, V., Bacqueville, D., Rouquette, J., Noaillac-Depeyre, J., Fribourg, S., Crétien, A., ... & Gleizes, P. E. (2007). Impaired ribosome biogenesis in Diamond-Blackfan anemia. Blood, 109(3), 1275-1283.
Cole, J. R., Chai, B., Marsh, T. L., Farris, R. J., Wang, Q., Kulam, S. A., ... & Tiedje, J. M. (2003). The Ribosomal Database Project (RDP-II): previewing a new autoaligner that allows regular updates and the new prokaryotic taxonomy. Nucleic acids research, 31(1), 442-443.
Creff, A., Sormani, R., & Desnos, T. (2010). The two Arabidopsis RPS6 genes, encoding for cytoplasmic ribosomal proteins S6, are functionally equivalent. Plant molecular biology, 73(4-5), 533-546.
Davies, B., & Fried, M. (1995). The L19 ribosomal protein gene (RPL19): Gene organization, chromosomal mapping, and novel promoter region. Genomics, 25(2), 372-380.
Enerly, E., Larsson, J., & Lambertsson, A. (2003). Silencing the Drosophila ribosomal protein L14 gene using targeted RNA interference causes distinct somatic anomalies. Gene, 320, 41-48.
Horiguchi, G., Mollá‐Morales, A., Pérez‐Pérez, J. M., Kojima, K., Robles, P., Ponce, M. R., ... & Tsukaya, H. (2011). Differential contributions of ribosomal protein genes to Arabidopsis thaliana leaf development. The Plant Journal, 65(5), 724-736.
Huber, F. M., & Hoelz, A. (2017). Molecular basis for protection of ribosomal protein L4 from cellular degradation. Nature communications, 8, 14354.
Ishii, K., Washio, T., Uechi, T., Yoshihama, M., Kenmochi, N., & Tomita, M. (2006). Characteristics and clustering of human ribosomal protein genes. BMC genomics, 7(1), 37.
Kenmochi, N., Yoshihama, M., Higa, S., & Tanaka, T. (2000). The human ribosomal protein L6 gene in a critical region for Noonan syndrome. Journal of human genetics, 45(5), 290.
Kim, D. U., Hayles, J., Kim, D., Wood, V., Park, H. O., Won, M., ... & Han, S. (2010). Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces pombe. Nature biotechnology, 28(6), 617.
Lewis, M. S., Pikaard, D. J., Nasrallah, M., Doelling, J. H., & Pikaard, C. S. (2007). Locus-specific ribosomal RNA gene silencing in nucleolar dominance. PLoS One, 2(8), e815.
Merret, R., Carpenier, M. C., Favory, J. J., Picart, C., Descombin, J., Bousquet-Antonelli, C., ... & Charng, Y. Y. (2017). Heat-shock protein HSP101 affects the release of ribosomal protein mRNAs for recovery after heat shock. Plant physiology, pp-00269.
Paredes, S., Branco, A. T., Hartl, D. L., Maggert, K. A., & Lemos, B. (2011). Ribosomal DNA deletions modulate genome-wide gene expression:“rDNA–sensitive” genes and natural variation. PLoS genetics, 7(4), e1001376.
Perry, R. P. (2007). Balanced production of ribosomal proteins. Gene, 401(1), 1-3.
Rosado, A., & Raikhel, N. V. (2010). Application of the gene dosage balance hypothesis to auxin-related ribosomal mutants in Arabidopsis. Plant signaling & behavior, 5(4), 450-452.
Spahn, C. M., Beckmann, R., Eswar, N., Penczek, P. A., Sali, A., Blobel, G., & Frank, J. (2001). Structure of the 80S ribosome from Saccharomyces cerevisiae—tRNA-ribosome and subunit-subunit interactions. Cell, 107(3), 373-386.
Topisirovic, I., & Sonenberg, N. (2011). Translational control by the eukaryotic ribosome. Cell, 145(3), 333-334.
Uechi, T., Nakajima, Y., Nakao, A., Torihara, H., Chakraborty, A., Inoue, K., & Kenmochi, N. (2006). Ribosomal protein gene knockdown causes developmental defects in zebrafish. PloS one, 1(1), e37.
Voutev, R., Killian, D. J., Ahn, J. H., & Hubbard, E. J. A. (2006). Alterations in ribosome biogenesis cause specific defects in C. elegans hermaphrodite gonadogenesis. Developmental biology, 298(1), 45-58.
Weinstein, L. B., & Steitz, J. A. (1999). Guided tours: from precursor snoRNA to functional snoRNP. Current opinion in cell biology, 11(3), 378-384.
Zhang, Z., Harrison, P., & Gerstein, M. (2002). Identification and analysis of over 2000 ribosomal protein pseudogenes in the human genome. Genome research, 12(10), 1466-1482.