The DOI matches its Crossref record; 104 of the 104 references it cites were found in a registry or an index.
The other lives of ribosomal proteins
Open accessAbstract
Despite the fact that ribosomal proteins are the constituents of an organelle that is present in every cell, they show a surprising level of regulation, and several of them have also been shown to have other extra-ribosomal functions, such in replication, transcription, splicing or even ageing. This review provides a comprehensive summary of these important aspects.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Some ribosomal proteins showed much lower abundance, however, supporting the view that they may have nonribosomal functions (Bhavsar et al., 2010).”
From Quantitative Analysis of Fission Yeast Transcriptomes and Proteomes in Proliferating and Quiescent Cells (2012) · cites this paper as Bhavsar et al., 2010
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Lodish, H. F. (1986) · Cited by 5,650
Genes that act downstream of DAF-16 to influence the lifespan of Caenorhabditis elegans
Murphy, C. T., McCarroll, S. A., Bargmann, C. I., Fraser, A., Kamath, R. S., Ahringer, J., Li, H., & Kenyon, C. (2003) · Nature · doi:10.1038/nature01789 · Cited by 2,280
Ribosomal Protein S6 Kinase 1 Signaling Regulates Mammalian Life Span
Selman, C., Tullet, J. M. A., Wieser, D., Irvine, E., Lingard, S. J., Choudhury, A. I., Claret, M., Al-Qassab, H., Carmignac, D., Ramadani, F., et al. (2009) · Science · doi:10.1126/science.1177221 · Cited by 1,120
Influence of TOR kinase on lifespan in C. elegans
Vellai, T., Takacs-Vellai, K., Zhang, Y., Kovacs, A. L., Orosz, L., & Müller, F. (2003) · Nature · doi:10.1038/426620a · Cited by 1,057
Identification of RPS14 as a 5q- syndrome gene by RNA interference screen
Ebert, B. L., Pretz, J. L., Bosco, J., Chang, C. Y., Tamayo, P., Galili, N., Raza, A., Root, D. E., Attar, E. C., Ellis, S. R., et al. (2008) · Nature · doi:10.1038/nature06494 · Cited by 953
Mapping the Genetic Architecture of Gene Expression in Human Liver
Schadt, E. E., Molony, C. M., Chudin, E., Hao, K., Yang, X., Lum, P. Y., Kasarskis, A., Zhang, B., Wang, S. S.-M., Suver, C., et al. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060107 · Cited by 918
The gene encoding ribosomal protein S19 is mutated in Diamond-Blackfan anaemia
Draptchinskaia, N., Gustavsson, P., Andersson, B., Pettersson, M., Willig, T.-N., Dianzani, I., Ball, S., Tchernia, G., Klar, J., Matsson, H., et al. (1999) · Nature Genetics · doi:10.1038/5951 · Cited by 795
How Common Are Extraribosomal Functions of Ribosomal Proteins?
Warner, J. R., & McIntosh, K. B. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.03.006 · Cited by 735
Regulation of p53 Translation and Induction after DNA Damage by Ribosomal Protein L26 and Nucleolin
Takagi, M., Absalon, M. J., McLure, K. G., & Kastan, M. B. (2005) · Cell · doi:10.1016/j.cell.2005.07.034 · Cited by 677
Extraribosomal functions of ribosomal proteins
Wool, I. G. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)20011-8 · Cited by 620
Cited by
Sorted by citations
Marguerat, S., Schmidt, A., Codlin, S., Chen, W., Aebersold, R., & Bähler, J. (2012) · Cell · doi:10.1016/j.cell.2012.09.019 · Cited by 571
The functional diversity of protein lysine methylation
Lanouette, S., Mongeon, V., Figeys, D., & Couture, J. (2014) · Molecular Systems Biology · doi:10.1002/msb.134974 · Cited by 285
Role of ribosomal protein mutations in tumor development (Review)
Goudarzi, K. M., & Lindström, M. S. (2016) · International Journal of Oncology · doi:10.3892/ijo.2016.3387 · Cited by 182
O’Leary, M. N., Schreiber, K. H., Zhang, Y., Duc, A. E., Rao, S., Hale, J. S., Academia, E. C., Shah, S. R., Morton, J., Holstein, C. A., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003708 · Cited by 141
RNA polymerase and the ribosome: the close relationship
McGary, K., & Nudler, E. (2013) · Current Opinion in Microbiology · doi:10.1016/j.mib.2013.01.010 · Cited by 127
Regulation of Ribosomal Proteins on Viral Infection
Li, S. (2019) · Cells · doi:10.3390/cells8050508 · Cited by 110
The role of exosomes in metastasis and progression of melanoma
Gowda, R., Robertson, B. M., Iyer, S., Barry, J., Dinavahi, S. S., & Robertson, G. P. (2020) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2020.101975 · Cited by 95
Cervantes-Salazar, M., Angel-Ambrocio, A. H., Soto-Acosta, R., Bautista‐Carbajal, P., Hurtado-Monzón, A. M., Alcaráz‐Estrada, S. L., Ludert, J. E., & Angel, R. M. D. (2015) · Virology · doi:10.1016/j.virol.2015.05.017 · Cited by 94
Coupled Transcription-Translation in Prokaryotes: An Old Couple With New Surprises
Irastortza‐Olaziregi, M., & Amster‐Choder, O. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.624830 · Cited by 91
Hu, J., & Gao, Z. (2012) · Journal of Applied Mathematics · doi:10.1155/2012/248658 · Cited by 84
Provost, E., Wehner, K. A., Zhong, X., Ashar, F. N., Nguyen, E. T., Green, R., Parsons, M. J., & Leach, S. D. (2012) · Development · doi:10.1242/dev.077107 · Cited by 74
Herpes Simplex Virus: The Hostile Guest That Takes Over Your Home
Banerjee, A., Kulkarni, S., & Mukherjee, A. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00733 · Cited by 62
Ribosomes: The New Role of Ribosomal Proteins as Natural Antimicrobials
Hurtado-Rios, J. J., Carrasco-Navarro, U., Almanza-Pérez, J. C., & Ponce‐Alquicira, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169123 · Cited by 59
Hu, H., Bienefeld, K., Wegener, J., Zautke, F., Hao, Y., Mao, F., Han, B., Fang, Y., Wubie, A. J., & Li, J. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00423 · Cited by 58
Bi, X., van Esse, G. W., Mulki, M. A., Kirschner, G. K., Zhong, J., Simon, R. G., & von Korff, M. (2019) · PLANT PHYSIOLOGY · doi:10.1104/pp.18.01454 · Cited by 51
Adaptive reduction of male gamete number in the selfing plant Arabidopsis thaliana
Tsuchimatsu, T., Kakui, H., Yamazaki, M., Marona, C., Tsutsui, H., Hedhly, A., Meng, D., Sato, Y., Städler, T., Grossniklaus, U., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16679-7 · Cited by 48
Subcellular and regional localization of mRNA translation in midbrain dopamine neurons
Hobson, B. D., Kong, L., Angelo, M. F., Lieberman, O. J., Mosharov, E. V., Herzog, É., Sulzer, D., & Sims, P. A. (2022) · Cell Reports · doi:10.1016/j.celrep.2021.110208 · Cited by 49
Crouzet, M., Claverol, S., Lomenech, A., Sénéchal, C. L., Costaglioli, P., Barthe, C., Garbay, B., Bonneu, M., & Vilain, S. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180341 · Cited by 49
Short, A. K., Thai, C. W., Chen, Y., Kamei, N., Pham, A. L., Birnie, M. T., Bolton, J. L., Mortazavi, A., & Baram, T. Z. (2021) · Biological Psychiatry Global Open Science · doi:10.1016/j.bpsgos.2021.12.006 · Cited by 44
Ribosomal protein S19 is a novel therapeutic agent in inflammatory kidney disease
Lv, J., Huang, X. R., Klug, J., Fröhlich, S., Lacher, P., Xu, A., Meinhardt, A., & Lan, H. Y. (2013) · Clinical Science · doi:10.1042/cs20120526 · Cited by 41
Ribosomal Protein RPL27a Promotes Female Gametophyte Development in a Dose-Dependent Manner
Zsögön, A., Szakonyi, D., Shi, X., & Byrne, M. E. (2014) · PLANT PHYSIOLOGY · doi:10.1104/pp.114.241778 · Cited by 40
Li, C., Ge, M., Chen, D., Sun, T., Jiang, H. L., Xie, Y., Lu, H., Zhang, B., Han, L., Chen, J., et al. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01730 · Cited by 38
Allen, S. L., Bonduriansky, R., & Chenoweth, S. F. (2013) · Genome Biology and Evolution · doi:10.1093/gbe/evt145 · Cited by 37
Jangravi, Z., Tabar, M. S., Mirzaei, M., Parsamatin, P., Vakilian, H., Alikhani, M., Shabani, M., Haynes, P. A., Goodchild, A. K., Gourabi, H., et al. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00333 · Cited by 38
Proteostasis regulated by testis-specific ribosomal protein RPL39L maintains mouse spermatogenesis
Zou, Q., Yang, L., Shi, R., Qi, Y., Zhang, X., & Qi, H. (2021) · iScience · doi:10.1016/j.isci.2021.103396 · Cited by 34
Liu, H., Wang, Z., Tian, L., Qin, Q., Wu, X., Yan, W., & Zeng, Z. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-744 · Cited by 34
Invariable stoichiometry of ribosomal proteins in mouse brain tissues with aging
Amirbeigiarab, S., Kiani, P., Sanchez, A. K. V., Krisp, C., Kazantsev, A., Fester, L., Schlüter, H., & Ignatova, Z. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1912060116 · Cited by 34
Rpl22 Loss Impairs the Development of B Lymphocytes by Activating a p53-Dependent Checkpoint
Fahl, S. P., Harris, B. D., Coffey, F. J., & Wiest, D. L. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1402242 · Cited by 32
Liu, C., Chi, L., Tu, P., Xue, J., Ru, H., & Lü, K. (2019) · Journal of Proteomics · doi:10.1016/j.jprot.2019.01.011 · Cited by 31
Provost, E., Weier, C. A., & Leach, S. D. (2013) · Zebrafish · doi:10.1089/zeb.2013.0884 · Cited by 31
Jiang, P., Hou, Z., Bolin, J. M., Thomson, J., & Stewart, R. (2017) · Toxicological Sciences · doi:10.1093/toxsci/kfx129 · Cited by 27
Miikkulainen, P., Högel, H., Rantanen, K., Suomi, T., Kouvonen, P., Elo, L. L., & Jaakkola, P. (2017) · Cancer & Metabolism · doi:10.1186/s40170-017-0167-y · Cited by 30
Das, S., Shah, P., Baharia, R. K., Tandon, R., Khare, P. S., Sundar, S., Sahasrabuddhe, A. A., Siddiqi, M. I., & Dube, A. (2013) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0002527 · Cited by 29
Root-Bernstein, R. S., & Root‐Bernstein, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20010140 · Cited by 30
The Tumor Suppressor rpl36 Restrains KRAS G12V -Induced Pancreatic Cancer
Provost, E., Bailey, J. M., Aldrugh, S., Liu, S., Iacobuzio–Donahue, C. A., & Leach, S. D. (2014) · Zebrafish · doi:10.1089/zeb.2014.1024 · Cited by 28
Human PDCD2L Is an Export Substrate of CRM1 That Associates with 40S Ribosomal Subunit Precursors
Landry-Voyer, A.-M., Bilodeau, S., Bergeron, D., Dionne, K. L., Port, S. A., Rouleau, C., Boisvert, F., Kehlenbach, R. H., & Bachand, F. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00303-16 · Cited by 28
Vitamin B2(riboflavin) increases drought tolerance ofAgaricus bisporus
Guhr, A., Horn, M. A., & Weig, A. R. (2017) · Mycologia · doi:10.1080/00275514.2017.1414544 · Cited by 27
RNase P protein subunit Rpp29 represses histone H3.3 nucleosome deposition
Newhart, A., Powers, S. L., Shastrula, P. K., Sierra, I., Joo, L. M., Hayden, J. E., Cohen, A. R., & Janicki, S. M. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-02-0099 · Cited by 26
Rerouting of ribosomal proteins into splicing in plant organelles
Wang, C., Fourdin, R., Quadrado, M., Dargel-Graffin, C., Tolleter, D., Macherel, D., & Mireau, H. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2004075117 · Cited by 26
Costes, A., Jang, S. M., de Vanssay, A., Rougeot, J., Bouceba, T., Randsholt, N. B., Gibert, J., Crom, S. L., Mouchel‐Vielh, E., Bloyer, S., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1003006 · Cited by 23
Pawłowski, K., Pires, J., Faulconnier, Y., Chambon, C., Germon, P., Boby, C., & Leroux, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20051156 · Cited by 23
Ribosomal proteins: the missing piece in the inflammation puzzle?
Das, A. S., Basu, A., & Mukhopadhyay, R. (2024) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-024-05050-9 · Cited by 23
Macromolecular assemblies supporting transcription-translation coupling
Webster, M. W., & Weixlbaumer, A. (2021) · Transcription · doi:10.1080/21541264.2021.1981713 · Cited by 22
Deryło, K., Michalec‐Wawiórka, B., Krokowski, D., Wawiórka, L., Hatzoglou, M., & Tchórzewski, M. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.10.002 · Cited by 22
Zafar, A., Jabbar, M., Manzoor, Y., Gulzar, H., Hassan, S. G., Nazir, M. A., Ain-ul-Haq, Mustafa, G., Sahar, R., Masood, A., et al. (2020) · Protein and Peptide Letters · doi:10.2174/0929866527666200110155609 · Cited by 21
Zhang, H., Wang, D., Xie, Z.-X., Zhang, S., Wang, M., & Lin, L. (2015) · Environmental Microbiology · doi:10.1111/1462-2920.12914 · Cited by 18
Sun, W., Zhu, Q., Yan, L., & Shao, F. (2019) · Annals of Translational Medicine · doi:10.21037/atm.2019.11.89 · Cited by 15
Human ribosomal protein L9 is a Bax suppressor that promotes cell survival in yeast
Eid, R., Sheibani, S., Gharib, N., Lapointe, J. F., Horowitz, A., Vali, H., Mandato, C. A., & Greenwood, M. T. (2013) · FEMS Yeast Research · doi:10.1111/1567-1364.12121 · Cited by 15
Li, C., Tong, X., Zuo, W., Luan, Y., Gao, R. C., Han, M., Xiong, G., Gai, T., Hu, H., Dai, F., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-18277-y · Cited by 15
RPL35 promotes neuroblastoma progression via the enhanced aerobic glycolysis.
Wu, W., Yu, N., Li, F., Gao, P., Lin, S., & Zhu, Y. (2021) · PubMed Central · Cited by 15
Sousounis, K., & Tsonis, P. A. (2012) · Human Genomics · doi:10.1186/1479-7364-6-14 · Cited by 12
Self-citationAnalyzing Ribosome Remodeling in Health and Disease
Petelski, A. A., & Slavov, N. (2020) · PROTEOMICS · doi:10.1002/pmic.202000039 · Cited by 13
Protein-Coding Region Derived Small RNA in Exosomes from Influenza A Virus–Infected Cells
Kwaśnik, M., Socha, W., Czech, B., Wasiak, M., Rola, J., & Rożek, W. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24010867 · Cited by 11
UBA80 and UBA52 fine-tune RNF168-dependent histone ubiquitination and DNA repair
Lee, S.-O., Kelliher, J. L., Song, W., Tengler, K., Sarkar, A., Dray, E. V., & Leung, J. W. C. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105043 · Cited by 13
Yarullina, L. G., Kalatskaja, J. N., Tsvetkov, V., Burkhanova, G. F., Yalouskaya, N. A., Rybinskaya, K. I., Заикина, Е. А., Cherepanova, E. A., Hileuskaya, K. S., & Nikalaichuk, V. V. (2024) · Plants · doi:10.3390/plants13162210 · Cited by 10
Identification of coilin interactors reveals coordinated control of Cajal body number and structure
Escayola, D. A., Zhang, C., Nischwitz, E., Schärfen, L., Dörner, K., Straube, K., Kutay, U., Butter, F., & Neugebauer, K. M. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202305081 · Cited by 10
Tian, Y., Babaylova, E. S., Gopanenko, A. V., Tupikin, A. E., Kabilov, M. R., Malygin, A. A., & Karpova, G. G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116174 · Cited by 10
Bolt, E. L., Jenkins, T., Russo, V. M., Ahmed, S., Cavey, J. R., & Cass, S. (2015) · Bioscience Reports · doi:10.1042/bsr20150249 · Cited by 9
Gershman, B. W., Pritchard, C. E., Chaney, K. P., & Ware, V. C. (2020) · Developmental Dynamics · doi:10.1002/dvdy.185 · Cited by 10
In silico analysis of proteins and microRNAs related to human African trypanosomiasis in tsetse fly
Yang, Z., Wang, M., Zeng, X., Wan, A. T., & Tsui, S. K. (2020) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2020.107347 · Cited by 9
Algarabel, M., Fernández-Rubio, C., Musilova, K., Guerrero, J. P., Vacas, A., Larrea, E., & Nguewa, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212592 · Cited by 8
Knockdown of RpL36 in testes impairs spermatogenesis in Drosophila melanogaster
Yang, F., Zong, Q., He, Z. J., Liu, C., & Wang, Y. (2021) · Journal of Experimental Zoology Part B Molecular and Developmental Evolution · doi:10.1002/jez.b.23040 · Cited by 8
Ribosomal proteins in hepatocellular carcinoma: mysterious but promising
Su, Q., Sun, H., Mei, L., Yan, Y., Ji, H., Chang, L., & Wang, L. (2024) · Cell & Bioscience · doi:10.1186/s13578-024-01316-3 · Cited by 9
Molecular cloning and characterization of porcine ribosomal protein L21
Sun, W.-S., Chun, J.-L., Kim, D.-H., Ahn, J. S., Kim, M.-K., Hwang, I., Kwon, D., Hwang, S., & Lee, J.-W. (2017) · Journal of Veterinary Science · doi:10.4142/jvs.2017.18.4.531 · Cited by 7
Guerrieri, A. N., Hattinger, C. M., Marchesini, F., Melloni, M., Serra, M., Ibrahim, T., & Penzo, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212031 · Cited by 6
de Lima, P. M., Vieira, J. C. S., Cavecci, B., Fleuri, L. F., Leite, A. D. L., Buzalaf, M. A. R., Pezzato, L. E., Braga, C. P., & Padilha, P. D. M. (2019) · Biological Trace Element Research · doi:10.1007/s12011-019-01765-9 · Cited by 6
Šimonji, K., Konjević, D., Bujanić, M., Rubić, I., Farkaš, V., Beletić, A. D., Grbavac, L., & Kuleš, J. (2022) · Pathogens · doi:10.3390/pathogens11121503 · Cited by 6
Berloco, M. F., Minervini, C. F., Moschetti, R., Palazzo, A., Viggiano, L., & Marsano, R. M. (2021) · Genes · doi:10.3390/genes12121997 · Cited by 6
Deficiency of ValRS-m Causes Male Infertility in Drosophila melanogaster
Duan, X., Wang, H., Cao, Z. X., Su, N., Wang, Y., & Zheng, Y. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137489 · Cited by 5
Molavi, G., Samadi, N., Hashemzadeh, S., Halimi, M., & Hosseingholi, E. Z. (2020) · Journal of Applied Biomedicine · doi:10.32725/jab.2020.008 · Cited by 5
Tramonti, A., & Saliola, M. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.01.021 · Cited by 5
Morphology and transcriptome differences between the haploid and diploid drones of Apis cerana
Yan, W.-Y., Gan, H., Li, S., Hu, J.-H., Wang, Z., Wu, X., & Zeng, Z. (2016) · Journal of Asia-Pacific Entomology · doi:10.1016/j.aspen.2016.10.010 · Cited by 5
Bunde, T. T., Pedra, A. C. K., de Oliveira, N. R., Dellagostin, O. A., & Bohn, T. L. O. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09950-3 · Cited by 4
Liang, W., Zhang, L., Xu, J.-L., Zhang, S.-Y., Lai, M.-X., Wang, T., Zhang, C.-X., & Shen, X. (2024) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2024.101191 · Cited by 4
Sun, L., Yang, X., Chen, F., Li, R., Li, X., Liu, Z., Gu, Y., Gong, X., Liu, Z., Wei, H., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060689 · Cited by 4
Das, D., Mallick, B., Sinha, S., Ganguli, S., Samanta, D., Banerjee, R., & Roy, D. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2298730 · Cited by 3
Ugo, U. A., Hamzat, M. O., Aisida, S. O., Udoh, I. P., Saha, G. C., Aima Airenobuwa, N. O. S. A., Olawale, A. O., Oluwaseun, A., & Nwaneri, M. G. U. (2024) · Open Access Research Journal of Biology and Pharmacy · doi:10.53022/oarjbp.2024.11.1.0021 · Cited by 3
Li, Z., Yu, X., Xu, R., Zhang, X., Shen, J., & Xu, W. (2025) · Cancer Cell International · doi:10.1186/s12935-025-03866-z · Cited by 4
Grunchec, H., Deraze, J., Dardalhon-Cuménal, D., Ribeiro, V., Costes, A., Dias, K., Bloyer, S., Mouchel‐Vielh, E., Peronnet, F., & Thomassin, H. (2022) · PLoS ONE · doi:10.1371/journal.pone.0273198 · Cited by 3
Бунеева, О. А., Fedchenko, V. I., Kaloshina, S. A., Zavialova, M. G., Zgoda, V. G., & Medvedev, A. E. (2024) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20247003145 · Cited by 3
Maeda, Y. (2015) · Biomolecules · doi:10.3390/biom5010113 · Cited by 3
Qian, J., Xu, L., Yu, W., Gu, X., Zuo, Y., Chen, Y., Xie, F., & Wei, L. (2020) · Cell & Bioscience · doi:10.1186/s13578-020-00463-7 · Cited by 3
Kellogg, R. M., Weber, M. K., Escalante, R. Y., Silva, J. C., & Bodnar, A. G. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1787989 · Cited by 3
Ribosomal Proteins in Cell Biology and Cancer
Zhang, A., Sun, Z., Song, X., Zhou, X., & Li, J. (2026) · MedComm – Oncology · doi:10.1002/mog2.70076 · Cited by 2
Ying, W., Qi, T., Shi, D., Zhang, J., Ye, G., Tian, X., & Wang, Q. (2023) · Indian Journal of Pharmaceutical Education and Research · doi:10.5530/001954641252 · Cited by 2
Бунеева, О. А., Fedchenko, V. I., Kaloshina, S. A., Zavialova, M. G., Zgoda, V. G., & Medvedev, A. E. (2025) · Biomeditsinskaya Khimiya · doi:10.18097/pbmcr1567 · Cited by 1
Schneider, M. C., Vedder, L., Oyiga, B. C., Mathew, B., Schoof, H., Léon, J., & Naz, A. A. (2022) · PLoS ONE · doi:10.1371/journal.pone.0265981 · Cited by 1
Capacity planning. Model behavior.
Moore, S. (2002) · PubMed · Cited by 1
Running title: Transcriptional response to temperature in K. olearia
Pollo, S. M. J., Adebusuyi, A. A., Straub, T. J., Foght, J. M., & Nesbø, C. L. (2016)
The evolution of sex-biased gene expression in Drosophila serrata
Allen, S. L. (2018) · The University of Queensland · doi:10.14264/uql.2018.246
Association Genetics and Local Adaptation of Populus trichocarpa Torr. & Gray
Chhetri, H. B. (2019) · The Research Repository @ WVU (West Virginia University) · doi:10.33915/etd.7478
Translationsinitiationsfaktoren in Haloferax volcanii
Schramm, F. V. (2021) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.62378
Effect of Human microRNA on Dengue Virus Genome: a cross-specie approachPreprint
Deb, A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.11.516157
Effect of Human microRNA on Dengue Virus Genome: a cross-specie approach
-, A. D. (2022) · International Journal For Multidisciplinary Research · doi:10.36948/ijfmr.2022.v04i06.1011
Yu, M. S. C., Chiang, D. M., Reithmair, M., Meidert, A. S., Brandes, F., Schelling, G., Ludwig, C., Meng, C., Kirchner, B., Zenner, C., et al. (2023) · Research Square · doi:10.21203/rs.3.rs-2817092/v1
Zhang, K., Shen, H., Wang, Y., Shen, H., Zhang, C., Zou, X., Yu, Y., Tian, X., & Wang, Y. (2024) · Acta Parasitologica · doi:10.1007/s11686-023-00774-y
Proteomic profiling of intracranial atherosclerotic plaque in the human brainPreprint
Hao, Q., Wang, E., Wang, J., Wu, Z., Crary, J. F., Sharma, S., Thorn, E. L., Elahi, F. M., Zhang, B., & Peng, J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.10.579787
Aslam, S., Aljawdah, H. M. A., Murshed, M., & Serrano, G. E. (2024) · Scientific Reports · doi:10.1038/s41598-024-63555-1
Yarullina, L. G., Цветков, В. О., Kalatskaja, J. N., Burkhanova, G. F., Cherepanova, E. A., Заикина, Е. А., & Yalouskaya, N. A. (2025) · Russian Journal of Plant Physiology · doi:10.1134/s1021443725603027
Metadata
- Authors
- Bhavsar, R. B., Makley, L. N., & Tsonis, P. A.
- Affiliations
- University of Dayton (US)
- Corresponding author
- Tsonis, Panagiotis A
- Venue
- Human Genomics
- Published
- 2010
- Volume
- 4
- Issue
- 5
- Pages
- 327
- ISSN
- 1473-9542 (ISSN-L)
- 1479-7364
- PMC
- PMC3500163
- OpenAlex
- W2145613496
- Cited by
- 107
- References
- 104
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 13 · 2023: 5 · 2022: 8 · 2021: 9 · 2020: 11 · 2019: 11 · 2018: 2 · 2017: 7 · 2016: 6 · 2015: 6 · 2014: 5 · 2013: 8 · 2012: 5
- FWCI
- 0.36
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Human Genomics (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- ribosomal proteins, DNA replication, transcription, RNA splicing, aging
- MeSH terms
- Animals, Gene Expression Regulation, Humans, Ribosomal Proteins, Ribosomes
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review