The nucleolus
Open accessAbstract
When cells are observed by phase contrast microscopy, nucleoli are among the most conspicuous structures. The nucleolus was formally described between 1835 and 1839, but it was another century before it was discovered to be associated with a specific chromosomal locus, thus defining it as a cytogenetic entity. Nucleoli were first isolated in the 1950s, from starfish oocytes. Then, in the early 1960s, a boomlet of studies led to one of the epochal discoveries in the modern era of genetics and cell biology: that the nucleolus is the site of ribosomal RNA synthesis and nascent ribosome assembly. This epistemologically repositioned the nucleolus as not merely an aspect of nuclear anatomy but rather as a cytological manifestation of gene action-a major heuristic advance. Indeed, the finding that the nucleolus is the seat of ribosome production constitutes one of the most vivid confluences of form and function in the history of cell biology. This account presents the nucleolus in both historical and contemporary perspectives. The modern era has brought the unanticipated discovery that the nucleolus is plurifunctional, constituting a paradigm shift.
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
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?
Multiplexed immunofluorescence and FISH can visualize whether the entire nucleolar assembly line is expanding or a specific sub-compartment is bottlenecked.
“By simultaneously tagging Pol I (initiation), fibrillarin (processing in the DFC), and nucleophosmin (assembly in the GC), researchers can visualize whether the entire nucleolar assembly line is expanding or if a specific sub-compartment is bottlenecked [79,80].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [79]
In “A QUADRIPARTITE NUCLEOLUS, OR MORE?” (page unavailable), the paper reports dual-color in situ hybridization that revealed distinct RNA distributions within the granular component. It also identifies fibrillarin as an rRNA-modifying enzyme in the dense fibrillar component. Our copy does not describe simultaneous Pol I, fibrillarin, and nucleophosmin tagging or establish that such imaging can distinguish overall expansion from a sub-compartment bottleneck. (LLM, conf=0.83)
Experimental — accuracy not yet measuredRigorous optimization for human muscle tissue autofluorescence mitigation and the high technological barrier of super-resolution platforms create significant infrastructural limitations, leaving the literature fragmented.
“However, the rigorous optimization required for human muscle tissue autofluorescence mitigation, combined with the high technological barrier of super-resolution platforms, creates significant infrastructural limitations, leaving the literature fragmented [78,79].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [79]
The passages in “The Nucleolus Is Neither as Static nor as Compact as First Thought” discuss fluorescence methods for studying nucleolar proteins, not autofluorescence mitigation in human muscle tissue. A search for super-resolution platforms and technological barriers likewise found no passage addressing infrastructural limitations or a fragmented literature. Page numbers are unavailable in our copy. (LLM, conf=0.78)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Alberts, B., Johnson, A., Lewis, J. H., Morgan, D. O., RAFF, M. C., Roberts, K. J., & Walter, P. (2017) · W.W. Norton eBooks · doi:10.1201/9781315735368 · Cited by 7,937 · see citing works
Boisvert, F., van Koningsbruggen, S., Navascués, J., & Lamond, A. (2007) · Nature reviews. Molecular cell biology · doi:10.1038/nrm2184 · Cited by 1,581 · see citing works
High mobility of proteins in the mammalian cell nucleus
Phair, R. D., & Misteli, T. (2000) · Nature · doi:10.1038/35007077 · Cited by 1,212 · see citing works
Directed Proteomic Analysis of the Human Nucleolus
Andersen, J., Lyon, C. E., Fox, A. H., Leung, A. K. L., Lam, Y. W., Steen, H., Mann, M., & Lamond, A. I. (2002) · Current Biology · doi:10.1016/s0960-9822(01)00650-9 · Cited by 1,024 · see citing works
Nucleolar Arf sequesters Mdm2 and activates p53
Weber, J. D., Taylor, L. J., Roussel, M. F., Sherr, C. J., & Bar-Sagi, D. (1999) · Nature Cell Biology · doi:10.1038/8991 · Cited by 940 · see citing works
Visualization of nucleolar genes
Miller, O. L., & Beatty, B. R. (1969) · Science · doi:10.1126/science.164.3882.955 · Cited by 876 · see citing works
Rubbi, C. P., & Milner, J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg579 · Cited by 811 · see citing works
Specific Gene Amplification in Oocytes
Brown, D. D., & Dawid, I. B. (1968) · Science · doi:10.1126/science.160.3825.272 · Cited by 809 · see citing works
Bachellerie, J., Cavaillé, J., & Hüttenhofer, A. (2002) · Biochimie · doi:10.1016/s0300-9084(02)01402-5 · Cited by 669 · see citing works
Pederson, T. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.17.3871 · Cited by 536 · see citing works
Self-citationABSENCE OF RIBOSOMAL RNA SYNTHESIS IN THE ANUCLEOLATE MUTANT OF XENOPUS LAEVIS
Brown, D. D., & Gurdon, J. B. (1964) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.51.1.139 · Cited by 498 · see citing works
Functional Proteomic Analysis of Human Nucleolus
Scherl, A., Couté, Y., Déon, C., Callé, A., Kindbeiter, K., Sanchez, J., Greco, A., Hochstrasser, D. F., & Diaz, J. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-05-0271 · Cited by 480 · see citing works
The U3 small nucleolar ribonucleoprotein functions in the first step of preribosomal RNA processing
Kass, S., Tyc, K., STEITZ, J. A., & Sollner-Webb, B. (1990) · Cell · doi:10.1016/0092-8674(90)90338-f · Cited by 451 · see citing works
A nucleolar mechanism controlling cell proliferation in stem cells and cancer cellsPreprint
Tsai, R. Y. L., & McKay, R. D. G. (2002) · Genes & Development · doi:10.1101/gad.55671 · Cited by 449 · see citing works
Fatica, A., & Tollervey, D. W. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00336-8 · Cited by 446 · see citing works
Small RNAs derived from snoRNAs
Taft, R. J., Glazov, E. A., Lassmann, T., Hayashizaki, Y., Carninci, P., & Mattick, J. S. (2009) · RNA · doi:10.1261/rna.1528909 · Cited by 436 · see citing works
Accelerated Aging and Nucleolar Fragmentation in Yeast <i>sgs1</i> Mutants
Sinclair, D. A., Mills, K., & Guarente, L. (1997) · Science · doi:10.1126/science.277.5330.1313 · Cited by 401 · see citing works
The nucleolus: an old factory with unexpected capabilities
Olson, M. O. J., Olson, M. O. J., Dundr, M., et al. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01738-4 · Cited by 398 · see citing works
Structure and function of the nucleolus
Scheer, U., & Hock, R. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)80054-4 · Cited by 393 · see citing works
A viral assembly factor promotes AAV2 capsid formation in the nucleolus
Sonntag, F., Schmidt, K., & Kleinschmidt, J. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001673107 · Cited by 392 · see citing works
Differential synthesis of the genes for ribosomal RNA during amphibian oögenesis.
Gall, J. G. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.60.2.553 · Cited by 383 · see citing works
Analysis of Nucleolar Protein Dynamics Reveals the Nuclear Degradation of Ribosomal Proteins
Lam, Y. W., Lamond, A. I., Mann, M., & Andersen, J. S. (2007) · Current Biology · doi:10.1016/j.cub.2007.03.064 · Cited by 369 · see citing works
Proteomic Analysis of theArabidopsisNucleolus Suggests Novel Nucleolar Functions
Pendle, A. F., Clark, G. P., Boon, R. A., Lewandowska, D., Lam, Y. W., Andersen, J., Mann, M., Lamond, A. I., Brown, J. W., & Shaw, P. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-09-0791 · Cited by 367 · see citing works
Intergenic Transcripts Regulate the Epigenetic State of rRNA Genes
Mayer, C., Schmitz, K., Li, J., Grummt, I., & Santoro, R. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.028 · Cited by 327 · see citing works
Chen, D., & Huang, S. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.1.169 · Cited by 323 · see citing works
Ghetti, A., Piñol-Roma, S., Michael, W. M., Morandi, C., & Dreyfuss, G. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.14.3671 · Cited by 311 · see citing works
Politz, J. C. R., BROWNE, E. S., Wolf, D. E., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6043 · Cited by 277 · see citing works
Handwerger, K. E., Cordero, J. A., & Gall, J. G. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0742 · Cited by 256 · see citing works
Ribosome biogenesis: of knobs and RNA processing
Granneman, S. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.03.016 · Cited by 232 · see citing works
Structure and function of the nucleolus in the spotlight
Raška, I., Shaw, P., & Cmarko, D. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.04.008 · Cited by 224 · see citing works
Conventional and nonconventional roles of the nucleolus
Olson, M. O. J., Hingorani, K., & Szebeni, A. (2002) · International review of cytology · doi:10.1016/s0074-7696(02)19014-0 · Cited by 214 · see citing works
Nucleolar localization of the Werner syndrome protein in human cells
Marciniak, R. A., Lombard, D. B., Johnson, F. B., & Guarente, L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.12.6887 · Cited by 210 · see citing works
The nucleolus: the magician’s hat for cell cycle tricks
Visintin, R., & Amon, A. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00102-2 · Cited by 196 · see citing works
Signal recognition particle components in the nucleolus
Politz, J. C. R., Yarovoi, S. V., Kilroy, S. M., Gowda, K., Zwieb, C. W., & Pederson, T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.1.55 · Cited by 188 · see citing works
Self-citationMicroRNAs with a nucleolar location
Politz, J. C. R., Hogan, E. M., & Pederson, T. (2009) · RNA · doi:10.1261/rna.1470409 · Cited by 183 · see citing works
Self-citationMatera, A. G. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.129.5.1181 · Cited by 171 · see citing works
Cajal bodies and the nucleolus are required for a plant virus systemic infection
Kim, S. H., Ryabov, E. V., Kalinina, N. O., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601674 · Cited by 162 · see citing works
Earley, K. W., Pontvianne, F., Wierzbicki, A. T., Blevins, T., Tucker, S., Costa‐Nunes, P., Pontes, O., & Pikaard, C. S. (2010) · Genes & Development · doi:10.1101/gad.1914110 · Cited by 161 · see citing works
Nascent ribosomes from HeLa cells.
Warner, J. R., & Soeiro, R. (1967) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.58.5.1984 · Cited by 157 · see citing works
Prieto, J.-L., & McStay, B. (2007) · Genes & Development · doi:10.1101/gad.436707 · Cited by 157 · see citing works
Ribosomal DNA contributes to global chromatin regulation
Paredes, S., & Maggert, K. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906811106 · Cited by 156 · see citing works
Localization of signal recognition particle RNA in the nucleolus of mammalian cells
Jacobson, M. R., & Pederson, T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.14.7981 · Cited by 155 · see citing works
Self-citationA multistep, GTP-driven mechanism controlling the dynamic cycling of nucleostemin
Tsai, R. Y. L., & McKay, R. D. G. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200409053 · Cited by 155 · see citing works
Gene expression profiling in Werner syndrome closely resembles that of normal aging
Kyng, K. J., May, A., Kølvraa, S., & Bohr, V. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2130723100 · Cited by 153 · see citing works
Calvet, J. P., & Pederson, T. (1981) · Cell · doi:10.1016/0092-8674(81)90205-1 · Cited by 149 · see citing works
Self-citationIn search of nonribosomal nucleolar protein function and regulation
Pederson, T., & Tsai, R. Y. L. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200812014 · Cited by 147 · see citing works
Self-citationPolitz, J. C. R., Zhang, F., & Pederson, T. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609466103 · Cited by 147 · see citing works
Self-citationGroßhans, H., Deinert, K., Hurt, E., & Simos, G. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.4.745 · Cited by 139 · see citing works
Koberna, K., Malínský, J., Pliss, A., Mašata, M., Večeřová, J., Fialová, M., Bednář, J., & Raška, I. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200202007 · Cited by 138 · see citing works
Bioinformatic analysis of the nucleolus
Leung, A. K. L., Andersen, J., Mann, M., et al. (2003) · Biochemical Journal · doi:10.1042/bj20031169 · Cited by 133 · see citing works
Emerging concepts of nucleolar assembly
Hernandez‐Verdun, D., Roussel, P., & Gébrane‐Younès, J. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.11.2265 · Cited by 131 · see citing works
Localization of pre-messenger RNA at discrete nuclear sites.
Wang, J., Cao, L. G., Wang, Y. L., et al. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.16.7391 · Cited by 130 · see citing works
Werner protein recruits DNA polymerase δ to the nucleolus
Szekely, A. M., Chen, Y.-H., Zhang, C., Oshima, J., & Weissman, S. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.21.11365 · Cited by 128 · see citing works
The Nucleolus and the Four Ribonucleoproteins of Translation
Pederson, T., & Politz, J. C. R. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.6.1091 · Cited by 125 · see citing works
Self-citationRegulatory RNAs derived from transfer RNA?
Pederson, T. (2010) · RNA · doi:10.1261/rna.2266510 · Cited by 121 · see citing works
Self-citationSantoro, R., Schmitz, K., Sandoval, J., & Grummt, I. (2009) · EMBO Reports · doi:10.1038/embor.2009.254 · Cited by 117 · see citing works
Characterization of ribosomal precursor particles from HeLa cell nucleoli
Kumar, A., & Warner, J. R. (1972) · Journal of Molecular Biology · doi:10.1016/0022-2836(72)90372-5 · Cited by 114 · see citing works
RIBOSOME PRECURSOR PARTICLES IN NUCLEOLI
Liau, M. C., & Perry, R. P. (1969) · The Journal of Cell Biology · doi:10.1083/jcb.42.1.272 · Cited by 112 · see citing works
A nucleolar TAR decoy inhibitor of HIV-1 replication
Michienzi, A., Li, S. X., Zaia, J. A., & Rossi, J. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212229599 · Cited by 110 · see citing works
Jacobson, M. R., Cao, L. G., Wang, Y. L., et al. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.6.1649 · Cited by 107 · see citing works
Depletion of the Nucleolar Protein Nucleostemin Causes G1 Cell Cycle Arrest via the p53 Pathway
Ma, H., & Pederson, T. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-03-0244 · Cited by 106 · see citing works
Self-citationLink between aging and the nucleolusPreprint
Guarente, L. (1997) · Genes & Development · doi:10.1101/gad.11.19.2449 · Cited by 105 · see citing works
Use of caged fluorochromes to track macromolecular movement in living cells
Politz, J. C. R. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01585-8 · Cited by 103 · see citing works
Protein Mobility within the Nucleus—What Are the Right Moves?
Pederson, T. (2001) · Cell · doi:10.1016/s0092-8674(01)00258-6 · Cited by 103 · see citing works
Self-citationNuclear domains of the RNA subunit of RNase P
Jacobson, M. R., Cao, L. G., Taneja, K. L., et al. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.7.829 · Cited by 101 · see citing works
Growth Factors in the Nucleolus?
Pederson, T. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.279 · Cited by 98 · see citing works
Self-citationKim, S. H., Koroleva, O., Lewandowska, D., Pendle, A. F., Clark, G. P., Simpson, C. G., Shaw, P., & Brown, J. W. S. (2009) · The Plant Cell · doi:10.1105/tpc.109.067736 · Cited by 97 · see citing works
Potential Roles for Ubiquitin and the Proteasome during Ribosome Biogenesis
Stavreva, D. A., Kawasaki, M., Dundr, M., Koberna, K., Müller, W. G., Tsujimura-Takahashi, T., Komatsu, W., Hayano, T., Isobe, T., Raška, I., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02227-05 · Cited by 96 · see citing works
Mdm2 facilitates the association of p53 with the proteasome
Kulikov, R., Letienne, J., Kaur, M., Grossman, S. R., Arts, J., & Blattner, C. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911716107 · Cited by 94 · see citing works
Leung, A. K. L., & Lamond, A. I. (2003) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukaryotgeneexpr.v13.i1.40 · Cited by 93 · see citing works
Nucleolar Proteins Suppress Caenorhabditis elegans Innate Immunity by Inhibiting p53/CEP-1
Fuhrman, L. E., Goel, A., Smith, J. P., Shianna, K. V., & Aballay, A. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000657 · Cited by 92 · see citing works
A Nonribosomal Landscape in the Nucleolus Revealed by the Stem Cell Protein Nucleostemin
Politz, J. C. R., Polena, I., Trask, I., et al. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-02-0106 · Cited by 91 · see citing works
Maggio, R., Siekevitz, P., & Palade, G. E. (1963) · The Journal of Cell Biology · doi:10.1083/jcb.18.2.293 · Cited by 88 · see citing works
Fichelson, P., Moch, C., Ivanovitch, K., Martin, C. A., Sidor, C., Lepesant, J., Bellaı̈che, Y., & Huynh, J. (2009) · Nature Cell Biology · doi:10.1038/ncb1874 · Cited by 87 · see citing works
The Isolation and Chemical Properties of the Nucleoli of Starfish Oocytes
Vincent, W. S. (1952) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.38.2.139 · Cited by 87 · see citing works
Review: Perinucleolar Structures
Huang, S. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4247 · Cited by 84 · see citing works
Nucleolar trafficking is essential for nuclear export of intronless herpesvirus mRNA
Boyne, J. R., & Whitehouse, A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604890103 · Cited by 83 · see citing works
Diffusion-based Transport of Nascent Ribosomes in the Nucleus
Politz, J. C. R., Tuft, R. A., & Pederson, T. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-06-0395 · Cited by 82 · see citing works
Self-citationOldies but goldies: searching for Christmas trees within the nucleolar architecture
Raška, I. (2003) · Trends in Cell Biology · doi:10.1016/j.tcb.2003.08.003 · Cited by 81 · see citing works
A nucleolar targeting sequence in the Werner syndrome protein resides within residues 949-1092
von Kobbe, C., & Bohr, V. A. (2002) · Journal of Cell Science · doi:10.1242/jcs.00076 · Cited by 80 · see citing works
Diffusional protein transport within the nucleus: a message in the medium
Pederson, T. (2000) · Nature Cell Biology · doi:10.1038/35010501 · Cited by 77 · see citing works
Self-citationReversible disassembly of somatic nucleoli by the germ cell proteins FRGY2a and FRGY2b
Gonda, K., Fowler, J., Katoku-Kikyo, N., et al. (2003) · Nature Cell Biology · doi:10.1038/ncb939 · Cited by 76 · see citing works
Nucleolar release of Hand1 acts as a molecular switch to determine cell fate
Martindill, D. M. J., Risebro, C. A., Smart, N., et al. (2007) · Nature Cell Biology · doi:10.1038/ncb1633 · Cited by 74 · see citing works
Ciufo, L. F., & Brown, J. D. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00743-0 · Cited by 69 · see citing works
Wang, C., Politz, J. C. R., Pederson, T., et al. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-12-0818 · Cited by 68 · see citing works
Self-citationThe Perinucleolar CompartmentPreprint
Pollock, C. B., & Huang, S. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000679 · Cited by 67 · see citing works
Net Results of Nucleolar Dynamics
Garcia, S. N., & Pillus, L. (1999) · Cell · doi:10.1016/s0092-8674(00)80794-1 · Cited by 66 · see citing works
Nucleostemin: a multiplex regulator of cell-cycle progression
Ma, H., & Pederson, T. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.09.003 · Cited by 63 · see citing works
Self-citationPolitz, J. C. R., Lewandowski, L. B., & Pederson, T. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200208037 · Cited by 56 · see citing works
Self-citationRelationship between protein synthesis and ribosome assembly in HeLa cells
Pederson, T., & Kumar, A. (1971) · Journal of Molecular Biology · doi:10.1016/0022-2836(71)90070-2 · Cited by 52 · see citing works
Self-citationPseudo-NORs: A novel model for studying nucleoli
Prieto, J.-L., & McStay, B. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.07.004 · Cited by 48 · see citing works
Dynamics of coilin in Cajal bodies of the Xenopus germinal vesicle
Deryusheva, S., & Gall, J. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401106101 · Cited by 43 · see citing works
Sommerville, J., Brumwell, C. L., Politz, J. C. R., et al. (2005) · Journal of Cell Science · doi:10.1242/jcs.01726 · Cited by 38 · see citing works
A 7-methylguanosine cap commits U3 and U8 small nuclear RNAs to the nucleolar localization pathway
Jacobson, M. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.3.756 · Cited by 33 · see citing works
Going in GTP cycles in the nucleolus
Misteli, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412038 · Cited by 28 · see citing works
Nucleophosmin Is a Binding Partner of Nucleostemin in Human Osteosarcoma Cells
Ma, H., & Pederson, T. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-02-0128 · Cited by 28 · see citing works
Self-citationFluorescent RNA cytochemistry: tracking gene transcripts in living cells
Pederson, T. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.5.1013 · Cited by 27 · see citing works
Self-citationSingle ovalbumin molecules exploring nucleoplasm and nucleoli of living cell nuclei
Speil, J., & Kubitscheck, U. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.10.010 · Cited by 24 · see citing works
Proteomics of the nucleolus: more proteins, more functions?
Pederson, T. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02063-7 · Cited by 23 · see citing works
Self-citationCosta‐Nunes, P., Pontes, O., Preuss, S. B., & Pikaard, C. S. (2010) · Nucleus · doi:10.4161/nucl.1.3.11741 · Cited by 23 · see citing works
Non-ribosomal nucleolar proteins in HeLa cells
Soeiro, R., & Basile, C. (1973) · Journal of Molecular Biology · doi:10.1016/0022-2836(73)90402-6 · Cited by 19 · see citing works
Comparative cytological studies with especial regard to the morphology of the nucleolus
Montgomery, T. H. (1898) · doi:10.5962/bhl.title.6592 · Cited by 19 · see citing works
Costa‐Nunes, P., Pontes, O., Preuss, S. B., & Pikaard, C. S. (2010) · Nucleus · doi:10.4161/nucl.11741 · Cited by 17 · see citing works
Cytologically "compact" nuclear domains
Pederson, T. (2010) · The Nucleus · doi:10.4161/nucl.1.5.13056 · Cited by 16 · see citing works
Self-citationSpatial link between nucleoli and expression of the Zac1 gene
Royo, F., Paz, N., Espinosa, L., et al. (2009) · Chromosoma · doi:10.1007/s00412-009-0229-1 · Cited by 13 · see citing works
Pederson, T. (2007) · The FASEB Journal · doi:10.1096/fj.07-8766hyp · Cited by 12 · see citing works
Self-citationA nucleolar disappearing act in somatic cloning
Misteli, T. (2003) · Nature Cell Biology · doi:10.1038/ncb0303-183 · Cited by 12 · see citing works
Ciufo, L. F., & Brown, J. D. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00841-1 · Cited by 9 · see citing works
Nucleolus: Structure and Function
Perry, R. P. (1966) · Science · doi:10.1126/science.153.3732.214 · Cited by 8 · see citing works
Fléchon, J. E. (2006) · Humana Press eBooks · doi:10.1385/1-59745-005-7:225 · Cited by 5 · see citing works
Protein Mobility within the Nucleus—What Are the Right Moves?
Pederson, T. (2001) · Cell · doi:10.1016/s0092-8674(02)01455-1 · Cited by 5 · see citing works
Self-citationPotential Roles for Ubiquitin and the Proteasome during Ribosome Biogenesis
(2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01146-06 · Cited by 4 · see citing works
Richter, J. D., & Fallon, J. R. (2007) · Nature Neuroscience · doi:10.1038/nn0407-399 · Cited by 3 · see citing works
Photoactivation-Based Labeling and In Vivo Tracking of RNA Molecules in the NucleusPreprint
Politz, J. C. R., Tuft, R. A., & Pederson, T. (2006) · Cold Spring Harbor Protocols · doi:10.1101/pdb.prot4600 · Cited by 3 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 3
- Harris H. 1974. Nucleus and Cytoplasm 3rd edition. Claren- don Press, Oxford.
- Lewin B. 1980. Gene Expression. Volume 2. Eukaryotic Chro- mosomes. 2nd edition. John Wiley & Sons, New York.
- Vincent WS, Miller OL. 1966. International symposium on the nucleolus. Its structure and function. Montevideo, Uruguay. J Natl Cancer Inst Monogr 23: 1-610.
Cited by
Sorted by citations
Higher-Order Inter-chromosomal Hubs Shape 3D Genome Organization in the Nucleus
Quinodoz, S. A., Ollikainen, N., Tabak, B., Palla, A., Schmidt, J. M., Detmar, E., Lai, M. M., Shishkin, A. A., Bhat, P., Takei, Y., et al. (2018) · Cell · doi:10.1016/j.cell.2018.05.024 · Cited by 892 · see citing works
Long-Range Chromatin Interactions
Dekker, J., & Misteli, T. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a019356 · Cited by 255 · see citing works
Earley, L. F., Powers, J. M., Adachi, K., Baumgart, J. T., Meyer, N. L., Xie, Q., Chapman, M. S., & Nakai, H. (2017) · Journal of Virology · doi:10.1128/jvi.01980-16 · Cited by 108 · see citing works
Transgenerational dynamics of rDNA copy number in drosophila male germline stem cells
Lu, K. L., Nelson, J. O., Watase, G. J., Warsinger-Pepe, N., & Yamashita, Y. M. (2018) · eLife · doi:10.7554/elife.32421 · Cited by 77 · see citing works
Tau liquid–liquid phase separation: At the crossroads of tau physiology and tauopathy
Islam, M., Shen, F., Regmi, D., Petersen, K., Karim, M. R. U., & Du, D. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.30853 · Cited by 28 · see citing works
Early nucleolar disorganization in Dictyostelium cell death
Luciani, M. F., Song, Y., Sahrane, A., Kosta, A., & Golstein, P. (2017) · Cell Death & Disease · doi:10.1038/cddis.2016.444 · Cited by 7 · see citing works
Muñoz López, M., López-Gil, J. F., Ramírez de la piscina Viúdez, X., Baz-Valle, E., & Tornero Aguilera, J. F. (2026) · Cells · doi:10.3390/cells15111041 · Cited by 1 · see citing works
“By simultaneously tagging Pol I (initiation), fib-rillarin (processing in the DFC), and nucleophosmin (assembly in the GC), researchers can visualize whether the entire nucleolar assembly line is expanding or if a specific sub-compartment is bottlenecked [79,80].”
- Authors
- Pederson, T.
- Affiliations
- University of Massachusetts Chan Medical School (US)
- Corresponding author
- Pederson, T.
- ORCID
- Pederson, T.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2010-11-24
- Volume
- 3
- Issue
- 3
- Pages
- a000638-a000638
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC3039934
- OpenAlex
- W4231439871
- Cited by
- 455
- References
- 114
- Citations by year
- 2026: 36 · 2025: 43 · 2024: 50 · 2023: 45 · 2022: 38 · 2021: 46 · 2020: 33 · 2019: 36 · 2018: 18 · 2017: 17 · 2016: 33 · 2015: 15 · 2014: 16 · 2013: 18 · 2012: 7
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation (0445841)
- National Institutes of Health (5r01gm021595-25)
- National Institute of General Medical Sciences (R01GM060551, R01 GM-60551, R01 GM-21595)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- nucleolus, history of cell biology, ribosomal RNA synthesis, ribosome assembly
- MeSH terms
- Cell Cycle, Cell Nucleolus, Cell Biology, RNA, Messenger, RNA, Ribosomal, Virus Replication, Signal Recognition Particle, History, 20th Century, History, 21st Century
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