Cited by 394RNA Research and SplicingNuclear Structure and FunctionRNA modifications and cancer

The DOI matches its Crossref record; 81 of the 81 references it cites were found in a registry or an index.

Biogenesis of small nucleolar ribonucleoproteins

Filipowicz, Witold, Pogačić, Vanda·2002·Current Opinion in Cell Biology

Open this paper in CoChat — free account

Abstract

Eukaryotic cells contain a very complex population of small nucleolar RNAs. They function, as small nucleolar ribonucleoproteins, in pre-ribosomal RNA processing reactions, and also guide methylation and pseudouridylation of ribosomal RNA, spliceosomal small nuclear RNAs, and possibly other cellular RNAs. Synthesis of small nucleolar RNAs frequently follows unusual strategies. Some newly discovered brain-specific small nucleolar RNAs of unknown function are encoded in introns of tandemly repeated units, expression of which is paternally imprinted. Recent studies of the protein components and factors participating in small nucleolar ribonucleoprotein assembly have revealed interesting connections with other classes of cellular ribonucleoproteins such as spliceosomal small nuclear ribonucleoproteins and telomerase. Cajal bodies emerge as nuclear structures important for the biogenesis and function of small nucleolar ribonucleoproteins.

Integrity signals

Registry

Crossref · 10.1016/s0955-0674(02)00334-4

Cites

81 of 81 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

microRNAs
Ambros, V. (2001) · Cell · doi:10.1016/s0092-8674(01)00616-x · Cited by 1,705
Non–coding RNA genes and the modern RNA world
Eddy, S. R. (2001) · Nature Reviews Genetics · doi:10.1038/35103511 · Cited by 1,455
A telomerase component is defective in the human disease dyskeratosis congenita
Mitchell, J. R., Wood, E., & Collins, K. (1999) · Nature · doi:10.1038/990141 · Cited by 1,168
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
X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions
Heiss, N. S., Knight, S. W., Vulliamy, T. J., Klauck, S. M., Wiemann, S., Mason, P. J., Poustka, A., & Dokal, I. (1998) · Nature Genetics · doi:10.1038/ng0598-32 · Cited by 976
The RNA component of telomerase is mutated in autosomal dominant dyskeratosis congenita
Vulliamy, T., Marrone, A., Goldman, F., Dearlove, A., Bessler, M., Mason, P. J., & Dokal, I. (2001) · Nature · doi:10.1038/35096585 · Cited by 960
Ribosome Synthesis in Saccharomyces cerevisiae
Venema, J., & Tollervey, D. W. (1999) · Annual Review of Genetics · doi:10.1146/annurev.genet.33.1.261 · Cited by 748
Genome Organization, Function, and Imprinting in Prader-Willi and Angelman Syndromes
Nicholls, R. D., & Knepper, J. L. (2001) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.2.1.153 · Cited by 625
Functions of the exosome in rRNA, snoRNA and snRNA synthesis
Allmang, C., Kufel, J., Chanfreau, G., Mitchell, P., Petfalski, E., & Tollervey, D. W. (1999) · The EMBO Journal · doi:10.1093/emboj/18.19.5399 · Cited by 618
Secondary Structure of Vertebrate Telomerase RNA
Chen, J.-L., Blasco, M. A., & Greider, C. W. (2000) · Cell · doi:10.1016/s0092-8674(00)80687-x · Cited by 605

Show all 81 references

Sorted by citations

Items 101–200 of 391

Interplay between pre-mRNA splicing and microRNA biogenesis within the supraspliceosome
Agranat-Tamir, L., Shomron, N., Sperling, J. M., & Sperling, R. (2014) · Nucleic Acids Research · doi:10.1093/nar/gkt1413 · Cited by 91
Cotranslational assembly of the yeast SET1C histone methyltransferase complex
Halbach, A., Zhang, H., Wengi, A., Jabłońska, Z., Gruber, I. M. L., Halbeisen, R. E., Dehé, P.-M., Kemmeren, P., Holstege, F. C. P., Géli, V., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.240 · Cited by 96
Guide RNAs with 5′ Caps and Novel Box C/D snoRNA-like Domains for Modification of snRNAs in Metazoa
Tycowski, K. T., Aab, A., & STEITZ, J. A. (2004) · Current Biology · doi:10.1016/j.cub.2004.11.003 · Cited by 96
Dyskerin Overexpression in Human Hepatocellular Carcinoma Is Associated with Advanced Clinical Stage and Poor Patient Prognosis
Liu, B., Zhang, J., Huang, C. L., & Liu, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043147 · Cited by 87
Perturbation of rRNA Synthesis in the bap28 Mutation Leads to Apoptosis Mediated by p53 in the Zebrafish Central Nervous System
Azuma, M., Toyama, R., Laver, E., & Dawid, I. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601892200 · Cited by 90
Npa1p, a Component of Very Early Pre-60S Ribosomal Particles, Associates with a Subset of Small Nucleolar RNPs Required for Peptidyl Transferase Center Modification
Dez, C., Froment, C., Noaillac‐Depeyre, J., Monsarrat, B., Caizergues‐Ferrer, M., & Henry, Y. A. L. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.14.6324-6337.2004 · Cited by 90
The Helicase Has1p Is Required for snoRNA Release from Pre-rRNA
Liang, X., & Fournier, M. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00664-06 · Cited by 90
Functional Association of the Microprocessor Complex with the Spliceosome
Kataoka, N., Fujita, M., & Ohno, M. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00360-09 · Cited by 91
The Cotranscriptional Assembly of snoRNPs Controls the Biosynthesis of H/ACA snoRNAs in Saccharomyces cerevisiae
Ballarino, M., Morlando, M., Pagano, F., Fatica, A., & Bozzoni, I. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5396-5403.2005 · Cited by 85
RNomics in Drosophila melanogaster: identification of 66 candidates for novel non-messenger RNAs
Yuan, G., Klämbt, C., Bachellerie, J., Brosius, J., & Hüttenhofer, A. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt119 · Cited by 85
Small nucleolar RNAs functioning and potential roles in cancer
Thorenoor, N., & Slabý, O. (2014) · Tumor Biology · doi:10.1007/s13277-014-2818-8 · Cited by 88
A Proteomic Screen for Nucleolar SUMO Targets Shows SUMOylation Modulates the Function of Nop5/Nop58
Westman, B. J., Verheggen, C., Hutten, S., Lam, Y. W., Bertrand, É., & Lamond, A. I. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.025 · Cited by 87
Characterization of Saccharomyces cerevisiae Nop17p, a Novel Nop58p-Interacting Protein that is Involved in Pre-rRNA Processing
Gonzales-Zubiate, F. A., Zanchin, N. I. T., da Luz, J. S., & Oliveira, C. C. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.11.071 · Cited by 93
The expanding transcriptome: the genome as the ‘Book of Sand’
Soares, L. M. M., & Valcárcel, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601023 · Cited by 83
Non-Coding RNAs in Psychiatric Disorders and Suicidal Behavior
Yoshino, Y., & Dwivedi, Y. (2020) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2020.543893 · Cited by 85
Efficient and specific knockdown of small non-coding RNAs in mammalian cells and in mice
Liang, X., Vickers, T. A., Guo, S., & Crooke, S. T. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1121 · Cited by 82
RNA editing and regulation ofDrosophila 4f-rnpexpression bysas-10antisense readthrough mRNA transcripts
Peters, N. T., ROHRBACH, J. A., ZALEWSKI, B. A., BYRKETT, C. M., & Vaughn, J. C. (2003) · RNA · doi:10.1261/rna.2120703 · Cited by 86
Noncoding RNA transcripts.
Szymański, M., Barciszewska, M. Z., Żywicki, M., & Barciszewski, J. (2003) · PubMed · Cited by 82
RNomics in Drosophila melanogaster: identification of 66 candidates for novel non-messenger RNAs
Yuan, G. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg361 · Cited by 86
Cotranscriptional Recognition of Human Intronic Box H/ACA snoRNAs Occurs in a Splicing-Independent Manner
Richard, P., Kiss, A. M., Darzacq, X., & Kiss, T. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.7.2540-2549.2006 · Cited by 80
cis - and trans -Acting Determinants of Transcription Termination by Yeast RNA Polymerase II
Steinmetz, E. J., Ng, S. B. H., Cloute, J. P., & Brow, D. A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.7.2688-2696.2006 · Cited by 80
Targeting MYC in cancer therapy: RNA processing offers new opportunities
Koh, C. M., Sabò, A., & Guccione, E. (2016) · BioEssays · doi:10.1002/bies.201500134 · Cited by 86
Constitutive splicing and economies of scale in gene expression
Ding, F., & Elowitz, M. B. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0226-x · Cited by 85
Structural and biochemical basis for misfolded RNA recognition by the Ro autoantigen
Fuchs, G., Stein, A. J., Fu, C., Reinisch, K. M., & Wolin, S. L. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1156 · Cited by 78
Rvb1–Rvb2: essential ATP-dependent helicases for critical complexesThis paper is one of a selection of papers published in this special issue entitled 8th International Conference on AAA Proteins and has undergone the Journal's usual peer review process.
Huen, J., Kakihara, Y., Ugwu, F., Cheung, K. L. Y., Ortega, J., & Houry, W. A. (2010) · Biochemistry and Cell Biology · doi:10.1139/o09-122 · Cited by 81
Sequential 2′-O-Methylation of Archaeal Pre-tRNATrp Nucleotides Is Guided by the Intron-encoded but trans-Acting Box C/D Ribonucleoprotein of Pre-tRNA
Singh, S. K., Gurha, P., Tran, E. J., Maxwell, E. S., & Gupta, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408868200 · Cited by 76
Naf1p is a box H/ACA snoRNP assembly factor
Fatica, A., Dlakić, M., & Tollervey, D. W. (2002) · RNA · doi:10.1017/s1355838202022094 · Cited by 88
A genome-wide analysis of C/D and H/ACA-like small nucleolar RNAs in Trypanosoma brucei reveals a trypanosome-specific pattern of rRNA modification
Liang, X., Uliel, S., Hury, A., Barth, S., Doniger, T., Unger, R., & Michaeli, S. (2005) · RNA · doi:10.1261/rna.7174805 · Cited by 76
The high diversity of snoRNAs in plants: identification and comparative study of 120 snoRNA genes from Oryza sativa
Chen, C.-L. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg373 · Cited by 76
Growth Arrest-Specific Transcript 5 Associated snoRNA Levels Are Related to p53 Expression and DNA Damage in Colorectal Cancer
Krell, J., Frampton, A. E., Mirnezami, R., Harding, V., de Giorgio, A., Roca-Alonso, L., Cohen, P., Ottaviani, S., Colombo, T., Jacob, J., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098561 · Cited by 75
Eukaryotic RNA 5′-End NAD + Capping and DeNADding
Kiledjian, M. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.005 · Cited by 78
Cotranscriptional Recruitment of the Pseudouridylsynthetase Cbf5p and of the RNA Binding Protein Naf1p during H/ACA snoRNP Assembly
Yang, P. K., Hoareau‐Aveilla, C., Froment, C., Monsarrat, B., Henry, Y. A. L., & Chanfreau, G. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.8.3295-3304.2005 · Cited by 87
Profiling of Small Nucleolar RNAs by Next Generation Sequencing: Potential New Players for Breast Cancer Prognosis
Krishnan, P., Ghosh, S., Wang, B., Heyns, M., Graham, K., Mackey, J. R., Kovalchuk, O., & Damaraju, S. (2016) · PLoS ONE · doi:10.1371/journal.pone.0162622 · Cited by 75
Evidence that the AAA+Proteins TIP48 and TIP49 Bridge Interactions between 15.5K and the Related NOP56 and NOP58 Proteins during Box C/D snoRNP Biogenesis
McKeegan, K. S., Debieux, C. M., & Watkins, N. J. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00752-09 · Cited by 74
Immunopurified Small Nucleolar Ribonucleoprotein Particles Pseudouridylate rRNA Independently of Their Association with Phosphorylated Nopp140
Wang, C., Query, C. C., & Meier, U. T. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.24.8457-8466.2002 · Cited by 80
Human Genome and Diseases:�Dyskeratosis congenita
Marrone, A., & Mason, P. J. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s000180300042 · Cited by 76
Annotation of snoRNA abundance across human tissues reveals complex snoRNA-host gene relationships
Fafard-Couture, É., Bergeron, D., Couture, S., Elela, S. A., & Scott, M. S. (2021) · Genome biology · doi:10.1186/s13059-021-02391-2 · Cited by 72
Arabidopsis nucleolar protein database (AtNoPDB)
Brown, J. W. (2004) · Nucleic Acids Research · doi:10.1093/nar/gki052 · Cited by 72
Gene and genon concept: coding versus regulation
Scherrer, K., & Jost, J. (2007) · Theory in Biosciences · doi:10.1007/s12064-007-0012-x · Cited by 75
Regulation of Alternative Splicing by snoRNAsPreprint
Kishore, S., & Stamm, S. (2006) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2006.71.024 · Cited by 71
Nucleolar methyltransferase fibrillarin: Evolution of structure and functions
Shubina, M. Y., Musinova, Y. R., & Sheval, E. V. (2016) · Biochemistry (Moscow) · doi:10.1134/s0006297916090030 · Cited by 78
Role for nsP2 Proteins in the Cessation of Alphavirus Minus-Strand Synthesis by Host Cells
Sawicki, D. L., Perri, S., Polo, J. M., & Sawicki, S. G. (2005) · Journal of Virology · doi:10.1128/jvi.80.1.360-371.2006 · Cited by 68
Splicing noncoding RNAs from the inside out
Yang, L. C. (2015) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1307 · Cited by 66
VRK1 regulates Cajal body dynamics and protects coilin from proteasomal degradation in cell cycle
Cantarero, L., Sanz-García, M., Vinograd-Byk, H., Renbaum, P., Levy‐Lahad, E., & Lazo, P. A. (2015) · Scientific Reports · doi:10.1038/srep10543 · Cited by 61
The nucleolar-related protein Dyskerin pseudouridine synthase 1 (DKC1) predicts poor prognosis in breast cancer
Elsharawy, K. A., Mohammed, O. J., Aleskandarany, M. A., Hyder, A., El-Gammal, H., Abou-Dobara, M. I., Green, A. R., Dalton, L. W., & Rakha, E. A. (2020) · British Journal of Cancer · doi:10.1038/s41416-020-01045-7 · Cited by 62
Guide snoRNAs: Drivers or Passengers in Human Disease?
Deogharia, M., & Majumder, M. (2018) · Biology · doi:10.3390/biology8010001 · Cited by 61
A Stochastic View of Spliceosome Assembly and Recycling in the Nucleus
Rino, J., Carvalho, T., Braga, J., Desterro, J. M. P., Lührmann, R., & Carmo‐Fonseca, M. (2007) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0030201 · Cited by 61
Mechanisms and functions of RNA-guided RNA modification
Yu, Y., Terns, R. M., & Terns, M. P. (2004) · Topics in current genetics · doi:10.1007/b105585 · Cited by 61
Processing and roles of snoRNA-ended long noncoding RNAs
Xing, Y., & Chen, L. (2018) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2018.1508411 · Cited by 60
New clues to the function of the Cajal body
Carmo‐Fonseca, M. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf154 · Cited by 60
Small nucleolar RNAs that guide modification in trypanosomatids: repertoire, targets, genome organisation, and unique functions
Uliel, S., Liang, X., Unger, R., & Michaeli, S. (2004) · International Journal for Parasitology · doi:10.1016/j.ijpara.2003.10.014 · Cited by 59
Cbf5p, the putative pseudouridine synthase of H/ACA-type snoRNPs, can form a complex with Gar1p and Nop10p in absence of Nhp2p and box H/ACA snoRNAs
Henras, A. K., Capeyrou, R., Henry, Y. A. L., & Caizergues‐Ferrer, M. (2004) · RNA · doi:10.1261/rna.7770604 · Cited by 59
NanoPARE: parallel analysis of RNA 5′ ends from low-input RNAPreprint
Schon, M. A., Kellner, M. J., Plotnikova, A., Hofmann, F., & Nodine, M. D. (2018) · Genome Research · doi:10.1101/gr.239202.118 · Cited by 59
Contextual fear conditioning regulates the expression of brain‐specific small nucleolar RNAs in hippocampus
Rogelj, B., Hartmann, C. E. A., Yeo, C. H., Hunt, S. P., & Giese, K.-P. (2003) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2003.03026.x · Cited by 58
Archaeal Pus10 proteins can produce both pseudouridine 54 and 55 in tRNA
Gurha, P., & Gupta, R. (2008) · RNA · doi:10.1261/rna.1276508 · Cited by 58
Dyskeratosis congenita and telomerase
Bessler, M., Wilson, D. B., & Mason, P. J. (2004) · Current Opinion in Pediatrics · doi:10.1097/00008480-200402000-00006 · Cited by 59
A new α‐helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III
Leulliot, N., Quevillon‐Chéruel, S., Graille, M., TILBEURGH, H. V., Leeper, T. C., Godin, K. S., Edwards, T. E., Sigurdsson, S. T., Rozenkrants, N., Nagel, R. J., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600260 · Cited by 58
Stem cells, telomerase and dyskeratosis congenita
Mason, P. J. (2003) · BioEssays · doi:10.1002/bies.10229 · Cited by 58
Circular box C/D RNAs in Pyrococcus furiosus
Starostina, N. G., Marshburn, S., Johnson, L. S., Eddy, S. R., Terns, R. M., & Terns, M. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403520101 · Cited by 57
Telomerase RNA deficiency in peripheral blood mononuclear cells in X-linked dyskeratosis congenita
Wong, J. M. Y., Kyasa, M. J., Hutchins, L. E., & Collins, K. (2004) · Human Genetics · doi:10.1007/s00439-004-1178-7 · Cited by 58
An Evolutionary Perspective of Animal MicroRNAs and Their Targets
Shomron, N., Golan, D., & Hornstein, E. (2009) · BioMed Research International · doi:10.1155/2009/594738 · Cited by 61
The structure of the endoribonuclease XendoU: From small nucleolar RNA processing to severe acute respiratory syndrome coronavirus replication
Renzi, F., Caffarelli, E., Laneve, P., Bozzoni, I., Brunori, M., & Vallone, B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602426103 · Cited by 56
Actively Transcribing RNA Polymerase II Concentrates on Spliced Leader Genes in the Nucleus of Trypanosoma cruzi
Dossin, F. D. M., & Schenkman, S. (2005) · Eukaryotic Cell · doi:10.1128/ec.4.5.960-970.2005 · Cited by 56
In vitro RNP assembly and methylation guide activity of an unusual box C/D RNA, cis-acting archaeal pre-tRNATrp
Bortolin‐Cavaillé, M. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg860 · Cited by 55
CoCo: RNA-seq read assignment correction for nested genes and multimapped reads
Deschamps-Francoeur, G., Boivin, V., Elela, S. A., & Scott, M. S. (2019) · Bioinformatics · doi:10.1093/bioinformatics/btz433 · Cited by 54
The dyskerin ribonucleoprotein complex as an OCT4/SOX2 coactivator in embryonic stem cells
Fong, Y. W., Ho, J. J., Inouye, C. J., & Tjian, R. (2014) · eLife · doi:10.7554/elife.03573 · Cited by 54
Proteomic analysis of heat stress resistance of cucumber leaves when grafted onto Momordica rootstock
Xu, Y., Yuan, Y., Du, N., Wang, Y., Shu, S., Sun, J., & ShiRong, G. (2018) · Horticulture Research · doi:10.1038/s41438-018-0060-z · Cited by 54
Characterization of a Short Isoform of Human Tgs1 Hypermethylase Associating with Small Nucleolar Ribonucleoprotein Core Proteins and Produced by Limited Proteolytic Processing
Girard, C., Verheggen, C., Neel, H., Cammas, A., Vagner, S., Soret, J., Bertrand, É., & Bordonné, R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704209200 · Cited by 53
Identification of differentially expressed non-coding RNAs in embryonic stem cell neural differentiation
Skreka, K., Schafferer, S., Nat, I.-R., Żywicki, M., Salti, A., Apostolova, G., Griehl, M., Rederstorff, M., Dechant, G., & Hüttenhofer, A. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks311 · Cited by 53
Species-specific alternative splicing leads to unique expression of sno-lncRNAs
Zhang, X.-O., Yin, Q.-F., Wang, H., Zhang, Y., Chen, T., Zheng, P., Lu, X., Chen, L., & Yang, L. C. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-287 · Cited by 55
SNORA42 enhances prostate cancer cell viability, migration and EMT and is correlated with prostate cancer poor prognosis
Yi, C., Wan, X., Zhang, Y., Fu, F., Zhao, C., Qin, R., Wu, H., Li, Y., & Huang, Y. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2018.07.009 · Cited by 52
Identification of discrete classes of small nucleolar RNA featuring different ends and RNA binding protein dependency
Deschamps-Francoeur, G., Garneau, D., Dupuis‐Sandoval, F., Roy, A., Frappier, M., Catala, M., Couture, S., Barbe-Marcoux, M., Elela, S. A., & Scott, M. S. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku664 · Cited by 51
Functional Characterization of XendoU, the Endoribonuclease Involved in Small Nucleolar RNA Biosynthesis
Gioia, U., Laneve, P., Dlakić, M., Arceci, M., Bozzoni, I., & Caffarelli, E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501160200 · Cited by 51
Elucidating the Role of H/ACA-like RNAs in trans-Splicing and rRNA Processing via RNA Interference Silencing of the Trypanosoma brucei CBF5 Pseudouridine Synthase
Barth, S., Hury, A., Liang, X., & Michaeli, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503465200 · Cited by 53
Sequence-structure-function relationships of Tgs1, the yeast snRNA/snoRNA cap hypermethylase
Mouaikel, J. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg656 · Cited by 51
Dyskeratosis Congenita: A Disorder of Defective Telomere Maintenance?
Walne, A. J., Marrone, A., & Dokal, I. S. (2005) · International Journal of Hematology · doi:10.1532/ijh97.05067 · Cited by 51
Linear Regression Links Transcriptomic Data and Cellular Raman Spectra
Kobayashi-Kirschvink, K. J., Nakaoka, H., Oda, A., Kamei, K.-I. F., Nosho, K., Fukushima, H., Kanesaki, Y., Yajima, S., Masaki, H., Ohta, K., et al. (2018) · Cell Systems · doi:10.1016/j.cels.2018.05.015 · Cited by 49
An H/ACA guide RNA directs U2 pseudouridylation at two different sites in the branchpoint recognition region in Xenopus oocytes
Zhao, X., Li, Z., Terns, R. M., Terns, M. P., & Yu, Y. (2002) · RNA · doi:10.1017/s1355838202022537 · Cited by 49
Elucidating the Role of C/D snoRNA in rRNA Processing and Modification inTrypanosoma brucei
Barth, S., Shalem, B., Hury, A., Tkacz, I. D., Liang, X., Uliel, S., Myslyuk, I., Doniger, T., Salmon‐Divon, M., Unger, R., et al. (2007) · Eukaryotic Cell · doi:10.1128/ec.00215-07 · Cited by 49
Coupling between snoRNP assembly and 3′ processing controls box C/D snoRNA biosynthesis in yeast
Morlando, M., Ballarino, M., Greco, P., Caffarelli, E., Dichtl, B., & Bozzoni, I. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600254 · Cited by 49
Small nucleolar RNA and its potential role in breast cancer – A comprehensive review
Dsouza, V. L., Adiga, D., Sriharikrishnaa, S., Suresh, P. S., Chatterjee, A., & Kabekkodu, S. P. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188501 · Cited by 48
The gene and the genon concept: a functional and information‐theoretic analysis
Scherrer, K., & Jost, J. (2007) · Molecular Systems Biology · doi:10.1038/msb4100123 · Cited by 48
Expression signature of six‐snoRNA serves as novel non‐invasive biomarker for diagnosis and prognosis prediction of renal clear cell carcinoma
Zhao, Y., Yan, Y., Ma, R., Lv, X., Zhang, L., Wang, J., Zhu, W., Zhao, L., Jiang, L., Zhao, L., et al. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14886 · Cited by 47
SnoRNA U50 Levels Are Regulated by Cell Proliferation and rRNA Transcription
Pacilli, A., Ceccarelli, C., Treré, D., & Montanaro, L. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140714923 · Cited by 46
Transcriptome analysis of skin fibroblasts with dominant negative COL3A1 mutations provides molecular insights into the etiopathology of vascular Ehlers-Danlos syndrome
Chiarelli, N., Carini, G., Zoppi, N., Ritelli, M., & Colombi, M. (2018) · PLOS ONE · doi:10.1371/journal.pone.0191220 · Cited by 45
Nol9 is a novel polynucleotide 5′‐kinase involved in ribosomal RNA processing
Heindl, K., & Martı̂nez, J. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.275 · Cited by 45
Non-Coding RNAs in Brain Tumors, the Contribution of lncRNAs, circRNAs, and snoRNAs to Cancer Development—Their Diagnostic and Therapeutic Potential
Latowska-Lysiak, J., Grabowska, A., Zarębska, Ż., Kuczyński, K., Kuczyńska, B., & Rolle, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197001 · Cited by 44
Tumor‐educated platelet SNORD55 as a potential biomarker for the early diagnosis of non‐small cell lung cancer
Dong, X., Song, X., Ding, S., Yu, M., Shang, X., Wang, K., Chang, M., Xie, L., & Song, X. (2021) · Thoracic Cancer · doi:10.1111/1759-7714.13823 · Cited by 43
Involvement of Nuclear Import and Export Factors in U8 Box C/D snoRNP Biogenesis
Watkins, N. J., Lemm, I., & Lührmann, R. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00516-07 · Cited by 43
Two different mechanisms for tRNA ribose methylation in Archaea: a short survey
Clouet-d’Orval, B., Gaspin, C., & Mougin, A. (2005) · Biochimie · doi:10.1016/j.biochi.2005.02.004 · Cited by 43
Noncoding RNAs of the H/ACA FamilyPreprint
Terns, M. P., & Terns, R. M. (2006) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2006.71.034 · Cited by 46
Non-coding RNAs in immunoregulation and autoimmunity: Technological advances and critical limitations
Kumar, D., Sahoo, S. S., Chauss, D., Kazemian, M., & Afzali, B. (2022) · Journal of Autoimmunity · doi:10.1016/j.jaut.2022.102982 · Cited by 44
Plant U13 orthologues and orphan snoRNAs identified by RNomics of RNA from Arabidopsis nucleoli
Kim, S. H., Spensley, M., Choi, S., Calixto, C. P. G., Pendle, A. F., Koroleva, O., Shaw, P., & Brown, J. W. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp1241 · Cited by 41
Beyond cleaved small RNA targets: unraveling the complexity of plant RNA degradome data
Hou, C., Wu, M., Lu, S.-H., Hsing, Y.-I. C., & Chen, H. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-15 · Cited by 40
Prader-Willi syndrome: reflections on seminal studies and future therapies
Chung, M. S., Langouët, M., Chamberlain, S. J., & Carmichael, G. (2020) · Open Biology · doi:10.1098/rsob.200195 · Cited by 39
Identification and analysis of the minimal promoter activity of a novel noncoding nuclear RNA gene, AncR-1, from the honeybee (Apis mellifera L.)
Sawata, M., Takeuchi, H., & Kubo, T. (2004) · RNA · doi:10.1261/rna.5231504 · Cited by 39
Components of U3 snoRNA-containing Complexes Shuttle between Nuclei and the Cytoplasm and Differentially Localize in Nucleoli: Implications for Assembly and Function
Leary, D. J., Terns, M. P., & Huang, S. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-06-0363 · Cited by 40
Interaction of Saccharomyces Cdc13p with Pol1p, Imp4p, Sir4p and Zds2p is involved in telomere replication, telomere maintenance and cell growth control
Hsu, C.-L. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh203 · Cited by 38
The snoRNA-like lncRNA LNC-SNO49AB drives leukemia by activating the RNA-editing enzyme ADAR1
Huang, W., Sun, Y., Pan, Q., Fang, K., Chen, X., Zeng, Z., Chen, T.-Q., Zhu, S.-X., Huang, L., Luo, X., et al. (2022) · Cell Discovery · doi:10.1038/s41421-022-00460-9 · Cited by 37
Non-coding RNAs in lung cancer
Ricciuti, B., Mecca, C., Crinò, L., Baglivo, S., Cenci, M., & Metro, G. (2014) · Oncoscience · doi:10.18632/oncoscience.98 · Cited by 38

Authors: Filipowicz, W., & Pogačić, V.
Affiliations: Friedrich Miescher Institute (CH)
Corresponding author: Filipowicz, Witold
Venue: Current Opinion in Cell Biology
Publisher: Elsevier BV
Published: 2002-06
Volume: 14
Issue: 3
Pages: 319-327
ISSN: 0955-0674 (ISSN-L)
DOI: 10.1016/s0955-0674(02)00334-4
OpenAlex: W2060678979
Cited by: 394
References: 81
Citations by year: 2026: 3 · 2025: 6 · 2024: 10 · 2023: 4 · 2022: 8 · 2021: 9 · 2020: 12 · 2019: 12 · 2018: 17 · 2017: 9 · 2016: 11 · 2015: 10 · 2014: 18 · 2013: 10 · 2012: 13
FWCI: 2.60
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Current Opinion in Cell Biology (publishedVersion)
PubMed (publishedVersion)
Topics: 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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
Keywords: small nucleolar ribonucleoproteins, pre-rRNA processing, ribosomal RNA methylation, pseudouridylation, small nuclear ribonucleoproteins, telomerase, Cajal bodies, paternal imprinting, ribonucleoprotein assembly
MeSH terms: Animals, Base Sequence, Brain, Cell Nucleolus, Models, Genetic, Nuclear Proteins, Ribonucleoproteins, RNA Processing, Post-Transcriptional, RNA, Small Nucleolar, Coiled Bodies

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

Biogenesis of small nucleolar ribonucleoproteins

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks