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A Human Telomerase Holoenzyme Protein Required for Cajal Body Localization and Telomere Synthesis
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Telomerase is a ribonucleoprotein (RNP) complex that synthesizes telomere repeats in tissue progenitor cells and cancer cells. Active human telomerase consists of at least three principal subunits, including the telomerase reverse transcriptase, the telomerase RNA (TERC), and dyskerin. Here, we identify a holoenzyme subunit, TCAB1 (telomerase Cajal body protein 1), that is notably enriched in Cajal bodies, nuclear sites of RNP processing that are important for telomerase function. TCAB1 associates with active telomerase enzyme, established telomerase components, and small Cajal body RNAs that are involved in modifying splicing RNAs. Depletion of TCAB1 by using RNA interference prevents TERC from associating with Cajal bodies, disrupts telomerase-telomere association, and abrogates telomere synthesis by telomerase. Thus, TCAB1 controls telomerase trafficking and is required for telomere synthesis in human cancer cells.
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“TCAB1 (also known as WDR79) is a WD40-repeat containing protein that associates with dyskerin and binds the CAB box in scaRNAs (46,47).”
From Telomeres and telomerase in cancer (2010) · cites this paper as [46]
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Cites
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
Non-coding RNAs: lessons from the small nuclear and small nucleolar RNAs
Matera, A. G., Terns, R. M., & Terns, M. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2124 · Cited by 877
Self-citationThe POT1-TPP1 telomere complex is a telomerase processivity factor.
Wang, F., Podell, E. R., Zaug, A. J., Yang, Y., Baciu, P., Cech, T. R., & Lei, M. (2007) · Nature · doi:10.1038/nature05454 · Cited by 704
Protein Composition of Catalytically Active Human Telomerase from Immortal Cells
Cohen, S. B., Graham, M. E., Lovrecz, G. O., Bache, N., Robinson, P. J., & Reddel, R. R. (2007) · Science · doi:10.1126/science.1138596 · Cited by 669
TPP1 is a homologue of ciliate TEBP-β and interacts with POT1 to recruit telomerase
Xin, H., Liu, D., Wan, M., Safari, A., Kim, H., Sun, W., O’Connor, M. S., & Songyang, Z. (2007) · Nature · doi:10.1038/nature05469 · Cited by 518
Cell Cycle-regulated Trafficking of Human Telomerase to Telomeres
Tomlinson, R. L., Ziegler, T. D., Supakorndej, T., Terns, R. M., & Terns, M. P. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-09-0903 · Cited by 339
Self-citationVenteicher, A. S., Meng, Z., Mason, P. J., Veenstra, T. D., & Artandi, S. E. (2008) · Cell · doi:10.1016/j.cell.2008.01.019 · Cited by 329
Self-citationHuman telomerase RNA and box H/ACA scaRNAs share a common Cajal body–specific localization signal
Jády, B. E., Bertrand, É., & Kiss, T. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200310138 · Cited by 287
The biogenesis and regulation of telomerase holoenzymes
Collins, K. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1961 · Cited by 287
The many facets of H/ACA ribonucleoproteins
Meier, U. T. (2005) · Chromosoma · doi:10.1007/s00412-005-0333-9 · Cited by 281
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The Noncoding RNA Revolution—Trashing Old Rules to Forge New Ones
Cech, T. R., & Steitz, J. A. (2014) · Cell · doi:10.1016/j.cell.2014.03.008 · Cited by 2,524
Genomic Maps of Long Noncoding RNA Occupancy Reveal Principles of RNA-Chromatin Interactions
Chu, C., Qu, K., Zhong, F. L., Artandi, S. E., & Chang, H. Y. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.027 · Cited by 1,293
Self-citationTelomeres: protecting chromosomes against genome instability
O’Sullivan, R. J., & Karlseder, J. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2848 · Cited by 1,043
Armanios, M., & Blackburn, E. H. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3246 · Cited by 982
Telomeres and telomerase in cancer
Artandi, S. E., & DePinho, R. A. (2010) · Carcinogenesis · doi:10.1093/carcin/bgp268 · Cited by 823
Self-citationRoles of telomeres and telomerase in cancer, and advances in telomerase-targeted therapies
Jafri, M. A., Ansari, S. A., Alqahtani, M. H., & Shay, J. W. (2016) · Genome Medicine · doi:10.1186/s13073-016-0324-x · Cited by 716
An RNA-dependent RNA polymerase formed by TERT and the RMRP RNA
Maida, Y., Yasukawa, M., Furuuchi, M., Lassmann, T., Possemato, R., Okamoto, N., Kasim, V., Hayashizaki, Y., Hahn, W. C., & Masutomi, K. (2009) · Nature · doi:10.1038/nature08283 · Cited by 384
Finding the end: recruitment of telomerase to telomeres
Nandakumar, J., & Cech, T. R. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3505 · Cited by 401
Regulation of human telomerase in homeostasis and disease
Roake, C. M., & Artandi, S. E. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0234-z · Cited by 356
Self-citationTelomerase: An RNP Enzyme Synthesizes DNAPreprint
Blackburn, E. H., & Collins, K. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003558 · Cited by 333
Telomeres and Telomere Length: A General Overview
Srinivas, N., Rachakonda, P. S., & Kumar, R. (2020) · Cancers · doi:10.3390/cancers12030558 · Cited by 336
Human telomerase: biogenesis, trafficking, recruitment, and activationPreprint
Schmidt, J. C., & Cech, T. R. (2015) · Genes & Development · doi:10.1101/gad.263863.115 · Cited by 309
Diverse role of survival motor neuron protein
Singh, R. N., Howell, M. D., Ottesen, E. W., & Singh, N. N. (2017) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2016.12.008 · Cited by 325
TPP1 OB-Fold Domain Controls Telomere Maintenance by Recruiting Telomerase to Chromosome Ends
Zhong, F. L., Batista, L. F. Z., Freund, A., Pech, M. F., Venteicher, A. S., & Artandi, S. E. (2012) · Cell · doi:10.1016/j.cell.2012.07.012 · Cited by 308
Self-citationRNA pseudouridylation: new insights into an old modification
Ge, J., & Yu, Y. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.01.002 · Cited by 285
The Cajal Body and Histone Locus BodyPreprint
Nizami, Z. F., Deryusheva, S., & Gall, J. G. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000653 · Cited by 276
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Kiss, T., Fayet-Lebaron, E., & Jády, B. E. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.032 · Cited by 285
Disruption of telomerase trafficking by TCAB1 mutation causes dyskeratosis congenita
Zhong, F., Savage, S. A., Shkreli, M., Giri, N., Jessop, L., Myers, T., Chen, R., Alter, B. P., & Artandi, S. E. (2011) · Genes & Development · doi:10.1101/gad.2006411 · Cited by 262
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Self-citationThe genetics and clinical manifestations of telomere biology disorders
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Targeting telomerase for cancer therapy
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Abreu, E. B., Aritonovska, E., Reichenbach, P., Cristofari, G., Culp, B. R., Terns, R. M., Lingner, J., & Terns, M. P. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00240-10 · Cited by 258
Self-citationTERT promoter mutations in cancer development
Heidenreich, B., Rachakonda, P. S., Hemminki, K., & Kumar, R. (2014) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2013.11.005 · Cited by 238
Genetics of human telomere biology disorders
Revy, P., Kannengiesser, C., & Bertuch, A. A. (2022) · Nature Reviews Genetics · doi:10.1038/s41576-022-00527-z · Cited by 250
Cryo-EM structure of substrate-bound human telomerase holoenzyme
Nguyen, T. H. D., Tam, J., Wu, R. A., Greber, B. J., Toso, D. B., Nogales, E., & Collins, K. (2018) · Nature · doi:10.1038/s41586-018-0062-x · Cited by 244
Structural biology of telomeres and telomerase
Smith, E. M., Pendlebury, D. F., & Nandakumar, J. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03369-x · Cited by 239
Telomerase Mechanism of Telomere Synthesis
Wu, R. A., Upton, H. E., Vogan, J. M., & Collins, K. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045019 · Cited by 215
A Conserved WD40 Protein Binds the Cajal Body Localization Signal of scaRNP Particles
Tycowski, K. T., Shu, M.-D., Kukoyi, A., & Steitz, J. A. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.020 · Cited by 212
Stewart, J. A., Fedor‐Chaiken, M., Wang, F., & Price, C. M. (2011) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2011.08.011 · Cited by 217
Ballew, B. J., & Savage, S. A. (2013) · Expert Review of Hematology · doi:10.1586/ehm.13.23 · Cited by 214
Structure of human telomerase holoenzyme with bound telomeric DNA
Ghanim, G. E., Fountain, A. J., van Roon, A. M., Rangan, R., Das, R., Collins, K., & Nguyen, T. H. D. (2021) · Nature · doi:10.1038/s41586-021-03415-4 · Cited by 198
Assembly and trafficking of box C/D and H/ACA snoRNPs
Massenet, S., Bertrand, É., & Verheggen, C. (2016) · RNA Biology · doi:10.1080/15476286.2016.1243646 · Cited by 221
TERT promoter mutations in telomere biology
Heidenreich, B., & Kumar, R. (2016) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2016.11.002 · Cited by 205
Schober, H., Ferreira, H. C., Kalck, V., Gehlen, L. R., & Gasser, S. M. (2009) · Genes & Development · doi:10.1101/gad.1787509 · Cited by 189
Nuclear Bodies: Random Aggregates of Sticky Proteins or Crucibles of Macromolecular Assembly?
Matera, A. G., Izaguire-Sierra, M., Praveen, K., & Rajendra, T. K. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.10.017 · Cited by 193
Live Cell Imaging Reveals the Dynamics of Telomerase Recruitment to Telomeres
Schmidt, J. C., Zaug, A. J., & Cech, T. R. (2016) · Cell · doi:10.1016/j.cell.2016.07.033 · Cited by 183
Cajal bodies: where form meets function
Machyna, M., Heyn, P. C., & Neugebauer, K. M. (2012) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1139 · Cited by 185
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Wyatt, H. D. M., West, S. C., & Beattie, T. L. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq370 · Cited by 190
Poly(A)-specific ribonuclease (PARN) mediates 3′-end maturation of the telomerase RNA component
Moon, D. H., Segal, M., Boyraz, B., Guinan, E. C., Hofmann, I., Cahan, P., Tai, A., & Agarwal, S. (2015) · Nature Genetics · doi:10.1038/ng.3423 · Cited by 192
Telomerase gene mutations are associated with cirrhosis formation
Hartmann, D., Srivastava, U., Thaler, M., Kleinhans, K. N., N'Kontchou, G., Scheffold, A., Bauer, K., Kratzer, R. F., Kloos, N., Katz, S.-F., et al. (2011) · Hepatology · doi:10.1002/hep.24217 · Cited by 173
Biogenesis of telomerase ribonucleoproteins
Egan, E. D., & Collins, K. (2012) · RNA · doi:10.1261/rna.034629.112 · Cited by 182
Niewisch, M. R., & Savage, S. A. (2019) · Expert Review of Hematology · doi:10.1080/17474086.2019.1662720 · Cited by 189
Nuclear bodies: multifunctional companions of the genome
Dundr, M. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.03.010 · Cited by 172
The molecular genetics of the telomere biology disorders
Bertuch, A. A. (2015) · RNA Biology · doi:10.1080/15476286.2015.1094596 · Cited by 173
A pathophysiological view of the long non-coding RNA world
Gesualdo, F. D., Capaccioli, S., & Lulli, M. (2014) · Oncotarget · doi:10.18632/oncotarget.2770 · Cited by 169
Cajal bodies are linked to genome conformation
Wang, Q., Sawyer, I. A., Sung, M.-H., Sturgill, D., Shevtsov, S. P., Pegoraro, G., Hakim, O., Baek, S., Hager, G. L., & Dundr, M. (2016) · Nature Communications · doi:10.1038/ncomms10966 · Cited by 164
Healthy aging and disease: role for telomere biology?
Zhu, H., Belcher, M. D., & van der Harst, P. (2011) · Clinical Science · doi:10.1042/cs20100385 · Cited by 169
The genetics of dyskeratosis congenita
Mason, P. J., & Bessler, M. (2011) · Cancer Genetics · doi:10.1016/j.cancergen.2011.11.002 · Cited by 167
Architecture of human telomerase RNA
Zhang, Q., Kim, N.-K., & Feigon, J. F. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100279108 · Cited by 162
Proteostatic Control of Telomerase Function through TRiC-Mediated Folding of TCAB1
Freund, A., Zhong, F. L., Venteicher, A. S., Meng, Z., Veenstra, T. D., Frydman, J., & Artandi, S. E. (2014) · Cell · doi:10.1016/j.cell.2014.10.059 · Cited by 155
Self-citationNuclear bodies: news insights into structure and function
Staněk, D., & Fox, A. H. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.05.001 · Cited by 149
Transcriptional Regulation of Telomerase Reverse Transcriptase (TERT) by MYC
Khattar, E., & Tergaonkar, V. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00001 · Cited by 154
Inventory of telomerase components in human cells reveals multiple subpopulations of hTR and hTERT
Xi, L., & Cech, T. R. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku560 · Cited by 147
It all comes together at the ends: Telomerase structure, function, and biogenesis
Podlevsky, J. D., & Chen, J. J. ‐. (2011) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2011.11.002 · Cited by 152
Human telomeric proteins occupy selective interstitial sites
Yang, D., Xiong, Y., Kim, H., He, Q., Li, Y., Chen, R., & Songyang, Z. (2011) · Cell Research · doi:10.1038/cr.2011.39 · Cited by 149
Replication of Telomeres and the Regulation of TelomerasePreprint
Pfeiffer, V., & Lingner, J. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a010405 · Cited by 150
Biogenesis of spliceosomal small nuclear ribonucleoproteins
Fischer, U., Englbrecht, C., & Chari, A. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.87 · Cited by 140
Zhu, R., Yan, T., Feng, Y., Liu, Y., Cao, H., Peng, G., Yang, Y., Xu, Z., Liu, J., Hou, W., et al. (2021) · Cell Research · doi:10.1038/s41422-021-00573-y · Cited by 139
Dyskeratosis congenita as a disorder of telomere maintenance
Nelson, N. D., & Bertuch, A. A. (2011) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2011.06.008 · Cited by 140
Telomere length regulation: coupling DNA end processing to feedback regulation of telomerase
Shore, D., & Bianchi, A. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.195 · Cited by 141
Gavia-García, G., Rosado-Pérez, J., Arista-Ugalde, T. L., Aguíñiga-Sánchez, I., Santiago‐Osorio, E., & Mendoza-Núñez, V. M. (2021) · Biology · doi:10.3390/biology10040253 · Cited by 148
Mahmoudi, S., Henriksson, S., Weibrecht, I., Smith, S., Söderberg, O., Strömblad, S., Wiman, K. G., & Farnebo, M. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000521 · Cited by 135
Structure of active dimeric human telomerase
Sauerwald, A., Sandin, S., Cristofari, G., Scheres, S. H. W., Lingner, J., & Rhodes, D. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2530 · Cited by 133
Beginning at the ends: telomeres and human disease
Savage, S. A. (2018) · F1000Research · doi:10.12688/f1000research.14068.1 · Cited by 124
Telomerase Recruitment Requires both TCAB1 and Cajal Bodies Independently
Stern, J. L., Zyner, K. G., Pickett, H. A., Cohen, S. B., & Bryan, T. M. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00379-12 · Cited by 131
Kasiappan, R., Shen, Z., Tse, A. K., Jinwal, U. K., Tang, J., Lungchukiet, P., Sun, Y., Kruk, P. A., Nicosia, S. V., Zhang, X. M., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407189 · Cited by 127
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Nuclear bodies: new insights into assembly/dynamics and disease relevance
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Evolutionary perspectives of telomerase RNA structure and function
Podlevsky, J. D., & Chen, J. J. ‐. (2016) · RNA Biology · doi:10.1080/15476286.2016.1205768 · Cited by 123
Guo, Y., Kartawinata, M., Li, J., Pickett, H. A., Teo, J., Kilo, T., Barbaro, P., Keating, B. J., Chen, Y., Tian, L., et al. (2014) · Blood · doi:10.1182/blood-2014-08-596445 · Cited by 123
New prospects for targeting telomerase beyond the telomere
Arndt, G. M., & MacKenzie, K. L. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.55 · Cited by 120
Gallardo, F., Laterreur, N., Cusanelli, E., Ouenzar, F., Querido, E., Wellinger, R. J., & Chartrand, P. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.020 · Cited by 118
Control of telomerase action at human telomeres
Hockemeyer, D. F., & Collins, K. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3083 · Cited by 124
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Baird, D. M. (2010) · Expert Reviews in Molecular Medicine · doi:10.1017/s146239941000147x · Cited by 117
Inhibition of telomerase RNA decay rescues telomerase deficiency caused by dyskerin or PARN defects
Shukla, S., Schmidt, J. C., Goldfarb, K. C., Cech, T. R., & Parker, R. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3184 · Cited by 120
Sizing the ends: Normal length of human telomeres
Samassékou, O., Gadji, M., Drouin, R., & Yan, J. (2010) · Annals of Anatomy - Anatomischer Anzeiger · doi:10.1016/j.aanat.2010.07.005 · Cited by 124
Telomeres and telomerase as therapeutic targets to prevent and treat age-related diseases
Bär, C., & Blasco, M. A. (2016) · F1000Research · doi:10.12688/f1000research.7020.1 · Cited by 117
Egan, E. D., & Collins, K. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00151-10 · Cited by 117
Telomere and Telomerase Therapeutics in Cancer
Xu, Y., & Goldkorn, A. (2016) · Genes · doi:10.3390/genes7060022 · Cited by 113
The regulations of telomerase reverse transcriptase (TERT) in cancer
Liu, M., Zhang, Y., Jian, Y., Gu, L., Zhang, D., Zhou, H., Wang, Y., & Xu, Z. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06454-7 · Cited by 119
Small-Molecule PAPD5 Inhibitors Restore Telomerase Activity in Patient Stem Cells
Nagpal, N., Wang, J., Zeng, J., Lo, E., Moon, D. H., Luk, K., Braun, R. O., Burroughs, L. M., Keel, S. B., Reilly, C., et al. (2020) · Cell Stem Cell · doi:10.1016/j.stem.2020.03.016 · Cited by 105
Sexton, A. N., & Collins, K. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01033-10 · Cited by 107
Identification of human TERT elements necessary for telomerase recruitment to telomeres
Schmidt, J. C., Dalby, A. B., & Cech, T. R. (2014) · eLife · doi:10.7554/elife.03563 · Cited by 111
Molecular mechanisms of telomere biology disorders
Grill, S., & Nandakumar, J. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.014017 · Cited by 114
Hu, G., Wu, Z., Uversky, V. N., & Kurgan, L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122761 · Cited by 107
Telomerase Activity and Telomere Length in Male Germ Cells
Öztürk, S. (2015) · Biology of Reproduction · doi:10.1095/biolreprod.114.124008 · Cited by 111
Telomerase and Telomere-Associated Proteins: Structural Insights into Mechanism and Evolution
Lewis, K. A., & Wuttke, D. S. (2012) · Structure · doi:10.1016/j.str.2011.10.017 · Cited by 106
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Machyna, M., Kehr, S., Straube, K., Kappei, D., Buchholz, F., Butter, F., Ule, J., Jana Hertel, A., Stadler, P. F., & Neugebauer, K. M. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.10.004 · Cited by 107
Transcriptional and epigenetic regulation of the p53 tumor suppressor gene
Saldaña-Meyer, R., & Targa, F. R. (2011) · Epigenetics · doi:10.4161/epi.6.9.16683 · Cited by 103
Garus, A., & Autexier, C. (2021) · RNA · doi:10.1261/rna.078953.121 · Cited by 104
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Meier, U. T. (2016) · RNA Biology · doi:10.1080/15476286.2016.1249091 · Cited by 105
Genomic sites hypersensitive to ultraviolet radiation
Premi, S., Han, L., Mehta, S., Knight, J., Zhao, D., Palmatier, M. A., Kornacker, K., & Brash, D. E. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1907860116 · Cited by 95
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Gormley, M. J., Ona, K., Kapidzic, M., Garrido‐Gómez, T., Zdravkovic, T., & Fisher, S. J. (2017) · American Journal of Obstetrics and Gynecology · doi:10.1016/j.ajog.2017.03.017 · Cited by 99
Commonly used tag combinations for tandem affinity purification
Li, Y. (2010) · Biotechnology and Applied Biochemistry · doi:10.1042/ba20090273 · Cited by 98
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Morimoto, M., & Boerkoel, C. F. (2013) · Biology · doi:10.3390/biology2030976 · Cited by 101
Reduced Viability, Fertility and Fecundity in Mice Lacking the Cajal Body Marker Protein, Coilin
Walker, M. P., Tian, L., & Matera, A. G. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006171 · Cited by 93
Telomerase in Cancer: Function, Regulation, and Clinical Translation
Robinson, N. J., & Schiemann, W. P. (2022) · Cancers · doi:10.3390/cancers14030808 · Cited by 105
Zhao, Y. B., Abreu, E. B., Kim, J., Stadler, G., Eskiocak, U., Terns, M. P., Terns, R. M., Shay, J. W., & Wright, W. E. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.020 · Cited by 92
Self-citationShort telomeres: from dyskeratosis congenita to sporadic aplastic anemia and malignancy
Gramatges, M. M., & Bertuch, A. A. (2013) · Translational research · doi:10.1016/j.trsl.2013.05.003 · Cited by 90
Telomeres: Implications for Cancer Development
Bernal, A., & Tusell, L. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19010294 · Cited by 92
Metadata
- Authors
- Venteicher, A. S., Abreu, E. B., Meng, Z., McCann, K. E., Terns, R. M., Veenstra, T. D., Terns, M. P., & Artandi, S. E.
- Affiliations
- Leidos (United States) (US)
- Corresponding author
- Abreu, Eladio B.
- Meng, Zhaojing
- Artandi, Steven E.
- ORCID
- Venue
- Science
- Published
- 2009-01-30
- Volume
- 323
- Issue
- 5914
- Pages
- 644-648
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC2728071
- OpenAlex
- W2014414194
- Cited by
- 522
- References
- 23
- Citations by year
- 2026: 13 · 2025: 16 · 2024: 20 · 2023: 18 · 2022: 22 · 2021: 30 · 2020: 29 · 2019: 27 · 2018: 28 · 2017: 29 · 2016: 43 · 2015: 39 · 2014: 40 · 2013: 37 · 2012: 35
- FWCI
- 29.03
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- DigitalCommons-Cedarville (Cedarville University) (submittedVersion)
- Funders
- National Institutes of Health (n01co12400-79-0-22)
- National Cancer Institute (N01CO12400, CA111691, N01-CO-012400, R01CA125453, CA125453, R01CA111691, CA104676, R01CA104676)
- National Institute of General Medical Sciences (T32GM007365, GM 07365)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Telomeres, Telomerase, and Senescence
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- telomerase, telomerase holoenzyme, Cajal bodies, telomere synthesis, dyskerin, ribonucleoprotein complexes, cancer cells
- MeSH terms
- Amino Acid Sequence, HeLa Cells, Humans, Molecular Sequence Data, Nuclear Proteins, RNA, Telomere, Cell Cycle Proteins, Molecular Chaperones, Telomerase, Coiled Bodies, RNA Interference, Cell Line, Tumor, Immunoprecipitation
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