The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
A Human Telomeric Protein
Abstract
Telomeres are multifunctional elements that shield chromosome ends from degradation and end-to-end fusions, prevent activation of DNA damage checkpoints, and modulate the maintenance of telomeric DNA by telomerase. A major protein component of human telomeres has been identified and cloned. This factor, TRF, contains one Myb-type DNA-binding repeat and an amino-terminal acidic domain. Immunofluorescent labeling shows that TRF specifically colocalizes with telomeric DNA in human interphase cells and is located at chromosome ends during metaphase. The presence of TRF along the telomeric TTAGGG repeat array demonstrates that human telomeres form a specialized nucleoprotein complex.
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Cites
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
Specific Association of Human Telomerase Activity with Immortal Cells and Cancer
Kim, N. W., Piatyszek, M. A., Prowse, K. R., Harley, C. B., West, M. D., Ho, P. L. C., Coviello, G. M., Wright, W. E., Weinrich, S. L., & Shay, J. W. (1994) · Science · doi:10.1126/science.7605428 · Cited by 7,091
Telomeres shorten during ageing of human fibroblasts
Harley, C. B., Futcher, A. B., & Greider, C. W. (1990) · Nature · doi:10.1038/345458a0 · Cited by 5,750
The RNA Component of Human Telomerase
Feng, J., Funk, W. D., Wang, S.-S., Weinrich, S. L., Avilion, A. A., Chiu, C.-P., Adams, R. R., Chang, E., Allsopp, R. C., Yu, J., et al. (1995) · Science · doi:10.1126/science.7544491 · Cited by 2,227
Counter, C. M., Avilion, A. A., LeFeuvre, C. E., Stewart, N. G., Greider, C. W., Harley, C. B., & Bacchetti, S. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05245.x · Cited by 2,096
Telomere reduction in human colorectal carcinoma and with ageing
Hastie, N. D., Dempster, M., Dunlop, M. G., Thompson, A. M., Green, D. K., & Allshire, R. C. (1990) · Nature · doi:10.1038/346866a0 · Cited by 1,650
Structure and variability of human chromosome ends.
de Lange, T., Shiue, L., Myers, R. M., Cox, D. R., Naylor, S. L., Killery, A. M., & Varmus, H. E. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.2.518 · Cited by 848
Telomerase activity in human ovarian carcinoma.
Counter, C. M., Hirte, H. W., Bacchetti, S., & Harley, C. B. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.8.2900 · Cited by 677
Hypervariable ultra-long telomeres in mice
Kipling, D., & Cooke, H. J. (1990) · Nature · doi:10.1038/347400a0 · Cited by 614
Counter, C. M., Botelho, F. M., Wang, P., Harley, C. B., & Bacchetti, S. (1994) · Journal of Virology · doi:10.1128/jvi.68.5.3410-3414.1994 · Cited by 355
Cited by
Shelterin: the protein complex that shapes and safeguards human telomeres
de Lange, T. (2005) · Genes & Development · doi:10.1101/gad.1346005 · Cited by 3,056
Mammalian Telomeres End in a Large Duplex Loop
Griffith, J. D., Comeau, L., Rosenfield, S., Stansel, R. M., Bianchi, A., Moss, H., & de Lange, T. (1999) · Cell · doi:10.1016/s0092-8674(00)80760-6 · Cited by 2,447
How Shelterin Protects Mammalian Telomeres
Palm, W., & de Lange, T. (2008) · Annual Review of Genetics · doi:10.1146/annurev.genet.41.110306.130350 · Cited by 1,802
Self-citationTRF2 Protects Human Telomeres from End-to-End Fusions
van Steensel, B., Smogorzewska, A., & de Lange, T. (1998) · Cell · doi:10.1016/s0092-8674(00)80932-0 · Cited by 1,709
Control of telomere length by the human telomeric protein TRF1
van Steensel, B., & de Lange, T. (1997) · Nature · doi:10.1038/385740a0 · Cited by 1,219
Aubert, G., & Lansdorp, P. M. (2008) · Physiological Reviews · doi:10.1152/physrev.00026.2007 · Cited by 1,188
p53- and ATM-Dependent Apoptosis Induced by Telomeres Lacking TRF2
Karlseder, J., Broccoli, D., Dai, Y., Hardy, S., & de Lange, T. (1999) · Science · doi:10.1126/science.283.5406.1321 · Cited by 1,086
Self-citationMammalian Telomeres Resemble Fragile Sites and Require TRF1 for Efficient Replication
Sfeir, A., Kosiyatrakul, S. T., Hockemeyer, D., MacRae, S. L., Karlseder, J., Schildkraut, C. L., & de Lange, T. (2009) · Cell · doi:10.1016/j.cell.2009.06.021 · Cited by 990
Human telomeres contain two distinct Myb–related proteins, TRF1 and TRF2
Broccoli, D., Smogorzewska, A., Chong, L., & de Lange, T. (1997) · Nature Genetics · doi:10.1038/ng1097-231 · Cited by 926
Self-citationTelomeres and telomerase: three decades of progress
Shay, J. W., & Wright, W. E. (2019) · Nature Reviews Genetics · doi:10.1038/s41576-019-0099-1 · Cited by 924
Control of Human Telomere Length by TRF1 and TRF2
Smogorzewska, A., van Steensel, B., Bianchi, A., Oelmann, S., Schaefer, M. R., Schnapp, G., & de Lange, T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.5.1659-1668.2000 · Cited by 768
McEachern, M. J., Krauskopf, A., & Blackburn, E. H. (2000) · Annual Review of Genetics · doi:10.1146/annurev.genet.34.1.331 · Cited by 716
The 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
The rate of telomere sequence loss in human leukocytes varies with age
Frenck, R. W., Blackburn, E. H., & Shannon, K. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.10.5607 · Cited by 675
Replicative Senescence: Implications for in Vivo Aging and Tumor Suppression
Smith, J. R., & Pereira-Smith, O. M. (1996) · Science · doi:10.1126/science.273.5271.63 · Cited by 547
TIN2, a new regulator of telomere length in human cells
Kim, S.-H., Kaminker, P., & Campisi, J. (1999) · Nature Genetics · doi:10.1038/70508 · Cited by 525
A Protein-Counting Mechanism for Telomere Length Regulation in Yeast
Marcand, S., Gilson, E., & Shore, D. (1997) · Science · doi:10.1126/science.275.5302.986 · Cited by 524
Hallmarks of senescence in carcinogenesis and cancer therapy
Shay, J. W., & Roninson, I. B. (2004) · Oncogene · doi:10.1038/sj.onc.1207518 · Cited by 502
Regulation of telomere length and function by a Myb-domain protein in fission yeast
Cooper, J. P., Nimmo, E. R., Allshire, R. C., & Cech, T. R. (1997) · Nature · doi:10.1038/385744a0 · Cited by 502
Human telomerase contains evolutionarily conserved catalytic and structural subunits
Harrington, L., Zhou, W., McPhail, T., Oulton, R., Yeung, D. S. K., Mar, V., Bass, M. B., & Robinson, M. O. (1997) · Genes & Development · doi:10.1101/gad.11.23.3109 · Cited by 465
Ye, J. Z.-S., Hockemeyer, D., Krutchinsky, A. N., Loayza, D., Hooper, S. M., Chait, B. T., & de Lange, T. (2004) · Genes & Development · doi:10.1101/gad.1215404 · Cited by 459
Zscan4 regulates telomere elongation and genomic stability in ES cells
Zalzman, M., Falco, G., Sharova, L. V., Nishiyama, A., Thomas, M., Lee, S.-L., Stagg, C. A., Hoang, H. G., Yang, H.-T., Indig, F. E., et al. (2010) · Nature · doi:10.1038/nature08882 · Cited by 441
The telomerase reverse transcriptase: components and regulation
Nugent, C. I., & Lundblad, V. (1998) · Genes & Development · doi:10.1101/gad.12.8.1073 · Cited by 438
Cellular senescence, cancer and aging: the telomere connection
Campisi, J., Kim, S.-H., Lim, C.-S., & Rubio, M. (2001) · Experimental Gerontology · doi:10.1016/s0531-5565(01)00160-7 · Cited by 400
Zhu, X.-D., Niedernhofer, L., Kuster, B., Mann, M., Hoeijmakers, J. H. J., & de Lange, T. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00478-7 · Cited by 386
Self-citationTRF1 is a dimer and bends telomeric DNA
Bianchi, A., Smith, S., Chong, L., Elias, P., & de Lange, T. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1785 · Cited by 358
Self-citationRegulation 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 346
Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins
Liou, Y.-C., Zhou, X. Z., & Lu, K. P. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.07.001 · Cited by 326
Role for the Related Poly(ADP-Ribose) Polymerases Tankyrase 1 and 2 at Human Telomeres
Cook, B. D., Dynek, J. N., Chang, W., Shostak, G., & Smith, S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.1.332-342.2002 · Cited by 316
The Pin2/TRF1-Interacting Protein PinX1 Is a Potent Telomerase Inhibitor
Zhou, X. Z., & Lu, K. P. (2001) · Cell · doi:10.1016/s0092-8674(01)00538-4 · Cited by 309
Telomerase and the maintenance of chromosome ends
Bryan, T. M., & Cech, T. R. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)80043-x · Cited by 301
The nature of telomere fusion and a definition of the critical telomere length in human cells
Capper, R., Britt-Compton, B., Tankimanova, M., Rowson, J., Letsolo, B., Man, S., Haughton, M., & Baird, D. M. (2007) · Genes & Development · doi:10.1101/gad.439107 · Cited by 294
Houghtaling, B. R., Cuttonaro, L., Chang, W., & Smith, S. (2004) · Current Biology · doi:10.1016/j.cub.2004.08.052 · Cited by 286
Functional Human Telomeres Are Recognized as DNA Damage in G2 of the Cell Cycle
Verdun, R. E., Crabbe, L., Haggblom, C., & Karlseder, J. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.024 · Cited by 284
Fission yeast Taz1 protein is required for meiotic telomere clustering and recombination
Cooper, J. P., Watanabe, Y., & Nurse, P. (1998) · Nature · doi:10.1038/33947 · Cited by 274
Regulation of the human catalytic subunit of telomerase (hTERT)
Daniel, M., Peek, G. W., & Tollefsbol, T. O. (2012) · Gene · doi:10.1016/j.gene.2012.01.095 · Cited by 266
Mice with Pulmonary Fibrosis Driven by Telomere Dysfunction
Povedano, J. M., Martinez, P., Flores, J. M., Mulero, F., & Blasco, M. A. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.06.028 · Cited by 225
“Out of the six shelterin components, TRF1 was the first to be identified (Chong et al., 1995).”
BackgroundA RAP1/TRF2 Complex Inhibits Nonhomologous End-Joining at Human Telomeric DNA Ends
Bae, N. S., & Baumann, P. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.023 · Cited by 215
TRF1 binds a bipartite telomeric site with extreme spatial flexibility
Bianchi, A., Stansel, R. M., Fairall, L., Griffith, J. D., Rhodes, D., & de Lange, T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.20.5735 · Cited by 217
Self-citationHuman RAP1 inhibits non‐homologous end joining at telomeres
Sarthy, J., Bae, N. S., Scrafford, J., & Baumann, P. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.275 · Cited by 151
TRF1 promotes parallel pairing of telomeric tracts in vitro
Griffith, J., Bianchi, A., & de Lange, T. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1686 · Cited by 148
A role for the Rb family of proteins in controlling telomere length
García-Cao, M., Gonzalo, S., Dean, D., & Blasco, M. A. (2002) · Nature Genetics · doi:10.1038/ng1011 · Cited by 120
Broccoli, D. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.1.69 · Cited by 103
Self-citationMarušić, L., Anton, M., Tidy, A., Wang, P., Villeponteau, B., & Bacchetti, S. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.11.6394 · Cited by 74
Telomere Length Maintenance, Shortening, and Lengthening
Zhao, Z., Pan, X., Liu, L., & Liu, N. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24537 · Cited by 66
The end protection problem—an unexpected twist in the tail
Ruis, P., & Boulton, S. J. (2021) · Genes & Development · doi:10.1101/gad.344044.120 · Cited by 57
Shelterin is a dimeric complex with extensive structural heterogeneity
Zinder, J. C., Olinares, P. D. B., Svetlov, V., Bush, M. W., Nudler, E., Chait, B. T., Walz, T., & de Lange, T. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2201662119 · Cited by 44
Self-citation(2023) · doi:10.1007/s11103-023-01348-2 · Cited by 19
Hematopoietic stem cells are acutely sensitive to Acd shelterin gene inactivation
Jones, M., Osawa, G., Regal, J. A., Weinberg, D. N., Taggart, J., Kocak, H., Friedman, A., Ferguson, D. O., Keegan, C. E., & Maillard, I. (2014) · Journal of Clinical Investigation · doi:10.1172/jci67871 · Cited by 18
Metadata
- Authors
- Chong, L., van Steensel, B., Broccoli, D., Erdjument-Bromage, H., Hanish, J., Tempst, P., & de Lange, T.
- Venue
- Science
- Published
- 1995-12-08
- Volume
- 270
- Issue
- 5242
- Pages
- 1663-1667
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2050674095
- Cited by
- 694
- References
- 12
- FWCI
- 23.01
- Type
- journal article
- Language
- en
- Open access
- closed
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