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POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex
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Human telomere length is controlled by a negative feedback loop based on the binding of TRF1 to double-stranded telomeric DNA. The TRF1 complex recruits POT1, a single-stranded telomeric DNA-binding protein necessary for cis-inhibition of telomerase. By mass spectrometry, we have identified a new telomeric protein, which we have named POT1-interacting protein 1 (PIP1). PIP1 bound both POT1 and the TRF1-interacting factor TIN2 and could tether POT1 to the TRF1 complex. Reduction of PIP1 or POT1 levels with shRNAs led to telomere elongation, indicating that PIP1 contributes to telomere length control through recruitment of POT1.
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“TRF1-interacting nuclear factor 2 also interacts with the subcomplex of shelterin that binds the single-stranded overhang-TPP1 and POT1, two oligonucleotide/ oligosaccharide binding (OB)-fold containing proteins (13)(14)(15).”
From Telomeres and telomerase in cancer (2010) · cites this paper as [14]
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Cites
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
Pot1, the Putative Telomere End-Binding Protein in Fission Yeast and Humans
Baumann, P., & Cech, T. R. (2001) · Science · doi:10.1126/science.1060036 · Cited by 1,028
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
Regulation of Telomerase by Telomeric Proteins
Smogorzewska, A., & de Lange, T. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.071403.160049 · Cited by 813
Senescence Induced by Altered Telomere State, Not Telomere Loss
Karlseder, J., Smogorzewska, A., & de Lange, T. (2002) · Science · doi:10.1126/science.1069523 · Cited by 796
A Complex with Chromatin Modifiers That Occupies E2F- and Myc-Responsive Genes in G 0 Cells
Ogawa, H., Ishiguro, K., Gaubatz, S., Livingston, D. M., & Nakatani, Y. (2002) · Science · doi:10.1126/science.1069861 · Cited by 785
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
POT1 as a terminal transducer of TRF1 telomere length control
Loayza, D., & de Lange, T. (2003) · Nature · doi:10.1038/nature01688 · Cited by 725
Self-citationChong, L., van Steensel, B., Broccoli, D., Erdjument‐Bromage, H., Hanish, J., Tempst, P., & de Lange, T. (1995) · Science · doi:10.1126/science.270.5242.1663 · Cited by 714
Li, B., Oestreich, S. C., & de Lange, T. (2000) · Cell · doi:10.1016/s0092-8674(00)80858-2 · Cited by 609
Research works printed but not linked: 2
- 1990, Mol. Cell. Biol., 10, 518
- Liu D ., Safari, A., O'Conner, M.S., Chan, D.W., Laegeler, A., Qin, L., and Songyang, Z. 2004. PTOP is a novel POT1 interacting protein that regulates POT1 telomeric localization. Nat. Cell Biol. (in press).
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de Lange, T. (2005) · Genes & Development · doi:10.1101/gad.1346005 · Cited by 3,056
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
Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1
Denchi, E. L., & de Lange, T. (2007) · Nature · doi:10.1038/nature06065 · Cited by 880
G-quadruplex structures: in vivo evidence and function
Lipps, H. J., & Rhodes, D. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.05.002 · Cited by 856
Telomeres and telomerase in cancer
Artandi, S. E., & DePinho, R. A. (2010) · Carcinogenesis · doi:10.1093/carcin/bgp268 · Cited by 823
Telomere length, stem cells and aging
Blasco, M. A. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.38 · Cited by 747
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 epigenetic regulation of mammalian telomeres
Blasco, M. A. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2047 · Cited by 600
Telomeric and extra-telomeric roles for telomerase and the telomere-binding proteins
Martínez, P., & Blasco, M. A. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3025 · Cited by 468
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
Lei, M., Podell, E. R., & Cech, T. R. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb867 · Cited by 489
Gilson, É., & Géli, V. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2259 · Cited by 496
Wu, L., Multani, A. S., He, H., Cosme-Blanco, W., Deng, Y., Deng, J. M., Bachilo, O., Pathak, S., Tahara, H., Bailey, S. M., et al. (2006) · Cell · doi:10.1016/j.cell.2006.05.037 · Cited by 422
Telosome, a Mammalian Telomere-associated Complex Formed by Multiple Telomeric Proteins
Liu, D., O'Connor, M. S., Qin, J., & Songyang, Z. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409293200 · Cited by 405
Hockemeyer, D., Daniels, J.-P., Takai, H., & de Lange, T. (2006) · Cell · doi:10.1016/j.cell.2006.04.044 · Cited by 397
Self-citationFinding 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
The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity
Nandakumar, J., Bell, C., Weidenfeld, I., Zaug, A. J., Leinwand, L. A., & Cech, T. R. (2012) · Nature · doi:10.1038/nature11648 · Cited by 357
TIN2 Binds TRF1 and TRF2 Simultaneously and Stabilizes the TRF2 Complex on Telomeres
Ye, J. Z.-S., Donigian, J. R., van Overbeek, M., Loayza, D., Luo, Y., Krutchinsky, A. N., Chait, B. T., & de Lange, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409047200 · Cited by 370
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 356
Telomeres: Cancer to Human Aging
Stewart, S. A., & Weinberg, R. A. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104518 · Cited by 349
Chemistry in human telomere biology: structure, function and targeting of telomere DNA/RNA
Xu, Y. (2011) · Chemical Society Reviews · doi:10.1039/c0cs00134a · Cited by 326
Hockemeyer, D., Sfeir, A. J., Shay, J. W., Wright, W. E., & de Lange, T. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600733 · Cited by 314
Self-citationSurovtseva, Y. V., Churikov, D., Boltz, K. A., Song, X., Lamb, J. C., Warrington, R. T., Leehy, K. A., Heacock, M. L., Price, C. M., & Shippen, D. E. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.017 · Cited by 304
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
Hug, N., & Lingner, J. (2006) · Chromosoma · doi:10.1007/s00412-006-0067-3 · Cited by 291
Houghtaling, B. R., Cuttonaro, L., Chang, W., & Smith, S. H. (2004) · Current Biology · doi:10.1016/j.cub.2004.08.052 · Cited by 305
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
Shaping human telomeres: from shelterin and CST complexes to telomeric chromatin organization
Lim, C. J., & Cech, T. R. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00328-y · Cited by 273
Dysfunctional telomeres activate an ATM‐ATR‐dependent DNA damage response to suppress tumorigenesis
Guo, X., Deng, Y., Lin, Y., Cosme‐Blanco, W., Chan, S., He, H., Yuan, G., Brown, E. J., & Chang, S. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601893 · Cited by 258
DNA and RNA Quadruplex-Binding Proteins
Brázda, V., Hároníková, L., Liao, J. C. C., & Fojta, M. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151017493 · Cited by 251
A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly
O’Connor, M. S., Safari, A., Xin, H., Liu, D., & Songyang, Z. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605303103 · Cited by 258
In Vivo Stoichiometry of Shelterin Components
Takai, K., Hooper, S., Blackwood, S., Gandhi, R., & de Lange, T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.038026 · Cited by 258
Self-citationTelomeres, chromosome instability and cancer
Bailey, S. M. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl303 · Cited by 245
TIN2-Tethered TPP1 Recruits Human Telomerase to Telomeres In Vivo
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
Telomere Protection by TPP1/POT1 Requires Tethering to TIN2
Takai, K., Kibe, T., Donigian, J. R., Frescas, D., & de Lange, T. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.043 · Cited by 255
Court, R., Chapman, L., Fairall, L., & Rhodes, D. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400314 · Cited by 240
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
The telosome/shelterin complex and its functions
Xin, H., Liu, D., & Songyang, Z. (2008) · Genome biology · doi:10.1186/gb-2008-9-9-232 · Cited by 240
A 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
TIN2 Mediates Functions of TRF2 at Human Telomeres
Kim, S., Beausejour, C. M., Davalos, A. R., Kaminker, P. G., Heo, S., & Campisi, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408650200 · Cited by 229
Human Protection of Telomeres 1 (POT1) Is a Negative Regulator of Telomerase Activity In Vitro
Kelleher, C. D., Kurth, I., & Lingner, J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.2.808-818.2005 · Cited by 216
Apollo, an Artemis-Related Nuclease, Interacts with TRF2 and Protects Human Telomeres in S Phase
van Overbeek, M., & de Lange, T. (2006) · Current Biology · doi:10.1016/j.cub.2006.05.022 · Cited by 204
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
Telomeric Strategies: Means to an End
Jain, D., & Cooper, J. P. (2010) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134841 · Cited by 205
Telomere protection by mammalian Pot1 requires interaction with Tpp1
Hockemeyer, D. F., Palm, W., Else, T., Daniels, J., Takai, K., Ye, J. Z.-S., Keegan, C. E., de Lange, T., & Hammer, G. D. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1270 · Cited by 214
Self-citationPathways connecting telomeres and p53 in senescence, apoptosis, and cancer
Artandi, S. E., & Attardi, L. D. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.211 · Cited by 194
POT1–TPP1 enhances telomerase processivity by slowing primer dissociation and aiding translocation
Latrick, C. M., & Cech, T. R. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.409 · Cited by 195
Nonsense Mutations in the Shelterin Complex Genes ACD and TERF2IP in Familial Melanoma
Aoude, L. G., Pritchard, A. L., Robles‐Espinoza, C. D., Wadt, K., Harland, M., Choi, J., Gartside, M. G., Quesada, V., Johansson, P. A., Palmer, J. M., et al. (2014) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/dju408 · Cited by 193
POT1 and TRF2 Cooperate To Maintain Telomeric Integrity
Yang, Q., Zheng, Y., & Harris, C. C. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.3.1070-1080.2005 · Cited by 190
Oligonucleotide/oligosaccharide-binding fold proteins: a growing family of genome guardians
Flynn, R. L., & Zou, L. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.488216 · Cited by 186
DNA damage response at functional and dysfunctional telomeresPreprint
Longhese, M. P. (2008) · Genes & Development · doi:10.1101/gad.1626908 · Cited by 184
Switching Human Telomerase On and Off with hPOT1 Protein in Vitro
Lei, M., Zaug, A. J., Podell, E. R., & Cech, T. R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502212200 · Cited by 175
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Denchi, E. L., & Sfeir, A. J. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.43 · Cited by 177
Role of shelterin in cancer and aging
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Genetics of familial melanoma: 20 years after CDKN 2 A
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Xu, L., Li, S., & Stohr, B. A. (2013) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-020712-164030 · Cited by 160
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Mice with bad ends: mouse models for the study of telomeres and telomerase in cancer and aging
Blasco, M. A. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600598 · Cited by 152
Familial Clonal Hematopoiesis in a Long Telomere Syndrome
DeBoy, E. A., Tassia, M. G., Schratz, K. E., Yan, S. M., Cosner, Z. L., McNally, E. J., Gable, D. L., Xiang, Z., Lombard, D. B., Antonarakis, E. S., et al. (2023) · New England Journal of Medicine · doi:10.1056/nejmoa2300503 · Cited by 148
Loss of hPot1 Function Leads to Telomere Instability and a cut-like Phenotype
Veldman, T., Etheridge, K. T., & Counter, C. M. (2004) · Current Biology · doi:10.1016/j.cub.2004.12.031 · Cited by 151
Unraveling the pathogenesis of Hoyeraal–Hreidarsson syndrome, a complex telomere biology disorder
Glousker, G., Touzot, F., Revy, P., Tzfati, Y., & Savage, S. A. (2015) · British Journal of Haematology · doi:10.1111/bjh.13442 · Cited by 149
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
ATM and ATR Signaling Regulate the Recruitment of Human Telomerase to Telomeres
Tong, A. S., Stern, J. L., Sfeir, A. J., Kartawinata, M., de Lange, T., Zhu, X., & Bryan, T. M. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.10.041 · Cited by 138
Paeschke, K., Juranek, S., Simonsson, T., Hempel, A., Rhodes, D., & Lipps, H. J. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1422 · Cited by 148
Wan, M., Qin, J., Songyang, Z., & Liu, D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.021105 · Cited by 140
Cancer and aging: the importance of telomeres in genome maintenance
Rodier, F., Kim, S.-H., Nijjar, T., Yaswen, P., & Campisi, J. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.10.012 · Cited by 132
Shakirov, E. V., Surovtseva, Y. V., Osbun, N. C., & Shippen, D. E. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.17.7725-7733.2005 · Cited by 130
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Hwang, H. H., Buncher, N. A., Opresko, P. L., & Myong, S. (2012) · Structure · doi:10.1016/j.str.2012.08.018 · Cited by 136
Koçak, H., Ballew, B. J., Bisht, K. K., Eggebeen, R., Hicks, B. D., Suman, S., O’Neil, A., Giri, N., NCI DCEG Cancer Sequencing Working Group, Maillard, I. P., et al. (2014) · Genes & Development · doi:10.1101/gad.248567.114 · Cited by 138
Functional interaction between telomere protein TPP1 and telomerasePreprint
Zaug, A. J., Podell, E. R., Nandakumar, J., & Cech, T. R. (2010) · Genes & Development · doi:10.1101/gad.1881810 · Cited by 139
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POT1b protects telomeres from end‐to‐end chromosomal fusions and aberrant homologous recombination
He, H., Multani, A. S., Cosme‐Blanco, W., Tahara, H., Ma, J., Pathak, S., Deng, Y., & Chang, S. S. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601294 · Cited by 135
The short and long telomere syndromes: paired paradigms for molecular medicine
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Replicating through telomeres: a means to an end
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Telomeres and telomerase in prostate cancer development and therapy
Graham, M. K., & Meeker, A. K. (2017) · Nature Reviews Urology · doi:10.1038/nrurol.2017.104 · Cited by 125
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Palm, W., Hockemeyer, D. F., Kibe, T., & de Lange, T. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01352-08 · Cited by 130
Self-citationSpeedy, H. E., Kinnersley, B., Chubb, D., Broderick, P., Law, P., Litchfield, K., Jayne, S., Dyer, M. J. S., Dearden, C. E., Follows, G., et al. (2016) · Blood · doi:10.1182/blood-2016-01-695692 · Cited by 126
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Rossignol, P., Collier, S., Bush, M., Shaw, P., & Doonan, J. H. (2007) · Journal of Cell Science · doi:10.1242/jcs.004119 · Cited by 124
Telomere Protection by TPP1 Is Mediated by POT1a and POT1b
Kibe, T., Osawa, G. A., Keegan, C. E., & de Lange, T. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01498-09 · Cited by 135
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
The Role of the Nonhomologous End-Joining DNA Double-Strand Break Repair Pathway in Telomere Biology
Říha, K., Heacock, M. L., & Shippen, D. E. (2006) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.110304.095755 · Cited by 122
Telomere uncapping and alternative lengthening of telomeres
Cesare, A. J., & Reddel, R. R. (2007) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.11.006 · Cited by 125
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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Human single-stranded DNA binding proteins are essential for maintaining genomic stability
Ashton, N. W., Bolderson, E., Cubeddu, L., O'Byrne, K. J., & Richard, D. J. (2013) · BMC Molecular Biology · doi:10.1186/1471-2199-14-9 · Cited by 118
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Rice, C., Shastrula, P. K., Kossenkov, A. V., Hills, R., Baird, D. M., Showe, L. C., Doukov, T. I., Janicki, S. M., & Skordalakes, E. (2017) · Nature Communications · doi:10.1038/ncomms14928 · Cited by 112
Telomere Maintenance through Spatial Control of Telomeric Proteins
Chen, L., Liu, D., & Songyang, Z. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00603-07 · Cited by 117
Sexton, A. N., Regalado, S. G., Lai, C. S., Cost, G. J., O’Neil, C. M., Urnov, F. D., Gregory, P. D., Jaenisch, R., Collins, K., & Hockemeyer, D. F. (2014) · Genes & Development · doi:10.1101/gad.246819.114 · Cited by 112
Self-citationA POT1 mutation implicates defective telomere end fill-in and telomere truncations in Coats plusPreprint
Takai, H., Jenkinson, E. M., Kabir, S., Babul‐Hirji, R., Najm-Tehrani, N., Chitayat, D. A., Crow, Y. J., & de Lange, T. (2016) · Genes & Development · doi:10.1101/gad.276873.115 · Cited by 109
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Chawla, R., Redon, S., Raftopoulou, C., Wischnewski, H., Gagos, S., & Azzalin, C. M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.280 · Cited by 112
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Canudas, S., Houghtaling, B. R., Bhanot, M., Sasa, G., Savage, S. A., Bertuch, A. A., & Smith, S. H. (2011) · Genes & Development · doi:10.1101/gad.17325211 · Cited by 108
Metadata
- Authors
- Ye, J. Z.-S., Hockemeyer, D., Krutchinsky, A. N., Loayza, D., Hooper, S. M., Chait, B. T., & de Lange, T.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2004-07-01
- Volume
- 18
- Issue
- 14
- Pages
- 1649-1654
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC478187
- OpenAlex
- W2155983703
- Cited by
- 459
- References
- 21
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 15 · 2023: 18 · 2022: 6 · 2021: 21 · 2020: 12 · 2019: 15 · 2018: 15 · 2017: 16 · 2016: 30 · 2015: 21 · 2014: 34 · 2013: 17 · 2012: 24
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (RR00862)
- National Cancer Institute (K08 CA93604, K08CA093604, T32 CA09673-26A1, T32CA009673)
- National Center for Research Resources (RR00862, P41RR000862)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Telomeres, Telomerase, and Senescence
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- PIP1, POT1, TIN2, TRF1, telomere length regulation, telomeric proteins, telomerase inhibition, telomere elongation, protein-protein interaction, telomeric DNA
- MeSH terms
- Shelterin Complex, Carrier Proteins, Cloning, Molecular, Fluorescent Antibody Technique, HeLa Cells, Humans, Mass Spectrometry, Telomere, Two-Hybrid System Techniques, Telomere-Binding Proteins, RNA Interference, Telomeric Repeat Binding Protein 1, Intracellular Signaling Peptides and Proteins
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