Smurf2 up-regulation activates telomere-dependent senescence

Zhang, Hong; Cohen, Stanley N.

doi:10.1101/gad.1253004

Cited by 100Telomeres, Telomerase, and SenescenceGenetics, Aging, and Longevity in Model OrganismsTGF-β signaling in diseases

Smurf2 up-regulation activates telomere-dependent senescence

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Zhang, Hong, Cohen, Stanley N.·2004·Genes & Development

DOI 10.1101/gad.1253004PMC PMC535914

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Abstract

Progressive telomere shortening activates replicative senescence, which prevents somatic cells from being propagated indefinitely in culture. The limitation of proliferative capacity imposed by replicative senescence is thought to contribute to both organismal aging and the prevention of tumor development. Here we report that up-regulation of Smurf2, an E3 ubiquitin ligase previously implicated in TGF-β signaling, is a specific consequence of telomere attrition in human fibroblasts and that such up-regulation is sufficient to produce the senescence phenotype. Adventitious production of the Smurf2 protein in early passage fibroblasts at the same physiological level observed during telomere-mediated senescence resulted in proliferative arrest in a viable state, morphological and biochemical alterations characteristic of senescence, acquisition of senescence-specific alterations in gene expression, and reversal of cellular immortalization by telomerase. We show that the senescence-inducing actions of Smurf2 occur in the absence of detectable DNA damage or stress response, that Smurf2's effects require a novel function distinct from its E3 activity, that Smurf2 recruits the Rb and p53 pathways for senescence induction, and that while p21 is elevated by Smurf2, Smurf2-mediated senescence is independent of p21. Smurf2 is the first gene found to be both up-regulated by telomere attrition and sufficient to induce senescence.

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The serial cultivation of human diploid cell strains
Hayflick, L., & Moorhead, P. S. (1961) · Experimental Cell Research · doi:10.1016/0014-4827(61)90192-6 · Cited by 8,508 · see citing works
A biomarker that identifies senescent human cells in culture and in aging skin in vivo.
Dimri, G. P., Lee, X., Basile, G., Acosta, M., Scott, G., Roskelley, C., Medrano, E. E., Linskens, M., Rubelj, I., & Pereira-Smith, O. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.20.9363 · Cited by 7,477 · see citing works
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 · cited 2× · see citing works
“Adventitious expression of the catalytic subunit of telomerase (hTERT), which normally is not produced in human somatic cells (Kim et al. 1994), can prevent such telomere shortening and abrogate senescence-related growth arrest (Bodnar et al.”
Background
CDK inhibitors: positive and negative regulators of G1-phase progression
Sherr, C. J., & Roberts, J. M. (1999) · Genes & Development · doi:10.1101/gad.13.12.1501 · Cited by 6,115 · see citing works
Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
Serrano, M., Lin, A. W., McCurrach, M. E., Beach, D., & Lowe, S. W. (1997) · Cell · doi:10.1016/s0092-8674(00)81902-9 · Cited by 5,178 · cited 1× · see citing works
“…of Rb and positive staining for -galactosidase activity at pH 6 (Di Leonardo et al. 1994; Chen et al. 1995; von Zglinicki et al. 1995; Serrano et al. 1997; Robles and Adami 1998), stress-induced proliferative arrest is not associated with telomere attrition and is not abrogated by…”
Background
Extension of Life-Span by Introduction of Telomerase into Normal Human Cells
Bodnar, A. G., Ouellette, M., Frolkis, M., Holt, S. E., Chiu, C.-P., Morin, G. B., Harley, C. B., Shay, J. W., Lichtsteiner, S., & Wright, W. E. (1998) · Science · doi:10.1126/science.279.5349.349 · Cited by 4,975 · see citing works
A DNA damage checkpoint response in telomere-initiated senescence
Fagagna, F. D. D., Reaper, P. M., Clay-Farrace, L., Fiegler, H., Carr, P., von Zglinicki, T., Saretzki, G., Carter, N. P., & Jackson, S. P. (2003) · Nature · doi:10.1038/nature02118 · Cited by 2,855 · cited 5× · see citing works
“…to be a response to DNA damage produced by uncapping or structural alteration of chromosome ends (Blackburn 2001; Karlseder et al. 2002; d’Adda di Fagagna et al. 2003; Takai et al. 2003), and recently, evidence for activation of a DNA damage response by dysfunctional telomeres has been obtained…”
BackgroundInfluential
G1 phase progression: Cycling on cue
Sherr, C. J. (1994) · Cell · doi:10.1016/0092-8674(94)90540-1 · Cited by 2,675 · see citing works
Advanced mammalian gene transfer: high titre retroviral vectors with multiple drug selection markers and a complementary helper-free packaging cell line
Morgenstern, J. P., & Land, H. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.12.3587 · Cited by 2,099 · see citing works
Switching and Signaling at the Telomere
Blackburn, E. H. (2001) · Cell · doi:10.1016/s0092-8674(01)00492-5 · Cited by 2,097 · see citing works
How cells read TGF-β signals
Massagué, J. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35043051 · Cited by 1,882 · see citing works
TRF2 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 · see citing works
Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation.
Kavsak, P., Rasmussen, R. K., Causing, C. G., Bonni, S., Zhu, H.-Q., Thomsen, G. H., & Wrana, J. (2000) · Molecules and Cells · doi:10.1016/s1097-2765(00)00134-9 · Cited by 1,449 · see citing works
DNA Damage Foci at Dysfunctional Telomeres
Takai, H., Smogorzewska, A., & de Lange, T. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00542-6 · Cited by 1,409 · see citing works
Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen
Noda, A., Ning, Y., Venable, S. F., Pereira-Smith, O. M., & Smith, J. R. (1994) · Experimental Cell Research · doi:10.1006/excr.1994.1063 · Cited by 1,351 · see citing works
Telomere Shortening Triggers Senescence of Human Cells through a Pathway Involving ATM, p53, and p21CIP1, but Not p16INK4a
Herbig, U., Jobling, W. A., Chen, B. P. C., Chen, D. J., & Sedivy, J. M. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00256-4 · Cited by 1,344 · see citing works
DNA damage triggers a prolonged p53-dependent G1 arrest and long-term induction of Cip1 in normal human fibroblasts.
Di Leonardo, A., Linke, S. P., Clarkin, K., & Wahl, G. M. (1994) · Genes & Development · doi:10.1101/gad.8.21.2540 · Cited by 1,215 · see citing works
Both Rb/p16INK4a inactivation and telomerase activity are required to immortalize human epithelial cells
Kiyono, T., Foster, S. A., Koop, J. I., McDougall, J. K., Galloway, D. A., & Klingelhutz, A. J. (1998) · Nature · doi:10.1038/23962 · Cited by 1,206 · cited 2× · see citing works
“Adventitious expression of the catalytic subunit of telomerase (hTERT), which normally is not produced in human somatic cells (Kim et al. 1994), can prevent such telomere shortening and abrogate senescence-related growth arrest (Bodnar et al. 1998; Kiyono et al. 1998; Vaziri and Benchimol 1998).”
Background
Telomere loss: mitotic clock or genetic time bomb?
Harley, C. B. (1991) · Mutation Research/DNAging · doi:10.1016/0921-8734(91)90018-7 · Cited by 1,139 · see citing works
Human Keratinocytes That Express hTERT and Also Bypass a p16 INK4a -Enforced Mechanism That Limits Life Span Become Immortal yet Retain Normal Growth and Differentiation Characteristics
Dickson, M. A., Hahn, W. C., Ino, Y., Ronfard, V., Wu, J. Y., Weinberg, R. A., Louis, D. N., Li, F. P., & Rheinwald, J. G. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.4.1436-1447.2000 · Cited by 1,104 · see citing works
Reconstitution of telomerase activity in normal human cells leads to elongation of telomeres and extended replicative life span
Vaziri, H., & Benchimol, S. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70109-5 · Cited by 1,003 · see citing works
Protection of mammalian telomeres
de Lange, T. (2002) · Oncogene · doi:10.1038/sj.onc.1205080 · Cited by 942 · see citing works
Gene transfer by lentiviral vectors is limited by nuclear translocation and rescued by HIV-1 pol sequences
Follenzi, A., Ailles, L., Bakovic, S., Geuna, M., & Naldini, L. (2000) · Nature Genetics · doi:10.1038/76095 · Cited by 926 · see citing works
Differential roles for cyclin-dependent kinase inhibitors p21 and p16 in the mechanisms of senescence and differentiation in human fibroblasts.
Stein, G. H., Drullinger, L. F., Soulard, A., & Dulić, V. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.3.2109 · Cited by 868 · see citing works
Mild hyperoxia shortens telomeres and inhibits proliferation of fibroblasts: a model for senescence?
von Zglinicki, T., Saretzki, G., Döcke, W., & Lotze, C. (1995) · Experimental Cell Research · doi:10.1006/excr.1995.1305 · Cited by 856 · see citing works
A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation
Zhu, H., Kavsak, P. A., Abdollah, S., Wrana, J. L., & Thomsen, G. H. (1999) · Nature · doi:10.1038/23293 · Cited by 847 · see citing works
Bypass of Senescence After Disruption of p21 CIP1/WAF1 Gene in Normal Diploid Human Fibroblasts
Brown, J. P., Wei, W., & Sedivy, J. M. (1997) · Science · doi:10.1126/science.277.5327.831 · Cited by 804 · see citing works
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 · see citing works
Human papillomavirus immortalization and transformation functions
Münger, K., & Howley, P. M. (2002) · Virus Research · doi:10.1016/s0168-1702(02)00190-9 · Cited by 768 · see citing works
A role for both RB and p53 in the regulation of human cellular senescence*1
SHAY, J. (1991) · Experimental Cell Research · doi:10.1016/0014-4827(91)90453-2 · Cited by 757 · see citing works
Oxidative DNA damage and senescence of human diploid fibroblast cells.
Chen, Q., Fischer, A., Reagan, J. D., Yan, L. J., & Ames, B. N. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.10.4337 · Cited by 720 · see citing works
Dissociation among in vitro telomerase activity, telomere maintenance, and cellular immortalization
Counter, C. M., Hahn, W. C., Wei, W., Caddle, S. D., Beijersbergen, R. L., Lansdorp, P. M., Sedivy, J. M., & Weinberg, R. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14723 · Cited by 649 · see citing works
Normal human mammary epithelial cells spontaneously escape senescence and acquire genomic changes
Romanov, S. R., Kozakiewicz, B. K., Holst, C. R., Stampfer, M. R., Haupt, L. M., & Tlsty, T. D. (2001) · Nature · doi:10.1038/35054579 · Cited by 560 · see citing works
A Self-Enabling TGFβ Response Coupled to Stress Signaling
Kang, Y., Chen, C.-R., & Massagué, J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00109-6 · Cited by 548 · see citing works
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase
Zhang, Y. E., Chang, C., Gehling, D. J., Hemmati‐Brivanlou, A., & Derynck, R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.974 · Cited by 523 · see citing works
Agents that cause DNA double strand breaks lead to p16INK4a enrichment and the premature senescence of normal fibroblasts
Robles, S. J., & Adami, G. R. (1998) · Oncogene · doi:10.1038/sj.onc.1201862 · Cited by 498 · see citing works
Smurf2 Is a Ubiquitin E3 Ligase Mediating Proteasome-dependent Degradation of Smad2 in Transforming Growth Factor-β Signaling
Lin, X., Liang, M., & Feng, X. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000580200 · Cited by 495 · see citing works
Different telomere damage signaling pathways in human and mouse cells
Smogorzewska, A., & de Lange, T. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf433 · Cited by 482 · see citing works
Putative telomere-independent mechanisms of replicative aging reflect inadequate growth conditions
Ramirez, R. D., Morales, C. P., Herbert, B.-S., Rohde, J. M., Passons, C., Shay, J. W., & Wright, W. E. (2001) · Genes & Development · doi:10.1101/gad.859201 · Cited by 444 · cited 3× · see citing works
“…p16INK4a during the process of selection from M0 arrest (Brenner et al. 1998; Huschtscha et al. 1998), or in HMECs cultured on feeder layers (Zhang et al. 2004), which do not go through the M0-selection process and maintain normal p16INK4a expression (Ramirez et al. 2001; Herbert et al. 2002).”
Background
Effects of p21 Waf1/Cip1/Sdi1 on cellular gene expression: Implications for carcinogenesis, senescence, and age-related diseases
Chang, B.-D., Watanabe, K., Broude, E. V., Fang, J., Poole, J. C., Kalinichenko, T. V., & Roninson, I. B. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.8.4291 · Cited by 432 · see citing works
A Mechanism of Cyclin D1 Action Encoded in the Patterns of Gene Expression in Human Cancer
Lamb, J., Ramaswamy, S., Ford, H. L., Contreras, B., Martinez, R. V. P., Kittrell, F. S., Zahnow, C. A., Patterson, N. J., Golub, T. R., & Ewen, M. E. (2003) · Cell · doi:10.1016/s0092-8674(03)00570-1 · Cited by 410 · see citing works
Is β-Galactosidase Staining a Marker of Senescence in Vitro and in Vivo?
Severino, J., Allen, R. G., Balin, S., Balin, A., & Cristofalo, V. J. (2000) · Experimental Cell Research · doi:10.1006/excr.2000.4875 · Cited by 370 · see citing works
Genetic analysis of indefinite division in human cells: identification of four complementation groups.
Pereira‐Smith, O. M., & Smith, J. R. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.16.6042 · Cited by 355 · see citing works
Historical claims and current interpretations of replicative aging
Wright, W. E., & Shay, J. W. (2002) · Nature Biotechnology · doi:10.1038/nbt0702-682 · Cited by 355 · see citing works
Erosion of the telomeric single-strand overhang at replicative senescence
Stewart, S. A., Ben-Porath, I., Carey, V. J., O'Connor, B. F., Hahn, W. C., & Weinberg, R. A. (2003) · Nature Genetics · doi:10.1038/ng1127 · Cited by 335 · see citing works
TGF-β induces assembly of a Smad2–Smurf2 ubiquitin ligase complex that targets SnoN for degradation
Bonni, S., Wang, H., Causing, C. G., Kavsak, P. A., Stroschein, S. L., Luo, K., & Wrana, J. L. (2001) · Nature Cell Biology · doi:10.1038/35078562 · Cited by 309 · see citing works
Cellular senescence as a tumor-protection mechanism: the essential role of counting
Wright, W. E., & Shay, J. W. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00163-5 · Cited by 306 · see citing works
Altered regulation of G1 cyclins in senescent human diploid fibroblasts: accumulation of inactive cyclin E-Cdk2 and cyclin D1-Cdk2 complexes.
Dulić, V, Drullinger, L. F., Lees, E., Reed, S. I., & Stein, G. H. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11034 · Cited by 279 · see citing works
Increased p16 expression with first senescence arrest in human mammary epithelial cells and extended growth capacity with p16 inactivation
Brenner, A. J., Stampfer, M. R., & Aldaz, C. M. (1998) · Oncogene · doi:10.1038/sj.onc.1201919 · Cited by 272 · cited 2× · see citing works
“1A), which lose the ability to express p16 during the process of selection from M0 arrest (Brenner et al. 1998; Huschtscha et al. 1998), or in HMECs cultured on feeder layers (Zhang et al.”
Background
Quantitation of the frequency of immortalization of normal human diploid fibroblasts by SV40 large T-antigen
Shay, J. W., & Wright, W. E. (1989) · Experimental Cell Research · doi:10.1016/0014-4827(89)90369-8 · Cited by 256 · see citing works
Expression of Human Telomerase (hTERT) Does Not Prevent Stress-induced Senescence in Normal Human Fibroblasts but Protects the Cells from Stress-induced Apoptosis and Necrosis
Gorbunova, V. A., Seluanov, A., & Pereira‐Smith, O. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202671200 · Cited by 253 · see citing works
Telomere positional effects and the regulation of cellular senescence
Wright, W. E., & Shay, J. W. (1992) · Trends in Genetics · doi:10.1016/0168-9525(92)90232-s · Cited by 246 · see citing works
The Cell Biology of Human Aging
Hayflick, L. (1976) · New England Journal of Medicine · doi:10.1056/nejm197612022952308 · Cited by 231 · see citing works
Telomeres, aging and cancer: In search of a happy ending
Kim, S.-H., Kaminker, P. G., & Campisi, J. (2002) · Oncogene · doi:10.1038/sj.onc.1205077 · Cited by 227 · see citing works
Role of p14ARF in Replicative and Induced Senescence of Human Fibroblasts
Wei, W., Hemmer, R. M., & Sedivy, J. M. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.20.6748-6757.2001 · Cited by 217 · see citing works
Senescence-specific gene expression fingerprints reveal cell-type-dependent physical clustering of up-regulated chromosomal loci
Zhang, H., Pan, K.-H., & Cohen, S. N. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2627983100 · Cited by 209 · see citing works
Self-citation
Refining the telomere-telomerase hypothesis of aging and cancer
Holt, S. E., Shay, J. W., & Wright, W. E. (1996) · Nature Biotechnology · doi:10.1038/nbt0796-836 · Cited by 167 · see citing works
Expression of catalytically active telomerase does not prevent premature senescence caused by overexpression of oncogenic Ha-Ras in normal human fibroblasts.
Wei, S., Wei, S., & Sedivy, J. M. (1999) · PubMed · Cited by 166 · see citing works
Loss of p16INK4 expression by methylation is associated with lifespan extension of human mammary epithelial cells.
Huschtscha, L. I., Noble, J. R., Neumann, A. A., Moy, E. L., Barry, P. A., Melki, J. R., Clark, S. J., & Reddel, R. R. (1998) · PubMed · Cited by 156 · see citing works
Overexpression of Cyclin D1 Blocks Proliferation of Normal Diploid Fibroblasts
Atadja, P. W., Wong, H., Veillette, C., & Riabowol, K. T. (1995) · Experimental Cell Research · doi:10.1006/excr.1995.1080 · Cited by 87 · see citing works
p16INK4a inactivation is not required to immortalize human mammary epithelial cells
Herbert, B., Wright, W. E., & Shay, J. W. (2002) · Oncogene · doi:10.1038/sj.onc.1205902 · Cited by 86 · see citing works
Expression of p21 is not required for senescence of human fibroblasts.
Medcalf, A. S. C., Klein-Szanto, A. J., & Cristofalo, V. J. (1996) · PubMed · Cited by 54 · see citing works
The alternative reading frame tumor suppressor inhibits growth through p21-dependent and p21-independent pathways.
Modestou, M., Puig-Antich, V., Korgaonkar, C. K., Eapen, A. K., & Quelle, D. E. (2001) · PubMed · Cited by 44 · see citing works
Increase in expression levels of interferon-inducible genes in senescent human diploid fibroblasts and in SV40-transformed human fibroblasts with extended lifespan.
Tahara, H., Kamada, K., Sato, E. F., Tsuyama, N., Kim, J.-K., Hara, E., Oda, K., & Ide, T. (1995) · PubMed · Cited by 37 · see citing works
Analysis of DNA microarrays using algorithms that employ rule-based expert knowledge
Pan, K., Lih, C., & Cohen, S. N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251687398 · Cited by 35 · see citing works
Self-citation
Disparate effects of telomere attrition on gene expression during replicative senescence of human mammary epithelial cells cultured under different conditions
Zhang, H., Herbert, B., Pan, K., Shay, J. W., & Cohen, S. N. (2004) · Oncogene · doi:10.1038/sj.onc.1207834 · Cited by 34 · see citing works
Self-citation

Flagged first, then by citations

Research works printed but not linked: 1

Chang, B.D., Watanabe, K., Broude, E.V., Fang, J., Poole, J.C., Kalinichenko, T.V., and Roninson, I.B. 2000. Effects of p21Waf1/Cip1/Sdi1 on cellular gene expression: Implica- tions for carcinogenesis, senescence, and age-related dis- eases. Proc. Natl. Acad. Sci. 97: 4291-4296.

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Campisi, J., & d'Adda di Fagagna, F. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2233 · Cited by 4,441 · see citing works
Living on a break: cellular senescence as a DNA-damage response
d'Adda di Fagagna, F. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2440 · Cited by 1,170 · see citing works
Critical pathways in cellular senescence and immortalization revealed by gene expression profiling
Fridman, A. L., & Tainsky, M. A. (2008) · Oncogene · doi:10.1038/onc.2008.213 · Cited by 385 · see citing works
Redox control of senescence and age-related disease.
Chandrasekaran, A., Idelchik, M. D. P. S., & Melendez, J. A. (2017) · Redox Biology · doi:10.1016/j.redox.2016.11.005 · Cited by 360 · see citing works
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Swanson, E. C., Manning, B., Zhang, H., & Lawrence, J. B. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201306073 · Cited by 251 · see citing works
“Just 2 d after selection of SMURF2 expressing cells, only 5% had SAHF, whereas 39% had SADS.”
BackgroundMethodInfluentialSelf-citation
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O’Sullivan, R. J., Arnoult, N., Lackner, D. H., Oganesian, L., Haggblom, C., Corpet, A., Almouzni, G., & Karlseder, J. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2754 · Cited by 259 · see citing works
Oncogene-induced senescence: the bright and dark side of the response
Gorgoulis, V. G., & Halazonetis, T. D. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.07.013 · Cited by 257 · see citing works
Characterization of novel markers of senescence and their prognostic potential in cancer
Althubiti, M., Lezina, L., Carrera, S., Jukes-Jones, R., Giblett, S. M., Antonov, A., Barlev, N., Saldanha, G. S., Pritchard, C. A., Cain, K., et al. (2014) · Cell Death & Disease · doi:10.1038/cddis.2014.489 · Cited by 256 · see citing works
Transforming growth factor-β and the hallmarks of cancer
Tian, M., Neil, J. R., & Schiemann, W. P. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.10.015 · Cited by 245 · see citing works
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Chen, C., & Matesic, L. E. (2007) · Cancer and Metastasis Reviews · doi:10.1007/s10555-007-9091-x · Cited by 228 · see citing works
Quantitative assay of senescence-associated β-galactosidase activity in mammalian cell extracts
Gary, R. K., & Kindell, S. M. (2005) · Analytical Biochemistry · doi:10.1016/j.ab.2005.06.003 · Cited by 195 · see citing works
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Lönn, P., Morén, A., Raja, E., Dahl, M., & Moustakas, A. (2008) · Cell Research · doi:10.1038/cr.2008.308 · Cited by 183 · see citing works
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Blank, M., Tang, Y., Yamashita, M., Burkett, S. S., Cheng, S. Y., & Zhang, Y. E. (2012) · Nature Medicine · doi:10.1038/nm.2596 · Cited by 156 · see citing works
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Fu, L., Cui, C., Zhang, X., & Zhang, L. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.12.023 · Cited by 118 · see citing works
Cellular senescence: hot or what?
Evan, G. I., & di Fagagna, F. D. (2009) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2008.11.009 · Cited by 109 · see citing works
Notch3 Functions as a Tumor Suppressor by Controlling Cellular Senescence
Cui, H., Kong, Y., Xu, M., & Zhang, H. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-3902 · Cited by 106 · see citing works
Self-citation
Effect of SMURF2 Targeting on Susceptibility to MEK Inhibitors in Melanoma
Smith, M. P., Ferguson, J., Arozarena, I., Hayward, R., Marais, R., Chapman, A., Hurlstone, A. F. L., & Wellbrock, C. (2012) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djs471 · Cited by 106 · see citing works
Telomeres in aging and disease: lessons from zebrafish
Carneiro, M. C., de Castro, I. P., & Ferreira, M. G. (2016) · Disease Models & Mechanisms · doi:10.1242/dmm.025130 · Cited by 105 · see citing works
HECT-Type E3 Ubiquitin Ligases in Cancer
Bernassola, F., Chillemi, G., & Melino, G. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.08.004 · Cited by 103 · see citing works
WNT16B Is a New Marker of Cellular Senescence That Regulates p53 Activity and the Phosphoinositide 3-Kinase/AKT Pathway
Binet, R., Ythier, D., Robles, A. I., Collado, M., Larrieu, D., Fonti, C., Brambilla, E., Brambilla, C., Serrano, M., Harris, C. C., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-1016 · Cited by 101 · see citing works
Smurf E3 ubiquitin ligases at the cross roads of oncogenesis and tumor suppression
David, D., Nair, S. A., & Pillai, M. R. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.11.003 · Cited by 89 · see citing works
Cellular Senescence in the Development and Treatment of Cancer
Saretzki, G. C. (2009) · Current Pharmaceutical Design · doi:10.2174/138161210789941874 · Cited by 88 · see citing works
Smurf2 Induces Ubiquitin-dependent Degradation of Smurf1 to Prevent Migration of Breast Cancer Cells
Fukunaga, E., Inoue, Y., Komiya, S., Horiguchi, K., Goto, K., Saitoh, M., Miyazawa, K., Koinuma, D., Hanyu, A., & Imamura, T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710496200 · Cited by 87 · see citing works
Breaking news: high-speed race ends in arrest – how oncogenes induce senescence
Micco, R. D., Fumagalli, M., & di Fagagna, F. D. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.07.012 · Cited by 80 · see citing works
Smad Ubiquitination Regulatory Factor 2 Promotes Metastasis of Breast Cancer Cells by Enhancing Migration and Invasiveness
Jin, C., Yang, Y.-A., Anver, M. R., Morris, N. L., Wang, X., & Zhang, Y. E. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-1463 · Cited by 80 · see citing works
Smad ubiquitination regulatory factor-2 in the fibrotic kidney: regulation, target specificity, and functional implication
Tan, R., He, W., Lin, X., Kiss, L. P., & Liu, Y. (2008) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00323.2007 · Cited by 77 · see citing works
Smurf2 suppresses B-cell proliferation and lymphomagenesis by mediating ubiquitination and degradation of YY1
Ramkumar, C., Cui, H., Kong, Y., Jones, S. N., Gerstein, R. M., & Zhang, H. (2013) · Nature Communications · doi:10.1038/ncomms3598 · Cited by 75 · see citing works
Self-citation
The ubiquitin ligase Smurf2 suppresses TGFβ-induced epithelial–mesenchymal transition in a sumoylation-regulated manner
Chandhoke, A. S., Karve, K., Dadakhujaev, S., Netherton, S. J., Deng, L., & Bonni, S. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.152 · Cited by 72 · see citing works
Markers of cellular senescence.
Carnero, A. (2013) · Methods in Molecular Biology · doi:10.1007/978-1-62703-239-1_4 · Cited by 68 · see citing works
SNEV overexpression extends the life span of human endothelial cells
Voglauer, R., Chang, M. W.-F., Dampier, B., Wieser, M., Baumann, K., Sterovsky, T., Schreiber, M., Katinger, H. W. D., & Grillari, J. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.11.025 · Cited by 65 · see citing works
Inhibition of Smurf2 translation by miR-322/503 modulates TGF-β/Smad2 signaling and intestinal epithelial homeostasis
Cao, S., Xiao, L., Rao, J. N., Zou, T., Liu, L., Zhang, D., Turner, D. J., Gorospe, M., & Wang, J. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-09-0560 · Cited by 65 · see citing works
The SWI/SNF ATPases Are Required for Triple Negative Breast Cancer Cell Proliferation
Wu, Q., Madany, P., Akech, J., Dobson, J. R., Douthwright, S., Browne, G., Colby, J. L., Winter, G. E., Bradner, J. E., Pratap, J., et al. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.24991 · Cited by 63 · see citing works
Smurf2‐mediated ubiquitination and degradation of Id1 regulates p16 expression during senescence
Kong, Y., Cui, H., & Zhang, H. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00746.x · Cited by 62 · see citing works
Self-citation
Transcriptomic profiling suggests a role for IGFBP5 in premature senescence of endothelial cells after chronic low dose rate irradiation
Rombouts, C., Aerts, A., Quintens, R., Baselet, B., Saghire, H. E., Harms‐Ringdahl, M., Haghdoost, S., Janssen, A., Michaux, A., Yentrapalli, R., et al. (2014) · International Journal of Radiation Biology · doi:10.3109/09553002.2014.905724 · Cited by 61 · see citing works
Ubiquitin-Dependent Regulation of TGβ Signaling in Cancer
Izzi, L., & Attisano, L. (2006) · Neoplasia · doi:10.1593/neo.06472 · Cited by 60 · see citing works
Gene expression changes in aging Zebrafish (Danio rerio) brains are sexually dimorphic
Arslan-Ergül, A., & Adams, M. M. (2014) · BMC Neuroscience · doi:10.1186/1471-2202-15-29 · Cited by 59 · see citing works
WW Domain-containing E3 Ubiquitin Protein Ligase 1 (WWP1) Delays Cellular Senescence by Promoting p27Kip1 Degradation in Human Diploid Fibroblasts
Cao, X., Xue, L., Han, L., Ma, L., Chen, T., & Tong, T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.225565 · Cited by 54 · see citing works
Smurf2 Regulates the Senescence Response and Suppresses Tumorigenesis in Mice
Ramkumar, C., Kong, Y., Cui, H., Hao, S., Jones, S. N., Gerstein, R. M., & Zhang, H. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-3773 · Cited by 47 · see citing works
Self-citation
Upregulation of SIRT1 by 17β-estradiol depends on ubiquitin-proteasome degradation of PPAR-γ mediated by NEDD4-1
Han, L., Wang, P., Zhao, G., Wang, H., Wang, M., Chen, J., & Tong, T. (2013) · Protein & Cell · doi:10.1007/s13238-013-2124-z · Cited by 45 · see citing works
Escape from oncogene-induced senescence is controlled by POU2F2 and memorized by chromatin scars
Martínez‐Zamudio, R. I., Stefa, A., de Freitas, J. A. N. L. F., Vasilopoulos, T., Simpson, M., Doré, G. R. G., Roux, P., Galan, M. A., Chokshi, R. J., Bischof, O., et al. (2023) · Cell Genomics · doi:10.1016/j.xgen.2023.100293 · Cited by 44 · see citing works
Cellular Senescence as a Target in Cancer Control
Vergel, M., Marín, J., Estévez, P., & Carnero, A. (2010) · Journal of Aging Research · doi:10.4061/2011/725365 · Cited by 43 · see citing works
Mechanisms of Action of TGF‐β in Cancer
Li, H., & Liu, J. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1396.016 · Cited by 42 · see citing works
Stress response decay with aging visualized using a dual-channel logic-based fluorescent probe
Tian, J., Shi, D., Zhang, Y., Li, X., Li, X., Teng, H. W., James, T. D., Li, J., & Guo, Y. (2021) · Chemical Science · doi:10.1039/d1sc04162b · Cited by 38 · see citing works
The ubiquitination ligase SMURF2 reduces aerobic glycolysis and colorectal cancer cell proliferation by promoting ChREBP ubiquitination and degradation
Li, Y., Yang, D., Tian, N., Zhang, P., Zhu, Y., Meng, J., Feng, M., Lu, Y., Liu, Q., Tong, L., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007508 · Cited by 39 · see citing works
Impaired osteogenesis of T1DM bone marrow-derived stromal cells and periosteum-derived cells and their differential in-vitro responses to growth factor rescue
Filion, T. M., Skelly, J. D., Huang, H. H., Greiner, D. L., Ayers, D. C., & Song, J. (2017) · Stem Cell Research & Therapy · doi:10.1186/s13287-017-0521-6 · Cited by 35 · see citing works
Post-Translational Modification of Cellular Proteins by Ubiquitin and Ubiquitin-Like Molecules: Role in Cellular Senescence and Aging
Grillari, J., Grillari‐Voglauer, R., & Jansen‐Dürr, P. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7002-2_13 · Cited by 34 · see citing works
Bypassing cellular senescence by genetic screening tools
Vergel, M., & Carnero, A. (2010) · Clinical & Translational Oncology · doi:10.1007/s12094-010-0528-2 · Cited by 30 · see citing works
Enhancing the regenerative effectiveness of growth factors by local inhibition of interleukin-1 receptor signaling
Julier, Z., Karami, R., Nayer, B., Lu, Y., Park, A. J., Maruyama, K., Kuhn, G. A., Müller, R., Akira, S., & Martino, M. M. (2020) · Science Advances · doi:10.1126/sciadv.aba7602 · Cited by 31 · see citing works
The MAPK Erk5 is necessary for proper skeletogenesis involving a Smurf-Smad-Sox9 molecular axis
Iezaki, T., Fukasawa, K., Horie, T., Park, G., Robinson, S. T., Nakaya, M., Fujita, H., Onishi, Y., Ozaki, K., Kanayama, T., et al. (2018) · Development · doi:10.1242/dev.164004 · Cited by 30 · see citing works
Beryllium Induces Premature Senescence in Human Fibroblasts
Coates, S. S. A., Lehnert, B. E., Sharma, S., Kindell, S. M., & Gary, R. K. (2007) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.118018 · Cited by 29 · see citing works
Effects of Cyclic Strain and Growth Factors on Vascular Smooth Muscle Cell Responses
Kona, S., Chellamuthu, P., Xu, H., Hills, S. R., & Nguyen, K. T. (2009) · The Open Biomedical Engineering Journal · doi:10.2174/1874120700903010028 · Cited by 28 · see citing works
Genomic profiling of acquired resistance to apoptosis in cells derived from human atherosclerotic lesions: Potential role of STATs, cyclinD1, BAD, and Bcl-X
Gagarin, D., Yang, Z., Butler, J. T., Wimmer, M. A., DU, B., Cahan, P., & McCaffrey, T. V. (2005) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.01.015 · Cited by 28 · see citing works
Overexpression of SnoN/SkiL, amplified at the 3q26.2 locus, in ovarian cancers: A role in ovarian pathogenesis
Nanjundan, M., Cheng, K. W., Zhang, F., Lahad, J., Kuo, W.-L., Schmandt, R., Smith-McCune, K., Fishman, D., Gray, J. W., & Mills, G. B. (2008) · Molecular Oncology · doi:10.1016/j.molonc.2008.05.001 · Cited by 26 · see citing works
Smurf2 Participates in Human Trophoblast Cell Invasion by Inhibiting TGF-β Type I Receptor
Yang, Q., Chen, S.-P., Zhang, X., Wang, H., Zhu, C., & Lin, H. (2009) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.2009.953166 · Cited by 26 · see citing works
The WW-HECT protein Smurf2 interacts with the Docking Protein NEDD9/HEF1 for Aurora A activation
Moore, F. E., Osmundson, E. C., Koblinski, J. E., Pugacheva, E. N., Golemis, E. A., Ray, D., & Kiyokawa, H. (2010) · Cell Division · doi:10.1186/1747-1028-5-22 · Cited by 24 · see citing works
Suppression of human tumor cell proliferation by Smurf2‐induced senescence
Zhang, H., Teng, Y., Kong, Y., Kowalski, P. E., & Cohen, S. N. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21337 · Cited by 23 · see citing works
Self-citation
Two Degradation Pathways of the p35 Cdk5 (Cyclin-dependent Kinase) Activation Subunit, Dependent and Independent of Ubiquitination
Takasugi, T., Minegishi, S., Asada, A., Saito, T., Kawahara, H., & Hisanaga, S. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.692871 · Cited by 22 · see citing works
Stress reactivity elicits a tissue-specific reduction in telomere length in aging zebrafish (Danio rerio)
Evans, J. R., Torres-Pérez, J. V., Petrazzini, M. E. M., Riley, R. J., & Brennan, C. H. (2021) · Scientific Reports · doi:10.1038/s41598-020-79615-1 · Cited by 20 · see citing works
Regulation of CNKSR2 protein stability by the HECT E3 ubiquitin ligase Smurf2, and its role in breast cancer progression
David, D., Surendran, A., Thulaseedharan, J. V., & Nair, S. A. (2018) · BMC Cancer · doi:10.1186/s12885-018-4188-x · Cited by 19 · see citing works
Intervertebral Disc Aging, Degeneration, and Associated Potential Molecular Mechanisms
Wu, Q. (2017) · Journal of Head Neck & Spine Surgery · doi:10.19080/jhnss.2017.01.555569 · Cited by 18 · see citing works
Smurf2 inhibition enhances chemotherapy and radiation sensitivity in non-small-cell lung cancer
Chaudhary, K. R., Kinslow, C. J., Cheng, H., Silva, J. M., Yu, J., Wang, T. J. C., Hei, T. K., Halmos, B., & Cheng, S. K. (2022) · Scientific Reports · doi:10.1038/s41598-022-14448-8 · Cited by 18 · see citing works
Senescence-associated exosomes transfer miRNA-induced fibrosis to neighboring cells
Lee, A. H., Ghosh, D., Koh, I. L., & Dawson, M. (2023) · Aging · doi:10.18632/aging.204539 · Cited by 18 · see citing works
The role of SMURFs in non‐cancerous diseases
Wang, D., Zou, Y., Huang, X., Yin, Z., Li, M., Xu, J., Wu, B., Li, D., Zhang, Y., Sun, Y., et al. (2023) · The FASEB Journal · doi:10.1096/fj.202300598r · Cited by 19 · see citing works
SMURF2 prevents detrimental changes to chromatin, protecting human dermal fibroblasts from chromosomal instability and tumorigenesis
Ayyathan, D. M., Koganti, P., Marcu‐Malina, V., Litmanovitch, T., Trakhtenbrot, L., Emanuelli, A., Apel‐Sarid, L., & Blank, M. (2020) · Oncogene · doi:10.1038/s41388-020-1226-3 · Cited by 18 · see citing works
The potential effect of fibroblast senescence on wound healing and the chronic wound environment
Henderson, E. A. (2006) · Journal of Wound Care · doi:10.12968/jowc.2006.15.7.26932 · Cited by 17 · see citing works
Cellular Senescence and Ageing
Reed, R., & Miwa, S. (2023) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-21410-3_7 · Cited by 16 · see citing works
Aberrant signaling and senescence associated protein degradation
Ferbeyre, G. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.06.016 · Cited by 16 · see citing works
Cellular Senescence and Anti-Cancer Therapy
You, J., Dong, R., Ying, M., He, Q., Cao, J., & Yang, B. (2018) · Current Drug Targets · doi:10.2174/1389450120666181217100833 · Cited by 16 · see citing works
Smurf2 regulates hematopoietic stem cell self‐renewal and aging
Ramkumar, C., Kong, Y., Trabucco, S. E., Gerstein, R. M., & Zhang, H. (2014) · Aging Cell · doi:10.1111/acel.12195 · Cited by 16 · see citing works
Self-citation
Smurf2 regulates IL17RB by proteasomal degradation of its novel binding partner DAZAP2
Popova, A., Kzhyshkowska, J. G., Nurgazieva, D., Goerdt, S., & Gratchev, A. N. (2011) · Immunobiology · doi:10.1016/j.imbio.2011.10.004 · Cited by 15 · see citing works
TGF‐β Initiates β‐Catenin‐Mediated CTGF Secretory Pathway in Old Bovine Nucleus Pulposus Cells: A Potential Mechanism for Intervertebral Disc Degeneration
Wu, Q., Mathers, C., Wang, E. W., Sheng, S., Wenkert, D., & Huang, J. H. (2018) · JBMR Plus · doi:10.1002/jbm4.10069 · Cited by 14 · see citing works
Assessing PCR Inhibition from Humic Substances
Matheson, C., Gurney, C., Esau, N., & Lehto, R. (2014) · The Open Enzyme Inhibition Journal · doi:10.2174/1874940201003010046 · Cited by 14 · see citing works
Expression Levels of SMAD Specific E3 Ubiquitin Protein Ligase 2 (Smurf2) and its Interacting Partners Show Region-specific Alterations During Brain Aging
Tuz-Sasik, M. U., Karoglu-Eravsar, E. T., Kinali, M., Ergul, A. A., & Adams, M. M. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.04.003 · Cited by 10 · see citing works
A Sulfated Nanofibrous Mesh Supporting the Osteogenic Differentiation of Periosteum-Derived Cells
Filion, T. M., & Song, J. (2013) · Journal of Biomaterials and Tissue Engineering · doi:10.1166/jbt.2013.1103 · Cited by 6 · see citing works
Expression of Smad Ubiquitin Regulatory Factor 2 (Smurf2) in Rhesus Monkey Endometrium and Placenta During Early Pregnancy
Yang, Q., Lin, H., Wang, H., Zhang, H., Zhang, X., Wang, H.-M., & Zhu, C. (2006) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.6a7069.2006 · Cited by 6 · see citing works
Self-citation
E3 ubiquitin ligases in B-cell malignancies
Choi, J., & Busino, L. (2019) · Cellular Immunology · doi:10.1016/j.cellimm.2019.02.004 · Cited by 6 · see citing works
Citronellal improves endothelial dysfunction by affecting the stability of the GCH1 protein
Guo, Y., Que, H., Chen, B., Chao, C.-Y., Li, S., Guo, S., Yin, Y., Wang, H., Zhu, M., & Li, P. (2024) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2024086 · Cited by 4 · see citing works
Regulation of Telomerase Through Transcriptional and Posttranslational Mechanisms
Depcrynski, A., Sachs, P. C., Elmore, L. W., & Holt, S. E. (2009) · Humana Press eBooks · doi:10.1007/978-1-60327-879-9_3 · Cited by 2 · see citing works
Higher-Order Unfolding of Peri/Centric Satellite Heterochromatin is an Early and Consistent Event in Cell Senescence: A Dissertation
Swanson, E. C. (2014) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/m2k30f · Cited by 1 · see citing works
Cancer, Senescence, and Aging: Translation from Basic Research to Clinics
LLeonart, M. E., Carnero, A., Paciucci, R., Wang, Z., & Shomron, N. (2011) · Journal of Aging Research · doi:10.4061/2011/692301 · Cited by 1 · see citing works
Upregulation of SIRT1 by 17β-estradiol depends on ubiquitin-proteasome degradation of PPAR-γ mediated by NEDD4-1 ESEARCH ARTICLE R
Han, L., Wang, P., Zhao, G., Wang, H., Wang, M., Chen, J., Tong, T., & Chen, J. (2013) · Cited by 1 · see citing works
Protein Quality Control Coming of Age
Meiners, S. (2014) · doi:10.1002/9781118396292.ch3 · Cited by 1 · see citing works
Transforming Growth Factor-β in Cancer Therapy: Smurfs in TGF-β Signaling and Regulation of Bone Homeostasis and Cancer
Zhang, Y. E., & Yamashita, M. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-292-2_10 · Cited by 1 · see citing works
Ubiquitin-Dependent Regulation of TGFB Signaling in Cancer1
Izzi, L., & Attisano, L. (2014) · Cited by 1 · see citing works
Analysis of senescence-like growth arrest induced by RUNX1 and its fusion derived oncoproteins
Wolyniec, K. (2008) · Enlighten: Theses (The University of Glasgow) · doi:10.5525/gla.thesis.578
TRANSCRIPTOME STUDIES OF CELL-FATE AND AGING
Larsson, O. S. (2005) · Figshare
Effect of SMURF2 targeting on susceptibility to MEK inhibitors in melanoma.
Smith, M. P., Ferguson, J., Arozarena, I., Hayward, R., Marais, R., Chapman, A., Hurlstone, A. F. L., & Wellbrock, C. (2013) · University of Huddersfield Repository (University of Huddersfield)
The primary cilium as a regulator of cellular senescence in human fibroblasts
Breslin, L. (2014) · ARAN (University of Galway Research Repository) (Ollscoil na Gaillimhe – University of Galway) · doi:10.13025/17764
TGF-β/Smad Signalling Pathway in Cancer
Hasanpourghadi, M., & Mustafa, M. R. (2018) · Springer eBooks · doi:10.1007/978-3-319-71553-7_9
The Molecular Physiology of Ageing: New Targets for Regenerative Medicine
Macip, S., & Althubiti, M. (2019) · Springer eBooks · doi:10.1007/978-3-030-15458-5_3
Characterization of Senescence Regulation by Smurf2 and Notch3 in vitro and in vivo
Wong, L. C. (2012) · Digital WPI
Faculty Opinions recommendation of Rapid induction of alternative lengthening of telomeres by depletion of the histone chaperone ASF1.
Hickson, I. D., & Mankouri, H. W. (2014) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.718235134.793493488
Senescence in Oncogenesis: From Molecular Mechanisms to Therapeutic Opportunities
Muñoz-Galván, S., & Carnero, A. (2014) · Springer eBooks · doi:10.1007/978-94-017-9421-3_7
Implication des protéines HMGA et HMGA2 dans les changements du programme de réplication au cours de la sénescence cellulaire
Kahli, M. (2011) · theses.fr (ABES) · doi:10.70675/bc7bcb93z46bdz473aza3ebz5cc713b77897
Rôle protecteur des cellules de Küpffer de phénotype M2 anti-inflammatoire dans la maladie alcoolique du foie
Benkdane, M. (2012) · doi:10.70675/45d1370fz6819z4b07zb446zd155483ab1de
Cellules souches dérivées du muscle humain « MuStem » : modalités de préparation in vitro et caractéristiques biologiques pour une application clinique
Saury, C. (2017) · doi:10.70675/5ad5ac21z12afz4845zb3e5zb9716e79df0b
The Senescent Cell Induced Bystander Effect
Wordsworth, J. (2014)

Authors: Zhang, H., & Cohen, S. N.
Affiliations: Stanford Medicine (US)
ORCID: Zhang, Hong
Venue: Genes & Development
Publisher: Cold Spring Harbor Laboratory
Published: 2004-12-01
Volume: 18
Issue: 24
Pages: 3028-3040
ISSN: 0890-9369 (ISSN-L)
1549-5477
DOI: 10.1101/gad.1253004
PMC: PMC535914
OpenAlex: W2147934454
Cited by: 100
References: 66
Citations by year: 2024: 1 · 2023: 4 · 2022: 1 · 2021: 3 · 2020: 3 · 2019: 5 · 2018: 5 · 2017: 4 · 2016: 2 · 2015: 3 · 2014: 14 · 2013: 7 · 2012: 7
Type: posted content
Language: en
Open access: bronze
doi.org
Locations: Genes & Development (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
eScholarship@UMassChan (submittedVersion)
Funders: Ellison Medical Foundation
National Foundation for Cancer Research
California Breast Cancer Research Program
Topics: Health Sciences › Medicine › Physiology › Telomeres, Telomerase, and Senescence
Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
Keywords: Smurf2, telomere shortening, replicative senescence, E3 ubiquitin ligase, human fibroblasts, telomerase, cell immortalization, p53 pathway, Rb pathway, p21, senescence-associated gene expression, aging, tumor suppression
MeSH terms: Cell Line, Fibroblasts, Fluorescent Antibody Technique, Genetic Vectors, Humans, Plasmids, Blotting, Northern, Blotting, Western, Up-Regulation, Tumor Suppressor Protein p53, Retinoblastoma Protein, Telomere, Cellular Senescence, Reverse Transcriptase Polymerase Chain Reaction, Oligonucleotide Array Sequence Analysis, Ubiquitin-Protein Ligases

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Smurf2 up-regulation activates telomere-dependent senescence

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