Multiple degradation pathways regulate versatile CIP/KIP CDK inhibitors

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

The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction

Glickman, M. H., & Ciechanover, A. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,216 · see citing works

p21 in cancer: Intricate networks and multiple activities

Abbas, T., & Dutta, A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2657 · Cited by 2,712 · see citing works

Function and regulation of cullin–RING ubiquitin ligases

Petroski, M. D., & Deshaies, R. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1547 · Cited by 2,148 · see citing works

PCNA, the Maestro of the Replication Fork

Moldovan, G.-L., Pfander, B., & Jentsch, S. (2007) · Cell · doi:10.1016/j.cell.2007.05.003 · Cited by 1,796 · see citing works

SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27

Carrano, A. C., Eytan, E., Hershko, A., & Pagano, M. (1999) · Nature Cell Biology · doi:10.1038/12013 · Cited by 1,544 · see citing works

CDK inhibitors: Cell cycle regulators and beyond

Besson, A., Dowdy, S. F., & Roberts, J. M. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.01.013 · Cited by 1,152 · see citing works

Recycling the Cell Cycle

Murray, A. W. (2004) · Cell · doi:10.1016/s0092-8674(03)01080-8 · Cited by 1,054 · see citing works

The Cdk inhibitor p27 in human cancer: prognostic potential and relevance to anticancer therapy

Chu, I. M., Hengst, L., & Slingerland, J. M. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2347 · Cited by 986 · see citing works

The energy sensing LKB1–AMPK pathway regulates p27kip1 phosphorylation mediating the decision to enter autophagy or apoptosis

Liang, J., Shao, S. H., Xu, Z.-X., Hennessy, B. T., Ding, Z., Larrea, M. D., Kondo, S., Dumont, D. J., Gutterman, J. U., Walker, C. L., et al. (2007) · Nature Cell Biology · doi:10.1038/ncb1537 · Cited by 868 · see citing works

Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation

Duda, D. M., Borg, L. A., Scott, D. C., Hunt, H. W., Hammel, M., & Schulman, B. A. (2008) · Cell · doi:10.1016/j.cell.2008.07.022 · Cited by 767 · see citing works

Systematic analysis and nomenclature of mammalian F-box proteinsPreprint

Jin, J., Cardozo, T. J., Lovering, R. C., Elledge, S. J., Pagano, M., & Harper, J. W. (2004) · Genes & Development · doi:10.1101/gad.1255304 · Cited by 716 · see citing works

ADF/Cofilin: a functional node in cell biology

Bernstein, B. W., & Bamburg, J. R. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.01.001 · Cited by 704 · see citing works

Apoptosis inhibitory activity of cytoplasmic p21Cip1/WAF1 in monocytic differentiation

Asada, M., Yamada, T., Ichijo, H., Delia, D., Miyazono, K., Fukumuro, K., & Mizutani, S. (1999) · The EMBO Journal · doi:10.1093/emboj/18.5.1223 · Cited by 586 · see citing works

Rho signaling, ROCK and mDia1, in transformation, metastasis and invasion

Narumiya, S., Tanji, M., & Ishizaki, T. (2009) · Cancer and Metastasis Reviews · doi:10.1007/s10555-008-9170-7 · Cited by 530 · see citing works

Control of the SCFSkp2–Cks1 ubiquitin ligase by the APC/CCdh1 ubiquitin ligase

Bashir, T., Dorrello, N. V., Amador, V., Guardavaccaro, D., & Pagano, M. (2004) · Nature · doi:10.1038/nature02330 · Cited by 504 · see citing works

The cofilin pathway in breast cancer invasion and metastasis

Wang, W., Eddy, R. J., & Condeelis, J. S. (2007) · Nature reviews. Cancer · doi:10.1038/nrc2148 · Cited by 487 · see citing works

VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligasesPreprint

Kamura, T., Maenaka, K., Kotoshiba, S., Matsumoto, M., Kohda, D., Conaway, R. C., Conaway, J. W., & Nakayama, K. I. (2004) · Genes & Development · doi:10.1101/gad.1252404 · Cited by 476 · see citing works

p21WAF1/Cip1: more than a break to the cell cycle?

Dotto, G. P. (2000) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(00)00019-6 · Cited by 474 · see citing works

p21 and p27: roles in carcinogenesis and drug resistance

Abukhdeir, A. M., & Park, B. H. (2008) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399408000744 · Cited by 463 · see citing works

Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27Kip1 at G1 phase

Kamura, T., Hara, T., Matsumoto, M., Ishida, N., Okumura, F., Hatakeyama, S., Yoshida, M., Nakayama, K., & Nakayama, K. (2004) · Nature Cell Biology · doi:10.1038/ncb1194 · Cited by 413 · see citing works

CRL4s: the CUL4-RING E3 ubiquitin ligases

Jackson, S., & Xiong, Y. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.07.002 · Cited by 410 · see citing works

Dynamics of Cullin-RING Ubiquitin Ligase Network Revealed by Systematic Quantitative Proteomics

Bennett, E. J., Rush, A. J., Gygi, S. P., & Harper, J. W. (2010) · Cell · doi:10.1016/j.cell.2010.11.017 · Cited by 386 · see citing works

p27 Phosphorylation by Src Regulates Inhibition of Cyclin E-Cdk2

Chu, I. M., Sun, J., Arnaout, A., Kahn, H., Hanna, W. M., Narod, S. A., Sun, P., Tan, C., Hengst, L., & Slingerland, J. M. (2007) · Cell · doi:10.1016/j.cell.2006.11.049 · Cited by 372 · see citing works

p27 kip1 independently promotes neuronal differentiation and migration in the cerebral cortexPreprint

Nguyen, L., Besson, A., Heng, J. I., Schuurmans, C. J., Teboul, L., Parras, C. M., Philpott, A., Roberts, J. M., & Guillemot, F. (2006) · Genes & Development · doi:10.1101/gad.377106 · Cited by 367 · see citing works

Skp2-Mediated Degradation of p27 Regulates Progression into Mitosis

Nakayama, K., Nagahama, H., Minamishima, Y. A., Miyake, S., Ishida, N., Hatakeyama, S., Kitagawa, M., Iemura, S.-I., Natsume, T., & Nakayama, K. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00131-5 · Cited by 364 · see citing works

Nuclear Accumulation of p21 Cip1 at the Onset of Mitosis: a Role at the G 2 /M-Phase Transition

Dulić, V., Stein, G. H., Far, D. F., & Reed, S. I. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.1.546 · Cited by 352 · see citing works

Cdk-Inhibitory Activity and Stability of p27 Are Directly Regulated by Oncogenic Tyrosine Kinases

Grimmler, M., Wang, Y., Mund, T., Cilenšek, Z., Keidel, E.-M., Waddell, M. B., Jäkel, H., Kullmann, M., Kriwacki, R. W., & Hengst, L. (2007) · Cell · doi:10.1016/j.cell.2006.11.047 · Cited by 337 · see citing works

The SOCS box of SOCS-1 accelerates ubiquitin-dependent proteolysis of TEL-JAK2

Kamizono, S., Hanada, T., Yasukawa, H., Minoguchi, S., Kato, R., Minoguchi, M., Hattori, K., Hatakeyama, S., Yada, M., Morita, S., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010074200 · Cited by 311 · see citing works

Cullin-RING ubiquitin ligases: global regulation and activation cycles

Bosu, D. R., & Kipreos, E. T. (2008) · Cell Division · doi:10.1186/1747-1028-3-7 · Cited by 309 · see citing works

The Cytoplasmic Shuttling and Subsequent Degradation of p27Kip1 Mediated by Jab1/CSN5 and the COP9 Signalosome Complex

Tomoda, K., Kubota, Y., Arata, Y., Mori, S., Maeda, M., Tanaka, T., Yoshida, M., Yoneda‐Kato, N., & Kato, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m104431200 · Cited by 307 · see citing works

p27 cytoplasmic localization is regulated by phosphorylation on Ser10 and is not a prerequisite for its proteolysis

Rodier, G., Montagnoli, A., Marcotullio, L. D., Coulombe, P., Draetta, G. F., Pagano, M., & Meloche, S. (2001) · The EMBO Journal · doi:10.1093/emboj/20.23.6672 · Cited by 286 · see citing works

MDM2 Is a Negative Regulator of p21 , Independent of p53

Zhang, Z., Wang, H., Li, M., Agrawal, S., Chen, X., & Zhang, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312264200 · Cited by 253 · see citing works

Regulation of Cell Division by Intrinsically Unstructured Proteins: Intrinsic Flexibility, Modularity, and Signaling Conduits

Galea, C. A., Wang, Y., Sivakolundu, S. G., & Kriwacki, R. W. (2008) · Biochemistry · doi:10.1021/bi8006803 · Cited by 243 · see citing works

The CRL4^Cdt2 ubiquitin ligase targets the degradation of p21^Cip1 to control replication licensing

Kim, Y., Starostina, N. G., & Kipreos, E. T. (2008) · Genes & Development · doi:10.1101/gad.1703708 · Cited by 240 · see citing works

Ubiquitylation and proteasomal degradation of the p21 Cip1 , p27 Kip1 and p57 Kip2 CDK inhibitors

Lu, Z., & Hunter, T. R. (2010) · Cell Cycle · doi:10.4161/cc.9.12.11988 · Cited by 225 · see citing works

Mechanism of CRL4Cdt2, a PCNA-dependent E3 ubiquitin ligasePreprint

Havens, C. G., & Walter, J. C. (2011) · Genes & Development · doi:10.1101/gad.2068611 · Cited by 223 · see citing works

Sustained Activation of the JNK Cascade and Rapamycin-Induced Apoptosis Are Suppressed by p53/p21Cip1

Huang, S., Shu, L., Dilling, M. B., Easton, J. B., Harwood, F. C., Ichijo, H., & Houghton, P. J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00180-1 · Cited by 216 · see citing works

APC/CCdc20 Controls the Ubiquitin-Mediated Degradation of p21 in Prometaphase

Amador, V., Ge, S., Santamarı́a, P. G., Guardavaccaro, D., & Pagano, M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.013 · Cited by 209 · see citing works

MDM2 promotes p21waf1/cip1 proteasomal turnover independently of ubiquitylation

Jin, Y., Lee, H., Zeng, S. X., Dai, M., & Lu, H. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg600 · Cited by 206 · see citing works

Association of human CUL‐1 and ubiquitin‐conjugating enzyme CDC34 with the F‐box protein p45SKP2: evidence for evolutionary conservation in the subunit composition of the CDC34–SCF pathway

Lisztwan, J. H., Marti, A., Sutterlüty, H., Gstaiger, M., Wirbelauer, C., & Krek, W. (1998) · The EMBO Journal · doi:10.1093/emboj/17.2.368 · Cited by 203 · see citing works

Characterization of Cullin-box Sequences That Direct Recruitment of Cul2-Rbx1 and Cul5-Rbx2 Modules to Elongin BC-based Ubiquitin Ligases

Mahrour, N., Redwine, W. B., Florens, L., Swanson, S. K., Martin-Brown, S., Bradford, W. D., Staehling-Hampton, K., Washburn, M. P., Conaway, R. C., & Conaway, J. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706987200 · Cited by 196 · see citing works

Docking of a Specialized PIP Box onto Chromatin-Bound PCNA Creates a Degron for the Ubiquitin Ligase CRL4Cdt2

Havens, C. G., & Walter, J. C. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.05.012 · Cited by 178 · see citing works

Cytoplasmic p21Cip1 Is Involved in Ras-induced Inhibition of the ROCK/LIMK/Cofilin Pathway

Lee, S., & Helfman, D. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306968200 · Cited by 163 · see citing works

Differential regulation of p53 and p21 by MKRN1 E3 ligase controls cell cycle arrest and apoptosis

Lee, E., Lee, M.-S., Camus, S., Ghim, J., Yang, M. R., Oh, W., Ha, N., Lane, D. P., & Song, J. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.164 · Cited by 158 · see citing works

p57KIP2: “Kip”ing the Cell under Control

Pateras, I. S., Apostolopoulou, K., Niforou, K., Kotsinas, A., & Gorgoulis, V. G. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-09-0317 · Cited by 150 · see citing works

CRL4Cdt2

Abbas, T., & Dutta, A. (2011) · Cell Cycle · doi:10.4161/cc.10.2.14530 · Cited by 144 · see citing works

Stabilizers and Destabilizers Controlling Cell Cycle Oscillators

Guardavaccaro, D., & Pagano, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.017 · Cited by 116 · see citing works

Transcriptional Regulation during p21/-induced Apoptosis in Human Ovarian Cancer Cells

Wu, Q. J., Kirschmeier, P. T., Hockenberry, T., Yang, T., Brassard, D., Wang, L., McClanahan, T., Black, S., Rizzi, G., Musco, M. L., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204962200 · Cited by 116 · see citing works

p57Kip2 Regulates Actin Dynamics by Binding and Translocating LIM-kinase 1 to the Nucleus

Yokoo, T., Toyoshima, H., Miura, M., Wang, Y., Iida, K., Suzuki, H., Sone, H., Shimano, H., Gotoda, T., Nishimori, S., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309334200 · Cited by 115 · see citing works

E6-associated protein (E6-AP) is a dual function coactivator of steroid hormone receptors

Ramamoorthy, S., & Nawaz, Z. (2008) · Nuclear Receptor Signaling · doi:10.1621/nrs.06006 · Cited by 109 · see citing works

Phosphorylation of Skp2 regulated by CDK2 and Cdc14B protects it from degradation by APCCdh1 in G1 phase

Rodier, G., Coulombe, P., Tanguay, P., Boutonnet, C., & Meloche, S. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.6 · Cited by 106 · see citing works

Stabilization of MyoD by Direct Binding to p57Kip2

Reynaud, E. G., Leibovitch, M.-P., Tintignac, L. A. J., Pelpel, K., Guillier, M., & Leibovitch, S. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m907412199 · Cited by 104 · see citing works

Cul4A and DDB1 Associate with Skp2 To Target p27Kip1 for Proteolysis Involving the COP9 Signalosome

Bondar, T., Kalinina, A., Khair, L., Kopanja, D., Nag, A., Bagchi, S., & Raychaudhuri, P. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.7.2531-2539.2006 · Cited by 103 · see citing works

Pirh2 Promotes Ubiquitin-Dependent Degradation of the Cyclin-Dependent Kinase Inhibitor p27 Kip1

Hattori, T., Isobe, T., Abe, K., Kikuchi, H., Kitagawa, K., Oda, T., Uchida, C., & Kitagawa, M. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-2033 · Cited by 91 · see citing works

Cul4A targets p27 for degradation and regulates proliferation, cell cycle exit, and differentiation during erythropoiesis

Li, B., Jia, N., Kapur, R., & Chun, K. T. (2006) · Blood · doi:10.1182/blood-2005-08-3349 · Cited by 89 · see citing works

UBE3A/E6-AP regulates cell proliferation by promoting proteasomal degradation of p27

Mishra, A., Godavarthi, S. K., & Jana, N. R. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.06.010 · Cited by 88 · see citing works

Procaspase 3/p21 complex formation to resist Fas-mediated cell death is initiated as a result of the phosphorylation of p21 by protein kinase A

Suzuki, A., Kawano, H., Hayashida, M., Hayasaki, Y., Tsutomi, Y., & Akahane, K. (2000) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400706 · Cited by 84 · see citing works

A functional link between Wnt signaling and SKP2-independent p27 turnover in mammary tumorsPreprint

Miranda‐Carboni, G. A., Krum, S. A., Yee, K. M., Nava, M., Deng, Q., Pervin, S., Collado-Hidalgo, A., Galić, Z., Zack, J. A., Nakayama, K., et al. (2008) · Genes & Development · doi:10.1101/gad.1692808 · Cited by 83 · see citing works

MDMX Promotes Proteasomal Turnover of p21 at G1 and Early S Phases Independently of, but in Cooperation with, MDM2

Jin, Y., Zeng, S. X., Sun, X., Lee, H., Blattner, C., Xiao, Z. J., & Lu, H. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01198-07 · Cited by 79 · see citing works

PARC and CUL7 Form Atypical Cullin RING Ligase Complexes

Skaar, J. R., Florens, L. A., Tsutsumi, T., Arai, T., Tron, A. E., Swanson, S. K., Washburn, M. P., & DeCaprio, J. A. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3241 · Cited by 77 · see citing works

p57KIP2 Modulates Stress-activated Signaling by Inhibiting c-Jun NH2-terminal Kinase/Stress-activated Protein Kinase

Chang, T.-S., Kim, M., Ryoo, K., Park, J., Eom, S. J., Shim, J., Nakayama, K., Nakayama, K., Takahashi, K., Lee, M.-J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309421200 · Cited by 74 · see citing works

Loss of p21CDKN1Aimpairs entry to quiescence and activates a DNA damage response in normal fibroblasts induced to quiescence

Perucca, P., Cazzalini, O., Madine, M. A., Savio, M., Laskey, R. A., Vannini, V., Prosperi, E., & Stivala, L. A. (2009) · Cell Cycle · doi:10.4161/cc.8.1.7507 · Cited by 71 · see citing works

State of the APC/C: Organization, function, and structure

McLean, J. R., Chaix, D., Ohi, M. D., & Gould, K. L. (2011) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.541420 · Cited by 70 · see citing works

Cyclin D2 Translocates p27 out of the Nucleus and Promotes Its Degradation at the G0-G1 Transition

Susaki, E. A., Nakayama, K., & Nakayama, K. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00862-06 · Cited by 65 · see citing works

The cell cycle inhibitor p57Kip2 promotes cell death via the mitochondrial apoptotic pathway

Engskog‐Vlachos, P., Nyman, U., Hajji, N., & Joseph, B. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402158 · Cited by 62 · see citing works

14-3-3τ Regulates Ubiquitin-Independent Proteasomal Degradation of p21, a Novel Mechanism of p21 Downregulation in Breast Cancer

Wang, B., Liu, K., Lin, H., Bellam, N., Ling, S., & Lin, W.-C. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01335-09 · Cited by 59 · see citing works

CRL2LRR-1 Targets a CDK Inhibitor for Cell Cycle Control in C. elegans and Actin-Based Motility Regulation in Human Cells

Starostina, N. G., Simpliciano, J. M., McGuirk, M. A., & Kipreos, E. T. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.10.013 · Cited by 58 · see citing works

Smad-mediated Transcription Is Required for Transforming Growth Factor-β1-induced p57Kip2 Proteolysis in Osteoblastic Cells

Nishimori, S., Tanaka, Y., Chiba, T., Fujii, M., Imamura, T., Miyazono, K., Ogasawara, T., Kawaguchi, H., Igarashi, T., Fujita, T., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007499200 · Cited by 57 · see citing works

Disruption of TGF-β growth inhibition by oncogenic ras is linked to p27Kip1 mislocalization

Liu, X., Sun, Y., Ehrlich, M., Lu, T., Kloog, Y., Weinberg, R. A., Lodish, H. F., & Henis, Y. I. (2000) · Oncogene · doi:10.1038/sj.onc.1203991 · Cited by 57 · see citing works

p53RFP, a p53-inducible RING-finger protein, regulates the stability of p21WAF1

Ng, C.-C., Arakawa, H., Fukuda, S., Kondoh, H., & Nakamura, Y. (2003) · Oncogene · doi:10.1038/sj.onc.1206586 · Cited by 54 · see citing works

p57: A multifunctional protein in cancer (Review)

Nan, N. (2010) · International Journal of Oncology · doi:10.3892/ijo_00000617 · Cited by 53 · see citing works

The Cdk inhibitor p57Kip2 controls LIM-kinase 1 activity and regulates actin cytoskeleton dynamics

Engskog‐Vlachos, P., & Joseph, B. (2009) · Oncogene · doi:10.1038/onc.2009.269 · Cited by 50 · see citing works

C. elegans CUL-4 Prevents Rereplication by Promoting the Nuclear Export of CDC-6 via a CKI-1-Dependent Pathway

Kim, J., Feng, H., & Kipreos, E. T. (2007) · Current Biology · doi:10.1016/j.cub.2007.04.055 · Cited by 48 · see citing works

A new ubiquitin ligase involved in p57KIP2 proteolysis regulates osteoblast cell differentiation

Kim, M., Nakamoto, T., Nishimori, S., Tanaka, K., & Chiba, T. (2008) · EMBO Reports · doi:10.1038/embor.2008.125 · Cited by 39 · see citing works

Involvement of Two Distinct Ubiquitin E3 Ligase Systems for p27 Degradation in Corneal Endothelial Cells

Lee, J. G., & Kay, E. P. (2008) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.07-0855 · Cited by 38 · see citing works

The p53‐inducible E3 ubiquitin ligase p53RFP induces p53‐dependent apoptosis

Huang, J., Xu, L., Liu, T., Zhai, Z., & Shu, H. (2006) · FEBS Letters · doi:10.1016/j.febslet.2005.09.105 · Cited by 37 · see citing works

The Initiation Step of Eukaryotic DNA Replication

Pospiech, H., Große, F., & Pisani, F. M. (2009) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-90-481-3471-7_5 · Cited by 34 · see citing works

Inflammation, antichymotrypsin, and lipid metabolism: autogenic etiology of alzheimer's disease

Janciauskiene, S. M., & Wright, H. T. (1999) · BioEssays · doi:10.1002/(sici)1521-1878(199812)20:12 · Cited by 24 · see citing works

The heart of the cycle

Lukas, J., & Bártek, J. (2004) · Nature · doi:10.1038/432564a · Cited by 23 · see citing works

DNA replication licensing control and rereplication prevention

Li, C., & Jin, J. (2010) · Protein & Cell · doi:10.1007/s13238-010-0032-z · Cited by 14 · see citing works

Short Linear Motifs: Ubiquitous and Functionally Diverse Protein Interaction Modules Directing Cell Regulation

Roey, K. V., Uyar, B., Weatheritt, R. J., Dinkel, H., Seiler, M., Budd, A., Gibson, T. J., & Davey, N. E. (2014) · Chemical Reviews · doi:10.1021/cr400585q · Cited by 496 · see citing works

DNA damage during S-phase mediates the proliferation-quiescence decision in the subsequent G1 via p21 expression

Barr, A. R., Cooper, S., Heldt, F. S., Butera, F., Stoy, H., Mansfeld, J., Novák, B., & Bakal, C. (2017) · Nature Communications · doi:10.1038/ncomms14728 · Cited by 403 · see citing works

Cyclin-dependent protein serine/threonine kinase inhibitors as anticancer drugs

Roskoski, R. J. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.11.035 · Cited by 401 · see citing works

The Multifaceted p21 (Cip1/Waf1/CDKN1A) in Cell Differentiation, Migration and Cancer Therapy

Kreis, N., Louwen, F., & Yuan, J. (2019) · Cancers · doi:10.3390/cancers11091220 · Cited by 309 · see citing works

Cyclin-dependent protein kinase inhibitors including palbociclib as anticancer drugs

Roskoski, R. J. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.03.012 · Cited by 238 · see citing works

The influence of reactive oxygen species on cell cycle progression in mammalian cells

Verbon, E. H., Post, J. A., & Boonstra, J. (2012) · Gene · doi:10.1016/j.gene.2012.08.038 · Cited by 234 · see citing works

Patterns of Early p21 Dynamics Determine Proliferation-Senescence Cell Fate after Chemotherapy

Hsu, C.-H., Altschuler, S. J., & Wu, L. F. (2019) · Cell · doi:10.1016/j.cell.2019.05.041 · Cited by 181 · see citing works

The Transcription Factor FOXM1 (Forkhead box M1)

Wierstra, I. (2013) · Advances in cancer research · doi:10.1016/b978-0-12-407173-5.00004-2 · Cited by 174 · see citing works

MicroRNA in pancreatic cancer

Yonemori, K., Kurahara, H., Maemura, K., & Natsugoe, S. (2016) · Journal of Human Genetics · doi:10.1038/jhg.2016.59 · Cited by 150 · see citing works

A Noncanonical Role for the CKI-RB-E2F Cell-Cycle Signaling Pathway in Plant Effector-Triggered Immunity

Wang, S., Gu, Y., Zebell, S. G., Anderson, L. K., Wang, W., Mohan, R., & Dong, X. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.10.005 · Cited by 125 · see citing works

Global Subcellular Characterization of Protein Degradation Using Quantitative Proteomics

Larance, M., Ahmad, Y., Kirkwood, K. J., Ly, T., & Lamond, A. I. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.024547 · Cited by 114 · see citing works

Less understood issues: p21Cip1 in mitosis and its therapeutic potential

Kreis, N., Louwen, F., & Yuan, J. (2014) · Oncogene · doi:10.1038/onc.2014.133 · Cited by 116 · see citing works

CDK-Independent and PCNA-Dependent Functions of p21 in DNA Replication

Mansilla, S. F., De La Vega, M. B., Calzetta, N. L., Siri, S. O., & Gottifredi, V. (2020) · Genes · doi:10.3390/genes11060593 · Cited by 114 · see citing works

NSun2 delays replicative senescence by repressing p27 (KIP1) translation and elevating CDK1 translation

Tang, H., Fan, X., Xing, J., Liu, Z., Jiang, B., Dou, Y., Gorospe, M., & Wang, W. (2015) · Aging · doi:10.18632/aging.100860 · Cited by 111 · see citing works

Distinct and overlapping functions of the cullin E3 ligase scaffolding proteins CUL4A and CUL4B

Hannah, J., & Zhou, P. (2015) · Gene · doi:10.1016/j.gene.2015.08.064 · Cited by 108 · see citing works

A p21-ZEB1 Complex Inhibits Epithelial-Mesenchymal Transition through the MicroRNA 183-96-182 Cluster

Li, X. L., Hara, T., Choi, Y., Subramanian, M., Francis, P., Bilke, S., Walker, R. L., Pineda, M. A., Zhu, Y. J., Yang, Y.-A., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01043-13 · Cited by 101 · see citing works

F-box protein interactions with the hallmark pathways in cancer

Randle, S. J., & Laman, H. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.09.013 · Cited by 95 · see citing works

The Complex Relationship between Liver Cancer and the Cell Cycle: A Story of Multiple Regulations

Bisteau, X., Caldez, M. J., & Kaldis, P. (2014) · Cancers · doi:10.3390/cancers6010079 · Cited by 91 · see citing works

Preparation for DNA replication: the key to a successful S phase

Limas, J. C., & Cook, J. G. (2019) · FEBS Letters · doi:10.1002/1873-3468.13619 · Cited by 88 · see citing works

SIRT1 Is Downregulated in Gastric Cancer and Leads to G1-phase Arrest via NF-κB/Cyclin D1 Signaling

Yang, Q., Wang, B., Gao, W., Huang, S., Liu, Z., Li, W., & Jia, J. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0214 · Cited by 86 · see citing works

Functions of Ubiquitin and SUMO in DNA Replication and Replication Stress

García‐Rodríguez, N., Wong, R. P. C., & Ulrich, H. D. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00087 · Cited by 82 · see citing works

Endothelial Side Population Cells Contribute to Tumor Angiogenesis and Antiangiogenic Drug Resistance

Naito, H., Wakabayashi, T., Kidoya, H., Muramatsu, F., Takara, K., Eino, D., Yamane, K., Iba, T., & Takakura, N. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2998 · Cited by 80 · see citing works

Tbx2 Controls Lung Growth by Direct Repression of the Cell Cycle Inhibitor Genes Cdkn1a and Cdkn1b

Lüdtke, T. H., Farin, H. F., Rudat, C., Schuster-Gossler, K., Petry, M., Barnett, P., Christoffels, V. M., & Kispert, A. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003189 · Cited by 79 · see citing works

A comprehensive model for the proliferation–quiescence decision in response to endogenous DNA damage in human cells

Heldt, F. S., Barr, A. R., Cooper, S., Bakal, C., & Novák, B. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1715345115 · Cited by 78 · see citing works

Cellular retinoic acid binding protein I mediates rapid non-canonical activation of ERK1/2 by all-trans retinoic acid

Persaud, S. D., Lin, Y.-W., Wu, C.-Y., Kagechika, H., & Wei, L. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.09.002 · Cited by 75 · see citing works

The Control of Arabidopsis thaliana Growth by Cell Proliferation and Endoreplication Requires the F-Box Protein FBL17

Noir, S., Marrocco, K., Masoud, K., Thomann, A., Gusti, A., Bitrián, M., Schnittger, A., & Genschik, P. (2015) · The Plant Cell · doi:10.1105/tpc.114.135301 · Cited by 71 · see citing works

p27 and Leukemia: Cell Cycle and Beyond

Roy, A., & Banerjee, S. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24819 · Cited by 64 · see citing works

Selective protein degradation: a rheostat to modulate cell-cycle phase transitions

Genschik, P., Marrocco, K., Bach, L., Noir, S., & Criqui, M. (2013) · Journal of Experimental Botany · doi:10.1093/jxb/ert426 · Cited by 60 · see citing works

Stat3 and C/EBPβ synergize to induce miR‐21 and miR‐181b expression during sepsis

McClure, C., McPeak, M. B., Youssef, D. A., Yao, Z. Q., McCall, C. E., & Gazzar, M. E. (2016) · Immunology and Cell Biology · doi:10.1038/icb.2016.63 · Cited by 60 · see citing works

Differential role of the estrogen receptors ESR1 and ESR2 on the regulation of proteins involved with proliferation and differentiation of Sertoli cells from 15-day-old rats

Lucas, T. F. G., Lazari, M. F. M., & Porto, C. S. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.09.015 · Cited by 59 · see citing works

PEG10 overexpression induced by E2F-1 promotes cell proliferation, migration, and invasion in pancreatic cancer

Peng, Y., Zhu, Y., Yin, L., Zhang, J., Wei, J., Liu, X., Liu, X., Gao, W., Jiang, K., & Miao, Y. (2017) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-017-0500-x · Cited by 57 · see citing works

Akt Regulated Phosphorylation of GSK-3β/Cyclin D1, p21 and p27 Contributes to Cell Proliferation Through Cell Cycle Progression From G1 to S/G2M Phase in Low-Dose Arsenite Exposed HaCat Cells

Chen, Y., Liu, X., Wang, H., Liu, S., Hu, N., & Li, X. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01176 · Cited by 57 · see citing works

A p53-Responsive miRNA Network Promotes Cancer Cell Quiescence

La, T., Liu, G., Farrelly, M. L., Cole, N., Feng, Y., Zhang, Y. Y., Sherwin, S. K., Yari, H., Tabatabaee, H., Yan, X. G., et al. (2018) · Cancer Research · doi:10.1158/0008-5472.can-18-1886 · Cited by 56 · see citing works

F-box protein FBXO31 is down-regulated in gastric cancer and negatively regulated by miR-17 and miR-20a

Zhang, X., Kong, Y., Xu, X., Xing, H., Zhang, Y., Han, F., Li, W., Yang, Q., Zeng, J., Jia, J., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.2183 · Cited by 53 · see citing works

Viral Cyclin promotes KSHV-induced cellular transformation and tumorigenesis by overriding contact inhibition

Jones, T., da Silva, S. R., Bedolla, R. G., Ye, F., Zhou, F., & Gao, S. (2014) · Cell Cycle · doi:10.4161/cc.27758 · Cited by 52 · see citing works

Ganoderic acid A inhibits proliferation and invasion, and promotes apoptosis in human hepatocellular carcinoma cells

Wang, X., Sun, D., Tai, J., & Wang, L. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7048 · Cited by 52 · see citing works

Coordination of cell growth and division by the ubiquitin–proteasome system

Benanti, J. A. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.04.005 · Cited by 51 · see citing works

All-trans Retinoic Acid as a Versatile Cytosolic Signal Modulator Mediated by CRABP1

Nagpal, I., & Wei, L. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153610 · Cited by 51 · see citing works

Porcine epidemic diarrhea virus through p53-dependent pathway causes cell cycle arrest in the G0/G1 phase

Pei, S., Wu, H., Huang, J., Xu, Y., Yang, F., Zhang, Q., & Xu, X. (2018) · Virus Research · doi:10.1016/j.virusres.2018.05.019 · Cited by 50 · see citing works

Cyclin-Dependent Kinase 4 and 6 Inhibitors in Cell Cycle Dysregulation for Breast Cancer Treatment

Susanti, N. M. P., & Tjahjono, D. H. (2021) · Molecules · doi:10.3390/molecules26154462 · Cited by 48 · see citing works

Stabilization of p21 (Cip1/WAF1) following Tip60-dependent acetylation is required for p21-mediated DNA damage response

Lee, M.-S., Seo, J., Choi, D. Y., Lee, E.-W., Ko, A., Ha, N., Yoon, J., Lee, H. W., Kim, K. P., & Song, J. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.159 · Cited by 47 · see citing works

Antitumor mechanisms when pRb and p53 are genetically inactivated

Zhu, L., Lu, Z., & Zhao, H.-T. (2014) · Oncogene · doi:10.1038/onc.2014.399 · Cited by 47 · see citing works

SIAMESE-RELATED1 Is Regulated Posttranslationally and Participates in Repression of Leaf Growth under Moderate Drought

Dubois, M., Selden, K., Bediée, A., Rolland, G., Baumberger, N., Noir, S., Bach, L., Lamy, G., Granier, C., & Genschik, P. (2018) · PLANT PHYSIOLOGY · doi:10.1104/pp.17.01712 · Cited by 46 · see citing works

PCNA-Mediated Degradation of p21 Coordinates the DNA Damage Response and Cell Cycle Regulation in Individual Cells

Sheng, C., Mendler, I.-H., Rieke, S., Snyder, P., Jentsch, M., Friedrich, D., Drossel, B., & Loewer, A. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.031 · Cited by 45 · see citing works

Alternative splicing of FBP-interacting repressor coordinates c-Myc, P27Kip1/cyclinE and Ku86/XRCC5 expression as a molecular sensor for bleomycin-induced DNA damage pathway

Rahmutulla, B., Matsushita, K., Satoh, M., Seimiya, M., Tsuchida, S., Kubo, S., Shimada, H., Ohtsuka, M., Miyazaki, M., & Nomura, F. (2013) · Oncotarget · doi:10.18632/oncotarget.1650 · Cited by 45 · see citing works

MicroRNA-155 controls RB phosphorylation in normal and malignant B lymphocytes via the noncanonical TGF-β1/SMAD5 signaling module

Jiang, D., & Aguiar, R. C. T. (2013) · Blood · doi:10.1182/blood-2013-07-515254 · Cited by 45 · see citing works

15-PGDH inhibits hepatocellular carcinoma growth through 15-keto-PGE2/PPARγ-mediated activation of p21WAF1/Cip1

Lu, D., Han, C. Q., & Wu, T. (2013) · Oncogene · doi:10.1038/onc.2013.69 · Cited by 45 · see citing works

SCFFbxw15 Mediates Histone Acetyltransferase Binding to Origin Recognition Complex (HBO1) Ubiquitin-Proteasomal Degradation to Regulate Cell Proliferation *

Zou, C., Chen, Y., Smith, R. M., Snavely, C. A., Li, J., Coon, T. A., Chen, B. B., Zhao, Y., & Mallampalli, R. K. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.426882 · Cited by 44 · see citing works

The lowdown on breakdown: Open questions in plant proteolysis

Eckardt, N. A., Avin‐Wittenberg, T., Bassham, D. C., Chen, P., Chen, Q., Fang, J., Genschik, P., Ghifari, A. S., Guercio, A. M., Gibbs, D. J., et al. (2024) · The Plant Cell · doi:10.1093/plcell/koae193 · Cited by 44 · see citing works

Re-expression of cell cycle markers in aged neurons and muscles: Whether cells should divide or die?

Sharma, R. R., Kumar, D., Jha, N. K., Jha, S. K., Ambasta, R. K., & Kumar, P. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.09.010 · Cited by 43 · see citing works

Role of p27Kip1 as a transcriptional regulator

Bachs, O., Gallastegui, E., Orlando, S., Bigas, A., Morante‐Redolat, J. M., Serratosa, J., Fariñas, I., Aligué, R., & Pujol, M. J. (2018) · Oncotarget · doi:10.18632/oncotarget.25447 · Cited by 43 · see citing works

Pharmacological relevance of CDK inhibitors in Alzheimer's disease

Malhotra, N., Gupta, R. V., & Kumar, P. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105115 · Cited by 42 · see citing works

F-Box Protein Specificity for G1 Cyclins Is Dictated by Subcellular Localization

Landry, B. D., Doyle, J. P., Toczyski, D. P., & Benanti, J. A. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002851 · Cited by 42 · see citing works

Withdrawal of skeletal muscle cells from cell cycle progression triggers differentiation ofToxoplasma gondiitowards the bradyzoite stage

Swierzy, I. J., & Lüder, C. G. K. (2014) · Cellular Microbiology · doi:10.1111/cmi.12342 · Cited by 41 · see citing works

Visualization of endogenous p27 and Ki67 reveals the importance of a c-Myc-driven metabolic switch in promoting survival of quiescent cancer cells

La, T., Chen, S., Guo, T., Zhao, X. H., Liu, T., Li, D., Carnell, M. J., Zhang, Y. Y., Feng, Y., Cole, N., et al. (2021) · Theranostics · doi:10.7150/thno.63763 · Cited by 41 · see citing works

Pristimerin enhances the effect of cisplatin by inhibiting the miR‑23a/Akt/GSK3β signaling pathway and suppressing autophagy in lung cancer cells

Zhang, Y., Wang, J., Hui, B., Sun, W., Li, B., Shi, F., Che, S., Chai, L., & Song, L. (2019) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2019.4057 · Cited by 40 · see citing works

Mitotic p21Cip1/CDKN1A is regulated by cyclin-dependent kinase 1 phosphorylation

Kreis, N., Friemel, A., Zimmer, B., Roth, S., Rieger, M. A., Rolle, U., Louwen, F., & Yuan, J. (2016) · Oncotarget · doi:10.18632/oncotarget.10330 · Cited by 39 · see citing works

Simulation of Stimulation: Cytokine Dosage and Cell Cycle Crosstalk Driving Timing-Dependent T Cell Differentiation

Barberis, M., Helikar, T., & Verbruggen, P. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00879 · Cited by 38 · see citing works

Increased Protein Stability of CDKN1C Causes a Gain-of-Function Phenotype in Patients with IMAGe Syndrome

Hamajima, N., Johmura, Y., Suzuki, S., Nakanishi, M., & Saitoh, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075137 · Cited by 37 · see citing works

Suppressor of cytokine signaling 1-dependent regulation of the expression and oncogenic functions of p21CIP1/WAF1 in the liver

Yeganeh, M., Gui, Y., Kandhi, R., Bobbala, D., Tobelaim, W.-S., Saucier, C., Yoshimura, A., Ferbeyre, G., Ramanathan, S., & Ilangumaran, S. (2016) · Oncogene · doi:10.1038/onc.2015.485 · Cited by 37 · see citing works

Cell Cycle–Dependent Regulation and Function of ARGONAUTE1 in Plants

Trolet, A., Baldrich, P., Criqui, M., Dubois, M., Clavel, M., Meyers, B. C., & Genschik, P. (2019) · The Plant Cell · doi:10.1105/tpc.19.00069 · Cited by 37 · see citing works

Cytotoxic unsaturated electrophilic compounds commonly target the ubiquitin proteasome system

Selvaraju, K., Mofers, A., Pellegrini, P., Salomonsson, J., Ahlner, A., Morad, V., Hillert, E., Espinosa, B., Arnér, E. S. J., Jensen, L. D., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-46168-x · Cited by 36 · see citing works

Potential roles of longan flower and seed extracts for anti-cancer

Lin, C. (2012) · World Journal of Experimental Medicine · doi:10.5493/wjem.v2.i4.78 · Cited by 36 · see citing works

Role of the ubiquitin proteasome system in hematologic malignancies

Sahasrabuddhe, A. A., & Elenitoba‐Johnson, K. S. J. (2014) · Immunological Reviews · doi:10.1111/imr.12236 · Cited by 35 · see citing works

Lymphoid Enhancer-binding Factor 1 Expression Precedes Dentin Sialophosphoprotein Expression during Rat Odontoblast Differentiation and Regeneration

Nakatomi, M., Ida‐Yonemochi, H., & Ohshima, H. (2013) · Journal of Endodontics · doi:10.1016/j.joen.2012.12.016 · Cited by 32 · see citing works

Tanshinone I induces apoptosis and protective autophagy in human glioblastoma cells via a reactive oxygen species‑dependent pathway

Shangguan, J., Liang, C., Lian, M., Hongmin, C., Ronghua, T., Xiaoxuan, F., Binbin, Z., & Guo, S. (2020) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2020.4499 · Cited by 31 · see citing works

Preterm birth disrupts cerebellar development by affecting granule cell proliferation program and Bergmann glia

Iskusnykh, I. Y., Buddington, R. K., & Chizhikov, V. V. (2018) · Experimental Neurology · doi:10.1016/j.expneurol.2018.05.015 · Cited by 30 · see citing works

Focal adhesion kinase antagonizes doxorubicin cardiotoxicity via p21Cip1

Cheng, Z., DiMichele, L. A., Rojas, M., Vaziri, C., Mack, C. P., & Taylor, J. M. (2013) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2013.12.002 · Cited by 29 · see citing works

The F-Box-Like Protein FBL17 Is a Regulator of DNA-Damage Response and Colocalizes with RETINOBLASTOMA RELATED1 at DNA Lesion Sites

Gentric, N., Masoud, K., Journot, R. P., Cognat, V., Chabouté, M., Noir, S., & Genschik, P. (2020) · PLANT PHYSIOLOGY · doi:10.1104/pp.20.00188 · Cited by 29 · see citing works

Molecular Mechanisms of DNA Replication Checkpoint Activation

Recolin, B., van der Laan, S., Tsanov, N., & Maiorano, D. (2014) · Genes · doi:10.3390/genes5010147 · Cited by 29 · see citing works

Caspases uncouple p27Kip1 from cell cycle regulated degradation and abolish its ability to stimulate cell migration and invasion

Podmirseg, S. R., Jäkel, H., Ranches, G., Kullmann, M. K., Sohm, B., Villunger, A., Lindner, H. H., & Hengst, L. (2016) · Oncogene · doi:10.1038/onc.2015.524 · Cited by 27 · see citing works

Knockdown of S ec8 promotes cell‐cycle arrest at G 1/ S phase by inducing p21 via control of FOXO proteins

Tanaka, T., & Iino, M. (2013) · FEBS Journal · doi:10.1111/febs.12669 · Cited by 26 · see citing works

Roles of proteolysis in regulation of GPCR function

Cottrell, G. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.02234.x · Cited by 26 · see citing works

MAPK Signaling Pathway Regulates p27 Phosphorylation at Threonin 187 as Part of the Mechanism Triggered by Early-Weaning to Induce Cell Proliferation in Rat Gastric Mucosa

Osaki, L. H., & Gama, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066651 · Cited by 26 · see citing works

p27T187A knockin identifies Skp2/Cks1 pocket inhibitors for advanced prostate cancer

Zhao, H.-T., Lu, Z., Bauzon, F., Fu, H., Cui, J., Locker, J. D., & Zhu, L. (2016) · Oncogene · doi:10.1038/onc.2016.175 · Cited by 25 · see citing works

p27 Kip1 V109G Polymorphism and Cancer Risk: A Systematic Review and Meta-Analysis

Wei, F., Xu, J., Tang, L., Shao, J.-Q., Wang, Y., Chen, L., & Guan, X. (2012) · Cancer Biotherapy and Radiopharmaceuticals · doi:10.1089/cbr.2012.1229 · Cited by 26 · see citing works

CIZ1, a p21Cip1/Waf1‐interacting protein, functions as a tumor suppressor in vivo

Nishibe, R., Watanabe, W., Ueda, T., Yamasaki, N., Koller, R. P., Wolff, L., Honda, Z., Ohtsubo, M., & Honda, H. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.03.034 · Cited by 25 · see citing works

p57Kip2 is an unrecognized DNA damage response effector molecule that functions in tumor suppression and chemoresistance

Jia, H., Cong, Q., Chua, J., Liu, H., Xia, X., Zhang, X., Lin, J., Habib, S. L., Ao, J., Zuo, Q., et al. (2014) · Oncogene · doi:10.1038/onc.2014.287 · Cited by 25 · see citing works

O-GlcNAc transferase regulates p21 protein levels and cell proliferation through the FoxM1–Skp2 axis in a p53-independent manner

de Queiroz, R. M., Moon, S.-H., & Prives, C. L. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102289 · Cited by 24 · see citing works

Interactions between SAP155 and FUSE-Binding Protein-Interacting Repressor Bridges c-Myc and P27Kip1 Expression

Matsushita, K., Tamura, M., Tanaka, N., Tomonaga, T., Matsubara, H., Shimada, H., Levens, D., He, L., Liu, J., Yoshida, M., et al. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-12-0673 · Cited by 24 · see citing works

A Circular RNA Generated from Nebulin ( NEB ) Gene Splicing Promotes Skeletal Muscle Myogenesis in Cattle as Detected by a Multi‐Omics Approach

Huang, K., Li, Z., Zhong, D., Yang, Y., Yan, X., Feng, T., Wang, X., Zhang, L., Shen, X., Chen, M., et al. (2023) · Advanced Science · doi:10.1002/advs.202300702 · Cited by 23 · see citing works

Novel Ferrocene Derivatives Induce Apoptosis through Mitochondria-Dependent and Cell Cycle Arrest via PI3K/Akt/mTOR Signaling Pathway in T Cell Acute Lymphoblastic Leukemia

Zeng, L., Tang, M., Pi, C., Zheng, J., Gao, S., Chabanne, T., Chauvin, R., Cheng, W., Lin, H., Xu, R., et al. (2021) · Cancers · doi:10.3390/cancers13184677 · Cited by 22 · see citing works

The Cell Cycle

Yang, V. W. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809954-4.00008-6 · Cited by 21 · see citing works

Icaritin inhibits CDK2 expression and activity to interfere with tumor progression

Zhang, C., Wang, X., & Zhang, C. (2022) · iScience · doi:10.1016/j.isci.2022.104991 · Cited by 22 · see citing works

RalGPS2 Is Essential for Survival and Cell Cycle Progression of Lung Cancer Cells Independently of Its Established Substrates Ral GTPases

Santos, A. O., Parrini, M. C., & Camonis, J. (2016) · PLoS ONE · doi:10.1371/journal.pone.0154840 · Cited by 22 · see citing works

The antioxidant butylated hydroxyanisole potentiates the toxic effects of propylparaben in cultured mammalian cells

Martín, J. M. P., Freire, P. F., Daimiel, L., Martı́nez-Botas, J., Martín-Sánchez, C., Lasunción, M. A., Peropadre, A., & Hazen, M. J. (2014) · Food and Chemical Toxicology · doi:10.1016/j.fct.2014.07.031 · Cited by 21 · see citing works

Proteasome inhibitors against amelanotic melanoma

Sidor-Kaczmarek, J., Cichorek, M., Spodnik, J. H., Wojcik, S. P., & Moryś, J. (2017) · Cell Biology and Toxicology · doi:10.1007/s10565-017-9390-0 · Cited by 20 · see citing works

c-Myc activation promotes cofilin-mediated F-actin cytoskeleton remodeling and telomere homeostasis as a response to oxidant-based DNA damage in medulloblastoma cells

Lewińska, A., Klukowska‐Rötzler, J., Deręgowska, A., Adamczyk‐Grochala, J., & Wnuk, M. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101163 · Cited by 20 · see citing works

Targeting PSMD14 inhibits melanoma growth through SMAD3 stabilization

Yokoyama, S., Iwakami, Y., Zhao, H., Kin, R., Zhou, Y., Yasuta, Y., Takahashi, A., Hayakawa, Y., & Sakurai, H. (2020) · Scientific Reports · doi:10.1038/s41598-020-76373-y · Cited by 19 · see citing works

Stabilization of p18 by deubiquitylase CYLD is pivotal for cell cycle progression and viral replication

Li, Y., Shi, F., Hu, J., Xie, L., Zhao, L., Tang, M., Luo, X., Ye, M., Zheng, H., Zhou, M., et al. (2021) · npj Precision Oncology · doi:10.1038/s41698-021-00153-8 · Cited by 19 · see citing works

p53-mediated G1 arrest requires the induction of both p21 and Killin in human colon cancer cells

Luo, D., Yu, C., Yu, J., Su, C., Li, S., & Liang, P. (2021) · Cell Cycle · doi:10.1080/15384101.2021.2014249 · Cited by 18 · see citing works

LncRNA LIMp27 Regulates the DNA Damage Response through p27 in p53‐Defective Cancer Cells

La, T., Chen, S., Zhao, X. H., Zhou, S. F., Xu, R., Liu, T., Zhang, Y. Y., Ye, K., Xu, L., Guo, T., et al. (2023) · Advanced Science · doi:10.1002/advs.202204599 · Cited by 18 · see citing works

Salviolone from Salvia miltiorrhiza Roots Impairs Cell Cycle Progression, Colony Formation, and Metalloproteinase-2 Activity in A375 Melanoma Cells: Involvement of P21(Cip1/Waf1) Expression and STAT3 Phosphorylation

Zanrè, V., Campagnari, R., Cerulli, A., Masullo, M., Cardile, A., Piacente, S., & Menegazzi, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031121 · Cited by 17 · see citing works

The c-Jun and JunB transcription factors facilitate the transit of classical Hodgkin lymphoma tumour cells through G1

Zhang, J., Wu, Z., Savin, A., Yang, M., Hsu, Y.-H. R., Jantuan, E., Bacani, J. T. C., & Ingham, R. J. (2018) · Scientific Reports · doi:10.1038/s41598-018-34199-9 · Cited by 17 · see citing works

CRL4 Ubiquitin Pathway and DNA Damage Response

Zhou, P., & Fan, Y. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_14 · Cited by 14 · see citing works

The Amelioration of Renal Damage in Skp2-Deficient Mice Canceled by p27 Kip1 Deficiency in Skp2−/− p27−/− Mice

Suzuki, S., Fukasawa, H., Misaki, T., Togawa, A., Ohashi, N., Kitagawa, K., Kotake, Y., Liu, N., Niida, H., Nakayama, K., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036249 · Cited by 16 · see citing works

Inhibitors of Cyclin-Dependent Kinase 1/2 for Anticancer Treatment

Mou, J., Chen, D., & Deng, Y. (2019) · Medicinal Chemistry · doi:10.2174/1573406415666190626113900 · Cited by 16 · see citing works

Upregulation of miR-34a-5p, miR-20a-3p and miR-29a-3p by Onconase in A375 Melanoma Cells Correlates with the Downregulation of Specific Onco-Proteins

Tomi, E. D., Campagnari, R., Orlandi, E., Cardile, A., Zanrè, V., Menegazzi, M., Gomez‐Lira, M., & Gotte, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031647 · Cited by 15 · see citing works

The role of estrogen receptors in rat Sertoli cells at different stages of development

Macheroni, C., Lucas, T. F. G., & Porto, C. S. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e05363 · Cited by 15 · see citing works

Ubiquitylation and proteasomal degradation of the p21 Cip1 , p27 Kip1 and p57 Kip2 CDK inhibitors

Lu, Z., & Hunter, T. R. (2010) · Cell Cycle · doi:10.4161/cc.9.12.11988 · Cited by 225 · see citing works

CDK inhibitors: Cell cycle regulators and beyond

Besson, A., Dowdy, S. F., & Roberts, J. M. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.01.013 · Cited by 1,152 · see citing works

Kip1 degradation via the ubiquitin-proteasome pathway.

Tam, S. W., Theodoras, A. M., & Pagano, M. (1997) · PubMed · Cited by 20 · see citing works

Cip/Kip proteins: more than just CDKs inhibitors: Figure 1.Preprint

Denicourt, C., & Dowdy, S. F. (2004) · Genes & Development · doi:10.1101/gad.1205304 · Cited by 203 · see citing works

Regulation of CIP/KIP cell cycle inhibitors and their biological implications

Lee, J. (2009) · Current Trends in Biotechnology and Pharmacy · Cited by 1 · see citing works