A leucine-rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011 · see citing works

p53, the cellular gatekeeper for growth and division

Levine, A. J. (1997) · Cell · doi:10.1016/s0092-8674(00)81871-1 · Cited by 7,693 · see citing works

Mdm2 promotes the rapid degradation of p53

Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506 · see citing works

Participation of p53 protein in the cellular response to DNA damage.

Kastan, M. B., Onyekwere, O. C., Sidransky, D., Vogelstein, B., & Craig, R. W. (1991) · PubMed · Cited by 3,761 · see citing works

Regulation of p53 stability by Mdm2

Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312 · see citing works

p53: puzzle and paradigm.Preprint

Ko, L. J., & Prives, C. L. (1996) · Genes & Development · doi:10.1101/gad.10.9.1054 · Cited by 2,338 · see citing works

Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain

Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206 · see citing works

DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2

Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80416-x · Cited by 2,100 · see citing works

CRM1 Is an Export Receptor for Leucine-Rich Nuclear Export Signals

Fornerod, M. W. J., Ohno, M., Yoshida, M., & Mattaj, I. W. (1997) · Cell · doi:10.1016/s0092-8674(00)80371-2 · Cited by 2,086 · see citing works

The p53-mdm-2 autoregulatory feedback loop.

Wu, X., Bayle, J. H., Olson, D., & Levine, A. J. (1993) · Genes & Development · doi:10.1101/gad.7.7a.1126 · Cited by 1,801 · see citing works

9-cis retinoic acid is a high affinity ligand for the retinoid X receptor

Heyman, R. A., Mangelsdorf, D. J., Dyck, J. A., Stein, R. B., Eichele, G., Evans, R. M., & Thaller, C. (1992) · Cell · doi:10.1016/0092-8674(92)90479-v · Cited by 1,780 · see citing works

Monoallelically Expressed Gene Related to p53 at 1p36, a Region Frequently Deleted in Neuroblastoma and Other Human Cancers

Kaghad, M., Bonnet, H., Yang, A., Créancier, L., Biscan, J.-C., Valent, A., Minty, A. J., Chalon, P., Lélias, J.-M., Dumont, X., et al. (1997) · Cell · doi:10.1016/s0092-8674(00)80540-1 · Cited by 1,630 · see citing works

Oncoprotein MDM2 conceals the activation domain of tumour suppressor p53

Oliner, J. D., Pietenpol, J. A., Thiagalingam, S., Gyuris, J., Kinzler, K. W., & Vogelstein, B. (1993) · Nature · doi:10.1038/362857a0 · Cited by 1,447 · see citing works

Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53

Jones, S. N., Roe, A. E., Donehower, L. A., & Bradley, A. (1995) · Nature · doi:10.1038/378206a0 · Cited by 1,280 · cited 2× · see citing works

Identification of a signal for rapid export of proteins from the nucleus

Wen, W., Meinkotht, J. L., Tsien, R. Y., & Taylor, S. S. (1995) · Cell · doi:10.1016/0092-8674(95)90435-2 · Cited by 1,190 · see citing works

The HIV-1 Rev Activation Domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs

Fischer, U., Huber, J., Boelens, W. C., Mattaj, I. W., & Lührmann, R. (1995) · Cell · doi:10.1016/0092-8674(95)90436-0 · Cited by 1,140 · see citing works

Nucleocytoplasmic Transport

Görlich, D., & Mattaj, I. W. (1996) · Science · doi:10.1126/science.271.5255.1513 · Cited by 1,093 · see citing works

The MDM2 gene amplification database

Momand, J. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.15.3453 · Cited by 982 · see citing works

The MIDAS display system

Ferrin, T. E., Huang, C. C., Jarvis, L. E., & Langridge, R. (1988) · Journal of Molecular Graphics · doi:10.1016/0263-7855(88)80054-7 · Cited by 950 · see citing works

Regulation of the specific DNA binding function of p53

Hupp, T. R., Meek, D. W., Midgley, C., & Lane, D. P. (1992) · Cell · doi:10.1016/0092-8674(92)90562-q · Cited by 910 · see citing works

Induction of nuclear accumulation of the tumor-suppressor protein p53 by DNA-damaging agents.

Fritsche, M., Haessler, C., & Brandner, G. (1993) · PubMed · Cited by 763 · see citing works

Evidence for a Role of CRM1 in Signal-Mediated Nuclear Protein Export

Ossareh‐Nazari, B., Bachelerie, F., & Dargemont, C. (1997) · Science · doi:10.1126/science.278.5335.141 · Cited by 723 · see citing works

Tumor surveillance via the ARF–p53 pathwayPreprint

Sherr, C. J. (1998) · Genes & Development · doi:10.1101/gad.12.19.2984 · Cited by 716 · see citing works

Phosphorylation of the MAP Kinase ERK2 Promotes Its Homodimerization and Nuclear Translocation

Khokhlatchev, A. V., Canagarajah, B. J., Wilsbacher, J. L., Robinson, M. J., Atkinson, M. A., Goldsmith, E. J., & Cobb, M. H. (1998) · Cell · doi:10.1016/s0092-8674(00)81189-7 · Cited by 675 · see citing works

Leptomycin B is an inhibitor of nuclear export: inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA

Wolff, B., Sanglier, J., & Wang, Y. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90257-x · Cited by 656 · see citing works

Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein.Preprint

Lin, J., Chen, J., Elenbaas, B., & Levine, A. J. (1994) · Genes & Development · doi:10.1101/gad.8.10.1235 · Cited by 652 · see citing works

A fast algorithm for rendering space-filling molecule pictures

Bacon, D., & Anderson, W. (1988) · Journal of Molecular Graphics · doi:10.1016/s0263-7855(98)80030-1 · Cited by 617 · see citing works

Nucleo‐cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein

Roth, J., Dobbelstein, M., Freedman, D. A., Shenk, T., & Levine, A. J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.2.554 · Cited by 610 · see citing works

Two distinct mechanisms alter p53 in breast cancer: mutation and nuclear exclusion.

Moll, U. M., RIOU, G. F., & Levine, A. J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.15.7262 · Cited by 575 · see citing works

Crystal Structure of the Tetramerization Domain of the p53 Tumor Suppressor at 1.7 Angstroms

Jeffrey, P. D., Gorina, S. S., & Pavletich, N. P. (1995) · Science · doi:10.1126/science.7878469 · Cited by 548 · see citing works

A reversible, p53-dependent G0/G1 cell cycle arrest induced by ribonucleotide depletion in the absence of detectable DNA damage.Preprint

Linke, S. P., Clarkin, K., Leonardo, A. D., Tsou, A.-P., & Wahl, G. M. (1996) · Genes & Development · doi:10.1101/gad.10.8.934 · Cited by 531 · see citing works

Cloning and functional analysis of human p51, which structurally and functionally resembles p53

Osada, M., Ohba, M., Kawahara, C., Ishioka, C., Kanamaru, R., Katoh, I., Ikawa, Y., Nimura, Y., Nakagawara, A., Obinata, M., et al. (1998) · Nature Medicine · doi:10.1038/nm0798-839 · Cited by 529 · see citing works

Nuclear Export Is Required for Degradation of Endogenous p53 by MDM2 and Human Papillomavirus E6

Freedman, D. A., & Levine, A. J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7288 · Cited by 513 · see citing works

ES cells do not activate p53-dependent stress responses and undergo p53-independent apoptosis in response to DNA damage

Aladjem, M. I., Spike, B. T., Rodewald, L. W., Hope, T. J., Klemm, M., Jaenisch, R., & Wahl, G. M. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70061-2 · Cited by 442 · see citing works

Wild-type p53 protein undergoes cytoplasmic sequestration in undifferentiated neuroblastomas but not in differentiated tumors.

Moll, U. M., LaQuaglia, M. P., Bénard, J., & RIOU, G. F. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.10.4407 · Cited by 426 · see citing works

Sequence-specific transcriptional activation is essential for growth suppression by p53.

Pietenpol, J. A., Tokino, T., Thiagalingam, S., El‐Deiry, W. S., Kinzler, K. W., & Vogelstein, B. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.6.1998 · Cited by 406 · see citing works

Functional inactivation but not structural mutation of p53 causes liver cancer

Ueda, H., Ullrich, S. J., Gangemi, J. D., Kappel, C. A., Ngo, L. T., Feitelson, M. A., & Jay, G. (1995) · Nature Genetics · doi:10.1038/ng0195-41 · Cited by 368 · see citing works

Protein Sequence Requirements for Function of the Human T-Cell Leukemia Virus Type 1 Rex Nuclear Export Signal Delineated by a Novel In Vivo Randomization-Selection Assay

Bogerd, H. P., Fridell, R. A., Benson, R. E., Hua, J., & Cullen, B. R. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.8.4207 · Cited by 351 · see citing works

Nuclear Accumulation of p53 Protein Is Mediated by Several Nuclear Localization Signals and Plays a Role in Tumorigenesis

Shaulsky, G., Goldfinger, N., Ben‐Ze'ev, A., & Rotter, V. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.12.6565-6577.1990 · Cited by 346 · see citing works

Human p53 is phosphorylated by p60-cdc2 and cyclin B-cdc2.

Bischoff, J. R., Friedman, P. N., Marshak, D. R., Prives, C. L., & Beach, D. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.12.4766 · Cited by 342 · see citing works

Control of Cyclin B1 localization through regulated binding of the nuclear export factor CRM1Preprint

Yang, J., Bardes, E. S. G., Moore, J. D., Brennan, J., Powers, M. A., & Kornbluth, S. A. (1998) · Genes & Development · doi:10.1101/gad.12.14.2131 · Cited by 323 · see citing works

Intramolecular Masking of Nuclear Import Signal on NF-AT4 by Casein Kinase I and MEKK1

Zhu, J., Shibasaki, F., Price, R., Guillemot, J.-C., Yano, T., Dötsch, V., Wagner, G., Ferrara, P., & McKeon, F. (1998) · Cell · doi:10.1016/s0092-8674(00)81445-2 · Cited by 307 · see citing works

Allosteric activation of latent p53 tetramers

Hupp, T. R., & Lane, D. P. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00195-0 · Cited by 300 · see citing works

Nuclear Export Receptors: From Importin to Exportin

Ullman, K. S., Powers, M. A., & Forbes, D. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80361-x · Cited by 280 · see citing works

Cytoplasmic Sequestration of Wild-Type p53 Protein Impairs the G 1 Checkpoint after DNA Damage

Moll, U. M., Ostermeyer, A. G., Haladay, R., Winkfield, B., Frazier, M., & Zambetti, G. P. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.3.1126 · Cited by 277 · see citing works

Solution structure of the tetrameric minimum transforming domain of p53

Lee, W., Harvey, T. S., Yin, Y., Yau, P., Litchfield, D. W., & Arrowsmith, C. H. (1994) · Nature Structural & Molecular Biology · doi:10.1038/nsb1294-877 · Cited by 265 · see citing works

The p53 protein is an unusually shaped tetramer that binds directly to DNA.

Friedman, P. N., Chen, X., Bargonetti, J., & Prives, C. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.8.3319 · Cited by 264 · see citing works

How p53 binds DNA as a tetramer

McLure, K. G., & Lee, P. W. K. (1998) · The EMBO Journal · doi:10.1093/emboj/17.12.3342 · Cited by 260 · see citing works

Phosphorylation of Serine 392 Stabilizes the Tetramer Formation of Tumor Suppressor Protein p53

Sakaguchi, K., Sakamoto, H., Lewis, M. S., Anderson, C. W., Erickson, J. W., Appella, E., & Xie, D. (1997) · Biochemistry · doi:10.1021/bi970759w · Cited by 247 · see citing works

Transcriptional activation by p53 correlates with suppression of growth but not transformation

Crook, T. J. (1994) · Cell · doi:10.1016/0092-8674(94)90071-x · Cited by 233 · see citing works

Nuclear export signals and the fast track to the cytoplasm

Gerace, L. (1995) · Cell · doi:10.1016/0092-8674(95)90420-4 · Cited by 233 · see citing works

Prognostic significance of cytoplasmic p53 oncoprotein in colorectal adenocarcinoma

Sun, X., Carstensen, J. M., Stål, O., et al. (1992) · The Lancet · doi:10.1016/0140-6736(92)92558-w · Cited by 224 · see citing works

Refined solution structure of the oligomerization domain of the tumour suppressor p53

Clore, G. M., Ernst, J. A., Clubb, R. T., Omichinski, J. G., Kennedy, W. P., Sakaguchi, K., Appella, E., & Gronenborn, A. M. (1995) · Nature Structural & Molecular Biology · doi:10.1038/nsb0495-321 · Cited by 222 · see citing works

The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP

Askjaer, P., Jensen, T. H., Nilsson, J., Englmeier, L., & Kjems, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.50.33414 · Cited by 219 · see citing works

Conformational shifts propagate from the oligomerization domain of p53 to its tetrameric DNA binding domain and restore DNA binding to select p53 mutants.

Halazonetis, T. D., & Kandil, A. N. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06199.x · Cited by 205 · see citing works

Structural Aspects of the p53 Protein in Relation to Gene Evolution: A Second Look

Soussi, T., & May, P. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0425 · Cited by 203 · see citing works

Subcellular distribution of the p53 protein during the cell cycle of Balb/c 3T3 cells.

Shaulsky, G., Ben‐Ze'ev, A., & Rotter, V. (1990) · PubMed · Cited by 168 · see citing works

Ultraviolet radiation, but not γ radiation or etoposide-induced DNA damage, results in the phosphorylation of the murine p53 protein at serine-389

Lu, H., Taya, Y., Ikeda, M., & Levine, A. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6399 · Cited by 162 · see citing works

p53 Domains: Structure, Oligomerization, and Transformation

Wang, P., Reed, M. J., Wang, Y., Mayr, G. A., Stenger, J. E., Anderson, M. E., Schwedes, J. F., & Tegtmeyer, P. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.8.5182-5191.1994 · Cited by 161 · see citing works

p53 gene mutations, p53 protein accumulation and compartmentalization in colorectal adenocarcinoma.

Bòsari, S., Viale, G., Roncalli, M. G., Graziani, D. M. G., Borsani, G., Lee, A. K. C., & Coggi, G. (1995) · Europe PMC (PubMed Central) · Cited by 155 · see citing works

Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain

Mateu, M. G., & Fersht, A. R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.10.2748 · Cited by 146 · see citing works

Conic: A fast renderer for spacefilling molecules with shadows

Huang, C. C., Pettersen, E. F., Klein, T. E., Ferrin, T. E., & Langridge, R. (1991) · Journal of Molecular Graphics · doi:10.1016/0263-7855(91)80016-s · Cited by 138 · see citing works

The dihedral symmetry of the p53 tetramerization domain mandates a conformational switch upon DNA binding.

Waterman, J. L. F., Shenk, J. L., & Halazonetis, T. D. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07027.x · Cited by 126 · see citing works

Cytoplasmically sequestered wild-type p53 protein in neuroblastoma is relocated to the nucleus by a C-terminal peptide

Ostermeyer, A. G., Runko, E., Winkfield, B., Ahn, B., & Moll, U. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15190 · Cited by 125 · see citing works

Maintaining genetic stability through TP53 mediated checkpoint control.

Wahl, G. M., Sp, L., Tg, P., & Huang, L. (1997) · PubMed · Cited by 115 · see citing works

Characterization of p53 oligomerization domain mutations isolated from Li–Fraumeni and Li–Fraumeni like family members

Lomax, M. E., Barnes, D. M., Hupp, T. R., Picksley, S. M., & Camplejohn, R. (1998) · Oncogene · doi:10.1038/sj.onc.1201974 · Cited by 100 · see citing works

Characterization of the Nuclear Export Signal of Human T-Cell Lymphotropic Virus Type 1 Rex Reveals that Nuclear Export Is Mediated by Position-Variable Hydrophobic Interactions

Kim, F. J., Beeche, A. A., Hunter, J., et al. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.9.5147 · Cited by 96 · see citing works

The tumor suppressor p53 is subject to both nuclear import and export, and both are fast, energy-dependent and lectin-inhibited

Middeler, G., Zerf, K., Jenovai, S., et al. (1997) · Oncogene · doi:10.1038/sj.onc.1200949 · Cited by 89 · see citing works

Gene Amplification in a p53-Deficient Cell Line Requires Cell Cycle Progression under Conditions That Generate DNA Breakage

Paulson, T. G., Almasan, A., Brody, L. L., & Wahl, G. M. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.5.3089 · Cited by 86 · see citing works

Stabilization and activation of p53 are regulated independently by different phosphorylation events

Chernov, M. V., Ramana, C. V., Adler, V., & Stark, G. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2284 · Cited by 78 · see citing works

Mouse-human heterokaryon analysis with a 33258 Hoechst-Giemsa technique.

Moser, F. G., Dorman, B. P., & Ruddle, F. H. (1975) · The Journal of Cell Biology · doi:10.1083/jcb.66.3.676 · Cited by 76 · see citing works

Nuclear Exclusion of Wild-Type p53 in Immortalized Human Retinoblastoma Cells

Schlamp, C. L., Poulsen, G. L., Nork, T. M., & Nickells, R. W. (1997) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/89.20.1530 · Cited by 75 · see citing works

MYC Abrogates p53-Mediated Cell Cycle Arrest in N -(Phosphonacetyl)- l -Aspartate-Treated Cells, Permitting CAD Gene Amplification

Chernova, O. B., Chernov, M. V., Ishizaka, Y., Agarwal, M. L., & Stark, G. R. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.1.536 · Cited by 62 · see citing works

Cellular accumulation of p53 protein: an independent prognostic factor in stage II breast cancer

Stenmark‐Askmalm, M., Stål, O., Sullivan, S., et al. (1994) · European Journal of Cancer · doi:10.1016/0959-8049(94)90082-5 · Cited by 62 · see citing works

Zebrafish (Danio rerio) p53 tumor suppressor gene: cDNA sequence and expression during embryogenesis.

Cheng, R., Ford, B. L., O'Neal, P. E., et al. (1997) · PubMed · Cited by 60 · see citing works

Cytoplasmic retention of mutant tsp53 is dependent on an intermediate filament protein (Vimentin) scaffold

Klotzsche, O., Etzrodt, D., Hohenberg, H., et al. (1998) · Oncogene · doi:10.1038/sj.onc.1202155 · Cited by 53 · see citing works

Cooperation of a Single Lysine Mutation and a C-terminal Domain in the Cytoplasmic Sequestration of the p53 Protein

Liang, S., Hong, D., & Clarke, M. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.31.19817 · Cited by 52 · see citing works

Intracellular localization of p53 tumor suppressor protein in gamma-irradiated cells is cell cycle regulated and determined by the nucleus.

Komarova, E. A., Zelnick, C. R., Chin, D., Zeremski, M., Gleiberman, A. S., Bacus, S. S., & Gudkov, A. V. (1997) · PubMed · Cited by 45 · see citing works

Cdk2 kinase phosphorylates serine 315 of human p53 in vitro.

Price, B. D., Hughes‐Davies, L., & Park, S. J. (1995) · PubMed · Cited by 43 · see citing works

Cell cycle-dependent regulation of nuclear p53 traffic occurs in one subclass of human tumor cells and in untransformed cells.

David-Pfeuty, T., Chakrani, F., Ory, K., & Nouvian-Dooghe, Y. (1996) · PubMed · Cited by 41 · see citing works

A previously undescribed mutation within the tetramerisation domain of TP53 in a family with Li-Fraumeni syndrome.

Varley, J. M., McGown, G., Thorncroft, M. R., Cochrane, S. M., Morrison, P., Woll, P. J., Kelsey, A. M., Mitchell, E. L. D., Boyle, J. M., Birch, J. M., et al. (1996) · PubMed · Cited by 40 · see citing works

Mutagenesis in the P53 gene

Pfeifer, G. P., & Holmquist, G. P. (1997) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(97)00004-8 · Cited by 38 · see citing works

Free radicals generated by ionizing radiation signal nuclear translocation of p53.

Martinez, J. D., Pennington, M. E., Craven, M., et al. (1997) · PubMed · Cited by 35 · see citing works

Analysis of p53 quaternary structure in relation to sequence-specific DNA binding.

Hainaut, P. L., Hall, A., & Milner, J. (1994) · PubMed · Cited by 31 · see citing works

Novel patterns of p53 abnormality in breast cancer from Taiwan: experience from a low-incidence area

Lou, M. A. A., Tseng, S.-L., Chang, S., et al. (1997) · British Journal of Cancer · doi:10.1038/bjc.1997.132 · Cited by 29 · see citing works

Oligomerization Is Not Essential for Growth Suppression by p53 in p53-Deficient Osteosarcoma Saos-2 Cells

Ishioka, C., Shimodaira, H., Englert, C., Shimada, A., Osada, M., Jia, L.-Q., Suzuki, T., Gamo, M., & Kanamaru, R. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6216 · Cited by 21 · see citing works

A fluorescent p53GFP fusion protein facilitates its detection in mammalian cells while retaining the properties of wild-type p53

Norris, P. S., & Haas, M. (1997) · Oncogene · doi:10.1038/sj.onc.1201406 · Cited by 21 · see citing works

Nuclear export signal of IκBα interferes with the Rev-dependent posttranscriptional regulation of human immunodeficiency virus type I

Bachelerie, F., Rodríguez, M. S., Dargemont, C., et al. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.22.2883 · Cited by 13 · see citing works

Selective loss of endogenous p21waf1/cip1 induction underlies the G1 checkpoint defect of monomeric p53 proteins.

Tarunina, M., Grimaldi, M., Ruaro, E. M., et al. (1996) · PubMed · Cited by 7 · see citing works

Cooperation of a single lysine mutation and a C-terminal domain in the cytoplasmic sequestration of the p53 protein.

Liang, S., Hong, D. S., & Clarke, M. F. (1998) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)60272-3 · Cited by 2 · see citing works

Regulating the p53 pathway: in vitro hypotheses, in vivo veritas

Toledo, F., & Wahl, G. M. (2006) · Nature reviews. Cancer · doi:10.1038/nrc2012 · Cited by 1,286 · see citing works

Post-translational modification of p53 in tumorigenesis

Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270 · see citing works

Targeting p53 pathways: mechanisms, structures, and advances in therapy

Wang, H., Guo, M., Wei, H., & Chen, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01347-1 · Cited by 1,016 · see citing works

p53 ubiquitination: Mdm2 and beyond

Brooks, C. L., & Gu, W. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.020 · Cited by 924 · see citing works

Mono- Versus Polyubiquitination: Differential Control of p53 Fate by Mdm2

Li, M., Brooks, C. L., Wu-Baer, F., Chen, D., Baer, R., & Gu, W. (2003) · Science · doi:10.1126/science.1091362 · Cited by 804 · see citing works

ATM-dependent phosphorylation of Mdm2 on serine 395: role in p53 activation by DNA damage

Maya, R., Balass, M., Kim, S.-T., Shkedy, D., Leal, J.-F. M., Shifman, O., Moas, M., Buschmann, T., Ronai, Z., Shiloh, Y., et al. (2001) · Genes & Development · doi:10.1101/gad.886901 · Cited by 716 · see citing works

USP10 Regulates p53 Localization and Stability by Deubiquitinating p53

Yuan, J., Luo, K., Zhang, L., Cheville, J. C., & Lou, Z. (2010) · Cell · doi:10.1016/j.cell.2009.12.032 · Cited by 637 · see citing works

The ARF/p53 pathway.

Sherr, C. J., & Weber, J. D. (2000) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(99)00038-6 · Cited by 654 · see citing works

MDM2 — master regulator of the p53 tumor suppressor protein

Momand, J., Wu, H.-H., & Dasgupta, G. (2000) · Gene · doi:10.1016/s0378-1119(99)00487-4 · Cited by 641 · see citing works

Distinct spatiotemporal dynamics of mammalian checkpoint regulators induced by DNA damage.

Lukas, C., Falck, J., Bartkova, J., Bartek, J., & Lukas, J. (2003) · Nature Cell Biology · doi:10.1038/ncb945 · Cited by 474 · see citing works

The p53 orchestra: Mdm2 and Mdmx set the tone

Wade, M., Wang, Y. V., & Wahl, G. M. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.01.009 · Cited by 450 · see citing works

Regulating tumor suppressor genes: post-translational modifications

Chen, L., Liu, S., & Tao, Y. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0196-9 · Cited by 449 · see citing works

Accelerated MDM2 auto‐degradation induced by DNA‐damage kinases is required for p53 activation

Stommel, J. M., & Wahl, G. M. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600145 · Cited by 386 · see citing works

A p53 Amino-Terminal Nuclear Export Signal Inhibited by DNA Damage-Induced Phosphorylation

Zhang, Y., & Xiong, Y. (2001) · Science · doi:10.1126/science.1058637 · Cited by 378 · see citing works

The MDM2 RING-finger domain is required to promote p53 nuclear export

Geyer, R. K., Yu, Z. K., & Maki, C. G. (2000) · Nature Cell Biology · doi:10.1038/35023507 · Cited by 361 · see citing works

Mdm2-mediated ubiquitylation: p53 and beyond

Marine, J.-C., & Lozano, G. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2009.68 · Cited by 354 · see citing works

An intact HDM2 RING-finger domain is required for nuclear exclusion of p53

Boyd, S. D., Tsai, K. Y., & Jacks, T. (2000) · Nature Cell Biology · doi:10.1038/35023500 · Cited by 334 · see citing works

The multiple levels of regulation by p53 ubiquitination

Lee, J. T., & Gu, W. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2009.77 · Cited by 289 · see citing works

Monoubiquitylation promotes mitochondrial p53 translocation

Marchenko, N. D., Wolff, S., Erster, S., Becker, K., & Moll, U. M. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601560 · Cited by 286 · see citing works

Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases

Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288 · see citing works

C-terminal modifications regulate MDM2 dissociation and nuclear export of p53

Carter, S., Bischof, O., Dejean, A., & Vousden, K. H. (2007) · Nature Cell Biology · doi:10.1038/ncb1562 · Cited by 225 · see citing works

MdmX Protects p53 from Mdm2-Mediated Degradation

Jackson, M. W., & Berberich, S. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.1001-1007.2000 · Cited by 211 · see citing works

Hsp90-binding immunophilins link p53 to dynein during p53 transport to the nucleus

Galigniana, M. D., Harrell, J. M., O'Hagen, H. M., Ljungman, M., & Pratt, W. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402223200 · Cited by 150 · see citing works

p53 accumulates but is functionally impaired when DNA synthesis is blocked

Gottifredi, V., Shieh, S.-Y., Taya, Y., & Prives, C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.1036 · Cited by 147 · see citing works

Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3

LeBron, C., Chen, L., Gilkes, D. M., & Chen, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601032 · Cited by 122 · see citing works

Stress-mediated nuclear stabilization of p53 is regulated by ubiquitination and importin-α3 binding

Marchenko, N. D., Hanel, W., Li, D., Becker, K., Reich, N., & Moll, U. M. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2009.173 · Cited by 123 · see citing works

c-Abl Regulates p53 Levels under Normal and Stress Conditions by Preventing Its Nuclear Export and Ubiquitination

Vogt Sionov, R., Coen, S., Goldberg, Z., Berger, M., Bercovich, B., Ben-Neriah, Y., Ciechanover, A., & Haupt, Y. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.17.5869-5878.2001 · Cited by 94 · see citing works

HDAC6 deacetylates p53 at lysines 381/382 and differentially coordinates p53-induced apoptosis

Ryu, H.-W., Shin, D.-H., Lee, D. H., Choi, J., Han, G., Lee, K. Y., & Kwon, S. H. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.01.033 · Cited by 82 · see citing works

Nitration of the tumor suppressor protein p53 at tyrosine 327 promotes p53 oligomerization and activation

Yakovlev, V. A., Bayden, A. S., Graves, P. R., Kellogg, G. E., & Mikkelsen, R. B. (2010) · Biochemistry · doi:10.1021/bi100564w · Cited by 56 · see citing works

Nuclear and cytoplasmic degradation of endogenous p53 and HDM2 occurs during down-regulation of the p53 response after multiple types of DNA damage

Joseph, T. W., Zaika, A., & Moll, U. M. (2003) · The FASEB Journal · doi:10.1096/fj.02-0931com · Cited by 50 · see citing works

Interleukin-1α associates with the tumor suppressor p53 following DNA damage

Novak, J., Zamostna, B., Vopalensky, V., Buryskova, M., Burysek, L., Doleckova, D., & Pospisek, M. (2020) · Scientific Reports · doi:10.1038/s41598-020-63779-x · Cited by 3 · see citing works

RKIP localizes to the nucleus through a bipartite nuclear localization signal and interaction with importin α to regulate mitotic progression

Argueta, C. E., Figy, C., Bouali, S., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.103023 · Cited by 4 · see citing works

Functional characterization of the nuclear localization signal of OREBP/TonEBP

Ko, B. C. B., Cheung, C., & Xu, S. (2011) · The FASEB Journal · doi:10.1096/fasebj.25.1_supplement.1047.8

Analysis of nuclear targeting activities of transport signals in the human immunodeficiency virus Rev protein

Demart, S., Ceccherini‐Silberstein, F., Schlicht, S., Walcher, S., Wolff, H., Neumann, M., Erfle, V., & Brack‐Werner, R. (2003) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.07.011 · Cited by 13 · see citing works

Nucleo-cytoplasmic shuttling of human Kank protein accompanies intracellular translocation of β-catenin

Wang, Y., Kakinuma, N., Zhu, Y., & Kiyama, R. (2006) · Journal of Cell Science · doi:10.1242/jcs.03169 · Cited by 34 · see citing works

Nuclear Exportin 1 (XPO1) Binds to the Nuclear Localization/Export Signal of the Turnip Mosaic Virus NIb to Promote Viral Infection

Zhang, M., Gong, P., Ge, L., et al. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.780724 · Cited by 12 · see citing works