Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53

NMRPipe: A multidimensional spectral processing system based on UNIX pipes

Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,994 · see citing works

THE UBIQUITIN SYSTEM

Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840 · see citing works

MOLMOL: A program for display and analysis of macromolecular structures

Koradi, R., Billeter, M., & Kurt Wüthrich, A. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00009-4 · Cited by 7,163 · see citing works

Surfing the p53 network

Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · see citing works

AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR

Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228148 · Cited by 5,502 · see citing works

In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2

Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661 · 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

Mechanisms Underlying Ubiquitination

Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,731 · 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

NMR View: A computer program for the visualization and analysis of NMR data

Johnson, B. A., & Blevins, R. A. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00404272 · Cited by 3,093 · see citing works

A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia

Kastan, M. B., Zhan, Q., El-Deiry, W. S., Carrier, F., Jacks, T., Walsh, W. V., Plunkett, B. S., Vogelstein, B., & Fornace, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90593-2 · Cited by 3,047 · see citing works

Protein backbone angle restraints from searching a database for chemical shift and sequence homology

Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957 · see citing works

Torsion angle dynamics for NMR structure calculation with the new program Dyana

Güntert, P., Mumenthaler, C., & Kurt Wüthrich, A. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1284 · Cited by 2,781 · see citing works

The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53

Scheffner, M., Huibregtse, J. M., Vierstra, R. D., & Howley, P. M. (1993) · Cell · doi:10.1016/0092-8674(93)90384-3 · Cited by 2,387 · 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

Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

Honda, R., Tanaka, H., & Yasuda, H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01480-4 · Cited by 1,951 · see citing works

Mdm2 Is a RING Finger-dependent Ubiquitin Protein Ligase for Itself and p53

Fang, S., Jensen, J. P., Ludwig, R. L., Vousden, K. H., & Weissman, A. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8945 · Cited by 1,044 · see citing works

Calculation of Hydrodynamic Properties of Globular Proteins from Their Atomic-Level Structure

de la Torre, J. G., Huertas, M. L., & Carrasco, B. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76630-6 · Cited by 1,034 · see citing works

Hydrodynamic Radii of Native and Denatured Proteins Measured by Pulse Field Gradient NMR Techniques

Wilkins, D. K., Grimshaw, S. B., Receveur‐Brechot, V., Dobson, C. M., Jones, J. A., & Smith, L. J. (1999) · Biochemistry · doi:10.1021/bi991765q · Cited by 1,013 · see citing works

Structure of a c-Cbl–UbcH7 Complex

Zheng, N., Wang, P., Jeffrey, P. D., & Pavletich, N. P. (2000) · Cell · doi:10.1016/s0092-8674(00)00057-x · Cited by 839 · see citing works

Extending the Applicability of the Nonlinear Poisson−Boltzmann Equation: Multiple Dielectric Constants and Multivalent Ions

Rocchia, W., Alexov, E., & Honig, B. H. (2001) · The Journal of Physical Chemistry B · doi:10.1021/jp010454y · Cited by 838 · see citing works

Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein

Grzesiek, S., & Bax, A. (1992) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(92)90099-s · Cited by 746 · see citing works

Pirh2, a p53-Induced Ubiquitin-Protein Ligase, Promotes p53 Degradation

Leng, R. P., Lin, Y., Ma, W., Wu, H., Lemmers, B., Chung, S., Parant, J. M., Lozano, G., Hakem, R., & Benchimol, S. (2003) · Cell · doi:10.1016/s0092-8674(03)00193-4 · Cited by 717 · see citing works

Small-molecule MDM2 antagonists reveal aberrant p53 signaling in cancer: implications for therapy

Tovar, C., Rosinski, J., Filipovic, Z., Higgins, B., Kolinsky, K., Hilton, H., Zhao, X., Vu, B. T., Qing, W., Packman, K., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507493103 · Cited by 708 · see citing works

The ubiquitin ligase COP1 is a critical negative regulator of p53

Dornan, D., Wertz, I. E., Shimizu, H., Arnott, D. P., Frantz, G. D., Dowd, P., Rourke, K. O., Koeppen, H., & Dixit, V. M. (2004) · Nature · doi:10.1038/nature02514 · Cited by 700 · see citing works

Touring protein fold space with Dali/FSSP

Holm, L. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.1.316 · Cited by 667 · see citing works

A novel gysteine-rich sequence motif

Freemont, P. S., Hanson, I. M., & Trowsdale, J. (1991) · Cell · doi:10.1016/0092-8674(91)90229-r · Cited by 545 · see citing works

ARF-BP1/Mule Is a Critical Mediator of the ARF Tumor Suppressor

Chen, D., Kon, N., Li, M., Zhang, W., Qin, J., & Gu, W. J. (2005) · Cell · doi:10.1016/j.cell.2005.03.037 · Cited by 539 · see citing works

Somatic point mutations in the p53 gene of human tumors and cell lines: updated compilation

Hollstein, M. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.1.141 · Cited by 499 · see citing works

Structure of a BRCA1-BARD1 heterodimeric RING-RING complex.

Brzović, P. S., Rajagopal, P., Hoyt, D. W., King, M., & Klevit, R. E. (2001) · Nature Structural Biology · doi:10.1038/nsb1001-833 · Cited by 494 · see citing works

A Comparison between the Sulfhydryl Reductants Tris(2-carboxyethyl)phosphine and Dithiothreitol for Use in Protein Biochemistry

Getz, E. B., Xiao, M., Chakrabarty, T., Cooke, R., & Selvin, P. R. (1999) · Analytical Biochemistry · doi:10.1006/abio.1999.4203 · Cited by 493 · see citing works

A Simple Method for Improving Protein Solubility and Long-Term Stability

Golovanov, A. P., Hautbergue, G. M., Wilson, S. A., & Lian, L. (2004) · Journal of the American Chemical Society · doi:10.1021/ja049297h · Cited by 469 · see citing works

Structure and E3‐ligase activity of the Ring–Ring complex of Polycomb proteins Bmi1 and Ring1b

Buchwald, G., van der Stoop, P. P. M., Weichenrieder, O., Anastassis Perrakis, A., van Lohuizen, M., & Sixma, T. K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601144 · Cited by 438 · see citing works

Chaperoned Ubiquitylation—Crystal Structures of the CHIP U Box E3 Ubiquitin Ligase and a CHIP-Ubc13-Uev1a Complex

Zhang, M., Windheim, M., Roe, S. M., Peggie, M. W., Cohen, P., Prodromou, C., & Pearl, L. H. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.023 · Cited by 420 · see citing works

Resolution enhancement and spectral editing of uniformly 13C-enriched proteins by homonuclear broadband 13C decoupling

Vuister, G. W., & Bax, A. (1992) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(92)90144-v · Cited by 402 · see citing works

Heteronuclear three-dimensional nmr spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra

Fesik, S. W., & Zuiderweg, E. R. P. (1988) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(88)90144-8 · Cited by 380 · see citing works

Molecular Mechanism of the Interaction between MDM2 and p53

Schön, O., Friedler, A., Bycroft, M., Freund, S. M. V., & Fersht, A. R. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00852-5 · Cited by 349 · see citing works

Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex

Brzovic, P. S., Keeffe, J. R., Nishikawa, H., Miyamoto, K., Fox, D., Fukuda, M., Ohta, T., & Klevit, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0836054100 · Cited by 346 · see citing works

FATCAT: a web server for flexible structure comparison and structure similarity searching

Ye, Y., & Godzik, A. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh430 · Cited by 340 · see citing works

Identification and preliminary characterization of a protein motif related to the zinc finger.

Lovering, R. C., Hanson, I. M., Borden, K. L. B., Martin, S. R., O’Reilly, N., Evan, G. I., Rahman, D., Pappin, D., Trowsdale, J., & Freemont, P. S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.6.2112 · Cited by 338 · see citing works

MDM2 interacts with MDMX through their RING finger domains

Tanimura, S., Ohtsuka, S., Mitsui, K., Shirouzu, K., Yoshimura, A., & Ohtsubo, M. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00254-9 · Cited by 324 · see citing works

Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells

Yang, Y., Ludwig, R. L., Jensen, J. P., Pierre, S. A., Medaglia, M. V., Davydov, I. V., Safiran, Y. J., Oberoi, P., Kenten, J. H., Phillips, A. C., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.04.029 · Cited by 321 · see citing works

Pathways of ubiquitin conjugation

Haas, A. L., & Siepmann, T. J. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.14.9409544 · Cited by 313 · see citing works

Counteraction of urea-induced protein denaturation by trimethylamine N -oxide: A chemical chaperone at atomic resolution

Bennion, B. J., & Daggett, V. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308633101 · Cited by 310 · see citing works

Structural insights into the U-box, a domain associated with multi-ubiquitination

Ohi, M. D., Kooi, C. W. V., Rosenberg, J. A., Chazin, W., & Gould, K. L. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb906 · Cited by 295 · see citing works

Tautomeric states of the active‐site histidines of phosphorylated and unphosphorylated IIIGlc, a signal‐transducing protein from escherichia coli, using two‐dimensional heteronuclear NMR techniques

Pelton, J. G., Torchia, D. A., Meadow, N. D., & Roseman, S. (1993) · Protein Science · doi:10.1002/pro.5560020406 · Cited by 293 · see citing works

Chalcone Derivatives Antagonize Interactions between the Human Oncoprotein MDM2 and p53

Stoll, R., Renner, C., Hansen, S., Palme, S., Klein, C., Belling, A., Żesławski, W., Kamionka, M., Rehm, T., Mühlhahn, P., et al. (2000) · Biochemistry · doi:10.1021/bi000930v · Cited by 275 · see citing works

Structure of the C3HC4 Domain by 1H-nuclear Magnetic Resonance Spectroscopy.

Barlow, P. N., Luisi, B. F., Milner, A., Elliott, M., & Everett, R. D. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1222 · Cited by 273 · see citing works

Role of Arginine in the Stabilization of Proteins against Aggregation

Baynes, B. M., Wang, D. I. C., & Trout, B. L. (2005) · Biochemistry · doi:10.1021/bi047528r · Cited by 261 · see citing works

Mdm4 and Mdm2 cooperate to inhibit p53 activity in proliferating and quiescent cells <i>in vivo</i>

Francoz, S., Froment, P., Bogaerts, S., De Clercq, S., Maetens, M., Doumont, G., Bellefroid, E., & Marine, J.-C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508476103 · Cited by 260 · see citing works

Identification of a ubiquitin–protein ligase subunit within the CCR4–NOT transcription repressor complex

Albert, T., Hanzawa, H., Legtenberg, Y. I. A., de Ruwe, M. J., van den Heuvel, F. A. J., Collart, M. A., Boelens, R., & Timmers, H. T. M. (2002) · The EMBO Journal · doi:10.1093/emboj/21.3.355 · Cited by 214 · see citing works

Topors Functions as an E3 Ubiquitin Ligase with Specific E2 Enzymes and Ubiquitinates p53

Rajendra, R., Malegaonkar, D., Pungaliya, P., Marshall, H., Rasheed, Z. A., Brownell, J. E., Liu, L. F., Lutzker, S. G., Saleem, A., & Rubin, E. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400300200 · Cited by 192 · see citing works

Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases

Özkan, E., Yu, H., & Deisenhofer, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509418102 · Cited by 192 · see citing works

Identification of a cryptic nucleolar-localization signal in MDM2

Lohrum, M. A. E., Ashcroft, M. A., Kubbutat, M. H. G., & Vousden, K. H. (2000) · Nature Cell Biology · doi:10.1038/35004057 · Cited by 186 · see citing works

Synergistic roles of Mdm2 and Mdm4 for p53 inhibition in central nervous system development

Xiong, S., Van Pelt, C. S., Elizondo-Fraire, A. C., Liu, G., & Lozano, G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508500103 · Cited by 155 · see citing works

Structural Details on mdm2-p53 Interaction

Chi, S., Lee, S., Kim, D., Ahn, M.-J., Js, K., Woo, J.-Y., Torizawa, T., Kainosho, M., & Han, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508578200 · Cited by 150 · see citing works

Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster

Bellon, S. F., Rodgers, K. K., Schatz, D. G., Coleman, J. E., & Steitz, T. A. (1997) · Nature Structural Biology · doi:10.1038/nsb0797-586 · Cited by 149 · see citing works

Tissue-specific differences of p53 inhibition by Mdm2 and Mdm4

Grier, J. D., Xiong, S., Elizondo-Fraire, A. C., Parant, J. M., & Lozano, G. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.192-198.2006 · Cited by 149 · see citing works

Molecular interaction map of the p53 and Mdm2 logic elements, which control the Off–On switch of p53 in response to DNA damage

Kohn, K. W., & Pommier, Y. G. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.186 · Cited by 117 · see citing works

The Prp19 U-box Crystal Structure Suggests a Common Dimeric Architecture for a Class of Oligomeric E3 Ubiquitin Ligases ,

Kooi, C. W. V., Ohi, M. D., Rosenberg, J. A., Oldham, M. L., Newcomer, M. E., Gould, K. L., & Chazin, W. (2005) · Biochemistry · doi:10.1021/bi051787e · Cited by 110 · see citing works

MdmX Is a RING Finger Ubiquitin Ligase Capable of Synergistically Enhancing Mdm2 Ubiquitination

Badciong, J. C., & Haas, A. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208593200 · Cited by 106 · see citing works

Differentiation of Hdm2-mediated p53 ubiquitination and Hdm2 autoubiquitination activity by small molecular weight inhibitors

Lai, Z., Yang, T., Kim, Y. B., Sielecki, T. M., Diamond, M. A., Strack, P. R., Rolfe, M., Caligiuri, M., Benfield, P. A., Auger, K. R., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212428599 · Cited by 106 · see citing works

Structure and Biochemical Function of a Prototypical Arabidopsis U-box Domain

Andersen, P., Kragelund, B. B., Olsen, A. N., Larsen, F. H., Chua, N., Poulsen, F. M., & Skriver, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405057200 · Cited by 100 · see citing works

The Structure of the C4C4RING Finger of Human NOT4 Reveals Features Distinct from Those of C3HC4 RING Fingers

Hanzawa, H., de Ruwe, M. J., Albert, T., van der Vliet, P. C., Timmers, H. T. M., & Boelens, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009298200 · Cited by 91 · see citing works

The p53-associated protein MDM2 contains a newly characterized zinc-binding domain called the RING finger

Boddy, M. N., Freemont, P. S., & Borden, K. L. B. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90020-5 · Cited by 91 · see citing works

Preventing Misfolding of the Prion Protein by Trimethylamine N-Oxide

Bennion, B. J., DeMarco, M. L., & Daggett, V. (2004) · Biochemistry · doi:10.1021/bi0486379 · Cited by 79 · see citing works

High Precision NMR Structure and Function of the RING-H2 Finger Domain of EL5, a Rice Protein Whose Expression Is Increased upon Exposure to Pathogen-derived Oligosaccharides

Katoh, S., Hong, C., Tsunoda, Y., Murata, K., Takai, R., Minami, E., Yamazaki, T., & Katoh, E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210531200 · Cited by 63 · see citing works

Structure and Interactions of the Helical and U-Box Domains of CHIP, the C Terminus of HSP70 Interacting Protein ,

Xu, Z., Devlin, K. I., Ford, M. G., Nix, J. C., Qin, J., & Misra, S. (2006) · Biochemistry · doi:10.1021/bi0601508 · Cited by 60 · see citing works

Binding of p53-derived Ligands to MDM2 Induces a Variety of Long Range Conformational Changes

Schön, O., Friedler, A., Freund, S. M. V., & Fersht, A. R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.11.051 · Cited by 58 · see citing works

Nucleotide Binding by the MDM2 RING Domain Facilitates Arf-Independent MDM2 Nucleolar Localization

Poyurovsky, M. V., Jacq, X., Ma, C., Karni-Schmidt, O., Parker, P. J., Chalfie, M., Manley, J. L., & Prives, C. L. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00400-3 · Cited by 58 · see citing works

Solution Structure of the N-terminal Domain of the Human TFIIH MAT1 Subunit

Gervais, V., Busso, D., Wasielewski, E., Poterszman, A., Egly, J., Thierry, J., & Kieffer, B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007963200 · Cited by 50 · see citing works

Metal and RNA Binding Properties of the hdm2 RING Finger Domain

Lai, Z., Freedman, D. A., Levine, A. J., & McLendon, G. L. (1998) · Biochemistry · doi:10.1021/bi980596r · Cited by 49 · see citing works

The CBP/p300 TAZ1 domain in its native state is not a binding partner of MDM2

Dunzendorfer-Matt, T., Martinez‐Yamout, M. A., Dyson, H. J., & Wright, P. E. (2004) · Biochemical Journal · doi:10.1042/bj20040564 · Cited by 42 · see citing works

Solution structure of the C4 zinc finger domain of HDM2

Yu, G. W., Allen, M. D., Andreeva, A. E., Fersht, A. R., & Bycroft, M. (2005) · Protein Science · doi:10.1110/ps.051927306 · Cited by 40 · see citing works

Solubilization and reconstitution of the Pseudomonas aeruginosa high affinity branched-chain amino acid transport system.

Hoshino, T., Kose-Terai, K., & Sato, K. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36610-4 · Cited by 25 · see citing works

ADAPT: A molecular mechanics approach for studying the structural properties of long DNA sequences

Lafontaine, I., & Lavery, R. (2000) · Biopolymers · doi:10.1002/1097-0282(2000)56:4 · Cited by 21 · see citing works

Purification, Refolding of Hybrid hIFNγ-Kringle 5 Expressed in Escherichia coli

Lu, H., Zhang, H., Wang, Q., Yuan, H., He, W., Zhao, Z., & Li, Y. (2001) · Current Microbiology · doi:10.1007/s002840010206 · Cited by 17 · see citing works

The first 30 years of p53: growing ever more complex.

Levine, A. J., & Oren, M. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2723 · Cited by 1,967 · 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

Mdm2-mediated ubiquitylation: p53 and beyond

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

E2 interaction and dimerization in the crystal structure of TRAF6

Yin, Q., Lin, S., Lamothe, B., Lu, M., Lo, Y.-C., Hura, G. L., Zheng, L., Rich, R. L., Campos, A. D., Myszka, D. G., et al. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1605 · Cited by 355 · see citing works

Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans

Linke, K., Mace, P. D., Smith, C. A., Vaux, D. L., Silke, J., & Day, C. L. (2008) · Cell Death &amp; Differentiation · doi:10.1038/sj.cdd.4402309 · Cited by 288 · see citing works

Targeted inactivation of Mdm2 RING finger E3 ubiquitin ligase activity in the mouse reveals mechanistic insights into p53 regulation

Itahana, K., Mao, H., Jin, A., Itahana, Y., Clegg, H. V., Lindström, M. S., Bhat, K. P., Godfrey, V. L., Evan, G. I., & Zhang, Y. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.09.007 · Cited by 245 · see citing works

Suprafacial Orientation of the SCFCdc4 Dimer Accommodates Multiple Geometries for Substrate Ubiquitination

Tang, X., Orlicky, S., Lin, Z., Willems, A., Neculai, D., Ceccarelli, D., Mercurio, F., Shilton, B. H., Sicheri, F., & Tyers, M. (2007) · Cell · doi:10.1016/j.cell.2007.04.042 · Cited by 209 · see citing works

RINGs hold the key to ubiquitin transfer

Budhidarmo, R., Nakatani, Y., & Day, C. L. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.11.001 · Cited by 206 · see citing works

The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activity

Poyurovsky, M. V., Priest, C., Kentsis, A., Borden, K. L., Pan, Z., Pavletich, N., & Prives, C. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601465 · Cited by 203 · see citing works

The regulation of MDM2 oncogene and its impact on human cancers

Zhao, Y., Yu, H., & Hu, W. (2014) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmt147 · Cited by 173 · see citing works

An essential function of the extreme C-terminus of MDM2 can be provided by MDMX

Uldrijan, S., Pannekoek, W., & Vousden, K. H. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601469 · Cited by 170 · see citing works

Targeting Mdm2 and Mdmx in cancer therapy: better living through medicinal chemistry?

Wade, M., & Wahl, G. M. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-08-0423 · Cited by 170 · see citing works

RING Domain–Mediated Interaction Is a Requirement for MDM2's E3 Ligase Activity

Kawai, H., Lopez-Pajares, V., Kim, M. M., Wiederschain, D., & Yuan, Z.-M. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1313 · Cited by 156 · see citing works

Regulation of p53: a collaboration between Mdm2 and MdmX

Pei, D., Zhang, Y., & Zheng, J. (2012) · Oncotarget · doi:10.18632/oncotarget.443 · Cited by 140 · see citing works

The roles and regulation of MDM2 and MDMX: it is not just about p53Preprint

Klein, A. M., de Queiroz, R. M., Venkatesh, D., & Prives, C. L. (2021) · Genes & Development · doi:10.1101/gad.347872.120 · Cited by 132 · see citing works

Intrinsic Disorder, Protein–Protein Interactions, and Disease

Uversky, V. N. (2017) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2017.06.005 · Cited by 118 · see citing works

Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators

Uversky, V. N. (2014) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2014.00006 · Cited by 107 · see citing works

Functional Analysis of Human Hub Proteins and Their Interactors Involved in the Intrinsic Disorder-Enriched Interactions

Hu, G., Wu, Z., Uversky, V. N., & Kurgan, L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122761 · Cited by 105 · see citing works

MDM2’s social network

Fåhræus, R., & Olivares‐Illana, V. (2013) · Oncogene · doi:10.1038/onc.2013.410 · Cited by 97 · see citing works

Assembling the building blocks: structure and function of inhibitor of apoptosis proteins

Mace, P. D., Shirley, S., & Day, C. L. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.45 · Cited by 96 · see citing works

Mdm2 and Mdm4 Loss Regulates Distinct p53 Activities

Barboza, J., Iwakuma, T., Terzian, T., El‐Naggar, A. K., & Lozano, G. (2008) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-07-2079 · Cited by 89 · see citing works

Small-molecule inhibitors of MDM2 as new anticancer therapeutics

Dickens, M. P., Fitzgerald, R. P., & Fischer, P. M. (2009) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2009.10.003 · Cited by 86 · see citing works

The MDM2 gene family

Mendoza, M. J., Mandani, G., & Momand, J. A. (2013) · BioMolecular Concepts · doi:10.1515/bmc-2013-0027 · Cited by 86 · see citing works

Contribution of E3-Ubiquitin Ligase Activity to HIV-1 Restriction by TRIM5α rh : Structure of the RING Domain of TRIM5α

Lienlaf, M., Hayashi, F., Nunzio, F. D., Tochio, N., Kigawa, T., Yokoyama, S., & Diaz‐Griffero, F. (2011) · Journal of Virology · doi:10.1128/jvi.00497-11 · Cited by 86 · see citing works

A Versatile Platform to Analyze Low-Affinity and Transient Protein-Protein Interactions in Living Cells in Real Time

Li, Y., Rodewald, L. W., Hoppmann, C., Wong, E. T., Lebreton, S., Šafář, P., Pátek, M., Wang, L., Wertman, K. F., & Wahl, G. M. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.058 · Cited by 83 · see citing works

The roles of intrinsic disorder-based liquid-liquid phase transitions in the “Dr. Jekyll–Mr. Hyde” behavior of proteins involved in amyotrophic lateral sclerosis and frontotemporal lobar degeneration

Uversky, V. N. (2017) · Autophagy · doi:10.1080/15548627.2017.1384889 · Cited by 76 · see citing works

The regulation of MDM2 by multisite phosphorylation—opportunities for molecular-based intervention to target tumours?

Meek, D. W., & Hupp, T. R. (2010) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2009.10.005 · Cited by 76 · see citing works

Regulation of MDM2 E3 Ligase Activity by Phosphorylation after DNA Damage

Cheng, Q., Cross, B. L., Li, B., Chen, L., Li, Z., & Chen, J. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05553-11 · Cited by 73 · see citing works

Structural analysis of MDM2 RING separates degradation from regulation of p53 transcription activity

Nomura, K., Klejnot, M., Kowalczyk, D., Hock, A. K., Sibbet, G. J., Vousden, K. H., & Huang, D. T. C. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3414 · Cited by 72 · see citing works

How to Inactivate Human Ubiquitin E3 Ligases by Mutation

Garcia-Barcena, C., Osinalde, N., Ramírez, J., & Mayor, U. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00039 · Cited by 72 · see citing works

β-arrestin 2 oligomerization controls the Mdm2-dependent inhibition of p53

Boularan, C., Scott, M. G. H., Bourougaa, K., Bellal, M., Estève, E., Thuret, A., Benmerah, A., Tramier, M., Coppey‐Moisan, M., Labbé‐Jullié, C., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705550104 · Cited by 71 · see citing works

Hetero-oligomerization with MdmX Rescues the Ubiquitin/Nedd8 Ligase Activity of RING Finger Mutants of Mdm2

Singh, R. K., Iyappan, S., & Scheffner, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610879200 · Cited by 69 · see citing works

Ribosomal protein S27-like is a physiological regulator of p53 that suppresses genomic instability and tumorigenesis

Xiong, X., Zhao, Y., Tang, F., Wei, D., Thomas, D. G., Wang, X., Liu, Y., Zheng, P., & Sun, Y. (2014) · eLife · doi:10.7554/elife.02236 · Cited by 66 · see citing works

RING Finger E3 Ubiquitin Ligases: Structure and Drug Discovery

Chasapis, C. T., & Spyroulias, G. A. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209789271825 · Cited by 62 · see citing works

MDMX contains an autoinhibitory sequence element

Biśta, M., Petrovich, M., & Fersht, A. R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317398110 · Cited by 57 · see citing works

The evolution of MDM2 family genes

Momand, J. A., Villegas, A., & Белый, В. А. (2011) · Gene · doi:10.1016/j.gene.2011.06.030 · Cited by 55 · see citing works

The MDM2 RING Domain and Central Acidic Domain Play Distinct Roles in MDM2 Protein Homodimerization and MDM2-MDMX Protein Heterodimerization

Leslie, P. L., Ke, H., & Zhang, Y. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.644435 · Cited by 50 · see citing works

Regulation of MDM2 Stability After DNA Damage

Li, J., & Kurokawa, M. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.24994 · Cited by 48 · see citing works

Detection and Characterization of the In Vitro E3 Ligase Activity of the Human MID1 Protein

Han, X., Du, H., & Massiah, M. A. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.01.048 · Cited by 48 · see citing works

Targeting TRIM Proteins: A Quest towards Drugging an Emerging Protein Class

D’Amico, F., Mukhopadhyay, R., Ovaa, H., & Mulder, M. P. C. (2021) · ChemBioChem · doi:10.1002/cbic.202000787 · Cited by 44 · see citing works

MAGE-A Cancer/Testis Antigens Inhibit MDM2 Ubiquitylation Function and Promote Increased Levels of MDM4

Marcar, L., Ihrig, B., Hourihan, J. M., Bray, S. E., Quinlan, P., Jordan, L. B., Thompson, A. M., Hupp, T. R., & Meek, D. W. (2015) · PLoS ONE · doi:10.1371/journal.pone.0127713 · Cited by 42 · see citing works

Structural and Functional Comparison of the RING Domains of Two p53 E3 Ligases, Mdm2 and Pirh2

Shloush, J., Vlassov, J. E., Engson, I., Duan, S., Saridakis, V., Dhe-paganon, S., Raught, B., Sheng, Y., & Arrowsmith, C. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.157669 · Cited by 42 · see citing works

Structural Analysis of B-Box 2 from MuRF1: Identification of a Novel Self-Association Pattern in a RING-like Fold

Mrosek, M., Meier, S., Ucurum-Fotiadis, Z., von Castelmur, E., Hedbom, E., Lustig, A., Grzesiek, S., Labeit, D., Labeit, S., & Mayans, O. M. (2008) · Biochemistry · doi:10.1021/bi800733z · Cited by 42 · see citing works

Competitive ubiquitination activates the tumor suppressor p53

Li, X., Guo, M., Cai, L., Du, T., Liu, Y., Ding, H., Wang, H., Zhang, J., Chen, X., & Yan, C. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0463-x · Cited by 41 · see citing works

Anatomy of Mdm2 and Mdm4 in evolution

Tan, B. X., Liew, H. P., Chua, J. S., Ghadessy, F. J., Tan, Y. S., Lane, D. P., & Coffill, C. R. (2017) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjx002 · Cited by 40 · see citing works

MDM4 (MDMX) and its Transcript Variants

Mancini, F., Conza, G. D., & Moretti, F. (2009) · Current Genomics · doi:10.2174/138920209787581280 · Cited by 39 · see citing works

Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain

Magnussen, H., Ahmed, S. F., Sibbet, G. J., Hristova, V. A., Nomura, K., Hock, A. K., Archibald, L. J., Jamieson, A. G., Fushman, D., Vousden, K. H., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15783-y · Cited by 37 · see citing works

Intrinsically Unstructured Domains of Arf and Hdm2 Form Bimolecular Oligomeric Structures In Vitro and In Vivo

Sivakolundu, S. G., Nourse, A., Moshiach, S., Bothner, B. B., Ashley, C., Satumba, J., Lahti, J. M., & Kriwacki, R. W. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.09.019 · Cited by 36 · see citing works

Regulation of the E3 ubiquitin ligase activity of MDM2 by an N-terminal pseudo-substrate motif

Worrall, E. G., Wawrzynów, B., Worrall, L. J., Walkinshaw, M. D., Ball, K. L., & Hupp, T. R. (2009) · Journal of Chemical Biology · doi:10.1007/s12154-009-0019-5 · Cited by 35 · see citing works

The roles of MDM2 and MDMX phosphorylation in stress signaling to p53

Chen, J. (2012) · Genes &amp; Cancer · doi:10.1177/1947601912454733 · Cited by 33 · see citing works

Mutational analysis of Mdm2 C-terminal tail suggests an evolutionarily conserved role of its length in Mdm2 activity toward p53 and indicates structural differences between Mdm2 homodimers and Mdm2/MdmX heterodimers

Doleželová, P., Cetkovská, K., Vousden, K. H., & Uldrijan, S. (2012) · Cell Cycle · doi:10.4161/cc.11.5.19445 · Cited by 33 · see citing works

Identification of a second N utlin‐3 responsive interaction site in the N ‐terminal domain of MDM 2 using hydrogen/deuterium exchange mass spectrometry

Hernychová, L., Man, P., Verma, C. S., Nicholson, J., Sharma, C.-A., Růčková, E., Teo, J. Y., Ball, K. L., Vojtesek, B., & Hupp, T. R. (2013) · PROTEOMICS · doi:10.1002/pmic.201300029 · Cited by 32 · see citing works

Inhibitors of MDM2 and MDMX: A Structural Perspective

Riedinger, C., & McDonnell, J. M. (2009) · Future Medicinal Chemistry · doi:10.4155/fmc.09.75 · Cited by 32 · see citing works

A Function for the RING Finger Domain in the Allosteric Control of MDM2 Conformation and Activity

Wawrzynów, B., Pettersson, S., Żylicz, M., Bramham, J., Worrall, E. G., Hupp, T. R., & Ball, K. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809294200 · Cited by 32 · see citing works

Targeting a Dark Excited State of HIV‐1 Nucleocapsid by Antiretroviral Thioesters Revealed by NMR Spectroscopy

Deshmukh, L., Tugarinov, V., Appella, D. H., & Clore, G. M. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201713172 · Cited by 32 · see citing works

Turning the RING Domain Protein MdmX into an Active Ubiquitin-Protein Ligase*

Iyappan, S., Wollscheid, H.-P., Rojas‐Fernández, A., Marquardt, A., Tang, H., Singh, R. K., & Scheffner, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.115113 · Cited by 29 · see citing works

The Effects of Phosphomimetic Lid Mutation on the Thermostability of the N-terminal Domain of MDM2

Worrall, E. G., Worrall, L. J., Blackburn, E. A., Walkinshaw, M. D., & Hupp, T. R. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.03.023 · Cited by 28 · see citing works

A strong 13C chemical shift signature provides the coordination mode of histidines in zinc-binding proteins

Barraud, P., Schubert, M., & Allain, F. H. ‐. (2012) · Journal of Biomolecular NMR · doi:10.1007/s10858-012-9625-6 · Cited by 28 · see citing works

Structure and putative function of NFX1‐like proteins in plants

Müssig, C., Schröder, F., Usadel, B., & Lisso, J. (2010) · Plant Biology · doi:10.1111/j.1438-8677.2009.00303.x · Cited by 28 · see citing works

NMR‐based insights into the conformational and interaction properties of Arkadia RING‐H2 E3 Ub ligase

Chasapis, C. T., Kandias, N. G., Episkopou, V., Bentrop, D., & Spyroulias, G. A. (2012) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24048 · Cited by 28 · see citing works

Allosteric Interactions by p53 mRNA Govern HDM2 E3 Ubiquitin Ligase Specificity under Different Conditions

Medina‐Medina, I., García-Beltrán, P., la Mora, I. D. L. M.-D., Oria‐Hernández, J., Millot, G., Fåhræus, R., Reyes‐Vivas, H., Sampedro, J. G., & Olivares‐Illana, V. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00113-16 · Cited by 27 · see citing works

DNA Binding by Sgf11 Protein Affects Histone H2B Deubiquitination by Spt-Ada-Gcn5-Acetyltransferase (SAGA)

Koehler, C. J., Bonnet, J., Stierlé, M., Romier, C., Devys, D., & Kieffer, B. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.500868 · Cited by 26 · see citing works

Isoforms of RNF128 Regulate the Stability of Mutant P53 in Barrett's Esophageal Cells

Ray, D., Ray, P., Ferrer-Torres, D., Wang, Z., Nancarrow, D. J., Yoon, H., Martinho, M. S., Hinton, T., Owens, S. R., Thomas, D. G., et al. (2019) · Gastroenterology · doi:10.1053/j.gastro.2019.10.040 · Cited by 25 · see citing works

Functional analysis and consequences of Mdm2 E3 ligase inhibition in human tumor cells

Wade, M. R., Li, Y. C., Matani, A. S., Braun, S. M. G., Milanesi, F., Rodewald, L. W., & Wahl, G. M. (2012) · Oncogene · doi:10.1038/onc.2011.625 · Cited by 25 · see citing works

The Fellowship of the RING: The RING–B-Box Linker Region Interacts with the RING in TRIM21/Ro52, Contains a Native Autoantigenic Epitope in Sjögren Syndrome, and is an Integral and Conserved Region in TRIM Proteins

Hennig, J., Bresell, A., Sandberg, M., Hennig, K. D., Wahren‐Herlenius, M., Persson, B., & Sunnerhagen, M. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.01.005 · Cited by 25 · see citing works

Use of E2~Ubiquitin Conjugates for the Characterization of Ubiquitin Transfer by RING E3 Ligases Such as the Inhibitor of Apoptosis Proteins

Middleton, A. J., Budhidarmo, R., & Day, C. L. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801430-1.00010-x · Cited by 24 · see citing works

Nanosensing protein allostery using a bivalent mouse double minute two (MDM2) assay

Robson, A. F., Hupp, T. R., Lickiss, F., Ball, K. L., Faulds, K., & Graham, D. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116637109 · Cited by 24 · see citing works

Protein–protein interactions regulate Ubl conjugation

Knipscheer, P., & Sixma, T. K. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.09.001 · Cited by 24 · see citing works

A Residue Specific Insight into the Arkadia E3 Ubiquitin Ligase Activity and Conformational Plasticity

Birkou, M., Chasapis, C. T., Marousis, K. D., Loutsidou, A. K., Bentrop, D., Lelli, M., Herrmann, T., Carthy, J. M., Episkopou, V., & Spyroulias, G. A. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.06.012 · Cited by 23 · see citing works

Development of a fluorescent monoclonal antibody‐based assay to measure the allosteric effects of synthetic peptides on self‐oligomerization of AGR2 protein

Gray, T. A., Murray, E., Nowicki, M. W., Remnant, L., Scherl, A., Müller, P., Vojtesek, B., & Hupp, T. R. (2013) · Protein Science · doi:10.1002/pro.2299 · Cited by 22 · see citing works

Discovery of N -(3,4-Dimethylphenyl)-4-(4-isobutyrylphenyl)-2,3,3a,4,5,9b-hexahydrofuro[3,2- c ]quinoline-8-sulfonamide as a Potent Dual MDM2/XIAP Inhibitor

Wu, Z., Gu, L., Zhang, S., Liu, T., Lukka, P. B., Meibohm, B., Bollinger, J. C., Zhou, M., & Li, W. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00932 · Cited by 21 · see citing works

Identification and Characterization of Two Novel Isoforms of Pirh2 Ubiquitin Ligase That Negatively Regulate p53 Independent of RING Finger Domains

Corcoran, C. A., Montalbano, J., Hong, S., He, Q., Huang, Y. K., & Sheikh, M. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.024232 · Cited by 21 · see citing works

5-Deazaflavin derivatives as inhibitors of p53 ubiquitination by HDM2

Dickens, M. P., Roxburgh, P., Hock, A., Mezna, M., Kellam, B., Vousden, K. H., & Fischer, P. M. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.09.038 · Cited by 21 · see citing works

p53 promotes its own polyubiquitination by enhancing the HDM2 and HDMX interaction

Medina‐Medina, I., Martínez‐Sánchez, M., Hernández‐Monge, J., Fåhræus, R., Müller, P., & Olivares‐Illana, V. (2018) · Protein Science · doi:10.1002/pro.3405 · Cited by 19 · see citing works

An observational study on the expression levels of MDM2 and MDMX proteins, and associated effects on P53 in a series of human liposarcomas

Touqan, N., Diggle, C. P., Verghese, E. T., Perry, S., Horgan, K. J., Merchant, W., Anwar, R., Markham, A. F., Carr, I., & Achuthan, R. (2013) · BMC Clinical Pathology · doi:10.1186/1472-6890-13-32 · Cited by 18 · see citing works

CD4 dimerization requires two cysteines in the cytoplasmic domain of the molecule and occurs in microdomains distinct from lipid rafts

Fournier, M., Peyrou, M., Bourgoin, L., Maeder, C., Tchou, I., & Foti, M. (2010) · Molecular Immunology · doi:10.1016/j.molimm.2010.06.010 · Cited by 17 · see citing works

Zinc Binding Properties of Engineered RING Finger Domain of Arkadia E3 Ubiquitin Ligase

Chasapis, C. T., Loutsidou, A. K., Orkoula, M. G., & Spyroulias, G. A. (2010) · Bioinorganic Chemistry and Applications · doi:10.1155/2010/323152 · Cited by 17 · see citing works

MDM2 oligomers: antagonizers of the guardian of the genome

Leslie, P. L., & Zhang, Y. (2016) · Oncogene · doi:10.1038/onc.2016.88 · Cited by 17 · see citing works

Deconstructing nucleotide binding activity of the Mdm2 RING domain

Priest, C., Prives, C. L., & Poyurovsky, M. V. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq669 · Cited by 16 · see citing works

A Single Conserved Amino Acid Residue as a Critical Context-Specific Determinant of the Differential Ability of Mdm2 and MdmX RING Domains to Dimerize

Kosztyu, P., Slaninová, I., Valčíková, B., Verlande, A., Müller, P., Palecek, J. J., & Uldrijan, S. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00390 · Cited by 15 · see citing works

The creation of the artificial RING finger from the cross-brace zinc finger by α-helical region substitution

Miyamoto, K., & Togiya, K. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.03.100 · Cited by 15 · see citing works

Bivalent binding of p14ARF to MDM2 RING and acidic domains inhibits E3 ligase function

Kowalczyk, D., Nakasone, M. A., Smith, B. O., & Huang, D. T. C. (2022) · Life Science Alliance · doi:10.26508/lsa.202201472 · Cited by 15 · see citing works

Phosphomimetic Mutation of the N-Terminal Lid of MDM2 Enhances the Polyubiquitination of p53 through Stimulation of E2-Ubiquitin Thioester Hydrolysis

Fraser, J. A., Worrall, E. G., Lin, Y., Landré, V., Pettersson, S., Blackburn, E. A., Walkinshaw, M. D., Müller, P., Vojtesek, B., Ball, K. L., et al. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.12.011 · Cited by 14 · see citing works

MDM2–MDM4 molecular interaction investigated by atomic force spectroscopy and surface plasmon resonance

Cannistraro, S., Moscetti, I., Teveroni, E., Moretti, F., & Bizzarri, A. R. (2016) · International Journal of Nanomedicine · doi:10.2147/ijn.s114705 · Cited by 13 · see citing works

Structural model of ubiquitin transfer onto an artificial RING finger as an E3 ligase

Miyamoto, K. (2014) · Scientific Reports · doi:10.1038/srep06574 · Cited by 11 · see citing works

NMR Studies of Metalloproteins

Li, H., & Sun, H. (2011) · Topics in current chemistry · doi:10.1007/128_2011_214 · Cited by 10 · see citing works

Cisplatin binds to the MDM2 RING finger domain and inhibits the ubiquitination activity

Cao, K., Ding, X., Sheng, Y., Wang, Y., & Liu, Y. (2020) · Chemical Communications · doi:10.1039/d0cc00203h · Cited by 9 · see citing works

Dynamics of the RING Domain from Human TRAF6 by 15N NMR Spectroscopy: Implications for Biological Function

Markin, C. J., Saltibus, L. F., & Spyracopoulos, L. (2008) · Biochemistry · doi:10.1021/bi800252x · Cited by 10 · see citing works

A site-directed mutagenesis study of the MdmX RING domain

Egorova, O., & Sheng, Y. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.04.065 · Cited by 10 · see citing works

Structural Insights into Functional Modes of Proteins Involved in Ubiquitin Family Pathways

Hänzelmann, P., Schäfer, A., Völler, D., & Schindelin, H. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-474-2_39 · Cited by 10 · see citing works

A p53 transcriptional signature in primary and metastatic cancers derived using machine learning

Keshavarz-Rahaghi, F., Pleasance, E., Kolisnik, T., & Jones, S. J. M. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.987238 · Cited by 9 · see citing works

p53 Regulation Goes Live--Mdm2 and MdmX Co-Star: Lessons Learned from Mouse Modeling

Tollini, L. A., & Zhang, Y. (2012) · Genes & Cancer · doi:10.1177/1947601912454732 · Cited by 9 · see citing works

Hierarchical core decomposition of RING structure as a method to capture novel functional residues within RING-type E3 ligases: a structural systems biology approach

Chasapis, C. T. (2018) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2018.06.033 · Cited by 9 · see citing works

1H, 15N and 13C backbone resonance assignments of the acidic domain of the human MDMX protein

Song, Q., Liu, X., & Rainey, J. K. (2022) · Biomolecular NMR Assignments · doi:10.1007/s12104-022-10081-8 · Cited by 8 · see citing works

Concise machinery for monitoring ubiquitination activities using novel artificial RING fingers

Miyamoto, K., & Saito, K. (2018) · Protein Science · doi:10.1002/pro.3427 · Cited by 8 · see citing works

Zinc-Binding B-Box Domains with RING Folds Serve Critical Roles in the Protein Ubiquitination Pathways in Plants and Animals

Massiah, M. A. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.85895 · Cited by 7 · see citing works

MDMX is essential for the regulation of p53 protein levels in the absence of a functional MDM2 C-terminal tail

Sanford, J. D., Yang, J., Han, J., Tollini, L. A., Jin, A., & Zhang, Y. (2021) · BMC Molecular and Cell Biology · doi:10.1186/s12860-021-00385-3 · Cited by 7 · see citing works

Alterations of the Mdm2 C-Terminus Differentially Impact Its Function In Vivo

Pant, V., Aryal, N. K., Xiong, S., Chau, G. P., Fowlkes, N. W., & Lozano, G. (2022) · Cancer Research · doi:10.1158/0008-5472.can-21-2381 · Cited by 6 · see citing works

Intra molecular interactions in the regulation of p53 pathway

Chen, J. (2016) · Translational Cancer Research · doi:10.21037/tcr.2016.09.23 · Cited by 5 · see citing works

Therapeutic considerations for Mdm2: not just a one trick pony

Lehman, J. A., Eitel, J. A., Batuello, C. N., & Mayo, L. D. (2008) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.3.11.1309 · Cited by 5 · see citing works

Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans

Linke, K., Mace, P. D., Smith, C. A., Vaux, D. L., Silke, J., & Day, C. L. (2008) · Cell Death &amp; Differentiation · doi:10.1038/sj.cdd.4402309 · Cited by 288 · see citing works

Solution structure of the C4 zinc finger domain of HDM2

Yu, G. W., Allen, M. D., Andreeva, A. E., Fersht, A. R., & Bycroft, M. (2005) · Protein Science · doi:10.1110/ps.051927306 · Cited by 40 · see citing works

A site-directed mutagenesis study of the MdmX RING domain

Egorova, O., & Sheng, Y. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.04.065 · Cited by 10 · see citing works

Structural characterisation of MDM2 RING domain: E2-ubiquitin binding and activation by phosphorylation

Magnussen, H. (2020) · Enlighten: Theses (The University of Glasgow) · doi:10.5525/gla.thesis.79033

Role of the RING domain in MDM2-mediated ubiquitination of p53

Lickiss, F. (2015) · ERA