41.1 KB · ⇊ 12 parts · ⤓ Micron 41.1 KB · ⤓ HTML 104.4 KB

top

mwbwMdm2 è il nome sia del mwcagene che della corrispettiva mwcqproteina che svolge la funzione di principale inibitore di mwcgp53, andandosi a legare ad esso ed inducendone l'mwcwubiquitinazione e quindi la degradazione tramite mwdaproteosoma. Mdm2 appartiene pertanto alla famiglia delle ligasi E3.cite-ref-1[1]cite-ref-2[2]

• Interazioni

• Interazioni farmacologiche

• Note

• Voci correlate

• Altri progetti

Mdm2 è regolata da molte proteine e mwgamiRNA per il suo ruolo centrale nel regolare p53. Interagisce con p53 inducendone la degradazione. Ciononostante p53 incrementa l'attività e la produzione di Mdm2 sia direttamente che indirettamente, formando così un feedback negativo autoregolatorio. La proteina mwgqARF (conosciuta anche come p14) è un inibitore di Mdm2.

Mdm2 interagisce con le seguenti proteine:

• ABL1,cite-ref-pmid12110584-3-0[3]

• ARRB1,cite-ref-pmid12538596-4-0[4]cite-ref-pmid18544533-5-0[5]

• ARRB2,cite-ref-pmid12538596-4-1[4]cite-ref-pmid18544533-5-1[5]cite-ref-pmid12488444-6-0[6]

• CCNG1,cite-ref-pmid12556559-7-0[7]

• CTBP1,cite-ref-pmid12867035-8-0[8]

• CTBP2,cite-ref-pmid12867035-8-1[8]

• DAXX,cite-ref-pmid18583933-9-0[9]

• DHFR,cite-ref-pmid18451149-10-0[10]

• EP300,cite-ref-pmid9809062-11-0[11]

• ERICH3,cite-ref-12[12]

• FKBP3,cite-ref-pmid19166840-13-0[13]

• FOXO4,cite-ref-pmid18665269-14-0[14]

• GNL3,cite-ref-pmid18426907-15-0[15]

• HDAC1,cite-ref-pmid12426395-16-0[16]

• HIF1A,cite-ref-pmid12606552-17-0[17]cite-ref-pmid10640274-18-0[18]

• HTATIP,cite-ref-pmid11927554-19-0[19]

• IGF1R,cite-ref-pmid18632619-20-0[20]

• MDM4,cite-ref-pmid12483531-21-0[21]cite-ref-pmid10218570-22-0[22]cite-ref-pmid12393902-23-0[23]cite-ref-pmid18219319-24-0[24]

• NUMB,cite-ref-pmid12646252-25-0[25]cite-ref-pmid18172499-26-0[26]

• P16,cite-ref-pmid18583933-9-1[9]cite-ref-pmid14612427-27-0[27]cite-ref-pmid9529249-28-0[28]cite-ref-pmid12085228-29-0[29]cite-ref-pmid9529248-30-0[30]

• P53,cite-ref-pmid9153395-31-0[31]cite-ref-pmid9450543-32-0[32]

• P73,cite-ref-pmid10435614-33-0[33]cite-ref-pmid10207051-34-0[34]

• PCAF,cite-ref-pmid12068014-35-0[35]

• PSMD10,cite-ref-pmid18332869-36-0[36]

• PSME3,cite-ref-pmid18309296-37-0[37]

• RPL5,cite-ref-pmid18426907-15-1[15]cite-ref-pmid14612427-27-1[27]cite-ref-pmid7935455-38-0[38]

• RPL11,cite-ref-pmid18426907-15-2[15]cite-ref-pmid14612427-27-2[27]

• PML,cite-ref-pmid15195100-39-0[39]cite-ref-pmid14507915-40-0[40]cite-ref-pmid12915590-41-0[41]cite-ref-pmid12759344-42-0[42]

• RPL26,cite-ref-pmid18951086-43-0[43]

• RRM2B,cite-ref-pmid19015526-44-0[44]

• RYBP,cite-ref-pmid19098711-45-0[45]

• TBP,cite-ref-pmid9388200-46-0[46]cite-ref-pmid9271120-47-0[47] and

• UBC.cite-ref-pmid18583933-9-2[9]cite-ref-pmid18566590-48-0[48]cite-ref-pmid18382127-49-0[49]

La molecola mw-gmw-wnutlina inibisce l'interazione tra Mdm2 e p53 incrementanto la stabilità di quest'ultimo, ciononostante è ancora in fase di sperimentazione.cite-ref-50[50]

cite-note-11. ↑ mwaqoJ. D. Oliner, K. W. Kinzler e P. S. Meltzer, mwaqsmwaqwAmplification of a gene encoding a p53-associated protein in human sarcomas, in mwaq0Nature, vol.mwaq4 358, n.mwaq8 6381, 2 luglio 1992, pp.mwara 80-83, mwareDOI:mwari10.1038/358080a0. mwarmURL consultato il 16 aprile 2018.

cite-note-22. ↑ mwarcMark Wade, Ee Tsin Wong e Mengjia Tang, mwargmwarkHdmx modulates the outcome of p53 activation in human tumor cells, in mwaroThe Journal of Biological Chemistry, vol.mwars 281, n.mwarw 44, 3 novembre 2006, pp.mwar0 33036-33044, mwar4DOI:mwar810.1074/jbc.M605405200. mwasaURL consultato il 16 aprile 2018.

cite-note-pmid12110584-33. ↑ mwasqGoldberg Z, Vogt Sionov R, Berger M, Zwang Y, Perets R, Van Etten RA, Oren M, Taya Y, Haupt Y, mwasumwasyTyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation, in mwascThe EMBO Journal, vol.mwasg 21, n.mwask 14, July 2002, pp.mwaso 3715-27, mwassDOI:mwasw10.1093/emboj/cdf384, mwas0PMCmwas4 mwas8125401, mwataPMIDmwate mwati12110584.

cite-note-pmid12538596-44. ↑ mwatkWang P, Wu Y, Ge X, Ma L, Pei G, mwatomwatsSubcellular localization of beta-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus, in mwatwThe Journal of Biological Chemistry, vol.mwat0 278, n.mwat4 13, March 2003, pp.mwat8 11648-53, mwauaDOI:mwaue10.1074/jbc.M208109200, mwauiPMIDmwaum mwauq12538596.

cite-note-pmid18544533-55. ↑ mwausShenoy SK, Xiao K, Venkataramanan V, Snyder PM, Freedman NJ, Weissman AM, mwauwmwau0Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor, in mwau4The Journal of Biological Chemistry, vol.mwau8 283, n.mwava 32, August 2008, pp.mwave 22166-76, mwaviDOI:mwavm10.1074/jbc.M709668200, mwavqPMCmwavu mwavy2494938, mwavcPMIDmwavg mwavk18544533.

cite-note-pmid12488444-66. ↑ mwav4Wang P, Gao H, Ni Y, Wang B, Wu Y, Ji L, Qin L, Ma L, Pei G, mwav8mwawaBeta-arrestin 2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2, in mwaweThe Journal of Biological Chemistry, vol.mwawi 278, n.mwawm 8, February 2003, pp.mwawq 6363-70, mwawuDOI:mwawy10.1074/jbc.M210350200, mwawcPMIDmwawg mwawk12488444.

cite-note-pmid12556559-77. ↑ mwaw4Zhao L, Samuels T, Winckler S, Korgaonkar C, Tompkins V, Horne MC, Quelle DE, mwaw8Cyclin G1 has growth inhibitory activity linked to the ARF-Mdm2-p53 and pRb tumor suppressor pathways, in mwaxaMolecular Cancer Research, vol.mwaxe 1, n.mwaxi 3, January 2003, pp.mwaxm 195-206, mwaxqPMIDmwaxu mwaxy12556559.

cite-note-pmid12867035-88. ↑ mwax0Mirnezami AH, Campbell SJ, Darley M, Primrose JN, Johnson PW, Blaydes JP, mwax4mwax8Hdm2 recruits a hypoxia-sensitive corepressor to negatively regulate p53-dependent transcription, in mwayaCurrent Biology, vol.mwaye 13, n.mwayi 14, July 2003, pp.mwaym 1234-9, mwayqDOI:mwayu10.1016/S0960-9822(03)00454-8, mwayyPMIDmwayc mwayg12867035.

cite-note-pmid18583933-99. ↑ mwazeIvanchuk SM, Mondal S, Rutka JT, mwazimwazmp14ARF interacts with DAXX: effects on HDM2 and p53, in mwazqCell Cycle, vol.mwazu 7, n.mwazy 12, June 2008, pp.mwazc 1836-50, mwazgDOI:mwazk10.4161/cc.7.12.6025, mwazoPMIDmwazs mwazw18583933.

cite-note-pmid18451149-1010. ↑ mwaaeMaguire M, Nield PC, Devling T, Jenkins RE, Park BK, Polański R, Vlatković N, Boyd MT, mwaaimwaamMDM2 regulates dihydrofolate reductase activity through monoubiquitination, in mwaaqCancer Research, vol.mwaau 68, n.mwaay 9, May 2008, pp.mwaac 3232-42, mwaagDOI:mwaak10.1158/0008-5472.CAN-07-5271, mwaaoPMCmwaas mwaaw3536468, mwaa0PMIDmwaa4 mwaa818451149.

cite-note-pmid9809062-1111. ↑ mwabqGrossman SR, Perez M, Kung AL, Joseph M, Mansur C, Xiao ZX, Kumar S, Howley PM, Livingston DM, mwabumwabyp300/MDM2 complexes participate in MDM2-mediated p53 degradation, in mwabcMolecular Cell, vol.mwabg 2, n.mwabk 4, October 1998, pp.mwabo 405-15, mwabsDOI:mwabw10.1016/S1097-2765(00)80140-9, mwab0PMIDmwab4 mwab89809062.

cite-note-1212. ↑ mwacqMiyamoto-Sato E, Fujimori S, Ishizaka M, Hirai N, Masuoka K, Saito R, Ozawa Y, Hino K, Washio T, Tomita M, Yamashita T, Oshikubo T, Akasaka H, Sugiyama J, Matsumoto Y, Yanagawa H, mwacumwacyA comprehensive resource of interacting protein regions for refining human transcription factor networks, in mwaccPLoS One, vol.mwacg 5, n.mwack 2, Feb 2010, pp.mwaco e9289, mwacsDOI:mwacw10.1371/journal.pone.0009289, mwac0PMCmwac4 mwac82827538, mwadaPMIDmwade mwadi20195357.

cite-note-pmid19166840-1313. ↑ mwadcOchocka AM, Kampanis P, Nicol S, Allende-Vega N, Cox M, Marcar L, Milne D, Fuller-Pace F, Meek D, mwadgmwadkFKBP25, a novel regulator of the p53 pathway, induces the degradation of MDM2 and activation of p53, in mwadoFEBS Letters, vol.mwads 583, n.mwadw 4, February 2009, pp.mwad0 621-6, mwad4DOI:mwad810.1016/j.febslet.2009.01.009, mwaeaPMIDmwaee mwaei19166840.

cite-note-pmid18665269-1414. ↑ mwaecBrenkman AB, de Keizer PL, van den Broek NJ, Jochemsen AG, Burgering BM, mwaegmwaekMdm2 induces mono-ubiquitination of FOXO4, in mwaeoPLoS One, vol.mwaes 3, n.mwaew 7, 2008, pp.mwae0 e2819, mwae4DOI:mwae810.1371/journal.pone.0002819, mwafaPMCmwafe mwafi2475507, mwafmPMIDmwafq mwafu18665269.

cite-note-pmid18426907-1515. ↑ mwaf4Dai MS, Sun XX, Lu H, mwaf8mwagaAberrant expression of nucleostemin activates p53 and induces cell cycle arrest via inhibition of MDM2, in mwageMolecular and Cellular Biology, vol.mwagi 28, n.mwagm 13, July 2008, pp.mwagq 4365-76, mwaguDOI:mwagy10.1128/MCB.01662-07, mwagcPMCmwagg mwagk2447154, mwagoPMIDmwags mwagw18426907.

cite-note-pmid12426395-1616. ↑ mwaheIto A, Kawaguchi Y, Lai CH, Kovacs JJ, Higashimoto Y, Appella E, Yao TP, mwahimwahmMDM2-HDAC1-mediated deacetylation of p53 is required for its degradation, in mwahqThe EMBO Journal, vol.mwahu 21, n.mwahy 22, November 2002, pp.mwahc 6236-45, mwahgDOI:mwahk10.1093/emboj/cdf616, mwahoPMCmwahs mwahw137207, mwah0PMIDmwah4 mwah812426395.

cite-note-pmid12606552-1717. ↑ mwaiqChen D, Li M, Luo J, Gu W, mwaiumwaiyDirect interactions between HIF-1 alpha and Mdm2 modulate p53 function, in mwaicThe Journal of Biological Chemistry, vol.mwaig 278, n.mwaik 16, April 2003, pp.mwaio 13595-8, mwaisDOI:mwaiw10.1074/jbc.C200694200, mwai0PMIDmwai4 mwai812606552.

cite-note-pmid10640274-1818. ↑ mwajqRavi R, Mookerjee B, Bhujwalla ZM, Sutter CH, Artemov D, Zeng Q, Dillehay LE, Madan A, Semenza GL, Bedi A, mwajumwajyRegulation of tumor angiogenesis by p53-induced degradation of hypoxia-inducible factor 1alpha, in mwajcGenes & Development, vol.mwajg 14, n.mwajk 1, January 2000, pp.mwajo 34-44, mwajsDOI:mwajw10.1101/gad.14.1.34, mwaj0PMCmwaj4 mwaj8316350, mwakaPMIDmwake mwaki10640274.

cite-note-pmid11927554-1919. ↑ mwakcLegube G, Linares LK, Lemercier C, Scheffner M, Khochbin S, Trouche D, mwakgmwakkTip60 is targeted to proteasome-mediated degradation by Mdm2 and accumulates after UV irradiation, in mwakoThe EMBO Journal, vol.mwaks 21, n.mwakw 7, April 2002, pp.mwak0 1704-12, mwak4DOI:mwak810.1093/emboj/21.7.1704, mwalaPMCmwale mwali125958, mwalmPMIDmwalq mwalu11927554.

cite-note-pmid18632619-2020. ↑ mwaloSehat B, Andersson S, Girnita L, Larsson O, mwalsmwalwIdentification of c-Cbl as a new ligase for insulin-like growth factor-I receptor with distinct roles from Mdm2 in receptor ubiquitination and endocytosis, in mwal0Cancer Research, vol.mwal4 68, n.mwal8 14, July 2008, pp.mwama 5669-77, mwameDOI:mwami10.1158/0008-5472.CAN-07-6364, mwammPMIDmwamq mwamu18632619.

cite-note-pmid12483531-2121. ↑ mwamoKadakia M, Brown TL, McGorry MM, Berberich SJ, mwamsmwamwMdmX inhibits Smad transactivation, in mwam0Oncogene, vol.mwam4 21, n.mwam8 57, December 2002, pp.mwana 8776-85, mwaneDOI:mwani10.1038/sj.onc.1205993, mwanmPMIDmwanq mwanu12483531.

cite-note-pmid10218570-2222. ↑ mwanoTanimura S, Ohtsuka S, Mitsui K, Shirouzu K, Yoshimura A, Ohtsubo M, mwansmwanwMDM2 interacts with MDMX through their RING finger domains, in mwan0FEBS Letters, vol.mwan4 447, n.mwan8 1, March 1999, pp.mwaoa 5-9, mwaoeDOI:mwaoi10.1016/S0014-5793(99)00254-9, mwaomPMIDmwaoq mwaou10218570.

cite-note-pmid12393902-2323. ↑ mwaooBadciong JC, Haas AL, mwaosmwaowMdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination, in mwao0The Journal of Biological Chemistry, vol.mwao4 277, n.mwao8 51, December 2002, pp.mwapa 49668-75, mwapeDOI:mwapi10.1074/jbc.M208593200, mwapmPMIDmwapq mwapu12393902.

cite-note-pmid18219319-2424. ↑ mwapoLinke K, Mace PD, Smith CA, Vaux DL, Silke J, Day CL, mwapsmwapwStructure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans, in mwap0Cell Death and Differentiation, vol.mwap4 15, n.mwap8 5, May 2008, pp.mwaqa 841-8, mwaqeDOI:mwaqi10.1038/sj.cdd.4402309, mwaqmPMIDmwaqq mwaqu18219319.

cite-note-pmid12646252-2525. ↑ mwaqoYogosawa S, Miyauchi Y, Honda R, Tanaka H, Yasuda H, mwaqsmwaqwMammalian Numb is a target protein of Mdm2, ubiquitin ligase, in mwaq0Biochemical and Biophysical Research Communications, vol.mwaq4 302, n.mwaq8 4, March 2003, pp.mwara 869-72, mwareDOI:mwari10.1016/S0006-291X(03)00282-1, mwarmPMIDmwarq mwaru12646252.

cite-note-pmid18172499-2626. ↑ mwaroColaluca IN, Tosoni D, Nuciforo P, Senic-Matuglia F, Galimberti V, Viale G, Pece S, Di Fiore PP, mwarsmwarwNUMB controls p53 tumour suppressor activity, in mwar0Nature, vol.mwar4 451, n.mwar8 7174, January 2008, pp.mwasa 76-80, mwaseDOI:mwasi10.1038/nature06412, mwasmPMIDmwasq mwasu18172499.

cite-note-pmid14612427-2727. ↑ mwas4Zhang Y, Wolf GW, Bhat K, Jin A, Allio T, Burkhart WA, Xiong Y, mwas8mwataRibosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway, in mwateMolecular and Cellular Biology, vol.mwati 23, n.mwatm 23, December 2003, pp.mwatq 8902-12, mwatuDOI:mwaty10.1128/MCB.23.23.8902-8912.2003, mwatcPMCmwatg mwatk262682, mwatoPMIDmwats mwatw14612427.

cite-note-pmid9529249-2828. ↑ mwaueZhang Y, Xiong Y, Yarbrough WG, mwauimwaumARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways, in mwauqCell, vol.mwauu 92, n.mwauy 6, March 1998, pp.mwauc 725-34, mwaugDOI:mwauk10.1016/S0092-8674(00)81401-4, mwauoPMIDmwaus mwauw9529249.

cite-note-pmid12085228-2929. ↑ mwaveClark PA, Llanos S, Peters G, mwavimwavmMultiple interacting domains contribute to p14ARF mediated inhibition of MDM2, in mwavqOncogene, vol.mwavu 21, n.mwavy 29, July 2002, pp.mwavc 4498-507, mwavgDOI:mwavk10.1038/sj.onc.1205558, mwavoPMIDmwavs mwavw12085228.

cite-note-pmid9529248-3030. ↑ mwawePomerantz J, Schreiber-Agus N, Liégeois NJ, Silverman A, Alland L, Chin L, Potes J, Chen K, Orlow I, Lee HW, Cordon-Cardo C, DePinho RA, mwawimwawmThe Ink4a tumor suppressor gene product, p19Arf, interacts with MDM2 and neutralizes MDM2's inhibition of p53, in mwawqCell, vol.mwawu 92, n.mwawy 6, March 1998, pp.mwawc 713-23, mwawgDOI:mwawk10.1016/S0092-8674(00)81400-2, mwawoPMIDmwaws mwaww9529248.

cite-note-pmid9153395-3131. ↑ mwaxeHaupt Y, Maya R, Kazaz A, Oren M, mwaximwaxmMdm2 promotes the rapid degradation of p53, in mwaxqNature, vol.mwaxu 387, n.mwaxy 6630, May 1997, pp.mwaxc 296-9, mwaxgDOI:mwaxk10.1038/387296a0, mwaxoPMIDmwaxs mwaxw9153395.

cite-note-pmid9450543-3232. ↑ mwayeHonda R, Tanaka H, Yasuda H, mwayimwaymOncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53, in mwayqFEBS Letters, vol.mwayu 420, n.mwayy 1, December 1997, pp.mwayc 25-7, mwaygDOI:mwayk10.1016/S0014-5793(97)01480-4, mwayoPMIDmways mwayw9450543.

cite-note-pmid10435614-3333. ↑ mwazeBálint E, Bates S, Vousden KH, mwazimwazmMdm2 binds p73 alpha without targeting degradation, in mwazqOncogene, vol.mwazu 18, n.mwazy 27, July 1999, pp.mwazc 3923-9, mwazgDOI:mwazk10.1038/sj.onc.1202781, mwazoPMIDmwazs mwazw10435614.

cite-note-pmid10207051-3434. ↑ mwa0eZeng X, Chen L, Jost CA, Maya R, Keller D, Wang X, Kaelin WG, Oren M, Chen J, Lu H, mwa0imwa0mMDM2 suppresses p73 function without promoting p73 degradation, in mwa0qMolecular and Cellular Biology, vol.mwa0u 19, n.mwa0y 5, May 1999, pp.mwa0c 3257-66, mwa0gDOI:mwa0k10.1128/mcb.19.5.3257, mwa0oPMCmwa0s mwa0w84120, mwa00PMIDmwa04 mwa0810207051.

cite-note-pmid12068014-3535. ↑ mwa1qJin Y, Zeng SX, Dai MS, Yang XJ, Lu H, mwa1umwa1yMDM2 inhibits PCAF (p300/CREB-binding protein-associated factor)-mediated p53 acetylation, in mwa1cThe Journal of Biological Chemistry, vol.mwa1g 277, n.mwa1k 34, August 2002, pp.mwa1o 30838-43, mwa1sDOI:mwa1w10.1074/jbc.M204078200, mwa10PMIDmwa14 mwa1812068014.

cite-note-pmid18332869-3636. ↑ mwa2qQiu W, Wu J, Walsh EM, Zhang Y, Chen CY, Fujita J, Xiao ZX, mwa2umwa2yRetinoblastoma protein modulates gankyrin-MDM2 in regulation of p53 stability and chemosensitivity in cancer cells, in mwa2cOncogene, vol.mwa2g 27, n.mwa2k 29, July 2008, pp.mwa2o 4034-43, mwa2sDOI:mwa2w10.1038/onc.2008.43, mwa20PMIDmwa24 mwa2818332869.

cite-note-pmid18309296-3737. ↑ mwa3qZhang Z, Zhang R, mwa3umwa3yProteasome activator PA28 gamma regulates p53 by enhancing its MDM2-mediated degradation, in mwa3cThe EMBO Journal, vol.mwa3g 27, n.mwa3k 6, March 2008, pp.mwa3o 852-64, mwa3sDOI:mwa3w10.1038/emboj.2008.25, mwa30PMCmwa34 mwa382265109, mwa4aPMIDmwa4e mwa4i18309296.

cite-note-pmid7935455-3838. ↑ mwa4cMarechal V, Elenbaas B, Piette J, Nicolas JC, Levine AJ, mwa4gmwa4kThe ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes, in mwa4oMolecular and Cellular Biology, vol.mwa4s 14, n.mwa4w 11, November 1994, pp.mwa40 7414-20, mwa44DOI:mwa4810.1128/mcb.14.11.7414, mwa5aPMCmwa5e mwa5i359276, mwa5mPMIDmwa5q mwa5u7935455.

cite-note-pmid15195100-3939. ↑ mwa5oBernardi R, Scaglioni PP, Bergmann S, Horn HF, Vousden KH, Pandolfi PP, mwa5smwa5wPML regulates p53 stability by sequestering Mdm2 to the nucleolus, in mwa50Nature Cell Biology, vol.mwa54 6, n.mwa58 7, July 2004, pp.mwa6a 665-72, mwa6eDOI:mwa6i10.1038/ncb1147, mwa6mPMIDmwa6q mwa6u15195100.

cite-note-pmid14507915-4040. ↑ mwa6oZhu H, Wu L, Maki CG, mwa6smwa6wMDM2 and promyelocytic leukemia antagonize each other through their direct interaction with p53, in mwa60The Journal of Biological Chemistry, vol.mwa64 278, n.mwa68 49, December 2003, pp.mwa7a 49286-92, mwa7eDOI:mwa7i10.1074/jbc.M308302200, mwa7mPMIDmwa7q mwa7u14507915.

cite-note-pmid12915590-4141. ↑ mwa7oKurki S, Latonen L, Laiho M, mwa7smwa7wCellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization, in mwa70Journal of Cell Science, vol.mwa74 116, Pt 19, October 2003, pp.mwa78 3917-25, mwa8aDOI:mwa8e10.1242/jcs.00714, mwa8iPMIDmwa8m mwa8q12915590.

cite-note-pmid12759344-4242. ↑ mwa8kWei X, Yu ZK, Ramalingam A, Grossman SR, Yu JH, Bloch DB, Maki CG, mwa8omwa8sPhysical and functional interactions between PML and MDM2, in mwa8wThe Journal of Biological Chemistry, vol.mwa80 278, n.mwa84 31, August 2003, pp.mwa88 29288-97, mwa9aDOI:mwa9e10.1074/jbc.M212215200, mwa9iPMIDmwa9m mwa9q12759344.

cite-note-pmid18951086-4343. ↑ mwa9kOfir-Rosenfeld Y, Boggs K, Michael D, Kastan MB, Oren M, mwa9omwa9sMdm2 regulates p53 mRNA translation through inhibitory interactions with ribosomal protein L26, in mwa9wMolecular Cell, vol.mwa90 32, n.mwa94 2, October 2008, pp.mwa98 180-9, mwa-aDOI:mwa-e10.1016/j.molcel.2008.08.031, mwa-iPMCmwa-m mwa-q2587494, mwa-uPMIDmwa-y mwa-c18951086.

cite-note-pmid19015526-4444. ↑ mwa-wChang L, Zhou B, Hu S, Guo R, Liu X, Jones SN, Yen Y, mwa-0mwa-4ATM-mediated serine 72 phosphorylation stabilizes ribonucleotide reductase small subunit p53R2 protein against MDM2 to DNA damage, in mwa-8Proceedings of the National Academy of Sciences of the United States of America, vol.mwa-a 105, n.mwa-e 47, November 2008, pp.mwa-i 18519-24, mwa-mDOI:mwa-q10.1073/pnas.0803313105, mwa-uPMCmwa-y mwa-c2587585, mwa-gPMIDmwa-k mwa-o19015526.

cite-note-pmid19098711-4545. ↑ mwa-8Chen D, Zhang J, Li M, Rayburn ER, Wang H, Zhang R, mwbaamwbaeRYBP stabilizes p53 by modulating MDM2, in mwbaiEMBO Reports, vol.mwbam 10, n.mwbaq 2, February 2009, pp.mwbau 166-72, mwbayDOI:mwbac10.1038/embor.2008.231, mwbagPMCmwbak mwbao2637313, mwbasPMIDmwbaw mwba019098711.

cite-note-pmid9388200-4646. ↑ mwbbiLéveillard T, Wasylyk B, mwbbmmwbbqThe MDM2 C-terminal region binds to TAFII250 and is required for MDM2 regulation of the cyclin A promoter, in mwbbuThe Journal of Biological Chemistry, vol.mwbby 272, n.mwbbc 49, December 1997, pp.mwbbg 30651-61, mwbbkDOI:mwbbo10.1074/jbc.272.49.30651, mwbbsPMIDmwbbw mwbb09388200.

cite-note-pmid9271120-4747. ↑ mwbciThut CJ, Goodrich JA, Tjian R, mwbcmmwbcqRepression of p53-mediated transcription by MDM2: a dual mechanism, in mwbcuGenes & Development, vol.mwbcy 11, n.mwbcc 15, August 1997, pp.mwbcg 1974-86, mwbckDOI:mwbco10.1101/gad.11.15.1974, mwbcsPMCmwbcw mwbc0316412, mwbc4PMIDmwbc8 mwbda9271120.

cite-note-pmid18566590-4848. ↑ mwbduSong MS, Song SJ, Kim SY, Oh HJ, Lim DS, mwbdymwbdcThe tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex, in mwbdgThe EMBO Journal, vol.mwbdk 27, n.mwbdo 13, July 2008, pp.mwbds 1863-74, mwbdwDOI:mwbd010.1038/emboj.2008.115, mwbd4PMCmwbd8 mwbea2486425, mwbeePMIDmwbei mwbem18566590.

cite-note-pmid18382127-4949. ↑ mwbegYang W, Dicker DT, Chen J, El-Deiry WS, mwbekmwbeoCARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2, in mwbesCell Cycle, vol.mwbew 7, n.mwbe0 5, March 2008, pp.mwbe4 670-82, mwbe8DOI:mwbfa10.4161/cc.7.5.5701, mwbfePMIDmwbfi mwbfm18382127.

cite-note-5050. ↑ mwbfgLyubomir T. Vassilev, Binh T. Vu e Bradford Graves, mwbfkmwbfoIn vivo activation of the p53 pathway by small-molecule antagonists of MDM2, in mwbfsScience (New York, N.Y.), vol.mwbfw 303, n.mwbf0 5659, 6 febbraio 2004, pp.mwbf4 844-848, mwbf8DOI:mwbga10.1126/science.1092472. mwbgeURL consultato il 16 aprile 2018.

• mwbguApoptosi

• mwbgcARF (proteina)

• mwbgkp53

Altri progetti

• Wikimedia Commons

• Wikimedia Commons contiene immagini o altri file su Mdm2