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231226s2023 xx |||||o 00| ||eng c |
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|a 10.1002/adma.202305164
|2 doi
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|a pubmed24n1199.xml
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|a (DE-627)NLM35974639X
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|a (NLM)37474204
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Li, Fangzhou
|e verfasserin
|4 aut
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| 245 |
1 |
0 |
|a MDM2-Targeting Reassembly Peptide (TRAP) Nanoparticles for p53-Based Cancer Therapy
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1 |
|c 2023
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 10.11.2023
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|a Date Revised 10.11.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2023 Wiley-VCH GmbH.
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|a Gene mutations and functional inhibition are the major obstacles for p53-mediated oncotherapy. For p53-wild-type tumors, the underlying mechanisms of functional inhibition of p53 during oncogenesis are unknown. The results reveal that the expression of the MDM2 inhibitor ARF is inhibited in p53-wild-type tumors, indicating that the restoration of ARF could be a potential oncotherapy strategy for p53-wild-type tumors. Therefore, ARF-mimetic MDM2-targeting reassembly peptide nanoparticles (MtrapNPs) for p53-based tumor therapy is developed. The results elucidated that the MtrapNPs respond to and form a nanofiber structure with MDM2. By trapping MDM2, the MtrapNPs stabilize and activate p53 for the inhibition of p53-wild-type tumors. In most cases, reactivated mutant p53 is inhibited and degraded by MDM2. In the present study, MtrapNPs are used to load and deliver arsenic trioxide, a p53 mutation rescuer, for p53-mutated tumor treatment in both orthotopic and metastatic models, and they exhibit significant therapeutic effects. Therefore, the study provides evidence supporting a link between decreased ARF expression and tumor development in patients with p53-wild-type tumors. Thus, the MDM2-trap strategy, which addresses both the inhibition and mutations of p53, is an efficient strategy for the treatment of p53-mutated tumors
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4 |
|a Journal Article
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4 |
|a ARF
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| 650 |
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4 |
|a MDM2 trap
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| 650 |
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|a arsenic trioxide
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| 650 |
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4 |
|a cancer therapy
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| 650 |
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4 |
|a mutant p53
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| 650 |
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4 |
|a peptides
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4 |
|a wild-type p53
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| 650 |
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|a Tumor Suppressor Protein p53
|2 NLM
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| 650 |
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|a Nuclear Proteins
|2 NLM
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| 650 |
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|a Tumor Suppressor Protein p14ARF
|2 NLM
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| 650 |
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7 |
|a Proto-Oncogene Proteins c-mdm2
|2 NLM
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| 650 |
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7 |
|a EC 2.3.2.27
|2 NLM
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| 650 |
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7 |
|a Peptides
|2 NLM
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| 650 |
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7 |
|a MDM2 protein, human
|2 NLM
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| 650 |
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7 |
|a EC 2.3.2.27
|2 NLM
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| 700 |
1 |
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|a Chen, Delin
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Sun, Qianqian
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Wu, Jiale
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Gan, Yaling
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Leong, Kam W
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Liang, Xing-Jie
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Advanced materials (Deerfield Beach, Fla.)
|d 1998
|g 35(2023), 45 vom: 19. Nov., Seite e2305164
|w (DE-627)NLM098206397
|x 1521-4095
|7 nnns
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| 773 |
1 |
8 |
|g volume:35
|g year:2023
|g number:45
|g day:19
|g month:11
|g pages:e2305164
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| 856 |
4 |
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|u http://dx.doi.org/10.1002/adma.202305164
|3 Volltext
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