Relevant bibliographies by topics / Mutants de p53

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Academic literature on the topic 'Mutants de p53'

Author: Grafiati
Published: 4 June 2021
Last updated: 12 February 2022

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Journal articles on the topic "Mutants de p53"

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Wang, GuoZhen, and Alan R. Fersht. "Propagation of aggregated p53: Cross-reaction and coaggregation vs. seeding." Proceedings of the National Academy of Sciences 112, no. 8 (February 9, 2015): 2443–48. http://dx.doi.org/10.1073/pnas.1500262112.

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Destabilized mutant p53s coaggregate with WT p53, p63, and p73 in cancer cell lines. We found that stoichiometric amounts of aggregation-prone mutants induced only small amounts of WT p53 to coaggregate, and preformed aggregates did not significantly seed the aggregation of bulk protein. Similarly, p53 mutants trapped only small amounts of p63 and p73 into their p53 aggregates. Tetrameric full-length protein aggregated at similar rates and kinetics to isolated core domains, but there was some induced aggregation of WT by mutants in hetero-tetramers. p53 aggregation thus differs from the usual formation of amyloid fibril or prion aggregates where tiny amounts of preformed aggregate rapidly seed further aggregation. The proposed aggregation mechanism of p53 of rate-determining sequential unfolding and combination of two molecules accounts for the difference. A molecule of fast-unfolding mutant preferentially reacts with another molecule of mutant and only occasionally traps a slower unfolding WT molecule. The mutant population rapidly self-aggregates before much WT protein is depleted. Subsequently, WT protein self-aggregates at its normal rate. However, the continual production of mutant p53 in a cancer cell would gradually trap more and more WT and other proteins, accounting for the observations of coaggregates in vivo. The mechanism corresponds more to trapping by cross-reaction and coaggregation rather than classical seeding and growth.
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Raycroft, L., J. R. Schmidt, K. Yoas, M. M. Hao, and G. Lozano. "Analysis of p53 mutants for transcriptional activity." Molecular and Cellular Biology 11, no. 12 (December 1991): 6067–74. http://dx.doi.org/10.1128/mcb.11.12.6067.

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The wild-type p53 protein functions to suppress transformation, but numerous mutant p53 proteins are transformation competent. To examine the role of p53 as a transcription factor, we made fusion proteins containing human or mouse p53 sequences fused to the DNA binding domain of a known transcription factor, GAL4. Human and mouse wild-type p53/GAL4 specifically transactivated expression of a chloramphenicol acetyltransferase reporter in HeLa, CHO, and NIH 3T3 cells. Several mutant p53 proteins, including a mouse p53 mutant which is temperature sensitive for suppression, were also analyzed. A p53/GAL4 fusion protein with this mutation was also transcriptionally active only at the permissive temperature. Another mutant p53/GAL4 fusion protein analyzed mimics the mutation inherited in Li-Fraumeni patients. This fusion protein was as active as wild-type p53/GAL4 in our assay. Two human p53 mutants that arose from alterations of the p53 gene in colorectal carcinomas were 30- to 40-fold less effective at activating transcription than wild-type p53/GAL4 fusion proteins. Thus, functional wild-type p53/GAL4 fusion proteins activate transcription, while several transformation competent mutants do so poorly or not at all. Only one mutant p53/GAL4 fusion protein remained transcriptionally active.
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Raycroft, L., J. R. Schmidt, K. Yoas, M. M. Hao, and G. Lozano. "Analysis of p53 mutants for transcriptional activity." Molecular and Cellular Biology 11, no. 12 (December 1991): 6067–74. http://dx.doi.org/10.1128/mcb.11.12.6067-6074.1991.

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The wild-type p53 protein functions to suppress transformation, but numerous mutant p53 proteins are transformation competent. To examine the role of p53 as a transcription factor, we made fusion proteins containing human or mouse p53 sequences fused to the DNA binding domain of a known transcription factor, GAL4. Human and mouse wild-type p53/GAL4 specifically transactivated expression of a chloramphenicol acetyltransferase reporter in HeLa, CHO, and NIH 3T3 cells. Several mutant p53 proteins, including a mouse p53 mutant which is temperature sensitive for suppression, were also analyzed. A p53/GAL4 fusion protein with this mutation was also transcriptionally active only at the permissive temperature. Another mutant p53/GAL4 fusion protein analyzed mimics the mutation inherited in Li-Fraumeni patients. This fusion protein was as active as wild-type p53/GAL4 in our assay. Two human p53 mutants that arose from alterations of the p53 gene in colorectal carcinomas were 30- to 40-fold less effective at activating transcription than wild-type p53/GAL4 fusion proteins. Thus, functional wild-type p53/GAL4 fusion proteins activate transcription, while several transformation competent mutants do so poorly or not at all. Only one mutant p53/GAL4 fusion protein remained transcriptionally active.
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Scian, Mariano J., Katherine E. R. Stagliano, Michelle A. E. Anderson, Sajida Hassan, Melissa Bowman, Mike F. Miles, Swati Palit Deb, and Sumitra Deb. "Tumor-Derived p53 Mutants Induce NF-κB2 Gene Expression." Molecular and Cellular Biology 25, no. 22 (November 15, 2005): 10097–110. http://dx.doi.org/10.1128/mcb.25.22.10097-10110.2005.

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ABSTRACT Overexpression of mutant p53 is a common theme in tumors, suggesting a selective pressure for p53 mutation in cancer development and progression. To determine how mutant p53 expression may lead to survival advantage in human cancer cells, we generated stable cell lines expressing p53 mutants p53-R175H, -R273H, and -D281G by use of p53-null human H1299 (lung carcinoma) cells. Compared to vector-transfected cells, H1299 cells expressing mutant p53 showed a survival advantage when treated with etoposide, a common chemotherapeutic agent; however, cells expressing the transactivation-deficient triple mutant p53-D281G (L22Q/W23S) had significantly lower resistance to etoposide. Gene expression profiling of cells expressing transcriptionally active mutant p53 proteins revealed the striking pattern that all three p53 mutants induced expression of approximately 100 genes involved in cell growth, survival, and adhesion. The gene NF-κB2 is a prominent member of this group, whose overexpression in H1299 cells also leads to chemoresistance. Treatment of H1299 cells expressing p53-R175H with small interfering RNA specific for NF-κB2 made these cells more sensitive to etoposide. We have also observed activation of the NF-κB2 pathway in mutant p53-expressing cells. Thus, one possible pathway through which mutants of p53 may induce loss of drug sensitivity is via the NF-κB2 pathway.
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Ohiro, Yoichi, Anny Usheva, Shinichiro Kobayashi, Shannon L. Duffy, Regan Nantz, David Gius, and Nobuo Horikoshi. "Inhibition of Stress-Inducible Kinase Pathways by Tumorigenic Mutant p53." Molecular and Cellular Biology 23, no. 1 (January 1, 2003): 322–34. http://dx.doi.org/10.1128/mcb.23.1.322-334.2003.

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ABSTRACT More than 50% of human cancers contain p53 gene mutations and as a result accumulate altered forms of the full-length p53 protein. Although certain tumor types expressing mutant p53 protein have a poor prognostic process, the precise role of mutant p53 protein in highly malignant tumor cells is not well defined. Some p53 mutants, but not wild-type p53, are shown here to interact with Daxx, a Fas-binding protein that activates stress-inducible kinase pathways. Interaction of Daxx with p53 is highly dependent upon the specific mutation of p53. Tumorigenic mutants of p53 bind to Daxx and inhibit Daxx-dependent activation of the apoptosis signal-regulating kinase 1 stress-inducible kinases and Jun NH2-terminal kinase. Mutant p53 forms complexes with Daxx in cells, and consequently, mutant p53 is able to rescue cells from Daxx-dependent inhibition of proliferation. Thus, the accumulation of mutant p53 in tumor cells may contribute to tumorigenesis by inhibiting stress-inducible kinase pathways.
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Hall, Callum, and Patricia A. J. Muller. "The Diverse Functions of Mutant 53, Its Family Members and Isoforms in Cancer." International Journal of Molecular Sciences 20, no. 24 (December 7, 2019): 6188. http://dx.doi.org/10.3390/ijms20246188.

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The p53 family of proteins has grown substantially over the last 40 years. It started with p53, then p63, p73, isoforms and mutants of these proteins. The function of p53 as a tumour suppressor has been thoroughly investigated, but the functions of all isoforms and mutants and the interplay between them are still poorly understood. Mutant p53 proteins lose p53 function, display dominant-negative (DN) activity and display gain-of-function (GOF) to varying degrees. GOF was originally attributed to mutant p53′s inhibitory function over the p53 family members p63 and p73. It has become apparent that this is not the only way in which mutant p53 operates as a large number of transcription factors that are not related to p53 are activated on mutant p53 binding. This raises the question to what extent mutant p53 binding to p63 and p73 plays a role in mutant p53 GOF. In this review, we discuss the literature around the interaction between mutant p53 and family members, including other binding partners, the functional consequences and potential therapeutics.
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Rockwell, Nathan, Max Staller, Maria Cannella, Barak Cohen, and Joshua Rubin. "GENE-59. NOT ALL p53 MUTATIONS ARE CREATED EQUAL: A MURINE ASTROCYTE MODEL FOR HIGH-THROUGHPUT FUNCTIONAL ASSESSMENT OF p53 MISSENSE MUTATIONS." Neuro-Oncology 21, Supplement_6 (November 2019): vi110. http://dx.doi.org/10.1093/neuonc/noz175.461.

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Abstract The tumor suppressor TP53 (p53) is the most commonly mutated gene in cancer and among the most frequently mutated genes in glioblastoma (GBM). The majority of p53 mutations in GBM are missense mutations in the DNA binding domain that lead to the production of full length mutant p53 protein. In addition to the complete loss of tumor suppressor function, these mutations have gain-of-function (GOF) properties either through attenuation of wild-type function or neomorphic functions. The variability in GOF mutations results in heterogeneity in cancer phenotypes between mutants that remain poorly understood. Here, we developed a murine astrocyte model to functionally assess a library of p53 mutants in parallel. Primary astrocytes were isolated from postnatal day one pups possessing a single copy of wild-type p53 flanked by loxP sites (TRP53f/-). We then built a library of 17 individual alleles of recurring mutations in GBM with flanking loxP sites. When co-transfected into the mouse astrocytes with a plasmid expressing Cre recombinase, the endogenous WT p53 was excised and replaced with a single copy of the mutant allele. In this way, all astrocytes expressed a single copy of mutant p53 from the endogenous p53 locus. As the mutant p53 cells expanded, aliquots of cells were extracted for targeted genomic sequencing of the p53 allele. Comparing the allelic frequencies of each mutant overtime revealed a wide distribution of growth rates between mutants. To validate the screen results, wildtype astrocytes were transduced with mutant p53-IRES-eGFP retrovirus to overexpress one of three mutations with divergent growth phenotypes. As observed in the initial screen, equivalent overexpression of the different p53 mutants was sufficient to induce significant differences in growth phenotype, with astrocytes expressing the Y217C growing the fastest, R172H second, and Y202C growing the slowest. Ongoing studies are evaluating mutation-specific p53 binding partners and transcriptional outputs.
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Shaulian, E., A. Zauberman, D. Ginsberg, and M. Oren. "Identification of a minimal transforming domain of p53: negative dominance through abrogation of sequence-specific DNA binding." Molecular and Cellular Biology 12, no. 12 (December 1992): 5581–92. http://dx.doi.org/10.1128/mcb.12.12.5581.

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Mutations in the p53 gene are most frequent in cancer. Many p53 mutants possess transforming activity in vitro. In cells transformed by such mutants, the mutant protein is oligomerized with endogenous cell p53. To determine the relevance of oligomerization for transformation, miniproteins containing C-terminal portions of p53 were generated. These miniproteins, although carrying no point mutation, transformed at least as efficiently as full-length mutant p53. Transforming activity was coupled with the ability to oligomerize with wild-type p53, as well as with the ability to abrogate sequence-specific DNA binding by coexpressed wild-type p53. These findings suggest that p53-mediated transformation may operate through a dominant negative mechanism, involving the generation of DNA binding-incompetent oligomers.
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Shaulian, E., A. Zauberman, D. Ginsberg, and M. Oren. "Identification of a minimal transforming domain of p53: negative dominance through abrogation of sequence-specific DNA binding." Molecular and Cellular Biology 12, no. 12 (December 1992): 5581–92. http://dx.doi.org/10.1128/mcb.12.12.5581-5592.1992.

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Mutations in the p53 gene are most frequent in cancer. Many p53 mutants possess transforming activity in vitro. In cells transformed by such mutants, the mutant protein is oligomerized with endogenous cell p53. To determine the relevance of oligomerization for transformation, miniproteins containing C-terminal portions of p53 were generated. These miniproteins, although carrying no point mutation, transformed at least as efficiently as full-length mutant p53. Transforming activity was coupled with the ability to oligomerize with wild-type p53, as well as with the ability to abrogate sequence-specific DNA binding by coexpressed wild-type p53. These findings suggest that p53-mediated transformation may operate through a dominant negative mechanism, involving the generation of DNA binding-incompetent oligomers.
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Muller, Patricia A. J., Karen H. Vousden, and Jim C. Norman. "p53 and its mutants in tumor cell migration and invasion." Journal of Cell Biology 192, no. 2 (January 24, 2011): 209–18. http://dx.doi.org/10.1083/jcb.201009059.

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In about half of all human cancers, the tumor suppressor p53 protein is either lost or mutated, frequently resulting in the expression of a transcriptionally inactive mutant p53 protein. Loss of p53 function is well known to influence cell cycle checkpoint controls and apoptosis. But it is now clear that p53 regulates other key stages of metastatic progression, such as cell migration and invasion. Moreover, recent data suggests that expression of mutant p53 is not the equivalent of p53 loss, and that mutant p53s can acquire new functions to drive cell migration, invasion, and metastasis, in part by interfering with p63 function.
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Dissertations / Theses on the topic "Mutants de p53"

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Ang, H. C. "Biophysical characterisation and rescue of p53 cancer mutants." Thesis, University of Cambridge, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.596120.

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The aim of this thesis was to use biophysical methods to characterise the stabilities and DNA binding properties of monomeric and tetrameric p53 cancer mutants, and to study various approaches aimed at rescuing structural mutants of p53. A detailed study of the destabilising effects of p53 mutations was performed using differential scanning calorimetry and urea denaturation, while equilibrium binding of p53 mutants to a specific promoter sequence, gadd45, was studied using fluorescence anisotropy and analytical ultracentrifugation. This thesis will also discuss how p53 structural mutants may be rescued by suppressor mutations that either increase the overall protein stability of compensate specifically for oncogenically induced loss of interactions. Stability and DNA-binding measurements showed that the destabilising effects of mutations H168R and R249S were not additive, and that these mutations in combination restored DNA binding. Similar biophysical techniques were used in analysing a series of p53 core domain mutants in which the residue Ser-116 in the middle of flexible loop L1 was mutated. One mutant, S1116C, was found to be more stable than previously predicted. The crystal structure showed how the mutation had led to formation of a new hydrogen-bonding network. Altogether, these protein-engineering studies provided useful insights into possible ways to rescue p53 function. A small set of compounds was selected based on the nature of proteins and peptides that were known to interact with p53. NMR spectroscopy was used to screen for compounds binding to the protein target and to probe for atomic detail of binding interactions. It was shown that 15N-1H HSQC could be used for screening and deconvoluting mixtures of compounds, in the presence of 5% v/v d6-DMSO, at relatively high throughput.
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Estevan, Barber Anna. "Influence of genotoxic drug-induced post-translational modifications on mutant p53 stability and oncogenic activities." Thesis, University of Dundee, 2018. https://discovery.dundee.ac.uk/en/studentTheses/1ec28205-8590-4044-91b0-0c5f68206c2c.

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The tumour suppressor p53 is often disrupted by missense mutations that can result in p53 protein accumulation and acquisition of novel oncogenic activities. Various studies have demonstrated that DNA-damaging drugs currently used in the clinic aimed at activating wild type p53, can also stabilise and activate mutant p53 oncogenic functions and thereby paradoxically enhance tumour progression, resulting in poor response to the treatment. In this study we aimed to investigate whether, like in wt p53, post-translational modifications (PTMs) drive such drug-induced mutant p53 accumulation and activation. For this purpose, we generated plasmids expressing non-phosphorylatable and phospho-mimic versions of R175H mutant p53 and tested them in different cell line models. We demonstrated that in response to DNA damage mutant p53 is accumulated and phosphorylated and these phenomena appeared to be mediated by ATM and ATR kinases. DNA-damage induced acetylation was also observed and occurred in a S15 phosphorylation-dependent manner. This suggested a role of the HAT p300, which is recruited by phosphorylated S15. Of note, other works have shown that p300 is required to trigger some oncogenic functions of mutant p53. We then aimed at developing systems to explore mutant p53 functions and their dependence on PTMs. Although we showed that cell growth is compromised upon endogenous mutant p53 depletion, exogenous expression of mutant p53 or its phosphorylation-site forms did not result in a successful rescue in our experimental conditions, thus we were unable to use this strategy to test the effect of PTMs. Ectopic expression of R175H mutant p53 or its phosphorylayion-site versions did not interfere with the growth rate and response to chemotherapy of the p53-null cell line H1299. We also found that mutant p53 phosphorylation does not affect subcellular localisation of mutant p53 and mutant p53-mediated inhibition of p63. Interestingly, ectopically expressed mutant p53 enhanced cell migration in H1299 cells. Notably, our results suggested an apparent threshold effect of mutant p53 levels required to induce migration. Due to the difficulty of obtaining cell lines expressing similar levels of the different phosphorylation-site mutants, the determination of the role of phosphorylation in mutant p53-induced migration was not conclusive. Remarkably, we found that, while S15 and S20 phosphorylation decreased MDM2-dependent degradation, only phosphorylated S20 interfered with CHIP-induced turnover in H1299 cells. Overall our data suggest that, despite exhibiting opposite biological effects, mutant and wt p53 can share upstream regulatory mechanisms and thus present phosphorylation as a promising target to prevent mutant p53 stabilisation and activation and improve response to therapy. Our results also highlight the challenge of developing a good system for determining the effects of the mutant p53 protein and its regulation by PTMs.
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Souza, Felipe da Costa. "Geração e caracterização de linhagens isogênicas portadoras de mutantes de p53: modelo para avaliar a estratégia de reparação dos genes p53 e p16 INK4A na presença dos mutantes p53R175H e p53R248Q." Universidade de São Paulo, 2012. http://www.teses.usp.br/teses/disponiveis/42/42134/tde-26072012-102241/.

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A destruição funcional das vias de controle do ciclo celular constituem um evento comuns em todos os tumores humanos. Muitos estudos associam mutações em p53 com mau prognostico no tratamento do câncer. Nesse trabalho, visamos a geração e caracterização de linhagens isogênicas portando diferentes mutantes de p53 como modelo de estudo para remediação simultânea de p53 e p16 na presença de mutantes hotspots específicos. Os mutantes R175H e R248Q não geraram alterações na cinética de proliferação da linhagem H358, mas levaram a um aumento de 27,5% na eficiência de plaqueamento e, no caso de R248Q, ao dobro de eficiência na formação de colônias em suspensão. Os resultados do tratamento das linhagens isogênicas com adenovírus Adp16 e Adp53 mostraram que os mutantes não interferiram no parada do ciclo celular em G1 induzida por p16.
Alterations of the cell cycle pathway are a common event in all human tumors. Several studies have shown a correlation between hotspot mutations and an unfavorable profile for cancer therapies. Hence, this study aims the generation and characterization of isogenic cell lines, harboring p53 mutants, as model to investigate the replacement of p53 and p16 genes on these mutant H358 cell lines. Our data identified that neither p53R175H nor p53R248Q mutants accelerated cell cycle progression. However, both leads to a 27,5% increased plate efficiency while R248Q leads to a two-fold increases in the number of colonies formed in soft agar. Our data also showed that the mutants did not affect the efficiency of p16 replacement.
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Roger, Lauréline. "Etude des mécanismes de la régulation de l'EMT par le suppresseur de tumeur p53 dans un modèle de cellules de carcinome du colon." Montpellier 2, 2007. http://www.theses.fr/2007MON20182.

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Le suppresseur de tumeur p53 est un facteur de transcription impliqué dans la progression du cycle cellulaire et dans l'apoptose. Outre ses fonctions majeures, p53 régule également la migration et l'adhérence cellulaire qui sont deux évènements impliqués dans le processus métastatique. L'évolution maligne d'un carcinome peut aussi impliquer la répression transcriptionnelle de CDH1, qui code pour la E-cadhérine, protéine constitutive des jonctions adhérentes. Nous avons recherché si et comment p53 régule certains évènements moléculaires qui contrôle le processus métastatique. Nous montrons que la forme sauvage de p53 réprime directement la transcription de CDH1 dans des lignées cellulaires humaines de carcinome du colon (HCT116). Cette répression est associée à une expression de novo de la vimentine et à l'acquisition d'une morphologie plus fibroblastique. L'une des cibles transcriptionnelle majeure de p53, p21WAF1 court-circuite l'effet répresseur de p53 sur la transcription de CDH1. Trois mutants dominant-négatifs de p53 (R273H, R175H et V143A) répriment également la transcription de CDH1. De plus, l'expression stable du mutant V143A dans les cellules HCT116 p53-/- mime partiellement le phénotype observé suite l'accumulation aberrante de p53. De façon surprenante, ce phénotype mésenchymateux n'est pas associé à une augmentation des propriétés invasives. Ce travail implique p53 dans la régulation d'évènements moléculaires qui peuvent conduire à l'acquisition d'un phénotype mésenchymateux
The p53 tumour suppressor gene encodes a transcriptional regulator that monitor proliferation signals to prevent cells from uncontrolled growth. However, p53 has also alternative functions. Notably, loss of p53 favours cell migration and invasion, processes involved in tumour metastasis. Given that epithelial to mesenchymal transition (EMT) also increases cell migration by altering the cell phenotype and morphology, we hypothesized that p53 controls molecular alterations that mediate EMT during cancer progression. Analysis of E-cadherin promoter activity and chromatin immunoprecipitation identified p53 as a direct transcriptional repressor of E-cadherin in human colon carcinoma cells, HCT116. Aberrant levels of p53 disrupted E-Cadherin-based cell-cell contacts and induced a more mesenchymal phenotype with downregulation of E-Cadherin and induction of the mesenchymal gene, vimentin. In addition, p21Waf-1 impeded p53 transcriptional repression and restored in part cell to cell adhesion. Furthermore, HCT116p53-/- cells overexpressing dominant-negative form of p53 also displayed the EMT-like phenotype. Neither p53 nor mutant p53–mediated shift toward mesenchymal morphology led to an increase of cell invasiveness. This work and our previous finding of mutant p53-mediated cell invasion identify p53 as a novel regulator of EMT and offer new perspectives in the comprehension of metastasis
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Li, Lianjie. "Mutations in tumor suppressor p53 and deregulation of cellular metabolism." Doctoral thesis, Humboldt-Universität zu Berlin, 2018. http://dx.doi.org/10.18452/19513.

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Mutation des p53 Gen ist die häufigste genetische Veränderung in allen humanen Tumoren. Weit verbreitete p53 misssense-Mutationen heben die Tumor suppressive Funktion auf und führen zu gain-of-function Eigenschaften, die Tumorproliferation, Chemoresistenz, Angiogenese, Migration, Invasion und Metastasen fördern. In dieser Arbeit haben ich für drei solche Hotspot-Mutationen, p53R245Q, p53R246S und p53R270H, eine höhere Sensitivität gegenüber Behandlung mit Piperlongumine in p53-defizienten MEFs und Eµ-myc Lymphomzellen im Vergleich zur Kontrolle und den anderen drei Hotspot-Mutationen, p53R172H, p53G242S und p53R279Q, gefunden. Nachfolgend, haben ich entdeckt, dass Piperlongumine-induzierter Zelltod durch ROS Akkumulation über die Aktivierung von p38 und JNK, vermittelt wurde. Das Antioxidans N-acetyl-L-cysteine (NAC) oder p38/JNK Inhibitoren konnten vollständig oder teilweise Piperlongumine-induzierten Zelltod unterdrücken. Nach Behandlung mit Piperlongumine, haben die p53R245Q, p53R246S und p53R270H-Mutanten die Aktivierung von p21 inhibiert und so die Aktivierung und Funktion von NRF2, durch Piperlongumine induziert, blockiert, dass zu dem massiven Zelltod in Zellen mit diesen Mutationen beiträgt. Auf ähnliche Weise, verursachte der klinisch verwendete Inhibitor von Crm1, KPT-330, schweren Zelltod in p53-/- MEFs mit den p53R245Q, p53R246S und p53R270H-Mutationen. Folglich könnte Crm1 als potenzielles Target für Lymphome mit p53R245Q, p53R246S und p53R270H-Mutationen berücksichtigt werden. Zusammenfassend bekräftigen die Daten in dieser Arbeit das Phänomen, dass oxidativer Stress oder Crm1 Inhibitoren effektiv Zellen mit p53R245Q, p53R246S und p53R270H-Mutationen eliminieren können, mit niedriger Toxizität für Kontrollzellen. Demzufolge, könnten oxidativer Stress Signalwege oder Crm1 als potenzielle Angriffsziele für Lymphome mit p53R245Q, p53R246S und p53R270H-Mutationen dienen.
Mutation of the p53 gene is the most common genetic alteration among all human cancers. Prevalent p53 missense mutations abrogate its tumor suppressive function and lead to gain-of-function properties that promote cancer cell proliferation, chemoresistance, angiogenesis, migration, invasion, and metastasis. This doctoral thesis aims to identify the metabolic vulnerabilities of six p53 hotspot mutants in lymphomas. In this work, three hotspot mutants, p53R245Q, p53R246S and p53R270H, were more sensitive to piperlongumine treatment in p53-deficient MEFs and Eμ-myc lymphoma cells than the empty control and the other three hotspot mutants, p53R172H, p53G242S and p53R279Q. Thereafter, I found piperlongumine-induced cell death was mediated by ROS accumulation via the activation of p38 and JNK. Antioxidant N-acetyl-L-cysteine (NAC) or p38/JNK inhibitors could completely or partially suppress piperlongumine-induced cell death. Upon piperlongumine treatment, p53R245Q, p53R246S and p53R270H-mutant inhibited piperlongumine-induced activation of p21 and consequently attenuated the activation and function of NRF2 induced by piperlongumine, contributing to the massive cell death in cells harboring these mutants. Similarly, KPT-330, a clinical inhibitor of Crm1, also caused severe cell death in p53-/- MEFs harboring p53R245Q, p53R246S and p53R270H-mutant. This implied that Crm1 could be also considered as a potential target for lymphomas harboring p53R245Q, p53R246S and p53R270H-mutant. Taken together, data presented in this work underscore the phenomenon that exogenous oxidative stress or Crm1 inhibitor is effective in eliminating cells harboring p53R245Q, p53R246S and p53R270H-mutant with low toxicity to cells harboring the empty control, suggesting oxidative stress pathways or Crm1 as potential targets in lymphomas with p53R245Q, p53R246S and p53R270H-mutant.
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Toppaldoddi, Katte Rao. "Role of rare calreticulin mutants and of the endoplasmic reticulum stress in the pathogenesis of myeloproliferative neoplasms." Thesis, Sorbonne Paris Cité, 2017. http://www.theses.fr/2017USPCC322/document.

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Après la découverte des mutations de la calréticuline dans les néoplasmes classiques myéloproliferatifs négatifs pour le Ph1, les travaux se sont focalisés sur les deux mutations les plus fréquentes, c'est-à-dire la calréticuline del52 et l’ins5, mais il existe environ 20% de mutants rares de la calréticuline (une cinquantaine), qui ont été classés en type-1 « like » et type-2 « like », classification basée sur leur structure. Cependant il reste à déterminer si cette classification est pertinente du point de vue fonctionnel, ce qui pourrait avoir des conséquences pour la prise en charge des patients et leur traitement. Ici, nous démontrons que deux mutants rares de type-1 (del34 et del46) et un de type-2 (del19) se comportent de manière similaire aux deux mutations fondatrices de cette classification, del52 et ins5, respectivement. Ces résultats ont été validés par des expériences in vivo chez la souris. Tous les mutants de la calréticuline (del19, del34 et del46) nécessitent absolument le récepteur de la thrombopoïétine, appelé MPL, pour induire une transformation cellulaire en provoquant une activation indépendante de la thrombopoïétine de la voie MPL / JAK2-STAT, comme les mutants del52 et ins5. Dans les expériences de transplantation de moelle osseuse de souris, les mutants rares de type-1 sont associés à une progression fréquente de la maladie d’un tableau proche d’une thrombocytémie essentielle à une myélofibrose, tandis que le mutant rare de type 2 est associé à une légère thrombocytose. Du point de vue hématopoïétique, les mutants rares de type-1 provoquent une amplification au niveau des cellules souches hématopoïétiques donc à un stade précoce tandis que les mutants rares de type-2 provoquent une amplification tardive de la mégacaryopoïèse. Grâce à une modélisation protéique basée sur l'homologie des mutants de calréticuline, nous avons identifié des domaines oncogènes qui seraient potentiellement responsables de l'interaction pathologique de la calréticuline et de MPL pour conduire à une activation indépendante de la thrombopoïétine. Maintenant, ces résultats in silico doivent être absolument validés par des études structure fonction. Enfin, nous avons modélisé un nouveau mécanisme de signalisation dans la leucémie myéloïde chronique comprenant IRE-1alpha, un bras de la voie de réponse des protéines mal repliées (UPR), qui pourrait être responsable de la perte de la fonction de la p53 pendant la progression de la leucémie myéloïde chronique vers une leucémie aiguë. Un tel mécanisme pourrait être impliqué dans les autres MPN
After the discovery of calreticulin mutations in classical Ph1- Myeloproliferative Neoplasms, extensive investigation is underway on the two most frequent mutations, i.e., del52 and ins5, but it remains that the rare calreticulin mutants, which include both type-1 like and type-2 like require a similar investigation for ascertaining whether the classification of type-1 and type-2 has a functional relevance as well as for therapeutic intervention and patient management. Here we demonstrate that type-1 like (del34 and del46) and type-2 like (del19) mutants behave similarly as del52 and ins5 mutants, respectively. Moreover, we validate our findings with in vivo experiments. All the calreticulin mutants (del19, del34 and del46) absolutely require the thrombopoietin receptor, MPL, to induce cell transformation by causing ligand independent activation of the MPL/JAK2-STAT pathway. In mouse bone marrow transplantation experiments, type-1 like mutants are associated with frequent progression from an essential thrombocythemia-like phenotype to myelofibrosis whereas type-2 like mutant is associated with mild thrombocytosis. Type-1 like mutants cause clonal amplification of early hematopoetic stem cells whereas the type-2 like mutant causes late platelet amplification. Further, by homology based protein modeling of calreticulin mutants, we have identified possible oncogenic domains responsible for pathologic interaction of CALR and MPL leading to ligand independent activation of MPL. Now they must be validated by structural-functional studies Finally, we have modelled a novel signaling mechanism in chronic myeloid leukemia comprising of IRE-1alpha, an unfolded protein response (UPR) pathway arm, which may be responsible for loss of the WT p53 function during leukemic development and progression. Such a mechanism may be involved in the other MPNs
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Osadchuk, Olha. "Optimalizace izolace mutantního proteinu p53 a jeho DNA vazebné vlastnosti." Master's thesis, Vysoké učení technické v Brně. Fakulta chemická, 2020. http://www.nusl.cz/ntk/nusl-413550.

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Protein p53 je jednou z nejdůležitějších molekul v lidském těle. P53 reguluje celou řadu procesů v buňce, jako je například oprava DNA, buněčný cyklus nebo indukce apoptózy. Protein p53 je známý i jako „strážce genomu“. DNA vazebné schopnosti proteinu p53 jsou důležité pro normální vývoj a růst buňky. Mutace genu pro p53 mohou vést ke ztrátě jeho DNA vazebných vlastností a funkce nádorového supresoru, což muže způsobit rozvoj rakoviny. Teoretická část této diplomové práce je zaměřena na popis vlastností, funkce a mechanismus aktivace proteinu p53 a popis lokálních sekundárních struktur DNA. Hlavním cílem experimentální části byla produkce čtyř mutantních forem proteinů p53 a wild-type p53 proteinu a studium jejich vazebných vlastnosti s různými lokálními sekundárními strukturami DNA. Pomoci Gateway klonovacího systému byly připraveny čtyři expresní vektory, které byly použity pro produkci proteinů v bakteriálním expresním systému. Celkem byly úspěšně připraveny čtyři mutantní formy a wild-type p53 protein. Jejich vazebné vlastnosti byly studovány gelovou retardační analýzu. Výsledky naznačují různé DNA-vazebné vlastnosti wild-type p53 a studovaných mutantních forem tohoto proteinu. Všechny mutantní proteiny ztratily schopnost sekvenčně specificky vázat DNA, zatímco nespecifická interakce s DNA byla pozorována u tří ze čtyř mutantních forem. Jeden ze studovaných mutantních proteinů se vázal jenom na superhelikální formu DNA.
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Pellerano, Morgan. "Développement d'un biosenseur fluorescent d'un mutant de p53 sujet à l'agrégation dans les cancers." Thesis, Montpellier, 2019. http://www.theses.fr/2019MONTT053.

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P53 est un suppresseur de tumeur qui joue un rôle clé dans la régulation de la transcription, la réparation de l'ADN, l'instabilité génétique, la sénescence, la régulation du cycle cellulaire et l'apoptose. Cette protéine, normalement nucléaire, se lie à l’ADN et régule la transactivation. Cependant, elle est souvent mutée dans les tumeurs humaines, entraînant une inactivation fonctionnelle et une prédisposition au cancer. Les mutants p53 se peuvent-être de deux catégories des mutants de « contact » ou « conformationnel ». Ces derniers entraînant des changements de conformation pouvant induire une agrégation de la protéine de type amyloïde. Des études récentes ont montré que l’agrégation de p53 pouvait être efficacement reversée, rétablissant ainsi la fonction de p53 chez la souris. Les approches de diagnostic actuelles basées sur le séquençage génétique permettent d'identifier le statut mutationnel de p53, mais ne renseignent pas sur son statut conformationnel. Le but de ma thèse est de développer un biosenseur peptidique fluorescent qui reconnaît et rend compte des mutants conformationnels de p53 exprimés dans des cancers humains. Nous avons caractérisé et optimisé la réponse de ce biosenseur par conjugaison avec différentes sondes sensibles à l'environnement. Nous avons également étudié leur capacité à signaler de manière sélective le mutant R248Q de p53 in vitro à l’aide de formes recombinantes de protéines p53 de type sauvage et mutantes, ainsi que de lysats de lignées cellulaires de cancer du poumon exprimant p53 de type sauvage (A549), le mutant R248Q (PC9) ou p53 - / - (H1299). Après avoir établi les conditions de travail optimales et les limites du biocapteur in vitro, nous avons appliqué ce biosenseur à l’imagerie de cellules vivantes par microscopie à fluorescence, après avoir procédé à l’internalisation cellulaire facilitée par un peptide vecteur (ou CPP : Cell Penetrating Peptide) afin d’établir son potentiel pour de futures applications de diagnostic et thérapeutiques. Nous avons de plus vérifié la réponse du biosenseur à l'expression induite de mutants conformationnels de p53, ainsi qu'à sa régulation négative, à la fois in vitro et dans des cellules vivantes
P53 is a tumour suppressor that plays a key role in transcriptional regulation, DNA repair, genetic instability, senescence, cell cycle regulation and apoptosis. This normally nuclear protein tetramerizes to bind DNA and regulate transactivation. However it is often mutated in human tumours, leading to functional inactivation and predisposing to cancer. p53 mutants are distinguished as “contact” or “structural”, the latter resulting in conformational changes which may induce amyloid-like protein aggregation. Recent studies have shown p53 aggregation may be effectively reversed thereby restoring p53 function in mice. Current diagnostic approaches based on genetic sequencing allow to identify the mutational status of p53, but do not inform on its conformational status. The aim of my thesis is to develop a fluorescent peptide biosensor that recognizes and reports on conformational mutants of p53 expressed in human cancers. We have characterized and optimized the response of this biosensor through conjugation to different environmentally-sensitive probes. We have further investigated their ability to report selectively on the R248Q mutant of p53 in vitro using recombinant forms of wildtype and mutant p53 proteins as well as lysates from lung cancer cell lines that express wild-type p53 (A549), the R248Q mutant (PC9), or p53 - / - (H1299). Having established the optimal working conditions and limitations of the biosensor in vitro, we applied this biosensor to image living cells by fluorescence microscopy, following facilitated cellular internalization by a cell-penetrating peptide, so as to establish its potential for therapeutic perspectives. We are further monitoring response of the biosensor to induced expression of conformational mutants of p53, as well as to its downregulation, both in vitro and in living cells
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Saundh, Harpal. "Targeting mutant p53 in cSCCs." Thesis, University of Dundee, 2016. https://discovery.dundee.ac.uk/en/studentTheses/29e37f0d-5ed7-483c-9a92-87212934d72b.

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Cutaneous squamous cell carcinoma (cSCC) is a type of non-melanoma skin cancer that is the 4th most common cancer registration in Scotland after BCC, lung and breast cancer. Over 30,000 cSCC incidences are reported each year in the United Kingdom. In addition, around 1 in 4 skin cancer deaths in the UK are due to cSCCs. Amongst those highly prone to developing cSCCs include organ transplant recipient, immunosuppressed, recessive dystrophic epidermolysis bullosa (RDEB) and Xeroderma Pigmentosum (XP) patients. cSCC patients that display regional metastasis have a 5-year survival rate of 25-50%, whilst this rate is close to 0% in RDEB patients with multiple cSCCs. Wild-type p53 (wt-p53) has been shown to prevent cSCC development and induce tanning and sunburn responses in skin cells. However, TP53 mutations are found in over half of all human cancers and cSCC is no exception as TP53 mutational frequency in cSCCs is around 64-87.5% (Durinck et al, 2011; South et al, 2014). The majority of TP53 mutations in cSCCs are UV-signature missense mutations, highlighting UV-radiation as one of the main risk factors for cSCC development. Mutant p53 proteins can lose wt-p53 functions, have dominant-negative effects against wt-p53 and acquire gain of function (GOF) activities. Mutant p53 GOF activity is induced by the accumulation of mutant p53 in tumour cells. Mutant p53 accumulation is not due to intrinsic properties of the mutants but requires other cellular events, possibly those known to stabilise wt-p53 under cellular stress. It is known that the TP53 mutations and mutant p53 accumulation are early steps in cSCC development. This makes skin an excellent system to investigate the early changes to p53. We have investigated the potential of targeting mutant p53 for cSCC therapy and mechanisms that promote mutant p53 accumulation in cSCCs. We selected low-passage cSCC cell lines that express hotspot mutant p53 proteins, in cSCCs and in general, by analysing TP53 mutational data from the IARC database and next generation sequencing studies performed on cSCC primary tumours by Dr South at Ninewells Hospital, Dundee. cSCC cell lines were generated from immunocompetent, transplant and RDEB patients by Dr South’s group at Ninewells Hospital, Dundee. We found that: 1. PRIMA-1MET, a small molecule reported to restore wt-p53 activity, lacked tumour selectivity as it is able to reduce cell viability in both normal skin and cSCC cells with similar potency. cSCC cell lines are relatively resistant to PRIMA-1MET compared to cell lines derived from other tumour types. 2. Mutant p53 knockdown studies performed on cSCC cell lines suggest that some p53 mutants play a pro-proliferative role. However, there is no evidence for a pro-migratory role of mutant p53 in cSCC. 3. There are no clear alterations in DNA-damage response pathways or the general ubiquitin proteasome system that could contribute to mutant p53 stabilisation in cSCC. 4. Heat shock factor 1 (HSF-1) is upregulated in cSCC compared to normal human keratinocytes (NHK). HSP90 inhibitors, 17-AAG and 17-DMAG, reduce mutant p53 protein levels suggesting that HSP90 plays a role in stabilising mutant p53 in cSCCs. 5. PR-619, a broad range deubiquitinating enzyme (DUB) inhibitor, reduces mutant p53 protein levels in a range of cSCC cell lines. This is rescued by the addition of bortezomib suggesting that DUBs can play a role in protecting mutant p53 from proteasomal degradation. Expression of HAUSP and USP10, which have been shown to stabilise wild-type p53, is generally elevated in cSCC compared to NHK. However, knockdown of these DUBs does not reduce protein levels of mutant p53 in cSCC cell lines. 6. A potential isoform of MDMX (51 kDa) is strongly upregulated in all cSCC cell lines examined. There is an association between the ability of MDMX siRNAs to deplete the 51 kDa protein and reduce mutant p53 protein levels and stability. Furthermore we show that the protein can form complexes with MDM2 in vitro and in cSCC cells. We propose that the MDMX isoform is able to stabilise mutant p53 in cSCC cells through this interaction with MDM2.
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Marini, Wanda. "Comparing mutant p53 and a wild-type p53 isoform, p47 : rationale for the selection of mutant p53 in tumours." Thesis, McGill University, 2009. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=116033.

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One of the major unresolved questions in cancer biology is why the majority of tumour cells express mutant p53 proteins. p53 is considered the prototype tumour suppressor protein, whose inactivation is the most frequent single genetic event in human cancer (Bourdon et al., 2005). Genetically-engineered p53-null knockout mice acquire multiple tumours very early on in life and human Li-Fraumeni families who carry germline mutations in p53 are highly cancer-prone (reviewed in Vousden and Lane, 2007). p53 mutant proteins have been found to acquire novel functions that promote cancer cell proliferation and survival, yet exactly why mutant p53s acquire oncogenic activity is still poorly understood. Mutant p53 has also been found to complex with wildtype p53, thus acting in a dominant negative way. However, this inhibition is incomplete since many cancers with mutant p53 alleles also have a loss of the second wild-type p53 allele and thus only express the mutant p53 (Baker et al., 1989). An N-terminal truncated p53 isoform, p47, arising from alternative splicing of the p53 gene (Ghosh et al., 2004) or by alternative initiation sites for translation (Yin et al. , 2002), has been described. Alternative splicing was found to be universal in all human multi-exon genes (Wang et al., 2008) and therefore determining the role of the p47 isoform with respect to the p53 gene is essential. Evidence in this study suggests that mutant p53 (p53RI75H) has a similar structure and function as p47, including the ability to complex with and impair both p53 and p73. Therefore, in addition to expressing a tumour suppressor protein, the p53 gene can also express an onco-protein (p47). This study therefore argues that tumours select for mutant p53 because it has gained the ability to function like p47, a wild-type p53 isoform.
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Books on the topic "Mutants de p53"

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Deb, Swati Palit, and Sumitra Deb, eds. Mutant p53 and MDM2 in Cancer. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-017-9211-0.

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Kuzniar, Beata. Human lymphoblastoid cell lines expressing mutant p53 exhibit decreased sensitivity to cisplatin-induced cytotoxicity. Ottawa: National Library of Canada, 1998.

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Haupt, Ygal, and Giovanni Blandino, eds. Human Tumor-Derived p53 Mutants: A Growing Family of Oncoproteins. Frontiers Media SA, 2016. http://dx.doi.org/10.3389/978-2-88919-961-7.

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Deb, Sumitra, and Swati Palit Deb. Mutant p53 and MDM2 in Cancer. Springer, 2016.

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Book chapters on the topic "Mutants de p53"

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Finlay, C. A., and R. S. Quartin. "Biological Phenotypes of Tumor-Derived Human p53 Mutants." In DNA Replication and the Cell Cycle, 231–36. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77040-1_19.

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Kamada, Rui. "Quantitative Analysis for p53 Tetramerization Domain Mutants Reveals a Low Threshold for Tumor Suppressor Inactivation." In Springer Theses, 13–43. Tokyo: Springer Japan, 2012. http://dx.doi.org/10.1007/978-4-431-54135-6_2.

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Monti, Olimpia, Alexander Damalas, Sabrina Strano, and Giovanni Blandino. "P73, P63 and Mutant P53: Members of Protein Complexs Floating in Cancer Cells." In 25 Years of p53 Research, 223–32. Dordrecht: Springer Netherlands, 2007. http://dx.doi.org/10.1007/978-1-4020-2922-6_10.

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Terzian, Tamara, and Guillermina Lozano. "Mutant p53-Driven Tumorigenesis." In p53 in the Clinics, 77–93. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-3676-8_5.

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Mukhopadhyay, Tapas, Steven A. Maxwell, and Jack A. Roth. "Wild-Type versus Mutant p53." In p53 Suppressor Gene, 19–54. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-662-22275-1_3.

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Shen, Jinfeng, Vladimir J. N. Bykov, and Klas G. Wiman. "Targeting Mutant p53 for Improved Cancer Therapy." In p53 in the Clinics, 257–73. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-3676-8_14.

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Joerger, Andreas C., Assaf Friedler, and Alan R. Fersht. "Wild Type p53 Conformation, Structural Consequences of p53 Mutations and Mechanisms of Mutant p53 Rescue." In 25 Years of p53 Research, 377–97. Dordrecht: Springer Netherlands, 2007. http://dx.doi.org/10.1007/978-1-4020-2922-6_17.

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Frum, Rebecca A., and Steven R. Grossman. "Mechanisms of Mutant p53 Stabilization in Cancer." In Subcellular Biochemistry, 187–97. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-017-9211-0_10.

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Santoro, Raffaela, Sabrina Strano, and Giovanni Blandino. "Transcriptional Regulation by Mutant p53 and Oncogenesis." In Subcellular Biochemistry, 91–103. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-017-9211-0_5.

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Yeudall, W. Andrew, Katharine H. Wrighton, and Sumitra Deb. "Mutant p53 in Cell Adhesion and Motility." In Methods in Molecular Biology, 135–46. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-236-0_11.

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Conference papers on the topic "Mutants de p53"

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Vidales, Karen Hernández, Edgar Guevara, Vanesa Olivares Illana, and Francisco Javier González. "Raman Spectroscopy of Wild Type and Mutants p53." In Latin America Optics and Photonics Conference. Washington, D.C.: OSA, 2018. http://dx.doi.org/10.1364/laop.2018.tu3c.4.

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Wang, Haijin, Ruhui Shen, Haichao Wang, and Haohan Wang. "Active learning framework of informative p53 cancer rescue mutants." In 2017 Third International Conference on Advances in Electrical, Electronics, Information, Communication and Bio-Informatics (AEEICB). IEEE, 2017. http://dx.doi.org/10.1109/aeeicb.2017.7972384.

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Hernández Vidales, Karen, Edgar Guevara Codina, Vanesa Olivares Illana, and Francisco Javier González Contreras. "Multivariate analysis of Raman spectroscopy of wild type and mutants p53 cancer biomarker." In Imaging Spectrometry XXIII: Applications, Sensors, and Processing, edited by Emmett J. Ientilucci. SPIE, 2019. http://dx.doi.org/10.1117/12.2529411.

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Vilimas, Tomas, Keith Collins, Theresa Guerin, Roackie Awasthi, Lionel Feigenbaum, Guillermina Lozano, Terry Van Dyke, and Serguei Kozlov. "Abstract A17: p53 missense mutants R172H and R270H exhibit differential effects on tumorigenesis." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics; November 5-9, 2015; Boston, MA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1535-7163.targ-15-a17.

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Yang, Lu. "Abstract 2487: disrupting binding of p53 mutants to PEPD unleashes their tumor suppressor activities." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-2487.

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Rodriguez, Olga Catalina, Vamsi Kokula, Jason Catania, Anju Preet, Arslaan Arshed,, Michael Pishvaian, Christopher Albanese, and Maria L. Avantaggiati. "Abstract 4833: Glucose restriction induces degradation of p53 mutants via a selective autophagy-mediated pathway." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-4833.

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Yu, Xin, David Lubin, Sumana Narayanan, Alexei Vazquez, Stewart Loh, Arnold J. Levine, and Darren R. Carpizo. "Abstract 2330: NSC319726 reactivates zinc-binding p53 mis-sense mutants using a novel dual mechanism." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-2330.

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Huun, Johanna, Elisabet O. Berge, Johan R. Lillehaug, Per Eystein Lonning, and Stian Knappskog. "Abstract 3139: Identification and functional studies of p53 mutants detected in breast cancers after chemotherapy treatment." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-3139.

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Yu, Valen Z., and Maria L. Lung. "Abstract 5462: Functional characterization of potential gain-of-function p53 mutants in esophageal squamous cell carcinoma." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-5462.

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Flores, Brianna, and Elizabeth E. Hull. "Abstract 556: Oncogenic properties and response to HDAC inhibitor treatment of H1299 cells expressing GOF p53 mutants." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-556.

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Reports on the topic "Mutants de p53"

1

Hildegund, Ertl C. Vaccines to Breast Cancer Based on p53 Mutants. Fort Belvoir, VA: Defense Technical Information Center, September 1998. http://dx.doi.org/10.21236/ada359979.

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Chen, Xiaoying. Restore Wild-Type Functions to P53 Mutants Using an RNA- Based Combinatorial Approach. Fort Belvoir, VA: Defense Technical Information Center, June 1998. http://dx.doi.org/10.21236/ada353779.

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Green, Christopher. Restore Wild-Type Functions to P53 Mutants Using an RNA-Based Combinatorial Approach. Fort Belvoir, VA: Defense Technical Information Center, June 2000. http://dx.doi.org/10.21236/ada392235.

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Murphy, Kristen, Renee O'Lear, and Jeffrey Rosen. Functional Significance of Mutant p53 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2000. http://dx.doi.org/10.21236/ada395615.

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O'Lear, Rene, and Jeffrey Rosen. Functional Significance of Mutant p53 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, July 2002. http://dx.doi.org/10.21236/ada409759.

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Prives, Carol. The Role of Mutant p53 Protein in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 1995. http://dx.doi.org/10.21236/ada300013.

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Prives, Carol L. The Role of Mutant p53 Protein in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 1998. http://dx.doi.org/10.21236/ada363399.

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Prives, Carol L. The Role of Mutant p53 Protein in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 1997. http://dx.doi.org/10.21236/ada344920.

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Liu, Gang. The Role of Mutant p53 in Progression of Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, December 2005. http://dx.doi.org/10.21236/ada483299.

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DeMasters, Gerald. Susceptibility to Radiation Induced Apoptosis and Senescence in p53 Wild Type and p53 Mutant Breast Tumor Cells. Fort Belvoir, VA: Defense Technical Information Center, July 2006. http://dx.doi.org/10.21236/ada463568.

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