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Metabolic stressors disrupt proteome homeostasis to suppress malignancy.

Molecular & cellular oncology

Dai C.
PMID: 26973866
Mol Cell Oncol. 2015;2(4). doi: 10.1080/23723556.2014.1002718. Epub 2015 Jan 23.

Within tumor cells the heat shock factor 1 (HSF1)-mediated stress response is constitutively mobilized to counter persistent proteotoxic stress, hence sustaining their fragile proteome homeostasis and supporting robust malignant phenotypes. Intriguingly, our new studies reveal that metabolic stressors, such...

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Dai C. Metabolic stressors disrupt proteome homeostasis to suppress malignancy. Mol Cell Oncol. 2015;2(4)doi: 10.1080/23723556.2014.1002718.
Dai, C. (2015). Metabolic stressors disrupt proteome homeostasis to suppress malignancy. Molecular & cellular oncology, 2(4), . https://doi.org/10.1080/23723556.2014.1002718
Dai, Chengkai. "Metabolic stressors disrupt proteome homeostasis to suppress malignancy." Molecular & cellular oncology vol. 2,4 (2015). doi: https://doi.org/10.1080/23723556.2014.1002718
Dai C. Metabolic stressors disrupt proteome homeostasis to suppress malignancy. Mol Cell Oncol. 2015;2(4). doi: 10.1080/23723556.2014.1002718. Epub 2015 Jan 23. PMID: 26973866; PMCID: PMC4786015.
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MHC-I genotype drives early immune selection of oncogenic mutations.

Molecular & cellular oncology

Marty R, de Prisco N, Carter H, Font-Burgada J.
PMID: 29487895
Mol Cell Oncol. 2018 Jan 25;5(2):e1409863. doi: 10.1080/23723556.2017.1409863. eCollection 2018.

MHC-I exposes the intracellular contents to immune cells for surveillance of cellular health. Due to high genomic variation, individuals' immune systems differ in their ability to expose and eliminate cancer-causing mutations. These personalized immune blind spots create specific oncogenic...

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Marty R, de Prisco N, Carter H, et al. MHC-I genotype drives early immune selection of oncogenic mutations. Mol Cell Oncol. 2018;5(2):e1409863doi: 10.1080/23723556.2017.1409863.
Marty, R., de Prisco, N., Carter, H., & Font-Burgada, J. (2018). MHC-I genotype drives early immune selection of oncogenic mutations. Molecular & cellular oncology, 5(2), e1409863. https://doi.org/10.1080/23723556.2017.1409863
Marty, Rachel, et al. "MHC-I genotype drives early immune selection of oncogenic mutations." Molecular & cellular oncology vol. 5,2 (2018): e1409863. doi: https://doi.org/10.1080/23723556.2017.1409863
Marty R, de Prisco N, Carter H, Font-Burgada J. MHC-I genotype drives early immune selection of oncogenic mutations. Mol Cell Oncol. 2018 Jan 25;5(2):e1409863. doi: 10.1080/23723556.2017.1409863. eCollection 2018. PMID: 29487895; PMCID: PMC5821412.
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Inhibiting system x.

Molecular & cellular oncology

Clemons NJ, Liu DS, Duong CP, Phillips WA.
PMID: 29057306
Mol Cell Oncol. 2017 Jul 05;4(5):e1344757. doi: 10.1080/23723556.2017.1344757. eCollection 2017.

Effective therapeutic strategies to target mutant tumor protein p53 (TP53, best known as p53) cancers remain an unmet medical need. We found that mutant p53 impairs the function of nuclear factor (erythroid-derived 2)-like 2 (NFE2L2, commonly known as NRF2),...

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Clemons NJ, Liu DS, Duong CP, et al. Inhibiting system x. Mol Cell Oncol. 2017;4(5):e1344757doi: 10.1080/23723556.2017.1344757.
Clemons, N. J., Liu, D. S., Duong, C. P., & Phillips, W. A. (2017). Inhibiting system x. Molecular & cellular oncology, 4(5), e1344757. https://doi.org/10.1080/23723556.2017.1344757
Clemons, Nicholas J, et al. "Inhibiting system x." Molecular & cellular oncology vol. 4,5 (2017): e1344757. doi: https://doi.org/10.1080/23723556.2017.1344757
Clemons NJ, Liu DS, Duong CP, Phillips WA. Inhibiting system x. Mol Cell Oncol. 2017 Jul 05;4(5):e1344757. doi: 10.1080/23723556.2017.1344757. eCollection 2017. PMID: 29057306; PMCID: PMC5644480.
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Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation.

Molecular & cellular oncology

Sidi S, Bouchier-Hayes L.
PMID: 29057309
Mol Cell Oncol. 2017 Jul 05;4(5):e1348325. doi: 10.1080/23723556.2017.1348325. eCollection 2017.

Despite being frequently mutated or deregulated in acute myeloid leukemia (AML) and many other cancers, the mechanisms by which nucleophosmin (NPM1) regulates oncogenesis remain elusive. We found that NPM1 plays a direct and conserved role in DNA damage-induced assembly...

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Sidi S, Bouchier-Hayes L. Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation. Mol Cell Oncol. 2017;4(5):e1348325doi: 10.1080/23723556.2017.1348325.
Sidi, S., & Bouchier-Hayes, L. (2017). Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation. Molecular & cellular oncology, 4(5), e1348325. https://doi.org/10.1080/23723556.2017.1348325
Sidi, Samuel, and Bouchier-Hayes, Lisa. "Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation." Molecular & cellular oncology vol. 4,5 (2017): e1348325. doi: https://doi.org/10.1080/23723556.2017.1348325
Sidi S, Bouchier-Hayes L. Direct pro-apoptotic role for NPM1 as a regulator of PIDDosome formation. Mol Cell Oncol. 2017 Jul 05;4(5):e1348325. doi: 10.1080/23723556.2017.1348325. eCollection 2017. PMID: 29057309; PMCID: PMC5644479.
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Targeting RNA binding protein in prostate cancer.

Molecular & cellular oncology

Fei T.
PMID: 29057311
Mol Cell Oncol. 2017 Jul 17;4(5):e1353855. doi: 10.1080/23723556.2017.1353855. eCollection 2017.

RNA binding protein (RBP) controls multiple aspects of RNA metabolism and plays crucial roles in many physiopathological contexts, including cancer. We recently identified an RBP HNRNPL as a novel prostate cancer dependency via regulation of RNA splicing, suggesting the...

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Fei T. Targeting RNA binding protein in prostate cancer. Mol Cell Oncol. 2017;4(5):e1353855doi: 10.1080/23723556.2017.1353855.
Fei, T. (2017). Targeting RNA binding protein in prostate cancer. Molecular & cellular oncology, 4(5), e1353855. https://doi.org/10.1080/23723556.2017.1353855
Fei, Teng. "Targeting RNA binding protein in prostate cancer." Molecular & cellular oncology vol. 4,5 (2017): e1353855. doi: https://doi.org/10.1080/23723556.2017.1353855
Fei T. Targeting RNA binding protein in prostate cancer. Mol Cell Oncol. 2017 Jul 17;4(5):e1353855. doi: 10.1080/23723556.2017.1353855. eCollection 2017. PMID: 29057311; PMCID: PMC5644478.
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Mitophagy, metabolism, and cell fate.

Molecular & cellular oncology

Esteban-Martínez L, Sierra-Filardi E, Boya P.
PMID: 29057310
Mol Cell Oncol. 2017 Jul 17;4(5):e1353854. doi: 10.1080/23723556.2017.1353854. eCollection 2017.

Mitophagy is the process by which cells eliminate damaged or superfluous mitochondria by degrading them within lysosomes. We show that during development, selective removal of mitochondria by autophagy induces a metabolic shift toward glycolysis that is essential for differentiation...

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Esteban-Martínez L, Sierra-Filardi E, Boya P. Mitophagy, metabolism, and cell fate. Mol Cell Oncol. 2017;4(5):e1353854doi: 10.1080/23723556.2017.1353854.
Esteban-Martínez, L., Sierra-Filardi, E., & Boya, P. (2017). Mitophagy, metabolism, and cell fate. Molecular & cellular oncology, 4(5), e1353854. https://doi.org/10.1080/23723556.2017.1353854
Esteban-Martínez, Lorena, et al. "Mitophagy, metabolism, and cell fate." Molecular & cellular oncology vol. 4,5 (2017): e1353854. doi: https://doi.org/10.1080/23723556.2017.1353854
Esteban-Martínez L, Sierra-Filardi E, Boya P. Mitophagy, metabolism, and cell fate. Mol Cell Oncol. 2017 Jul 17;4(5):e1353854. doi: 10.1080/23723556.2017.1353854. eCollection 2017. PMID: 29057310; PMCID: PMC5644481.
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Corrigendum.

Molecular & cellular oncology

[No authors listed]
PMID: 29487898
Mol Cell Oncol. 2018 Feb 20;5(2):e1422340. doi: 10.1080/23723556.2017.1422340. eCollection 2018.

[This corrects the article DOI: 10.1080/23723556.2017.1285385.].

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Corrigendum. Mol Cell Oncol. 2018;5(2):e1422340doi: 10.1080/23723556.2017.1422340.
(2018). Corrigendum. Molecular & cellular oncology, 5(2), e1422340. https://doi.org/10.1080/23723556.2017.1422340
"Corrigendum." Molecular & cellular oncology vol. 5,2 (2018): e1422340. doi: https://doi.org/10.1080/23723556.2017.1422340
Corrigendum. Mol Cell Oncol. 2018 Feb 20;5(2):e1422340. doi: 10.1080/23723556.2017.1422340. eCollection 2018. PMID: 29487898; PMCID: PMC5821414.
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TAK1-dependent autophagy: A suppressor of fatty liver disease and hepatic oncogenesis.

Molecular & cellular oncology

Seki E.
PMID: 26709386
Mol Cell Oncol. 2014;1(4). doi: 10.4161/23723548.2014.968507. Epub 2014 Dec 31.

In addition to regulating the activation of nuclear factor (NF)-κB and c-Jun N-terminal kinase (JNK), TGF-β activated kinase 1 (TAK1) also upregulates the activation of AMP-activated protein kinase (AMPK) and autophagy. In the liver, TAK1-mediated autophagy plays a role...

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Seki E. TAK1-dependent autophagy: A suppressor of fatty liver disease and hepatic oncogenesis. Mol Cell Oncol. 2014;1(4)doi: 10.4161/23723548.2014.968507.
Seki, E. (2014). TAK1-dependent autophagy: A suppressor of fatty liver disease and hepatic oncogenesis. Molecular & cellular oncology, 1(4), . https://doi.org/10.4161/23723548.2014.968507
Seki, Ekihiro. "TAK1-dependent autophagy: A suppressor of fatty liver disease and hepatic oncogenesis." Molecular & cellular oncology vol. 1,4 (2014). doi: https://doi.org/10.4161/23723548.2014.968507
Seki E. TAK1-dependent autophagy: A suppressor of fatty liver disease and hepatic oncogenesis. Mol Cell Oncol. 2014;1(4). doi: 10.4161/23723548.2014.968507. Epub 2014 Dec 31. PMID: 26709386; PMCID: PMC4687902.
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(-)-Oleocanthal rapidly and selectively induces cancer cell death via lysosomal membrane permeabilization.

Molecular & cellular oncology

LeGendre O, Breslin PA, Foster DA.
PMID: 26380379
Mol Cell Oncol. 2015;2(4):e1006077. doi: 10.1080/23723556.2015.1006077.

(-)-Oleocanthal (OC), a phenolic compound present in extra-virgin olive oil (EVOO), has been implicated in the health benefits associated with diets rich in EVOO. We investigated the effect of OC on human cancer cell lines in culture and found...

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LeGendre O, Breslin PA, Foster DA. (-)-Oleocanthal rapidly and selectively induces cancer cell death via lysosomal membrane permeabilization. Mol Cell Oncol. 2015;2(4):e1006077doi: 10.1080/23723556.2015.1006077.
LeGendre, O., Breslin, P. A., & Foster, D. A. (2015). (-)-Oleocanthal rapidly and selectively induces cancer cell death via lysosomal membrane permeabilization. Molecular & cellular oncology, 2(4), e1006077. https://doi.org/10.1080/23723556.2015.1006077
LeGendre, Onica, et al. "(-)-Oleocanthal rapidly and selectively induces cancer cell death via lysosomal membrane permeabilization." Molecular & cellular oncology vol. 2,4 (2015): e1006077. doi: https://doi.org/10.1080/23723556.2015.1006077
LeGendre O, Breslin PA, Foster DA. (-)-Oleocanthal rapidly and selectively induces cancer cell death via lysosomal membrane permeabilization. Mol Cell Oncol. 2015;2(4):e1006077. doi: 10.1080/23723556.2015.1006077. PMID: 26380379; PMCID: PMC4568762.
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Autophagic degradation of focal adhesions underlies metastatic cancer dissemination.

Molecular & cellular oncology

Sharifi MN, Mowers EE, Macleod KF.
PMID: 28401177
Mol Cell Oncol. 2016 Jun 10;4(2):e1198299. doi: 10.1080/23723556.2016.1198299. eCollection 2017.

Autophagy inhibition is being evaluated as a novel therapeutic strategy in multiple tumor types, but little is known about its implications for metastatic dissemination. We recently reported that autophagic degradation of paxillin through direct interaction with the autophagy protein...

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Sharifi MN, Mowers EE, Macleod KF. Autophagic degradation of focal adhesions underlies metastatic cancer dissemination. Mol Cell Oncol. 2016;4(2):e1198299doi: 10.1080/23723556.2016.1198299.
Sharifi, M. N., Mowers, E. E., & Macleod, K. F. (2017). Autophagic degradation of focal adhesions underlies metastatic cancer dissemination. Molecular & cellular oncology, 4(2), e1198299. https://doi.org/10.1080/23723556.2016.1198299
Sharifi, Marina N, et al. "Autophagic degradation of focal adhesions underlies metastatic cancer dissemination." Molecular & cellular oncology vol. 4,2 (2017): e1198299. doi: https://doi.org/10.1080/23723556.2016.1198299
Sharifi MN, Mowers EE, Macleod KF. Autophagic degradation of focal adhesions underlies metastatic cancer dissemination. Mol Cell Oncol. 2016 Jun 10;4(2):e1198299. doi: 10.1080/23723556.2016.1198299. eCollection 2017. PMID: 28401177; PMCID: PMC5383354.
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Targeting the AXL signaling pathway in ovarian cancer.

Molecular & cellular oncology

Huang RY, Antony J, Tan TZ, Tan DS.
PMID: 28401178
Mol Cell Oncol. 2016 Nov 28;4(2):e1263716. doi: 10.1080/23723556.2016.1263716. eCollection 2017.

In a recent publication in

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Huang RY, Antony J, Tan TZ, et al. Targeting the AXL signaling pathway in ovarian cancer. Mol Cell Oncol. 2016;4(2):e1263716doi: 10.1080/23723556.2016.1263716.
Huang, R. Y., Antony, J., Tan, T. Z., & Tan, D. S. (2017). Targeting the AXL signaling pathway in ovarian cancer. Molecular & cellular oncology, 4(2), e1263716. https://doi.org/10.1080/23723556.2016.1263716
Huang, Ruby Yun-Ju, et al. "Targeting the AXL signaling pathway in ovarian cancer." Molecular & cellular oncology vol. 4,2 (2017): e1263716. doi: https://doi.org/10.1080/23723556.2016.1263716
Huang RY, Antony J, Tan TZ, Tan DS. Targeting the AXL signaling pathway in ovarian cancer. Mol Cell Oncol. 2016 Nov 28;4(2):e1263716. doi: 10.1080/23723556.2016.1263716. eCollection 2017. PMID: 28401178; PMCID: PMC5383361.
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KAT2-mediated PLK4 acetylation contributes to genomic stability by preserving centrosome number.

Molecular & cellular oncology

Fournier M, Tora L.
PMID: 28401181
Mol Cell Oncol. 2016 Dec 16;4(2):e1270391. doi: 10.1080/23723556.2016.1270391. eCollection 2017.

We have recently identified the first human lysine (K) acetyltransferase 2A and 2B (called KAT2A/2B; known also as GCN5/PCAF, respectively)-dependent acetylome and revealed a mechanism by which KAT2A/2B-mediated acetylation of serine/threonine polo-like kinase 4 (PLK4) maintains correct centrosome number...

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Fournier M, Tora L. KAT2-mediated PLK4 acetylation contributes to genomic stability by preserving centrosome number. Mol Cell Oncol. 2016;4(2):e1270391doi: 10.1080/23723556.2016.1270391.
Fournier, M., & Tora, L. (2017). KAT2-mediated PLK4 acetylation contributes to genomic stability by preserving centrosome number. Molecular & cellular oncology, 4(2), e1270391. https://doi.org/10.1080/23723556.2016.1270391
Fournier, Marjorie, and Tora, László. "KAT2-mediated PLK4 acetylation contributes to genomic stability by preserving centrosome number." Molecular & cellular oncology vol. 4,2 (2017): e1270391. doi: https://doi.org/10.1080/23723556.2016.1270391
Fournier M, Tora L. KAT2-mediated PLK4 acetylation contributes to genomic stability by preserving centrosome number. Mol Cell Oncol. 2016 Dec 16;4(2):e1270391. doi: 10.1080/23723556.2016.1270391. eCollection 2017. PMID: 28401181; PMCID: PMC5383365.
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Showing 1 to 12 of 995 entries