@article{MTMT:33541689,
	title = {Protein Kinase D3 (PKD3) Requires Hsp90 for Stability and Promotion of Prostate Cancer Cell Migration},
	url = {https://m2.mtmt.hu/api/publication/33541689},
	author = {Varga, Attila and Nguyen, Minh Tu and Pénzes, Kinga and Bátai, Bence and Gyulavári, Pál and Gurbi, Bianka and Murányi, József and Csermely, Péter and Csala, Miklós and Vántus, Tibor and Sőti, Csaba},
	doi = {10.3390/cells12020212},
	journal-iso = {CELLS-BASEL},
	journal = {CELLS},
	volume = {12},
	unique-id = {33541689},
	abstract = {Prostate cancer metastasis is a significant cause of mortality in men. PKD3 facilitates tumor growth and metastasis, however, its regulation is largely unclear. The Hsp90 chaperone stabilizes an array of signaling client proteins, thus is an enabler of the malignant phenotype. Here, using different prostate cancer cell lines, we report that Hsp90 ensures PKD3 conformational stability and function to promote cancer cell migration. We found that pharmacological inhibition of either PKDs or Hsp90 dose-dependently abrogated the migration of DU145 and PC3 metastatic prostate cancer cells. Hsp90 inhibition by ganetespib caused a dose-dependent depletion of PKD2, PKD3, and Akt, which are all involved in metastasis formation. Proximity ligation assay and immunoprecipitation experiments demonstrated a physical interaction between Hsp90 and PKD3. Inhibition of the chaperone–client interaction induced misfolding and proteasomal degradation of PKD3. PKD3 siRNA combined with ganetespib treatment demonstrated a specific involvement of PKD3 in DU145 and PC3 cell migration, which was entirely dependent on Hsp90. Finally, ectopic expression of PKD3 enhanced migration of non-metastatic LNCaP cells in an Hsp90-dependent manner. Altogether, our findings identify PKD3 as an Hsp90 client and uncover a potential mechanism of Hsp90 in prostate cancer metastasis. The molecular interaction revealed here may regulate other biological and pathological functions.},
	year = {2023},
	eissn = {2073-4409},
	orcid-numbers = {Nguyen, Minh Tu/0000-0003-1653-8377; Gyulavári, Pál/0000-0002-5850-0441; Gurbi, Bianka/0000-0002-5635-6255; Csermely, Péter/0000-0001-9234-0659; Csala, Miklós/0000-0002-3829-4361; Vántus, Tibor/0000-0002-7894-017X; Sőti, Csaba/0000-0002-4057-7678}
}

@article{MTMT:31173123,
	title = {Heat shock protein 90 chaperones and protein kinase D3 regulates androgen-independent prostate cancer development},
	url = {https://m2.mtmt.hu/api/publication/31173123},
	author = {Varga, Attila and Batai, B. and Gyulavári, Pál and Nguyen, Minh Tu and Sőti, Csaba and Vántus, Tibor},
	journal-iso = {ANN ONCOL},
	journal = {ANNALS OF ONCOLOGY},
	volume = {30},
	unique-id = {31173123},
	issn = {0923-7534},
	year = {2019},
	eissn = {1569-8041},
	orcid-numbers = {Gyulavári, Pál/0000-0002-5850-0441; Nguyen, Minh Tu/0000-0003-1653-8377; Sőti, Csaba/0000-0002-4057-7678; Vántus, Tibor/0000-0002-7894-017X}
}

@article{MTMT:30789521,
	title = {Glomerular Collagen Deposition and Lipocalin-2 Expression Are Early Signs of Renal Injury in Prediabetic Obese Rats},
	url = {https://m2.mtmt.hu/api/publication/30789521},
	author = {Bukosza, Éva Nóra and Kaucsár, Tamás and Godó, Mária and Lajtár, Enikő and Tod, Pál and Koncsos, Gábor and Varga, Zoltán and Baranyai, Tamás and Nguyen, Minh Tu and Schachner, Helga and Sőti, Csaba and Ferdinandy, Péter and Giricz, Zoltán and Szénási, Gábor and Hamar, Péter},
	doi = {10.3390/ijms20174266},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {20},
	unique-id = {30789521},
	issn = {1661-6596},
	abstract = {Feeding rats with high-fat diet (HFD) with a single streptozotocin (STZ) injection induced obesity, slightly elevated fasting blood glucose and impaired glucose and insulin tolerance, and caused cardiac hypertrophy and mild diastolic dysfunction as published before by Koncsos et al. in 2016. Here we aimed to explore the renal consequences in the same groups of rats. Male Long-Evans rats were fed normal chow (CON; n = 9) or HFD containing 40% lard and were administered STZ at 20 mg/kg (i.p.) at week four (prediabetic rats, PRED, n = 9). At week 21 blood and urine samples were taken and kidney and liver samples were collected for histology, immunohistochemistry and for analysis of gene expression. HFD and STZ increased body weight and visceral adiposity and plasma leptin concentration. Despite hyperleptinemia, plasma C-reactive protein concentration decreased in PRED rats. Immunohistochemistry revealed elevated collagen IV protein expression in the glomeruli, and Lcn2 mRNA expression increased, while Il-1β mRNA expression decreased in both the renal cortex and medulla in PRED vs. CON rats. Kidney histology, urinary protein excretion, plasma creatinine, glomerular Feret diameter, desmin protein expression, and cortical and medullary mRNA expression of TGF-β1, Nrf2, and PPARγ were similar in CON and PRED rats. Reduced AMPKα phosphorylation of the autophagy regulator Akt was the first sign of liver damage, while plasma lipid and liver enzyme concentrations were similar. In conclusion, glomerular collagen deposition and increased lipocalin-2 expression were the early signs of kidney injury, while most biomarkers of inflammation, oxidative stress and fibrosis were negative in the kidneys of obese, prediabetic rats with mild heart and liver injury.},
	keywords = {Inflammation; OBESITY; Collagen Type IV; Lipocalin-2; Renal Injury},
	year = {2019},
	eissn = {1422-0067},
	orcid-numbers = {Kaucsár, Tamás/0000-0003-4460-1265; Tod, Pál/0000-0001-9163-7071; Koncsos, Gábor/0000-0001-5451-8719; Varga, Zoltán/0000-0002-2758-0784; Baranyai, Tamás/0000-0002-9378-8938; Nguyen, Minh Tu/0000-0003-1653-8377; Sőti, Csaba/0000-0002-4057-7678; Ferdinandy, Péter/0000-0002-6424-6806; Giricz, Zoltán/0000-0003-2036-8665; Szénási, Gábor/0000-0002-7350-6091; Hamar, Péter/0000-0002-1095-3564}
}

@article{MTMT:30334331,
	title = {Hsp90 Stabilizes SIRT1 Orthologs in Mammalian Cells and C. elegans},
	url = {https://m2.mtmt.hu/api/publication/30334331},
	author = {Nguyen, Minh Tu and Somogyvári, Milán and Sőti, Csaba},
	doi = {10.3390/ijms19113661},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {19},
	unique-id = {30334331},
	issn = {1661-6596},
	abstract = {Sirtuin 1 (SIRT1) othologs are ubiquitous NAD⁺-dependent deacetylases that act as nutrient sensors and modulate metabolism and stress responses in diverse organisms. Both mammalian SIRT1 and Caenorhabditis elegans SIR-2.1 have been implicated in dietary restriction, longevity, and healthspan. Hsp90 is an evolutionarily conserved molecular chaperone that stabilizes a plethora of signaling 'client' proteins and regulates fundamental biological processes. Here we report that Hsp90 is required for conformational stabilization of SIRT1 and SIR-2.1. We find that inhibition of Hsp90 by geldanamycin (GA) induces the depletion of mammalian SIRT1 protein in a concentration and time dependent manner in COS-7 and HepG2 cells. In contrast to SIRT1, SIRT2 level remains unchanged by GA treatment, reflecting a specific Hsp90 SIRT1 interaction. Hsp90 inhibition leads to the destabilization and proteasomal degradation of SIRT1. Moreover, we observe a GA-sensitive physical interaction between SIRT1 and Hsp90 by immunoprecipitation. We also demonstrate that hsp-90 gene silencing also induces SIR-2.1 protein depletion and proteasomal degradation in C. elegans. Our findings identify metazoan SIRT1 orthologs as Hsp90 clients and reveal a novel crosstalk between the proteostasis and nutrient signaling networks, which may have implications in various age related diseases.},
	keywords = {metabolism; STRESS; Aging; signaling; epigenetics; HDAC; Proteostasis; daf-21; sir-2.1},
	year = {2018},
	eissn = {1422-0067},
	orcid-numbers = {Nguyen, Minh Tu/0000-0003-1653-8377; Somogyvári, Milán/0000-0002-6257-4849; Sőti, Csaba/0000-0002-4057-7678}
}

@mastersthesis{MTMT:2815014,
	title = {A Hsp90 és az adipogenezis kapcsolatának vizsgálata},
	url = {https://m2.mtmt.hu/api/publication/2815014},
	author = {Nguyen, Minh Tu},
	doi = {10.14753/SE.2014.1971},
	unique-id = {2815014},
	year = {2014},
	orcid-numbers = {Nguyen, Minh Tu/0000-0003-1653-8377}
}

@article{MTMT:2437212,
	title = {Hsp90 chaperones PPARγ and regulates differentiation and survival of 3T3-L1 adipocytes},
	url = {https://m2.mtmt.hu/api/publication/2437212},
	author = {Nguyen, Minh Tu and Csermely, Péter and Sőti, Csaba},
	doi = {10.1038/cdd.2013.129},
	journal-iso = {CELL DEATH DIFFER},
	journal = {CELL DEATH AND DIFFERENTIATION},
	volume = {20},
	unique-id = {2437212},
	issn = {1350-9047},
	abstract = {Adipose tissue dysregulation has a major role in various human diseases. The peroxisome proliferator-activated receptor-γ (PPARγ) is a key regulator of adipocyte differentiation and function, as well as a target of insulin-sensitizing drugs. The Hsp90 chaperone stabilizes a diverse set of signaling 'client' proteins, thereby regulates various biological processes. Here we report a novel role for Hsp90 in controlling PPARγ stability and cellular differentiation. Specifically, we show that the Hsp90 inhibitors geldanamycin and novobiocin efficiently impede the differentiation of murine 3T3-L1 preadipocytes. Geldanamycin at higher concentrations also inhibits the survival of both developing and mature adipocytes, respectively. Further, Hsp90 inhibition disrupts an Hsp90-PPARγ complex, leads to the destabilization and proteasomal degradation of PPARγ, and inhibits the expression of PPARγ target genes, identifying PPARγ as an Hsp90 client. A similar destabilization of PPARγ and a halt of adipogenesis also occur in response to protein denaturing stresses caused by a single transient heat-shock or proteasome inhibition. Recovery from stress restores PPARγ stability and adipocyte differentiation. Thus, our findings reveal Hsp90 as a critical stress-responsive regulator of adipocyte biology and offer a potential therapeutic target in obesity and the metabolic syndrome.Cell Death and Differentiation advance online publication, 4 October 2013; doi:10.1038/cdd.2013.129.},
	year = {2013},
	eissn = {1476-5403},
	pages = {1654-1663},
	orcid-numbers = {Nguyen, Minh Tu/0000-0003-1653-8377; Csermely, Péter/0000-0001-9234-0659; Sőti, Csaba/0000-0002-4057-7678}
}

@article{MTMT:1934743,
	title = {RNA interference links oxidative stress to the inhibition of heat stress adaptation.},
	url = {https://m2.mtmt.hu/api/publication/1934743},
	author = {Spiro, Z and Arslan, Mehmet Alper and Somogyvári, Milán and Nguyen, Minh Tu and Smolders, A and Dancso, B and Németh, Nóra and Molnár, Zsuzsanna and Braeckman, B and Csermely, Péter and Sőti, Csaba},
	doi = {10.1089/ars.2011.4161},
	journal-iso = {ANTIOXID REDOX SIGNAL},
	journal = {ANTIOXIDANTS & REDOX SIGNALING},
	volume = {17},
	unique-id = {1934743},
	issn = {1523-0864},
	abstract = {Increased oxidative stress is associated with various diseases and aging, while adaptation to heat stress is an important determinant of survival and contributes to longevity. However, the impact of oxidative stress on heat resistance remains largely unclear. Aim: In this study we investigated how oxidative stress impinges on heat stress responses. Results: We report that H2O2 pretreatment inhibits both acquired thermotolerance and heat-induced Hsp70 expression in mammalian cells, as well as acquired thermotolerance in the nematode Caenorhabditis elegans, via RNA interference. Moreover, we demonstrate that elimination of RNA interference by silencing key enzymes in microRNA biogenesis, dcr-1 or pash-1, restores the diminished intrinsic thermotolerance of aged and H2O2-elimination compromised (catalase-2 and peroxiredoxin-2 deficient) worms. Innovation and Conclusion: These results uncover a novel post-transcriptional element in the regulation of heat stress adaptation under oxidative conditions which may have implications in disease susceptibility and aging.},
	year = {2012},
	eissn = {1557-7716},
	pages = {890-901},
	orcid-numbers = {Somogyvári, Milán/0000-0002-6257-4849; Nguyen, Minh Tu/0000-0003-1653-8377; Molnár, Zsuzsanna/0000-0002-4598-3608; Csermely, Péter/0000-0001-9234-0659; Sőti, Csaba/0000-0002-4057-7678}
}

@{MTMT:1923793,
	title = {Expected functions of salivary HSP70 in the oral cavity},
	url = {https://m2.mtmt.hu/api/publication/1923793},
	author = {Fábián, Tibor Károly and Sőti, Cs and Nguyen, Minh Tu and Csermely, P and Fejérdy, Pál},
	booktitle = {Advances in medicine and biology, vol 19},
	unique-id = {1923793},
	year = {2011},
	pages = {289-308},
	orcid-numbers = {Nguyen, Minh Tu/0000-0003-1653-8377; Fejérdy, Pál/0000-0002-1412-7462}
}

@article{MTMT:1343074,
	title = {The heat shock connection of metabolic stress and dietary restriction},
	url = {https://m2.mtmt.hu/api/publication/1343074},
	author = {Dancsó, B and Spiró, Z and Arslan, Mehmet Alper and Nguyen, Minh Tu and Papp, Diána and Csermely, Péter and Sőti, Csaba},
	doi = {10.2174/138920110790909704},
	journal-iso = {CURR PHARM BIOTECHNO},
	journal = {CURRENT PHARMACEUTICAL BIOTECHNOLOGY},
	volume = {11},
	unique-id = {1343074},
	issn = {1389-2010},
	year = {2010},
	eissn = {1873-4316},
	pages = {139-145},
	orcid-numbers = {Nguyen, Minh Tu/0000-0003-1653-8377; Csermely, Péter/0000-0001-9234-0659; Sőti, Csaba/0000-0002-4057-7678}
}

@{MTMT:1493558,
	title = {Betegségkép a különböző vallásokban},
	url = {https://m2.mtmt.hu/api/publication/1493558},
	author = {Fábián, Tibor Károly and Nguyen, Minh Tu},
	booktitle = {Vallás és hit a gyógyításban},
	unique-id = {1493558},
	year = {2008},
	pages = {101-112},
	orcid-numbers = {Nguyen, Minh Tu/0000-0003-1653-8377}
}