@article{MTMT:35299583,
	title = {Venom variation among the three subspecies of the North African mountain viper Vipera monticola Saint Girons 1953},
	url = {https://m2.mtmt.hu/api/publication/35299583},
	author = {Damm, M. and Avella, I. and Merzara, R. and Lucchini, N. and Buldain, J. and Corga, F. and Bouazza, A. and Fahd, S. and Süssmuth, R.D. and Martínez-Freiría, F.},
	doi = {10.1016/j.biochi.2024.07.008},
	journal-iso = {BIOCHIMIE},
	journal = {BIOCHIMIE},
	unique-id = {35299583},
	issn = {0300-9084},
	year = {2024},
	eissn = {1638-6183}
}

@article{MTMT:35282532,
	title = {Crosstalk between protein misfolding and endoplasmic reticulum stress during ageing and their role in age-related disorders},
	url = {https://m2.mtmt.hu/api/publication/35282532},
	author = {Hemagirri, Manisekaran and Chen, Yeng and Gopinath, Subash C. B. and Sahreen, Sumaira and Adnan, Mohd and Sasidharan, Sreenivasan},
	doi = {10.1016/j.biochi.2023.10.019},
	journal-iso = {BIOCHIMIE},
	journal = {BIOCHIMIE},
	volume = {221},
	unique-id = {35282532},
	issn = {0300-9084},
	keywords = {Ageing; Unfolded protein response; Protein misfolding; Proteostasis; Endoplasmic reticulum stress response; Age-related diseases},
	year = {2024},
	eissn = {1638-6183},
	orcid-numbers = {Adnan, Mohd/0000-0002-7080-6822}
}

@article{MTMT:35198681,
	title = {Characterization of the Arabidopsis thaliana chromatin remodeler DEK3 for its interaction with histones and DNA},
	url = {https://m2.mtmt.hu/api/publication/35198681},
	author = {Sundaram, R. and Gandhi, S. and Jonak, C. and Vasudevan, D.},
	doi = {10.1016/j.biochi.2024.07.018},
	journal-iso = {BIOCHIMIE},
	journal = {BIOCHIMIE},
	unique-id = {35198681},
	issn = {0300-9084},
	year = {2024},
	eissn = {1638-6183}
}

@article{MTMT:35185086,
	title = {The mitochondrial translocator protein (TSPO) in Alzheimer's disease: Therapeutic and immunomodulatory functions},
	url = {https://m2.mtmt.hu/api/publication/35185086},
	author = {Fairley, L.H. and Lai, K.O. and Grimm, A. and Eckert, A. and Barron, A.M.},
	doi = {10.1016/j.biochi.2024.07.003},
	journal-iso = {BIOCHIMIE},
	journal = {BIOCHIMIE},
	volume = {224},
	unique-id = {35185086},
	issn = {0300-9084},
	abstract = {The translocator protein (TSPO) has been widely investigated as a PET-imaging biomarker of neuroinflammation and, more recently, as a therapeutic target for the treatment of neurodegenerative disease. TSPO ligands have been shown to exert neuroprotective effects in vivo and in vitro models of Alzheimer's disease (AD), by reducing toxic beta amyloid peptides, and attenuating brain atrophy. Recent transcriptomic and proteomic analyses, and the generation of TSPO-KO mice, have enabled new insights into the mechanistic function of TSPO in AD. Using a multi-omics approach in both TSPO-KO- and TSPO ligand-treated mice, we have demonstrated a key role for TSPO in microglial respiratory metabolism and phagocytosis in AD. In this review, we discuss emerging evidence for therapeutic and immunomodulatory functions of TSPO in AD, and new tools for studying TSPO in the brain. © 2024 The Authors},
	keywords = {Inflammation; DEMENTIA; Mitochondria; Alzheimer's disease; positron emission tomography},
	year = {2024},
	eissn = {1638-6183},
	pages = {120-131}
}

@article{MTMT:35151542,
	title = {Stealing survival: Iron acquisition strategies of Mycobacterium tuberculosis},
	url = {https://m2.mtmt.hu/api/publication/35151542},
	author = {Shankar, G. and Akhter, Y.},
	doi = {10.1016/j.biochi.2024.06.006},
	journal-iso = {BIOCHIMIE},
	journal = {BIOCHIMIE},
	unique-id = {35151542},
	issn = {0300-9084},
	year = {2024},
	eissn = {1638-6183}
}

@article{MTMT:35076764,
	title = {DNA methyltransferase isoforms regulate endothelial cell exosome proteome composition},
	url = {https://m2.mtmt.hu/api/publication/35076764},
	author = {Vasishta, S. and Ammankallu, S. and Umakanth, S. and Keshava, Prasad T.S. and Joshi, M.B.},
	doi = {10.1016/j.biochi.2024.05.010},
	journal-iso = {BIOCHIMIE},
	journal = {BIOCHIMIE},
	volume = {223},
	unique-id = {35076764},
	issn = {0300-9084},
	abstract = {Extrinsic and intrinsic pathological stimuli in vascular disorders induce DNA methylation based epigenetic reprogramming in endothelial cells, which leads to perturbed gene expression and subsequently results in endothelial dysfunction (ED). ED is also characterized by release of exosomes with altered proteome leading to paracrine interactions in vasculature and subsequently contributing to manifestation, progression and severity of vascular complications. However, epigenetic regulation of exosome proteome is not known. Hence, our present study aimed to understand influence of DNA methylation on exosome proteome composition and their influence on endothelial cell (EC) function. DNMT isoforms (DNMT1, DNMT3A, and DNMT3B) were overexpressed using lentivirus in ECs. Exosomes were isolated and characterized from ECs overexpressing DNMT isoforms and C57BL/6 mice plasma treated with 5-aza-2′-deoxycytidine. 3D spheroid assay was performed to understand the influence of exosomes derived from cells overexpressing DNMTs on EC functions. Further, the exosomes were subjected to TMT labelled proteomics analysis followed by validation. 3D spheroid assay showed increase in the pro-angiogenic activity in response to exosomes derived from DNMT overexpressing cells which was impeded by inclusion of 5-aza-2′-deoxycytidine. Our results showed that exosome proteome and PTMs were significantly modulated and were associated with dysregulation of vascular homeostasis, metabolism, inflammation and endothelial cell functions. In vitro and in vivo validation showed elevated DNMT1 and TGF-β1 exosome proteins due to DNMT1 and DNMT3A overexpression, but not DNMT3B which was mitigated by 5-aza-2′-deoxycytidine indicating epigenetic regulation. Further, exosomes induced ED as evidenced by reduced expression of phospho-eNOSser1177. Our study unveils epigenetically regulated exosome proteins, aiding management of vascular complications. © 2024 The Authors},
	keywords = {Adult; Female; Male; ARTICLE; MOUSE; human; disease association; controlled study; nonhuman; animal experiment; in vitro study; Gene Expression; human cell; endothelial dysfunction; in vivo study; endothelium cell; proteomics; proteomics; DNA methylation; DNA methylation; Transforming Growth Factor beta1; cell metabolism; proteome; non insulin dependent diabetes mellitus; gene overexpression; exosome; C57BL 6 mouse; epigenetics; DNA methyltransferase 3B; DNA methyltransferase; Vascular complications; lentivirus; Exosomes; DNA methyltransferase 3A; DNA (cytosine 5) methyltransferase 1; decitabine; umbilical vein endothelial cell},
	year = {2024},
	eissn = {1638-6183},
	pages = {98-115}
}

@article{MTMT:35063716,
	title = {Advances in nuclear proteostasis of metazoans},
	url = {https://m2.mtmt.hu/api/publication/35063716},
	author = {Buggiani, J. and Meinnel, T. and Giglione, C. and Frottin, F.},
	doi = {10.1016/j.biochi.2024.04.006},
	journal-iso = {BIOCHIMIE},
	journal = {BIOCHIMIE},
	unique-id = {35063716},
	issn = {0300-9084},
	abstract = {The proteostasis network and associated protein quality control (PQC) mechanisms ensure proteome functionality and are essential for cell survival. A distinctive feature of eukaryotic cells is their high degree of compartmentalization, requiring specific and adapted proteostasis networks for each compartment. The nucleus, essential for maintaining the integrity of genetic information and gene transcription, is one such compartment. While PQC mechanisms have been investigated for decades in the cytoplasm and the endoplasmic reticulum, our knowledge of nuclear PQC pathways is only emerging. Recent developments in the field have underscored the importance of spatially managing aberrant proteins within the nucleus. Upon proteotoxic stress, misfolded proteins and PQC effectors accumulate in various nuclear membrane-less organelles. Beyond bringing together effectors and substrates, the biophysical properties of these organelles allow novel PQC functions. In this review, we explore the specificity of the nuclear compartment, the effectors of the nuclear proteostasis network, and the PQC roles of nuclear membrane-less organelles in metazoans. © 2024 The Authors},
	keywords = {chaperone; protein degradation; Protein quality control; membrane-less organelle; liquid-liquid phase separation; nuclear proteostasis},
	year = {2024},
	eissn = {1638-6183}
}

@article{MTMT:35000534,
	title = {The molecular crosstalk of the hippo cascade in breast cancer: A potential central susceptibility},
	url = {https://m2.mtmt.hu/api/publication/35000534},
	author = {Parambil, Sulfath Thottungal and Antony, Gisha Rose and Flower, Ajeesh Babu Little and Subhadradevi, Lakshmi},
	doi = {10.1016/j.biochi.2024.03.008},
	journal-iso = {BIOCHIMIE},
	journal = {BIOCHIMIE},
	volume = {222},
	unique-id = {35000534},
	issn = {0300-9084},
	keywords = {metabolism; signal transduction; immune response; breast cancer; hippo signaling; Stemness},
	year = {2024},
	eissn = {1638-6183},
	pages = {132-150},
	orcid-numbers = {Subhadradevi, Lakshmi/0000-0003-1916-0015}
}

@article{MTMT:34956484,
	title = {Renal ischemia and reperfusion impact the purinergic signaling in a vascular bed distant from the injured site},
	url = {https://m2.mtmt.hu/api/publication/34956484},
	author = {Stabile, Jeferson and Neres-Santos, Raquel Silva and Hernandes, Isabela Dorta Molina and Junho, Carolina Victoria Cruz and Alves, Geovane Felippe and Silva, Isabella Cardoso and Carneiro-Ramos, Marcela Sorelli and Furstenau, Cristina Ribas},
	doi = {10.1016/j.biochi.2024.02.003},
	journal-iso = {BIOCHIMIE},
	journal = {BIOCHIMIE},
	volume = {222},
	unique-id = {34956484},
	issn = {0300-9084},
	keywords = {Aorta; adenosine; vascular inflammation; Purinergic signaling; acute kidney injury},
	year = {2024},
	eissn = {1638-6183},
	pages = {37-44},
	orcid-numbers = {Stabile, Jeferson/0000-0002-1671-8522; Carneiro-Ramos, Marcela Sorelli/0000-0003-2666-1280}
}

@article{MTMT:34950028,
	title = {Targeting of CRISPR-Cas12a crRNAs into human mitochondria},
	url = {https://m2.mtmt.hu/api/publication/34950028},
	author = {Nikitchina, Natalia and Ulashchik, Egor and Shmanai, Vadim and Heckel, Anne -Marie and Tarassov, Ivan and Mazunin, Ilya and Entelis, Nina},
	doi = {10.1016/j.biochi.2023.09.006},
	journal-iso = {BIOCHIMIE},
	journal = {BIOCHIMIE},
	volume = {217},
	unique-id = {34950028},
	issn = {0300-9084},
	keywords = {Targeting; crRNA; Cas12a; Human mitochondria; RNA import; MitoCRISPR},
	year = {2024},
	eissn = {1638-6183},
	pages = {74-85},
	orcid-numbers = {Tarassov, Ivan/0000-0001-8763-6703}
}