@article{MTMT:34832853,
	title = {Long-timescale atomistic simulations uncover loss-of-function mechanisms of uncharacterized Angiogenin mutants associated with ALS},
	url = {https://m2.mtmt.hu/api/publication/34832853},
	author = {Dewangan, Deeksha and Joshi, Aryaman and Padhi, Aditya K.},
	doi = {10.1016/j.abb.2024.110000},
	journal-iso = {ARCH BIOCHEM BIOPHYS},
	journal = {ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS},
	volume = {756},
	unique-id = {34832853},
	issn = {0003-9861},
	year = {2024},
	eissn = {1096-0384},
	pages = {110000},
	orcid-numbers = {Dewangan, Deeksha/0009-0007-4037-9077; Joshi, Aryaman/0000-0002-9837-673X; Padhi, Aditya K./0000-0001-6732-2547}
}

@article{MTMT:34770344,
	title = {Network of extracellular vesicles surrounding senescent cells},
	url = {https://m2.mtmt.hu/api/publication/34770344},
	author = {Okawa, H. and Tanaka, Y. and Takahashi, A.},
	doi = {10.1016/j.abb.2024.109953},
	journal-iso = {ARCH BIOCHEM BIOPHYS},
	journal = {ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS},
	volume = {754},
	unique-id = {34770344},
	issn = {0003-9861},
	year = {2024},
	eissn = {1096-0384}
}

@article{MTMT:34765474,
	title = {Activation of adenosine A2B receptor alleviates myocardial ischemia-reperfusion injury by inhibiting endoplasmic reticulum stress and restoring autophagy flux},
	url = {https://m2.mtmt.hu/api/publication/34765474},
	author = {He, F. and Wang, F. and Xiang, H. and Ma, Y. and Lu, Q. and Xia, Y. and Zhou, H. and Wang, Y. and Ke, J.},
	doi = {10.1016/j.abb.2024.109945},
	journal-iso = {ARCH BIOCHEM BIOPHYS},
	journal = {ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS},
	volume = {754},
	unique-id = {34765474},
	issn = {0003-9861},
	year = {2024},
	eissn = {1096-0384}
}

@article{MTMT:34761757,
	title = {Peculiarities of ion homeostasis in neurons containing calcium-permeable AMPA receptors},
	url = {https://m2.mtmt.hu/api/publication/34761757},
	author = {Maiorov, S.A. and Kairat, B.K. and Berezhnov, A.V. and Zinchenko, V.P. and Gaidin, S.G. and Kosenkov, A.M.},
	doi = {10.1016/j.abb.2024.109951},
	journal-iso = {ARCH BIOCHEM BIOPHYS},
	journal = {ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS},
	volume = {754},
	unique-id = {34761757},
	issn = {0003-9861},
	year = {2024},
	eissn = {1096-0384}
}

@article{MTMT:34744044,
	title = {Structural determination and characterisation of the CYP105Q4 cytochrome P450 enzyme from Mycobacterium marinum},
	url = {https://m2.mtmt.hu/api/publication/34744044},
	author = {Mohamed, H. and Child, S.A. and Doherty, D.Z. and Bruning, J.B. and Bell, S.G.},
	doi = {10.1016/j.abb.2024.109950},
	journal-iso = {ARCH BIOCHEM BIOPHYS},
	journal = {ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS},
	volume = {754},
	unique-id = {34744044},
	issn = {0003-9861},
	year = {2024},
	eissn = {1096-0384}
}

@article{MTMT:34742354,
	title = {Mechanical and signaling responses of unloaded rat soleus muscle to chronically elevated β-myosin activity},
	url = {https://m2.mtmt.hu/api/publication/34742354},
	author = {Sergeeva, K.V. and Tyganov, S.A. and Zaripova, K.A. and Bokov, R.O. and Nikitina, L.V. and Konstantinova, T.S. and Kalamkarov, G.R. and Shenkman, B.S.},
	doi = {10.1016/j.abb.2024.109961},
	journal-iso = {ARCH BIOCHEM BIOPHYS},
	journal = {ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS},
	volume = {754},
	unique-id = {34742354},
	issn = {0003-9861},
	year = {2024},
	eissn = {1096-0384}
}

@article{MTMT:34736510,
	title = {Dye-decolorizing peroxidase of Thermobifida halotolerance displays complex kinetics with both substrate inhibition and apparent positive cooperativity},
	url = {https://m2.mtmt.hu/api/publication/34736510},
	author = {Pupart, H. and Lukk, T. and Väljamäe, P.},
	doi = {10.1016/j.abb.2024.109931},
	journal-iso = {ARCH BIOCHEM BIOPHYS},
	journal = {ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS},
	volume = {754},
	unique-id = {34736510},
	issn = {0003-9861},
	year = {2024},
	eissn = {1096-0384}
}

@article{MTMT:34632928,
	title = {G protein-coupled estrogen receptor (GPER)/GPR30 forms a complex with the β1-adrenergic receptor, a membrane-associated guanylate kinase (MAGUK) scaffold protein, and protein kinase A anchoring protein (AKAP) 5 in MCF7 breast cancer cells},
	url = {https://m2.mtmt.hu/api/publication/34632928},
	author = {Tutzauer, J. and Serafin, D.S. and Schmidt, T. and Olde, B. and Caron, K.M. and Leeb-Lundberg, L.M.F.},
	doi = {10.1016/j.abb.2024.109882},
	journal-iso = {ARCH BIOCHEM BIOPHYS},
	journal = {ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS},
	volume = {752},
	unique-id = {34632928},
	issn = {0003-9861},
	abstract = {G protein-coupled receptor 30 (GPR30), also named G protein-coupled estrogen receptor (GPER), and the β1-adrenergic receptor (β1AR) are G protein-coupled receptors (GPCR) that are implicated in breast cancer progression. Both receptors contain PSD-95/Discs-large/ZO-1 homology (PDZ) motifs in their C-terminal tails through which they interact in the plasma membrane with membrane-associated guanylate kinase (MAGUK) scaffold proteins, and in turn protein kinase A anchoring protein (AKAP) 5. GPR30 constitutively and PDZ-dependently inhibits β1AR-mediated cAMP production. We hypothesized that this inhibition is a consequence of a plasma membrane complex of these receptors. Using co-immunoprecipitation, confocal immunofluorescence microscopy, and bioluminescence resonance energy transfer (BRET), we show that GPR30 and β1AR reside in close proximity in a plasma membrane complex when transiently expressed in HEK293. Deleting the GPR30 C-terminal PDZ motif (-SSAV) does not interfere with the receptor complex, indicating that the complex is not PDZ-dependent. MCF7 breast cancer cells express GPR30, β1AR, MAGUKs, and AKAP5 in the plasma membrane, and co-immunoprecipitation revealed that these proteins exist in close proximity also under native conditions. Furthermore, expression of GPR30 in MCF7 cells constitutively and PDZ-dependently inhibits β1AR-mediated cAMP production. AKAP5 also inhibits β1AR-mediated cAMP production, which is not additive with GPR30-promoted inhibition. These results argue that GPR30 and β1AR form a PDZ-independent complex in MCF7 cells through which GPR30 constitutively and PDZ-dependently inhibits β1AR signaling via receptor interaction with MAGUKs and AKAP5. © 2024 The Authors},
	keywords = {Female; Female; Humans; metabolism; ARTICLE; signal transduction; MCF-7 CELLS; human; protein localization; controlled study; nonhuman; animal cell; GUANYLATE KINASES; Breast Neoplasms; GUANYLATE KINASE; human cell; breast tumor; carboxy terminal sequence; breast cancer; breast cancer; cancer growth; carrier protein; Carrier Proteins; Receptors, Estrogen; Cyclic AMP-Dependent Protein Kinases; cyclic AMP dependent protein kinase; Estrogen receptor; cancer cell; G protein coupled receptor; G protein coupled receptor; guanine nucleotide binding protein; Receptors, Adrenergic; adrenergic receptor; GTP-Binding Proteins; Receptors, G-Protein-Coupled; PROTEIN COMPLEX; bioluminescence resonance energy transfer; HEK293 Cells; immunofluorescence microscopy; PDZ DOMAIN; PDZ DOMAIN; HEK293 cell line; A Kinase Anchor Proteins; MCF-7 cell line; MCF-7 cell line; GPR30; GPER; beta 1 adrenergic receptor; AKAP5 protein, human; cyclic AMP dependent protein kinase anchoring protein; cyclic AMP dependent protein kinase anchoring protein; G protein coupled receptor 30; coimmunoprecipitation; HEK293S cell line; β1-Adrenergic receptor},
	year = {2024},
	eissn = {1096-0384}
}

@article{MTMT:34624236,
	title = {Knockdown of LOX-1 ameliorates bone quality and generation of type H blood vessels in diabetic mice},
	url = {https://m2.mtmt.hu/api/publication/34624236},
	author = {Qiu, Jumei and Liu, Jing and Tian, Limin and Yu, Jing and Duan, Qidang and Liu, Yaqian and Zhao, Wenshu and Si, Huiling and Lu, Xun and Zhang, Qi},
	doi = {10.1016/j.abb.2023.109870},
	journal-iso = {ARCH BIOCHEM BIOPHYS},
	journal = {ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS},
	volume = {752},
	unique-id = {34624236},
	issn = {0003-9861},
	keywords = {BMP2; Bone quality; Lox-1; Diabetic osteoporosis; TRAcP5b; type H blood vessel},
	year = {2024},
	eissn = {1096-0384}
}

@article{MTMT:34582642,
	title = {A time-resolved Förster resonance energy transfer assay to investigate drug and inhibitor binding to ABCG2},
	url = {https://m2.mtmt.hu/api/publication/34582642},
	author = {Mitchell-White, J.I. and Briggs, D.A. and Mistry, S.J. and Mbiwan, H.A. and Kellam, B. and Holliday, N.D. and Briddon, S.J. and Kerr, I.D.},
	doi = {10.1016/j.abb.2024.109915},
	journal-iso = {ARCH BIOCHEM BIOPHYS},
	journal = {ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS},
	volume = {753},
	unique-id = {34582642},
	issn = {0003-9861},
	abstract = {The human ATP-binding cassette (ABC) transporter, ABCG2, is responsible for multidrug resistance in some tumours. Detailed knowledge of its activity is crucial for understanding drug transport and resistance in cancer, and has implications for wider pharmacokinetics. The binding of substrates and inhibitors is a key stage in the transport cycle of ABCG2. Here, we describe a novel binding assay using a high affinity fluorescent inhibitor based on Ko143 and time-resolved Förster resonance energy transfer (TR-FRET) to measure saturation binding to ABCG2. This binding is displaced by Ko143 and other known ABCG2 ligands, and is sensitive to the addition of AMP-PNP, a non-hydrolysable ATP analogue. This assay complements the arsenal of methods for determining drug:ABCG2 interactions and has the possibility of being adaptable for other multidrug pumps. © 2024 The Author(s)},
	keywords = {PHARMACOLOGY; FRET; ABCG2; multidrug resistance; ABC1 transporter},
	year = {2024},
	eissn = {1096-0384}
}