https://m2.mtmt.hu/ hun 2026-09-20 23:13 JournalArticle 34830192 VALIDATED true Funding Agency and Grant Number: National Research Development and Innovation Office (NRDI) Fund [FK-137582, K-119493, K-135231]; Hungarian Academy of Sciences [BO/00175/21, TKP-6-6/PALY-2021]; Ministry of Culture and Innovation of Hungary from the National Research, Development and Innovation Fund [TKP-6-6/PALY-2021, TKP2021-NVA, NKP-22-4-II-BME-158, NKP-23-5-BME-430, RRF-2.3.1-21-2022-000 15]; European Union Funding text: This research has been supported by the National Research Development and Innovation Office (NRDI) Fund via grant FK-137582 (D.B. W.) , K-119493 (B.G.V.) and K-135231 (B.G.V.) . D.B.W. also acknowledges the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences (BO/00175/21) . The authors acknowledge the Project no. TKP-6-6/PALY-2021 has been implemented with the support provided by the Ministry of Culture and Innovation of Hungary from the National Research, Development and Innovation Fund, financed under the TKP2021-NVA funding scheme. The support of & Uacute;NKP-22-4-II-BME-158 (Z.M.) and & Uacute;NKP-23-5-BME-430 (D.B.W.) has been acknowledged. The research has been supported by Project RRF-2.3.1-21-2022-000 15, which has been implemented with the support provided by the European Union. Part number: 2 0 false 2026-08-27T10:09:58.992+0000 2025-01-20T10:16:25.533+0000 2024-04-30T21:28:51.019+0000 true 10042617 Balogh Weiser Diána /api/author/10042617 Author Balogh Weiser Diána (szerves kémia, anyagtudomány, nanobiotechnológia) true 10042617 2025-01-20T10:16:20.952+0000 2025-01-20T10:16:20.952+0000 2025-01-20T10:16:25.542+0000 true 10058176 Nagyné Tari Emese /api/admin/10058176 Admin Nagyné Tari Emese (SZTE admin5) true 10058176 true false true 24 24 /api/publicationtype/24 PublicationType Folyóiratcikk 1 true 24 JournalArticle true 10000059 Article true 24 24 /api/publicationtype/24 PublicationType Folyóiratcikk 1 true 24 JournalArticle /api/subtype/10000059 Szakcikk SubType Szakcikk (Folyóiratcikk) 101 true 10000059 true 1 /api/category/1 Category Tudományos true 1 Molnár, Zsófia true true /api/journal/2002 REVIEWED INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 0141-8130 1879-0003 true false 2002 false 2002 true 0141-8130 1879-0003 Journal FOREIGN 268 2 131939 131939 11 2024 Human tyrosine hydroxylase (hTH) has key role in the production of catecholamine neurotransmitters. The structure, function and regulation of hTH has been extensively researched area and the possibility of enzyme replacement therapy (ERT) involving hTH through nanocarriers has been raised as well. However, our understanding on how hTH may interact with nanocarriers is still lacking. In this work, we attempted to investigate the immobilization of hTH on magnetic nanoparticles (MNPs) with various surface linkers in quantitative and mechanistic detail. Our results showed that the activity of hTH was retained after immobilization via secondary and covalent interactions as well. The colloidal stability of hTH could be also enhanced proved by Dynamic light scattering and Zeta potential analysis and a homogenous enzyme layer could be achieved, which was investigated by Raman mapping. The covalent attachment of hTH on MNPs via aldehyde or epoxy linkers provide irreversible immobilization and 38.1 % and 16.5 % recovery (ER). The hTH-MNPs catalyst had 25 % ER in average in simulated nasal electrolyte solution (SNES). This outcome highlights the relevance of immobilization applying MNPs as a potential formulation tool of sensitive therapeutic enzymes offering new opportunities for ERT related to neurodegenerative disorders. © 2024 The Author(s) Funding 2040145 /api/funding/2040145 (FK-137582) false true Funding 2040146 /api/funding/2040146 (K119493) false true Funding 2040147 /api/funding/2040147 (K135231) false true Funding 2040148 /api/funding/2040148 (BO/00175/21) false true Funding 2040149 /api/funding/2040149 TKP-6-6/PALY-2021(TKP-6-6/PALY-2021) Támogató: NKFI false true Funding 2040150 /api/funding/2040150 (TKP2021-NVA) false true Funding 2040151 /api/funding/2040151 Nemzeti Gyógyszerkutatási és Fejlesztési Laboratórium (PharmaLab)(RRF-2.3.1-21-2022-00015) Támogató: NKFIH false true true true 2024 true true true false true false GOLD 2026-08-27 true https://doi.org/10.1016/j.ijbiomac.2024.131939 5 0 5 4 1 5 5 3 4 5 5 4 4 4 1 0 5 4 5 4 0 0 0 Folyóiratcikk Journal Article 24 4 Könyvrészlet Chapter in Book 25 1 Könyv Book 23 0 Egyéb konferenciaközlemény Conference paper 31 0 Egyéb konferenciakötet Conference proceedings 32 0 Oltalmi formák Protection forms 26 0 Disszertáció Thesis 28 0 Egyéb Miscellaneous 29 0 Alkotás Achievement 22 0 Kutatási adat Research data 33 0 Folyóiratcikk Journal Article 24 0 0 0 Könyvrészlet Chapter in Book 25 0 0 0 Könyv Book 23 0 0 0 Egyéb konferenciaközlemény Conference paper 31 0 0 0 Egyéb konferenciakötet Conference proceedings 32 0 0 0 Oltalmi formák Protection forms 26 0 0 0 Disszertáció Thesis 28 0 0 0 Egyéb Miscellaneous 29 0 0 0 Alkotás Achievement 22 0 0 0 Kutatási adat Research data 33 0 0 0 2025 0 4 4 4 4 2026 0 1 0 1 0 D1 B nemzetközi false 10095315,10042617 false false false 2024-05-13T07:59:36.107+0000 Alkalmazott Biotechnológia és Élelmiszertudomán... 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(SZTE / GYTK); Gyógyszerészi Kémiai Intézet (SE / GYTK); Kémiai és Környezeti Folyamatmérnöki Tanszék (BME / VBK); Szerves Kémia és Technológia Tanszék (BME / VBK) 9 34 6 10 0 true Language 10002 /api/language/10002 Angol Angol English true 2 true PersonAuthorship 116453422 /api/authorship/116453422 Molnár, Zsófia [Molnár, Zsófia Klára (biokatalízis, mol...), szerző] Szerves Kémia és Technológia Tanszék (BME / VBK) 1 0.1 true false false Author 10061364 /api/author/10061364 Molnár Zsófia Klára (biokatalízis, molekuláris biológia, szerkezeti biológia) Molnár Zsófia Klára true 10061364 true Molnár Zsófia true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 116453423 /api/authorship/116453423 Koplányi, Gábor [Koplányi, Gábor (nanobiotechnológia), szerző] Szerves Kémia és Technológia Tanszék (BME / VBK) 2 0.1 false false false Author 10078139 /api/author/10078139 Koplányi Gábor (nanobiotechnológia) Koplányi Gábor true true Koplányi Gábor true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 116453424 /api/authorship/116453424 Farkas, Réka 3 0.1 false false false Farkas Réka true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 116453425 /api/authorship/116453425 Péli, Noémi [Péli, Noémi (enzimek, fehérjék...), szerző] Szerves Kémia és Technológia Tanszék (BME / VBK) 4 0.1 false false false Author 10095315 /api/author/10095315 Péli Noémi (enzimek, fehérjék, nanobiotechnológia) Péli Noémi true true Péli Noémi true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 116453426 /api/authorship/116453426 Kenéz, Balázs [Kenéz, Balázs (Enzimek, fehérjék...), szerző] Szerves Kémia és Technológia Tanszék (BME / VBK) 5 0.1 false false false Author 10087555 /api/author/10087555 Kenéz Balázs (Enzimek, fehérjék interakcióinak vizsgálata Lab-on-a-Chip rendszerekben) Kenéz Balázs true true Kenéz Balázs true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 116453427 /api/authorship/116453427 Decsi, Balázs [Decsi, Balázs (kémiai tudományok), szerző] 6 0.1 false false false Author 10077243 /api/author/10077243 Decsi Balázs (kémiai tudományok) Decsi Balázs true true Decsi Balázs true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 116453428 /api/authorship/116453428 Katona, Gábor [Katona, Gábor (Gyógyszertechnológia), szerző] Gyógyszertechnológiai és Gyógyszerfelügyeleti I... (SZTE / GYTK) 7 0.1 false false false Author 10045672 /api/author/10045672 Katona Gábor (Gyógyszertechnológia) Katona Gábor true 10045672 true Katona Gábor true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 116453429 /api/authorship/116453429 Balogh, György T. [Balogh, György Tibor (Gyógyszerkémia), szerző] Gyógyszerészi Kémiai Intézet (SE / GYTK); Kémiai és Környezeti Folyamatmérnöki Tanszék (BME / VBK) 8 0.1 false false false Author 10011949 /api/author/10011949 Balogh György Tibor (Gyógyszerkémia) Balogh György Tibor true 10011949 true Balogh György T. true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 116453430 /api/authorship/116453430 Vértessy, Beáta G. [Vértessy, Beáta (Grolmuszné) (Biokémia), szerző] Alkalmazott Biotechnológia és Élelmiszertudomán... 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Targets, 21, p. 167, DOI: 10.1080/14728222.2017.1272581 1 10.1080/14728222.2017.1272581 false true Reference 52443923 /api/reference/52443923 2. Roberts 2013: Mechanisms of tryptophan and tyrosine hydroxylase., IUBMB Life, 65, p. 350, DOI: 10.1002/iub.1144 2 10.1002/iub.1144 false true Reference 52443924 /api/reference/52443924 3. Groaz 2020: Cell-free synthesis of dopamine and serotonin in two steps with purified enzymes., Adv. Biosyst., 2000118, p. 2 3 false true Reference 52443925 /api/reference/52443925 4. Satoh 2012: Engineering of L-tyrosine oxidation in Escherichia coli and microbial production of hydroxytyrosol., Metab. Eng., 14, p. 603, DOI: 10.1016/j.ymben.2012.08.002 4 10.1016/j.ymben.2012.08.002 false true Reference 52443926 /api/reference/52443926 5. Peralta-Yahya 5 false true Reference 52443927 /api/reference/52443927 6. Bueno-Carrasco 2022: Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation., Nat. Commun., 13, p. 1, DOI: 10.1038/s41467-021-27657-y 6 10.1038/s41467-021-27657-y false true Reference 52443928 /api/reference/52443928 7. Almas 1992: Regulation of recombinant human tyrosine hydroxylase isozymes by catecholamine binding and phosphorylation Structurelactivity studies and mechanistic implications., Eur. J. Biochem., 209, p. 249, DOI: 10.1111/j.1432-1033.1992.tb17283.x 7 10.1111/j.1432-1033.1992.tb17283.x false true Reference 52443929 /api/reference/52443929 8. Dickson 2013: Tyrosine hydroxylase. Regulation by feedback inhibition and phosphorylation.Adv. Pharmacol, p. 13, DOI: 10.1016/B978-0-12-411512-5.00002-6 8 10.1016/B978-0-12-411512-5.00002-6 false true Reference 52443930 /api/reference/52443930 9. Lehmann 2006: Differential regulation of the human tyrosine hydroxylase isoforms via hierarchical phosphorylation., J. Biol. Chem., 281, p. 17644, DOI: 10.1074/jbc.M512194200 9 10.1074/jbc.M512194200 false true Reference 52443931 /api/reference/52443931 10. Goodwill 1997: Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases., Nat. Struct. Biol., 4, p. 578, DOI: 10.1038/nsb0797-578 10 10.1038/nsb0797-578 false true Reference 52443932 /api/reference/52443932 11. Hillas 1996: A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines., Biochemistry, 35, p. 6969, DOI: 10.1021/bi9606861 11 10.1021/bi9606861 false true Reference 52443933 /api/reference/52443933 12. Fitzpatrick 1999: Tetrahydropterin-dependent amino acid hydroxylases., Annu. Rev. Biochem., 68, p. 355, DOI: 10.1146/annurev.biochem.68.1.355 12 10.1146/annurev.biochem.68.1.355 false true Reference 52443934 /api/reference/52443934 13. Szigetvari 2019: The quaternary structure of human tyrosine hydroxylase: effects of dystonia-associated missense variants on oligomeric state and enzyme activity., J. Neurochem., 148, p. 291, DOI: 10.1111/jnc.14624 13 10.1111/jnc.14624 false true Reference 52443935 /api/reference/52443935 14. Nagatsu 2019: Human tyrosine hydroxylase in Parkinson's disease and in related disorders., J. Neural Transm., 126, p. 397, DOI: 10.1007/s00702-018-1903-3 14 10.1007/s00702-018-1903-3 false true Reference 52443936 /api/reference/52443936 15. Nygaard 2021: Personalized medicine to improve treatment of dopa-responsive dystonia — a focus on tyrosine hydroxylase deficiency., J. Pers. Med., 11, p. 1, DOI: 10.3390/jpm11111186 15 10.3390/jpm11111186 false true Reference 52443937 /api/reference/52443937 16. Nagatsu 2009: L-dopa therapy for Parkinson's disease: past, present, and future., Parkinsonism Relat. Disord., 1, p. 3, DOI: 10.1016/S1353-8020(09)70004-5 16 10.1016/S1353-8020(09)70004-5 false true Reference 52443938 /api/reference/52443938 17. Willemsen 2010: Tyrosine hydroxylase deficiency: a treatable disorder of brain catecholamine biosynthesis., Brain, 133, p. 1810, DOI: 10.1093/brain/awq087 17 10.1093/brain/awq087 false true Reference 52443939 /api/reference/52443939 18. Pardridge 2005: Tyrosine hydroxylase replacement in experimental Parkinson's disease with transvascular., Gene Ther., 2, p. 129 18 false true Reference 52443940 /api/reference/52443940 19. Bezem 2018: Stabilization of human tyrosine hydroxylase in maltodextrin nanoparticles for delivery to neuronal cells and tissue., Bioconjug. Chem., 29, p. 493, DOI: 10.1021/acs.bioconjchem.7b00807 19 10.1021/acs.bioconjchem.7b00807 false true Reference 52443941 /api/reference/52443941 20. Bezem 2021: Relevance of electrostatics for the interaction of tyrosine hydroxylase with porous silicon nanoparticles., Mol. Pharm., 18, p. 976, DOI: 10.1021/acs.molpharmaceut.0c00960 20 10.1021/acs.molpharmaceut.0c00960 false true Reference 52443942 /api/reference/52443942 21. Bilal 2018: Magnetic nanoparticles as versatile carriers for enzymes immobilization: a review., Int. J. Biol. Macromol., 120, p. 2530, DOI: 10.1016/j.ijbiomac.2018.09.025 21 10.1016/j.ijbiomac.2018.09.025 false true Reference 52443943 /api/reference/52443943 22. Niculescu 2022: Magnetite nanoparticles: synthesis methods – a comparative review., Methods, 199, p. 16, DOI: 10.1016/j.ymeth.2021.04.018 22 10.1016/j.ymeth.2021.04.018 false true Reference 52443944 /api/reference/52443944 23. Wu 2022: Application prospects and opportunities of inorganic nanomaterials for enzyme immobilization in the food-processing industry., Curr. Opin. Food Sci., 47 23 false true Reference 52443945 /api/reference/52443945 24. Bohara 2016: Role of functionalization: strategies to explore potential nano-bio applications of magnetic nanoparticles., RSC Adv., 6, p. 43989, DOI: 10.1039/C6RA02129H 24 10.1039/C6RA02129H false true Reference 52443946 /api/reference/52443946 25. Williams 2017: The application of magnetic nanoparticles in the treatment and monitoring of cancer and infectious diseases., Biosci. Horizons Int. J. Student Res., 10, p. 2017, DOI: 10.1093/biohorizons/hzx009 25 10.1093/biohorizons/hzx009 false true Reference 52443947 /api/reference/52443947 26. Socas-Rodríguez 2020: Process, 8, p. 1140, DOI: 10.3390/pr8091140 26 10.3390/pr8091140 false true Reference 52443948 /api/reference/52443948 27. Yu 2022: Design, preparation, and application of magnetic nanoparticles for food safety analysis: a review of recent advances., J. Agric. Food Chem., 70, p. 46, DOI: 10.1021/acs.jafc.1c03675 27 10.1021/acs.jafc.1c03675 false true Reference 52443949 /api/reference/52443949 28. Busquets 2015: Magnetic nanoparticles cross the blood-brain barrier: when physics rises to a challenge., Nanomaterials, 5, p. 2231, DOI: 10.3390/nano5042231 28 10.3390/nano5042231 false true Reference 52443950 /api/reference/52443950 29. Qiao 2012: Receptor-mediated delivery of magnetic nanoparticles across the blood-brain barrier., ACS Nano, 5, p. 3304, DOI: 10.1021/nn300240p 29 10.1021/nn300240p false true Reference 52443951 /api/reference/52443951 30. Thomsen 2015: Targeted drug delivery to the brain using magnetic nanoparticles., Ther. Deliv., 6, p. 1145, DOI: 10.4155/tde.15.56 30 10.4155/tde.15.56 false true Reference 52443952 /api/reference/52443952 31. Gkountas 2021: Simulation of magnetic nanoparticles crossing through a simplified blood-brain barrier model for glioblastoma multiforme treatment., Comput. Methods Programs Biomed., 212, DOI: 10.1016/j.cmpb.2021.106477 31 10.1016/j.cmpb.2021.106477 false true Reference 52443953 /api/reference/52443953 32. Chen 2022: Blood-brain barrier crossing using magnetic stimulated nanoparticles., J. Control. Release, 345, p. 557, DOI: 10.1016/j.jconrel.2022.03.007 32 10.1016/j.jconrel.2022.03.007 false true Reference 52443954 /api/reference/52443954 33. Morales 2021: Nanomedicines for Brain Drug Delivery 33 false true Reference 52443955 /api/reference/52443955 34. Johnson 2018: Tyrosine hydroxylase as a sentinel for central and peripheral tissue responses in Parkinson's progression: evidence from clinical studies and neurotoxin models., Prog. Neurobiol., 165–167, p. 1, DOI: 10.1016/j.pneurobio.2018.01.002 34 10.1016/j.pneurobio.2018.01.002 false true Reference 52443956 /api/reference/52443956 35. Thoenen 1970: Induction of tyrosine hydroxylase in peripheral and central adrenergic neurones by cold-exposure of rats., Nature, 228, p. 861, DOI: 10.1038/228861a0 35 10.1038/228861a0 false true Reference 52443957 /api/reference/52443957 36. Vermeer 2013: Real-time monitoring of tyrosine hydroxylase activity using a plate reader assay., Anal. Biochem., 432, p. 11, DOI: 10.1016/j.ab.2012.09.005 36 10.1016/j.ab.2012.09.005 false true Reference 52443958 /api/reference/52443958 37. Liu 2011: Aggregation kinetics and ζ-potential of soy protein during fractionation., Food Res. Int., 44, p. 1392, DOI: 10.1016/j.foodres.2011.01.054 37 10.1016/j.foodres.2011.01.054 false true Reference 52443959 /api/reference/52443959 38. Ross 2004: Protein aggregation and neurodegenerative disease., Nat. Med., 10, p. 10, DOI: 10.1038/nm1066 38 10.1038/nm1066 false true Reference 52443960 /api/reference/52443960 39. Baumann 2016: Tyrosine hydroxylase binding to phospholipid membranes prompts its amyloid aggregation and compromises bilayer integrity., Sci. Rep., 6, p. 1, DOI: 10.1038/srep39488 39 10.1038/srep39488 false true Reference 52443961 /api/reference/52443961 40. Flydal 2021: Levalbuterol lowers the feedback inhibition by dopamine and delays misfolding and aggregation in tyrosine hydroxylase., Biochimie, 183, p. 126, DOI: 10.1016/j.biochi.2020.12.002 40 10.1016/j.biochi.2020.12.002 false true Reference 52443962 /api/reference/52443962 41. Kirby 2010: Micro-and Nanoscale Fluid Mechanics: Transport in Microfluidic Devices 41 false true Reference 52443963 /api/reference/52443963 42. Chapman 2018: Industrial applications of enzymes: recent advances, techniques, and outlooks., Catalysts, 8, p. 1, DOI: 10.3390/catal8060238 42 10.3390/catal8060238 false true Reference 52443964 /api/reference/52443964 43. Li 2012: Infrared and Raman spectroscopic studies on iron oxide magnetic nano-particles and their surface modifications., J. Magn. Magn. Mater., 324, p. 1543, DOI: 10.1016/j.jmmm.2011.11.065 43 10.1016/j.jmmm.2011.11.065 false true Reference 52443965 /api/reference/52443965 44. Hagemans 2015: A script to highlight hydrophobicity and charge on protein surfaces., Front. Mol. Biosci., 2, p. 1, DOI: 10.3389/fmolb.2015.00056 44 10.3389/fmolb.2015.00056 false true Reference 52443966 /api/reference/52443966 45. Dolinsky 2004: PDB2PQR: an automated pipeline for the setup of Poisson – Boltzmann electrostatics calculations., Nucleic Acids Res., 32, p. W665, DOI: 10.1093/nar/gkh381 45 10.1093/nar/gkh381 false true Reference 52443967 /api/reference/52443967 46. Jeong 2023: Drug delivery to the brain via the nasal route of administration: exploration of key targets and major consideration factors., J. Pharm. Investig., 53, p. 119, DOI: 10.1007/s40005-022-00589-5 46 10.1007/s40005-022-00589-5 false true Reference 52443968 /api/reference/52443968 47. Castile 2013: Development of in vitro models to demonstrate the ability of PecSys®, an in situ nasal gelling technology, to reduce nasal run-off and drip., Drug Dev. Ind. Pharm., 39, p. 816, DOI: 10.3109/03639045.2012.707210 47 10.3109/03639045.2012.707210 false true Reference 52443969 /api/reference/52443969 48. Bezem 2016: Stable preparations of tyrosine hydroxylase provide the solution structure of the full-length enzyme., Sci. Rep., 6, p. 30390, DOI: 10.1038/srep30390 48 10.1038/srep30390 false true /api/publication/34830192 Molnár Zsófia et al. Immobilization of human tyrosine hydroxylase onto magnetic nanoparticles – A novel formulation of a therapeutic enzyme. (2024) INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 0141-8130 1879-0003 268 2<div class="JournalArticle Publication long-list"> <div class="authors"> <img title="Forrásközlemény" style="float: left" src="/frontend/resources/grid/publication-core-icon.png"> <div class="autype autype0"> <span class="author-name" mtid="10061364"><a href="/gui2/?type=authors&mode=browse&sel=10061364" target="_blank">Molnár Zsófia (<span class="authorship-author-name">Molnár Zsófia Klára</span> <span class="authorAux-mtmt"> biokatalízis, molekuláris biológia, szerkezeti ...</span>) </a> </span> <span class="author-affil"><span title="Budapesti Műszaki és Gazdaságtudományi Egyetem">BME</span>/<span title="Vegyészmérnöki és Biomérnöki Kar">VBK</span>/Szerves Kémia és Technológia Tanszék</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10078139"><a href="/gui2/?type=authors&mode=browse&sel=10078139" target="_blank">Koplányi Gábor (<span class="authorship-author-name">Koplányi Gábor</span> <span class="authorAux-mtmt"> nanobiotechnológia</span>) </a> </span> <span class="author-affil"><span title="Budapesti Műszaki és Gazdaságtudományi Egyetem">BME</span>/<span title="Vegyészmérnöki és Biomérnöki Kar">VBK</span>/Szerves Kémia és Technológia Tanszék</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" >Farkas Réka </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10095315"><a href="/gui2/?type=authors&mode=browse&sel=10095315" target="_blank">Péli Noémi (<span class="authorship-author-name">Péli Noémi</span> <span class="authorAux-mtmt"> enzimek, fehérjék, nanobiotechnológia</span>) </a> </span> <span class="author-affil"><span title="Budapesti Műszaki és Gazdaságtudományi Egyetem">BME</span>/<span title="Vegyészmérnöki és Biomérnöki Kar">VBK</span>/Szerves Kémia és Technológia Tanszék</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10087555"><a href="/gui2/?type=authors&mode=browse&sel=10087555" target="_blank">Kenéz Balázs (<span class="authorship-author-name">Kenéz Balázs</span> <span class="authorAux-mtmt"> Enzimek, fehérjék interakcióinak vizsgálata Lab...</span>) </a> </span> <span class="author-affil"><span title="Budapesti Műszaki és Gazdaságtudományi Egyetem">BME</span>/<span title="Vegyészmérnöki és Biomérnöki Kar">VBK</span>/Szerves Kémia és Technológia Tanszék</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10077243"><a href="/gui2/?type=authors&mode=browse&sel=10077243" target="_blank">Decsi Balázs (<span class="authorship-author-name">Decsi Balázs</span> <span class="authorAux-mtmt"> kémiai tudományok</span>) </a> </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10045672"><a href="/gui2/?type=authors&mode=browse&sel=10045672" target="_blank">Katona Gábor (<span class="authorship-author-name">Katona Gábor</span> <span class="authorAux-mtmt"> Gyógyszertechnológia</span>) </a> </span> <span class="author-affil"><span title="Szegedi Tudományegyetem">SZTE</span>/<span title="Gyógyszerésztudományi Kar">GYTK</span>/Gyógyszertechnológiai és Gyógyszerfelügyeleti Intézet</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10011949"><a href="/gui2/?type=authors&mode=browse&sel=10011949" target="_blank">Balogh György T. (<span class="authorship-author-name">Balogh György Tibor</span> <span class="authorAux-mtmt"> Gyógyszerkémia</span>) </a> </span> <span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Gyógyszerésztudományi Kar">GYTK</span>/Gyógyszerészi Kémiai Intézet; <span title="Budapesti Műszaki és Gazdaságtudományi Egyetem">BME</span>/<span title="Vegyészmérnöki és Biomérnöki Kar">VBK</span>/Kémiai és Környezeti Folyamatmérnöki Tanszék</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10001312"><a href="/gui2/?type=authors&mode=browse&sel=10001312" target="_blank">Vértessy Beáta G. (<span class="authorship-author-name">Vértessy Beáta (Grolmuszné)</span> <span class="authorAux-mtmt"> Biokémia</span>) </a> </span> <span class="author-affil"><span title="Budapesti Műszaki és Gazdaságtudományi Egyetem">BME</span>/<span title="Vegyészmérnöki és Biomérnöki Kar">VBK</span>/Alkalmazott Biotechnológia és Élelmiszertudományi Tanszék</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10042617"><a href="/gui2/?type=authors&mode=browse&sel=10042617" target="_blank">Balogh-Weiser Diána ✉ (<span class="authorship-author-name">Balogh Weiser Diána</span> <span class="authorAux-mtmt"> szerves kémia, anyagtudomány, nanobiotechnológia</span>) </a> </span> <span class="author-affil"><span title="Budapesti Műszaki és Gazdaságtudományi Egyetem">BME</span>/<span title="Vegyészmérnöki és Biomérnöki Kar">VBK</span>/Fizikai Kémia és Anyagtudományi Tanszék; <span title="Budapesti Műszaki és Gazdaságtudományi Egyetem">BME</span>/<span title="Vegyészmérnöki és Biomérnöki Kar">VBK</span>/Szerves Kémia és Technológia Tanszék</span> </div> </div> <div class="title"><a href="/gui2/?mode=browse&params=publication;34830192" target="_blank">Immobilization of human tyrosine hydroxylase onto magnetic nanoparticles – A novel formulation of a therapeutic enzyme</a></div> <div> <span class="journal-title">INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES</span> <span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/0141-8130">0141-8130</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/1879-0003">1879-0003</a>)</span>: <span class="journal-volume">268</span> <span class="journal-issue">2</span> <span class="page"> Paper 131939. 11 p. </span> <span class="year">(2024)</span> </div> <div class="pub-footer"> <span class="language" xmlns="http://www.w3.org/1999/html">Nyelv: Angol | </span> <span class="identifiers"> <span class="id identifier oa_GOLD" title=" Gold "> <a style="color:blue" title="10.1016/j.ijbiomac.2024.131939" target="_blank" href="https://doi.org/10.1016/j.ijbiomac.2024.131939"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="001238090200001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/001238090200001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="85191821440" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-85191821440"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="38692555" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=38692555&dopt=Abstract"> PubMed </a> </span> <span class="id identifier oa_GREEN" title=" Green "> <a style="color:blue" title="35646" target="_blank" href="http://publicatio.bibl.u-szeged.hu/35646"> SZTE Publicatio </a> </span> </span> <OnlyViewableByAuthor><div class="ratings"> <div class="journal-subject">Folyóirat szakterülete: Scopus - Food Science&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;D1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Biochemistry&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Biomaterials&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Molecular Biology&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q2</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Structural Biology&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q2</div> <div class="journal-subject">Gazdaságtudományi Doktori Minősítő Bizottság IXGJO GMB [1901-]&nbsp;&nbsp;&nbsp;B nemzetközi</div> </div></OnlyViewableByAuthor> <div class="publication-citation" style="margin-left: 0.5cm;"> <span title="Nyilvános idézőközlemények összesen, említések nélkül" class="citingPub-count">Nyilvános idéző összesen: 5</span> | Független: 4 | Függő: 1 | Nem jelölt: 0 | WoS jelölt: 3 | Scopus jelölt:&nbsp;4 | WoS/Scopus jelölt:&nbsp;5 | DOI jelölt:&nbsp;5 </div> <div class="mtid"><span class="long-pub-mtid">Közlemény: 34830192</span> | <span class="status-data status-VALIDATED"> Egyeztetett </span> Forrás | <span class="type-subtype">Folyóiratcikk ( Szakcikk ) </span> | <span class="pub-category">Tudományos</span> | <span class="publication-sourceOfData">kézi felvitel</span> </div> <div class="funder"> (FK-137582), (K119493), (K135231), (BO/00175/21), TKP-6-6/PALY-2021(TKP-6-6/PALY-2021) Támogató: NKFI, (TKP2021-NVA), Nemzeti Gyógyszerkutatási és Fejlesztési Laboratórium (PharmaLab)(RRF-2.3.1-21-2022-00015) Támogató: NKFIH </div> <div class="lastModified">Utolsó módosítás: 2025.01.20. 11:16 Nagyné Tari Emese (SZTE admin5) </div> <pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Funding Agency and Grant Number: National Research Development and Innovation Office (NRDI) Fund [FK-137582, K-119493, K-135231]; Hungarian Academy of Sciences [BO/00175/21, TKP-6-6/PALY-2021]; Ministry of Culture and Innovation of Hungary from the National Research, Development and Innovation Fund [TKP-6-6/PALY-2021, TKP2021-NVA, NKP-22-4-II-BME-158, NKP-23-5-BME-430, RRF-2.3.1-21-2022-000 15]...</pre> </div></div>