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1.

001-es BibID:BIBFORM034958
Első szerző:Berényi Sándor (vegyész)
Cím:Recent Developments in the Chemistry of Thebaine and its Transformation Products as Pharmacological Targets / Sándor Berényi, Csaba Csutorás, Attila Sipos
Dátum:2009
Megjegyzések:The most practical synthetic routes to the preparation of as important pharmaceuticals as oxycodone, naloxone, naltrexone, nalbuphine and buprenorphine have utilized the alkaloid, thebaine, as a starting material. This review intends to focus on chemical transformations of morphinans which resulted in morphinandiene derivatives with well-established and novel pharmacological potencies. These chemical transformations were mainly associated with the formation and substitution of the unique diene structure of the ring C of the morphinan backbone.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Currerrent Medicinal Chemistry. - 16 : 25 (2009), p. 3215-3242. -
További szerzők:Csutorás Csaba Sipos Attila (1977-) (vegyész, angol-magyar szakfordító)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM100448
Első szerző:Bíró Linda (vegyész)
Cím:Factors Determining the Metal Ion Binding Ability and Selectivity of Hydroxamate-Based Compounds / Bíró Linda, Buglyó Péter, Farkas Etelka
Dátum:2021
ISSN:0929-8673
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Current Medicinal Chemistry. - 28 : 35 (2021), p. 7209-7237. -
További szerzők:Buglyó Péter (1965-) (vegyész) Farkas Etelka (1948-) (vegyész) Buglyó Péter (1965-) (vegyész)
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Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM107634
035-os BibID:(Wos)000724573400005 (Scopus)85104557504
Első szerző:Chaves, Sílvia
Cím:Recent Multi-target Approaches on the Development of Anti- Alzheimer's Agents Integrating Metal Chelation Activity / Sílvia Chaves, Katalin Várnagy, M. Amélia Santos
Dátum:2021
ISSN:0929-8673
Megjegyzések:Alzheimer's disease (AD) is the most common and severe age-dependent neurodegenerative disorder, worldwide. Notwithstanding the large amount of research dedicated to both the elucidation of this pathology and the development of an effective drug, the multifaceted nature and complexity of the disease are certainly a rationale for the absence of cure so far. Current available drugs are used, mainly, to compensate the decline of the neurotransmitter acetylcholine by acetylcholinesterase (AChE) inhibition, though they only provide temporary symptomatic benefits and cannot stop AD progression. Although the multiple factors that contribute to trigger AD onset and progression are not yet fully understood, several pathological features and underneath pathways have been recognized to contribute to its pathology, such as metal dyshomeostasis, protein misfolding, oxidative stress and neurotransmitter deficiencies, some of them being interconnected. Thus, there is a widespread recent interest in the development of multitarget-directed ligands (MTDLs) for simultaneous interaction with several pathological targets of AD. In this review, a selection of the most recent reports (2016-up to present) on metal chelators of MTDLs with multifunctionalities is presented. These compounds enable the hitting of several AD targets or pathways, such as modulation of specific biometal ions (e.g. Cu, Fe, Zn) and of protein misfolding (?-amyloid and tau protein), anti-oxidant activity and AChE inhibition. The properties found for these hybrids are discussed in comparison with the original reference compounds, some MTDLs being outlined as leading compounds for pursuing future studies in view of efficient potential applications in AD therapy.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Alzheimer's disease
multitarget drugs
biometals
metal chelators
AChE inhibitors
antioxidant properties
drug repositioning
Megjelenés:Current Medicinal Chemistry. - 28 : 35 (2021), p. 7247-7277. -
További szerzők:Várnagy Katalin (1961-) (vegyész) Santos, M. Amélia
Pályázati támogatás:OTKA-115480
OTKA
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4.

001-es BibID:BIBFORM067615
Első szerző:Máthé Csaba (biológus)
Cím:Cellular effects of cylindrospermopsin (Cyanobacterial Alkaloid Toxin) and its potential medical consequences / Máthé C., M-Hamvas M., Garda T., Beyer D., Vasas G.
Dátum:2017
ISSN:0929-8673 1875-533X
Megjegyzések:Cylindrospermopsin (CYN) is a tricyclic guanidino derivative, an alkaloid toxin produced by several cyanobacterial genera. It alters cellular functioning in eukaryotes, including animal and plant organisms. Over the past decades, more and more evidence shows its potential hazardous effects on animal and human health. In this review, we give a critical survey and interpretation of data currently available on its biochemical and consequently, cellular effects. CYN is considered to be a cytotoxin. Several reports suggest that it is a potent inhibitor of eukaryotic protein synthesis, though the exact mechanisms are far from not completely understood. Here we show that the biochemical changes induced by CYN suggest are complex, and possibly involving multiple modes of action. Glutathione metabolism and pyrimidine nucleotide synthesis is affected besides the proposed protein synthesis inhibition. Biochemical alterations lead to the following cellular/subcellular alterations both in animals and plants: (i) changes in cell division rates due to perturbations in chromatin and cytoskeleton; (ii) perturbations of structure and functioning of endomembranes including endoplasmic reticulum; (iii) general metabolic alterations leading to genotoxicity and programmed cell death/apoptosis. The underlying mechanisms and possible health consequences are discussed.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Cylindrospermopsin
cyanobacteria,
protein synthesis
cell cycle
endomembranes
cytoskeleton
programmed cell death
Megjelenés:Current Medicinal Chemistry 24 : 1 (2017), p. 91-109. -
További szerzők:Mikóné Hamvas Márta (1963-) (biológus) Garda Tamás (1990-) (biológus) Beyer Dániel (1982-) (molekuláris biológus) Vasas Gábor (1975-) (biológus-vegyész)
Pályázati támogatás:K120638
OTKA
K119647
OTKA
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5.

001-es BibID:BIBFORM006384
Első szerző:Somsák László (vegyész)
Cím:New inhibitors of glycogen phosphorylase as potential antidiabetic agents / L. Somsák, K. Czifrák, M. Tóth, É. Bokor, E. D. Chrysina, K.-M. Alexacou, J. M. Hayes, C. Tiraidis, E. Lazoura, D. D. Leonidas, S. E. Zographos, N. G. Oikonomakos
Dátum:2008
ISSN:0929-8673
Megjegyzések:The protein glycogen phosphorylase has been linked to type 2 diabetes, indicating the importance of this target to human health. Hence, the search for potent and selective inhibitors of this enzyme, which may lead to antihyperglycaemic drugs, has received particular attention. Glycogen phosphorylase is a typical allosteric protein with five different ligand binding sites, thus offering multiple opportunities for modulation of enzyme activity. The present survey is focused on recent new molecules, potential inhibitors of the enzyme. The biological activity can be modified by these molecules through direct binding, allosteric effects or other structural changes. Progress in our understanding of the mechanism of action of these inhibitors has been made by the determination of high-resolution enzyme inhibitor structures (both muscle and liver). The knowledge of the three-dimensional structures of protein-ligand complexes allows analysis of how the ligands interact with the target and has the potential to facilitate structure-based drug design. In this review, the synthesis, structure determination and computational studies of the most recent inhibitors of glycogen phosphorylase at the different binding sites are presented and analyzed.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
glycogen phosphorylase
inhibitor
type 2 diabetes
structure-based drug design
antidiabetic agent
Megjelenés:Current Medicinal Chemistry. - 15 : 28 (2008), p. 2933-2983. -
További szerzők:Czifrák Katalin (1978-) (vegyész) Tóth Marietta (1974-) (vegyész) Bokor Éva (1982-) (vegyész) Chrysina, Evangelia D. Alexacou, Kyra-Melinda Hayes, Joseph M. Tiraidis, Costantinos Lazoura, E. Leonidas, Demetres D. Zographos, Spyros E. Oikonomakos, George N.
Internet cím:elektronikus változat
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6.

001-es BibID:BIBFORM107637
035-os BibID:(Scopus)85161610965 (WoS)001028904000001
Első szerző:Sóvágó Imre (vegyész)
Cím:Interactions of copper(II) and zinc(II) ions with the peptide fragments of proteins related to neurodegenerative disorders: similarities and differences / Imre Sóvágó, Katalin Várnagy, Csilla Kállay, Ágnes Grenács
Dátum:2023
ISSN:0929-8673
Megjegyzések:Metal binding ability and coordination modes of the copper(II) and zinc(II) complexes of various peptide fragments of prion, amyloid-beta and tau proteins are summarized in this review. Imidazole-N donors are the primary metal binding sites of all three proteins but the difference in the location of these residues and the presence or absence of other coordinating side chains results in significant differences in the complex formation processes. The presence of macrochelates and the possibility of the formation of multi-copper complexes is the most characteristic for prion fragments. Amyloid-? can form high stability complexes with both copper(II) and zinc(II) ions but the preferred binding sites are different for the two metal ions. Similar observations have been obtained for the tau fragments but the metal ion selectivity of the various fragments is even more pronounced. In addition to the complex formation, copper(II) ions can play an important role in the various oxidative reactions of peptides. Results of the metal ion catalyzed oxidation of peptide fragments of prion, amyloid-? and tau proteins are also summarized. Amino acid side chain oxidation (mostly methionine, histidine and aspartic acid) and protein fragmentations are the most common consequences of this process.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Current Medicinal Chemistry. - 30 : 36 (2023), p. 4050-4071. -
További szerzők:Várnagy Katalin (1961-) (vegyész) Kállay Csilla (1978-) (vegyész) Grenács Ágnes (1988-) (vegyész, analitikus)
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