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1.

001-es BibID:BIBFORM028259
Első szerző:Dombrádi Viktor (biokémikus)
Cím:Purification and characterization of glycogen phosphorylase from Drosophila melanogaster / V. Dombrádi, J. Hajdú, P. Friedrich, G. Bot
Dátum:1985
Megjegyzések:Glycogen phosphorylase View the MathML source was purified from Drosophila melanogaster with a yield of 15% by low speed centrifugation, DEAE-Sepharose CL-6B chromatography and affinity chromatography on 5-AMP-Sepharose 4B. The preparation proved to be homogeneous by SDS-polyacrylamide gel electrophoresis and showed a subunit molecular weight of 95,000. Gel filtration of the native enzyme on Sephacryl S-300 revealed a molecular weight of 176,000 suggesting that phosphorylase View the MathML source is a dimer composed of two identical subunits. The fruit fly phosphorylase View the MathML source has a maximal specific activity of 36 U/mg when assayed in the direction of glycogen synthesis. It requires AMP for activity (View the MathML source mM, Hill coefficient: 1.8). The View the MathML source for glycogen is 0.4% and the View the MathML source for glucose-1-phosphate is 20 mM (Hill coefficient: 1.3). The enzyme is inhibited by glucose, UDPG, caffeine, glucose-6-phosphate, ATP and IMP.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Drosophila melanogaster
glycogen phosphorylase b
isolation
molecular weight
kinetic properties
egyetemen (Magyarországon) készült közlemény
Megjelenés:Insect Biochemistry. - 15 : 3 (1985), p. 403-410. -
További szerzők:Hajdu János Friedrich Péter Bot György (1917-1998) (biokémikus, vegyész)
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2.

001-es BibID:BIBFORM028256
Első szerző:Dombrádi Viktor (biokémikus)
Cím:Regulation of glycogen phosphorylase in Drosophila melanogaster by reversible phosphorylation-dephosphorylation / V. Dombrádi, P. Dévay, P. Friedrich, G. Bot
Dátum:1986
Megjegyzések:Homogeneous glycogen phosphorylase b purified from Drosophila melanogaster was activated by phosphorylase kinase isolated from rabbit skeletal muscle. The activation generated phosphorylase a containing 1.1 ± 0.1 phosphoryl group per subunit. Phosphorylase a prepared in this way had a s20w = 8.5S and a subunit molecular mass of 95,000. It could be inactivated (dephosphorylated) by the catalytic subunit of rabbit muscle protein phosphatase-1. The activation-inactivation of phosphorylase by endogenous phosphorylase kinase and phosphatase was also demonstrated in crude homogenates of D. melanogaster. The main protein phosphorylated in the fruit fly homogenate comigrated with purified Drosophila phosphorylse a in sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis. Phosphate incorporation into this protein was correlated with phosphorylase activation. Phosphorylase was partially purified from flies fed on [32P]phosphate by 5-AMP Sepharose affinity chromatography. SDS gel electrophoresis followed by autoradiography revealed that it was phosphorylated in vivo. 20 ± 5% of the total phosphorylase was found to be in the active a form in the anaesthetized insects. Our findings indicate that Drosophila phosphorylase undergoes reversible phosphorylation-dephosphorylation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Drosophila melanogaster
protein phosphorylation
regulatioin
glycogen phosphorylase a
glycogen phosphorylase b
egyetemen (Magyarországon) készült közlemény
Megjelenés:Insect Biochemistry. - 16 : 3 (1986), p. 557-565. -
További szerzők:Dévay Piroska Friedrich Péter Bot György (1917-1998) (biokémikus, vegyész)
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3.

001-es BibID:BIBFORM028164
Első szerző:Dombrádi Viktor (biokémikus)
Cím:Regulation of phosphorylase kinase in Drosophila melanogaster / V. Dombrádi, V. Risnik, F. Erdődi, G. Bot, P. Friedrich
Dátum:1987
Megjegyzések:The regulation of phosphorylase kinase has been studied in crude homogenates of adult flies and larval brains of Drosophila melanogaster. The kinase has an alkaline pH optimum (about pH 8.6), is inhibited by an excess of Mg2+ and is stimulated by Ca2+ in the homogenates. Incubation of larval brains with octopamine, especially in the presence of theophylline, or with forskolin, markedly elevated the level of cAMP with no, or marginal, activation of phosphorylase. In contrast, Ca2+ in the presence of A-23187 caused a two-fold increase in phosphorylase View the MathML source. The mutant dunceM11 flies contain six to seven times as much cAMP as the wild type Canton-S flies and have a somewhat elevated phosphorylase View the MathML source level.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
phosphorylase kinase
glycogen phosphorylase
calcium ion
cyclic AMP
Drosophila
egyetemen (Magyarországon) készült közlemény
Megjelenés:Insect Biochemistry. - 17 : 4 (1987), p. 579-585. -
További szerzők:Risnik V. Friedrich Péter Erdődi Ferenc (1953-) (biokémikus) Bot György (1917-1998) (biokémikus, vegyész)
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4.

001-es BibID:BIBFORM083629
035-os BibID:(WoS)000518872600011 (Scopus)85078049471 (PMID)31870846
Első szerző:Jin, Jiayi
Cím:Weaponisation 'on the fly' : convergent recruitment of knottin and defensin peptide scaffolds into the venom of predatory assassin flies / Jiayi Jin, Akello J. Agwa, G. Tibor Szanto, Agota Csóti, Gyorgy Panyi, Christina I. Schroeder, Andrew A. Walker, Glenn F. King
Dátum:2020
ISSN:0965-1748
Megjegyzések:Many arthropod venom peptides have potential as bioinsecticides, drug leads, and pharmacological tools due to their specific neuromodulatory functions. Assassin flies (Asilidae) are a family of predaceous dipterans that produce a unique and complex peptide-rich venom for killing insect prey and deterring predators. However, very little is known about the structure and function of their venom peptides. We therefore used an E. coli periplasmic expression system to express four disulfide-rich peptides that we previously reported to exist in venom of the giant assassin fly Dolopus genitalis. After purification, each recombinant peptide eluted from a C18 column at a position closely matching its natural counterpart, strongly suggesting adoption of the native tertiary fold. Injection of purified recombinant peptides into blowflies (Lucilia cuprina) and crickets (Acheta domestica) revealed that two of the four recombinant peptides, named rDg3b and rDg12, inhibited escape behaviour in a manner that was rapid in onset (<1 min) and reversible. Homonuclear NMR solution structures revealed that rDg3b and rDg12 adopt cystine-stabilised α/ß defensin and inhibitor cystine knot folds, respectively. Although the closest known homologues of rDg3b at the level of primary structure are dipteran antimicrobial peptides such as sapecin and lucifensin, a DALI search showed that the tertiary structure of rDg3b most closely resembles the KV11.1-specific α-potassium channel toxin CnErg1 from venom of the scorpion Centruroides noxius. This is mainly due to the deletion of a large, unstructured loop between the first and second cysteine residues present in Dg3b homologues from non-asiloid, but not existing in asiloid, species. Patch-clamp electrophysiology experiments revealed that rDg3b shifts the voltage-dependence of KV11.1 channel activation to more depolarised potentials, but has no effect on KV1.3, KV2.1, KV10.1, KCa1.1, or the Drosophila Shaker channel. Although rDg12 shares the inhibitor cystine knot structure of many gating modifier toxins, rDg12 did not affect any of these KV channel subtypes. Our results demonstrate that multiple disulfide-rich peptide scaffolds have been convergently recruited into asilid and other animal venoms, and they provide insight into the molecular evolution accompanying their weaponisation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Diptera
Dolopus genitalis
Ion channel
K(V)11.1 (hERG)
Toxin
Megjelenés:Insect Biochemistry and Molecular Biology. - 118 (2020), p. 1-12. -
További szerzők:Agwa, Akello J. Szántó Gábor Tibor (1980-) (vegyész) Csóti Ágota (1989-) (biológus) Panyi György (1966-) (biofizikus) Schroeder, Christina I. Walker, Andrew A. King, Glenn F.
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5.

001-es BibID:BIBFORM051766
035-os BibID:PMID:24727027
Első szerző:Kerekes Éva (Ph.D hallgató)
Cím:Functional analysis of the glycogen binding subunit CG9238/Gbs-70E of protein phosphatase 1 in Drosophila melanogaster / Éva Kerekes, Endre Kókai, Ferenc Sándor Páldy, Viktor Dombrádi
Dátum:2014
ISSN:0965-1748
Megjegyzések:The product of the CG9238 gene that we termed glycogen binding subunit 70E (Gbs-70E) was characterized by biochemical and molecular genetics methods. The interaction between Gbs-70E and all catalytic subunits of protein phosphatase 1 (Pp1-87B, Pp1-9C, Pp1-96A and Pp1-13C) of Drosophila melanogaster was confirmed by pairwise yeast two-hybrid tests, co-immunoprecipitation and pull down experiments. The binding of Gbs-70E to glycogen was demonstrated by sedimentation analysis. With RT-PCR we found that the mRNAs coding for the longer Gbs-70E PB/PC protein were expressed in all developmental stages of the fruit flies while the mRNA for the shorter Gbs-70E PA was restricted to the eggs and the ovaries of the adult females. The development specific expression of the shorter splice variant was not conserved in different Drosophila species. The expression level of the gene was manipulated by P-element insertions and gene deletion to analyze the functions of the gene product. A small or moderate reduction in the gene expression resulted in no significant changes, however, a deletion mutant expressing very low level of the transcript lived shorter and exhibited reduced glycogen content in the imagos. In addition, the gene deletion decreased the fertility of the fruit flies. Our results prove that Gbs-70E functions as the glycogen binding subunit of protein phosphatase 1 that regulates glycogen content and plays a role in the development of eggs in D. melanogaster.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
CG9238
Drosophila melanogaster
Fertility
Gbs-70E
Glycogen binding targeting subunit
Glycogen content
Longevity
Protein phosphatase 1
Doktori iskola
Megjelenés:Insect Biochemistry and Molecular Biology. - 49 (2014), p. 70-79. -
További szerzők:Kókai Endre (1971-) (biokémikus, biológus) Páldy Ferenc Sándor Dombrádi Viktor (1953-) (biokémikus)
Pályázati támogatás:TÁMOP-4.2.2/B-10/1-2010-0024
TÁMOP
Molekuláris Orvostudomány Doktori Iskola
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