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1.

001-es BibID:BIBFORM027872
Első szerző:Ayaydin, Ferhan
Cím:Inhibition of serine/threonine-specific protein phosphatases causes premature activation of cdc2MsF kinase at G2/M transition and early mitotic microtubule organisation in alfalfa / Ferhan Ayaydin, Emese Vissi, Tamás Mészáros, Pál Miskolczi, Izabella Kovács, Attila Fehér, Viktor Dombrádi, Ferenc Erdődi, Pál Gergely, Dénes Dudits
Dátum:2000
Megjegyzések:Reversible phosphorylation of serine/threonine residues of cell cycle-regulatory proteins is one of the key molecular mechanisms controlling eukaryotic cell division. In plants, the protein kinase partners (i.e. p34cdc2/CDC28-related kinases) have been extensively studied, while the role of counter-acting protein phosphatases is less well understood. We used endothall (ET) as a cell-permeable inhibitor of serine/threonine-specific protein phosphatases to alter cytological and biochemical characteristics of cell division in cultured alfalfa cells. A high concentration of ET (10 and 50 microM) inhibited both protein phosphatases 1 and 2 (PP1 and PP2A), while a low concentration (1 microM) of ET-treatment primarily reduced the PP2A activity. High concentrations of the inhibitor increased the frequency of hypercondensed early and late prophase chromosomes that could not enter metaphase. In contrast, a low concentration of ET did not interfere with chromosomal events but caused significant alterations in the organisation of microtubules. Exposure of cells to 1 microM ET resulted in disturbance of preprophase band formation, increase in the number of nuclei with prophase microtubule assembly, premature polarisation of the spindle, and abnormal phragmoplast maturation. Under the same conditions, the ET-treated cells exhibited an early increase in cdc2MsF kinase activity. These results suggest that PP2A contributes to the control of mitotic kinase activities and microtubule organisation. Normal chromosome condensation and mitotic progression are dependent on both PP1 and PP2A activities. The presented data support the functional role of protein phosphatases in the co-ordination of chromosomal and microtubule events in dividing plant cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
serine/threonine phosphatases
chromosome condensation
preprophase band
Cdc2-related kinase
endothall
Medicago sativa L
egyetemen (Magyarországon) készült közlemény
Megjelenés:The Plant Journal. - 23 : 1 (2000), p. 85-96. -
További szerzők:Mészáros Tamás (Szeged) Miskolczi Pál (Szeged) Kovács Izabella (Szeged) Fehér Attila (Szeged) Dudits Dénes Vissi Emese (1968-) (biokémikus, biológus) Dombrádi Viktor (1953-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus) Gergely Pál (1947-) (biokémikus)
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2.

001-es BibID:BIBFORM028159
Első szerző:Bakó Éva (biokémikus)
Cím:Purification and partial characterization of protein phosphatases from rat thymus / Éva Bakó, Viktor Dombrádi, Ferenc Erdődi, Lawrence Zumo, Pál Kertai, Pál Gergely
Dátum:1989
ISSN:0167-4889
Megjegyzések:Protein phosphatases assayed with phosphorylase alpha are present in the soluble and particulate fractions of rat thymocytes. Phosphorylase phosphatase activity in the cytosol fraction was resolved by heparin-Sepharose chromatography into type-1 and type-2A enzymes. Similarities between thymocyte and muscle or liver protein phosphatase-1 included preferential dephosphorylation of the beta subunit of phosphorylase kinase, inhibition by inhibitor-2 and retention by heparin-Sepharose. Similarities between thymocyte and muscle or liver protein phosphatase-2A included specificity for the alpha subunit of phosphorylase kinase, insensitivity to the action of inhibitor-2, lack of retention by heparin-Sepharose and stimulation by polycationic macromolecules such as polybrene, protamine and histone H1. Protein phosphatase-1 from the cytosol fraction of thymocytes had an apparent molecular mass of 120 kDa as determined by gel filtration. The phosphatase-2A separated from the cytosol of thymocytes may correspond to phosphatase-2A0, since it was completely inactive (latent) in the absence of polycation and had activity only in the presence of polycations. The apparent molecular mass of phosphatase-2A0 from thymocytes was 240 kDa as determined by gel filtration. The catalytic subunit of thymocyte type-1 protein phosphatase was purified with heparin-Sepharose chromatography followed by gel filtration and fast protein liquid chromatography on Mono Q column. The purified type-1 catalytic subunit exhibited a specific activity of 8.2 U/mg and consisted of a single protein of 35 kDa as judged by SDS-gel electrophoresis. The catalytic subunit of type-2A phosphatase from thymocytes appearing in the heparin-Sepharose flow-through fraction was further purified on protamine-Sepharose, followed by gel filtration. The specific activity of the type-2A catalytic subunit was 2.1 U/mg and consisted of a major protein of 34.5 kDa, as revealed by SDS-gel electrophoresis.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
protein phosphatase-1
protein phosphatase-2A
polycation
heparin-Sepharose
thymocyte
rat
egyetemen (Magyarországon) készült közlemény
Megjelenés:Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1013 : 3 (1989), p. 300-305. -
További szerzők:Kertai Pál (1927-2016) (népegészségügyi szakember) Dombrádi Viktor (1953-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus) Zumo, Lawrence (1966-) Gergely Pál (1947-) (biokémikus)
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3.

001-es BibID:BIBFORM065307
Első szerző:Chen, Emily
Cím:Molecular Insights into the Fungus-Specific Serine/Threonine Protein Phosphatase Z1 in Candida albicans / Emily Chen, Meng S. Choy, Katalin Petrényi, Zoltán Kónya, Ferenc Erdődi, Viktor Dombrádi, Wolfgang Peti, Rebecca Page
Dátum:2016
ISSN:2150-7511
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:mBio 7 : 4 (2016), p. e00872-16. -
További szerzők:Choy, Meng S. Petrényi Katalin (1988-) (Ph.D hallgató) Kónya Zoltán (1986-) (molekuláris biológus, biokémikus) Erdődi Ferenc (1953-) (biokémikus) Dombrádi Viktor (1953-) (biokémikus) Peti, Wolfgang Page, Rebecca
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4.

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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5.

001-es BibID:BIBFORM065083
035-os BibID:(cikkazonosító)e0160965 (WOS)000381374200086 (Scopus)84983761118
Első szerző:Petrényi Katalin (Ph.D hallgató)
Cím:Analysis of Two Putative Candida albicans Phosphopantothenoylcysteine Decarboxylase / Protein Phosphatase Z Regulatory Subunits Reveals an Unexpected Distribution of Functional Roles / Katalin Petrényi, Cristina Molero, Zoltán Kónya, Ferenc Erdődi, Joaquín Ariño, Viktor Dombrádi
Dátum:2016
ISSN:1932-6203
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Plos One. - 11 : 8 (2016), p. e0160965. -
További szerzők:Molero, Cristina Kónya Zoltán (1986-) (molekuláris biológus, biokémikus) Erdődi Ferenc (1953-) (biokémikus) Ariño, Joaquín Dombrádi Viktor (1953-) (biokémikus)
Pályázati támogatás:K-108989
OTKA
K-109249
OTKA
TAMOP 4.2.4.A/2-11-1-2012-0001
TÁMOP
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6.

001-es BibID:BIBFORM076787
035-os BibID:(cikkazonosító)e0211426 (WOS)000457742900024 (Scopus)85060915949
Első szerző:Szabó Krisztina (molekuláris biológus)
Cím:Dissection of the regulatory role for the N-terminal domain in Candida albicans protein phosphatase Z1 / Krisztina Szabó, Zoltán Kónya, Ferenc Erdődi, Ilona Farkas, Viktor Dombrádi
Dátum:2019
ISSN:1932-6203
Megjegyzések:The novel type, fungus specific protein phosphatase Z1 of the opportunistic pathogen, Candida albicans (CaPpz1) has several important physiological roles. It consists of a conserved C-terminal catalytic domain and a variable, intrinsically disordered, N-terminal regulatory domain. To test the function of these domains we modified the structure of CaPpz1 by in vitro mutagenesis. The two main domains were separated, four potential protein binding regions were deleted, and the myristoylation site as well as the active site of the enzyme was crippled by point mutations G2A and R262L, respectively. The in vitro phosphatase activity assay of the bacterially expressed recombinant proteins indicated that the N-terminal domain was inactive, while the C-terminal domain became highly active against myosin light chain substrate. The deletion of the N-terminal 1-16 amino acids and the G2A mutation significantly decreased the specific activity of the enzyme. Complementation of the ppz1 Saccharomyces cerevisiae deletion mutant strain with the different CaPpz1 forms demonstrated that the scission of the main domains, the two point mutations and the N-terminal 1-16 deletion rendered the phosphatase incompetent in the in vivo assays of LiCl tolerance and caffeine sensitivity. Thus our results confirmed the functional role of the N-terminal domain and highlighted the significance of the very N-terminal part of the protein in the regulation of CaPpz1.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Plos One. - 14 : 2 (2019), p. 1-27. -
További szerzők:Kónya Zoltán (1986-) (molekuláris biológus, biokémikus) Erdődi Ferenc (1953-) (biokémikus) Farkas Ilona (1953-) (biokémikus) Dombrádi Viktor (1953-) (biokémikus)
Pályázati támogatás:K-108989
NKFIH
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7.

001-es BibID:BIBFORM028068
Első szerző:Szöőr Balázs (biokémikus)
Cím:Isolation and characterization of the catalytic subunit of protein phosphatase 2A from Neurospora crassa / Balázs Szöőr, Zsigmond Fehér, Éva Bakó, Ferenc Erdődi, Gábor Szabó, Pál Gergely, Viktor Dombrádi
Dátum:1995
ISSN:1096-4959
Megjegyzések:The catalytic subunit of protein phosphatase 2A (PP2Ac) was purified from Neurospora crassa extract by (NH4)2SO4-ethanol precipitation followed by DEAE-Sephacel, heparin-Sepharose, and MonoQ chromatography steps about 900-fold to a specific activity of 1200 U/g with a 2% yield. The apparent M(r) of PP2Ac was estimated to be 35 kDa by gel filtration and 33 kDa by SDS polyacrylamide gel electrophoresis. Half maximal inhibition of PP2Ac was achieved at 0.3 nM okadaic acid, 0.1 nM microcystin-LR, 56 nM cantharidin and 280 nM endothall concentrations. The preparation was completely inhibited by 20 mM NaF, was insensitive to rabbit muscle inhibitor-2, and was specific for the alpha-subunit of rabbit muscle phosphorylase kinase. According to its biochemical properties, N. crassa PP2Ac is very similar to its mammalian counterparts. Antipeptide antibodies raised against the N-terminal and C-terminal ends of human PP2Ac did not cross-react with N. crassa PP2Ac, indicating sequence differences outside the catalytic core of the enzyme.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
protein phosphorylation
protein phosphatase 2A
Neurospora crassa
heparin-Sepharose
okadaic acid
microcystin-LR
cantharidin
endothall
Megjelenés:Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology. - 112 : 3 (1995), p. 515-522. -
További szerzők:Fehér Zsigmond (1949-) (molekuláris genetikus) Szabó Gábor (1927-1996) (biológus, genetikus) Bakó Éva (1958-) (biokémikus) Erdődi Ferenc (1953-) (biokémikus) Gergely Pál (1947-) (biokémikus) Dombrádi Viktor (1953-) (biokémikus)
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