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1.

001-es BibID:BIBFORM027855
Első szerző:Alexa Anita (MTA)
Cím:The phosphorylation state of threonine-220, a uniquely phosphatase-sensitive protein kinase A site in microtubule-associated protein MAP2c, regulates microtubule binding and stability / A. Alexa, G. Schmidt, P. Tompa, S. Ogueta, J. Vázquez, P. Kulcsár, J. Kovács, V. Dombrádi, P. Friedrich
Dátum:2002
ISSN:0006-2960
Megjegyzések:Phosphorylation of microtubule-associated protein 2 (MAP2) has a profound effect on microtubule stability and organization. In this work a consensus protein kinase A (PKA) phosphorylation site, T(220), of juvenile MAP2c is characterized. As confirmed by mass spectrometry, this site can be phosphorylated by PKA but shows less than average reactivity among the 3.5 +/- 0.5 phosphate residues incorporated into the protein. In contrast, T(220) is uniquely sensitive to dephosphorylation: three major Ser/Thr protein phosphatases, in the order of efficiency PP2B > PP2A(c) > PP1(c), remove this phosphate group first. MAP2c specifically dephosphorylated at this site binds and stabilizes microtubules stronger than either fully phosphorylated or nonphosphorylated MAP2c. Phosphorylation of this site also affects proteolytic sensitivity of MAP2c, which might represent a further level of control in this system. Thus, the phosphorylation state of T(220) may be a primary determinant of microtubule function.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
threonine-220
protein kinase A
MAP2c
Megjelenés:Biochemistry. - 41 : 41 (2002), p. 12427-12435. -
További szerzők:Schmidt, G. (MTA) Tompa Péter Ogueta, S. Vázquez, J. Kulcsár P. (MTA) Kovács J. (ELTE) Friedrich Péter Dombrádi Viktor (1953-) (biokémikus)
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2.

001-es BibID:BIBFORM030133
Első szerző:Bíró Judit (Szeged)
Cím:The histone phosphatase inhibitory property of plant nucleosome assembly protein-related proteins (NRPs) / Judit Bíró, Ilona Farkas, Mónika Domoki, Krisztina Ötvös, Sándor Bottka, Viktor Dombrádi, Attila Fehér
Dátum:2012
ISSN:0981-9428
Megjegyzések:SET/I(2)(PP2A), a member of the family of nucleosome assembly proteins (NAPs), has been previously described as a multifunctional protein inhibiting protein phosphatase 2A (PP2A)-mediated histone H3((pSer10)) dephosphorylation during the heat shock response in animal cells. In the present work we demonstrate that its plant orthologs, designated as NAP-related proteins (NRPs), have a similar in vitro biochemical activity and interact with PP2A and histone H3((pSer10))in vivo. Although heat shock gene promoters were found to be associated with histone H3((pSer10))-marked chromatin following a high temperature treatment, heat shock gene expression was not affected in NRP-deficient mutant Arabidopsis thaliana (L.) plantlets. These observations indicate that NRPs are potential regulators of histone dephosphorylation in plants, but they are dispensable for gene expression reorganization in response to heat shock.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Plant Physiology And Biochemistry. - 52 (2012), p. 162-168. -
További szerzők:Domoki Mónika (Szeged) Ötvös Krisztina (Szeged) Bottka Sándor Fehér Attila (Szeged) Farkas Ilona (1953-) (biokémikus) Dombrádi Viktor (1953-) (biokémikus)
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3.

001-es BibID:BIBFORM066241
Első szerző:Boratkó Anita (biokémikus, molekuláris biológus)
Cím:Regulation of merlin by protein phosphatase 1-TIMAP and EBP50 in endothelial cells / Anita Boratkó, Margit Péter, Csilla Csortos
Dátum:2017
Megjegyzések:Merlin (moesin-ezrin-radixin like protein), the product of neurofibromatosis type 2 gene, was primarily recognized as a tumor suppressor, but it also functions as a membrane-cytoskeletal linker and regulator of multiple signaling pathways. The activity and localization of merlin is regulated by head to tail folding that is controlled by phosphorylation of the Ser518 side chain. Merlin localizes in the nucleus when the Ser518 side chain is not phosphorylated, while the phosphorylated form is present in the cytoplasm and the plasma membrane. In this work interactions and their impact on the subcellular localization and phosphorylation state of the Ser518 side chain of merlin were investigated in endothelial cells. It is shown that merlin (dephospho-Ser518 form) interacts in the nucleus of endothelial cells with the scaffolding protein EBP50, a member of the Na+/H+exchanger regulatory factor family. Upon EBP50 depletion, merlin translocated from the nucleus, suggesting that binding of merlin to EBP50 is critical in the nuclear localization of merlin. Along with the translocation, the phosphorylation level of phospho-Ser518-merlin was increased in EBP50 depleted cells. TIMAP (TGF?-inhibited membrane-associated protein), a type 1 protein phosphatase (PP1) regulatory subunit, was newly recognized as an interacting partner for merlin. Domain mapping using truncated mutant forms in GST pull down revealed that the N-terminal half of TIMAP (aa 1-290) and the FERM domain of merlin are the regions responsible for the interaction.The catalytic subunit of PP1 (PP1c) was present in all merlin-TIMAP pull down or immunoprecipitation samples demonstrating that merlin actually interacts with the PP1c-TIMAP holoenzyme. On the other hand, from TIMAP depleted cells, without its targeting protein, PP1c could not bind to merlin. Also, when the phosphatase activity of PP1c-TIMAP was inhibited either with depletion of TIMAP or by treatment of the cells with specific PP1 inhibitor, there was an increase in the amount of phospho-Ser518 form of merlin in the membrane of the cells. These data strongly suggest that the PP1c-TIMAP- complex dephosphorylates phospho-Ser518-merlin. ECIS measurements indicate that phospho-merlin accelerates in vitro wound healing of the endothelial monolayer. In conclusion, in endothelial cells, EBP50 is required for the nuclear localization of merlin and the PP1c-TIMAP holoenzyme plays an important role in the dephosphorylation of merlin on its Ser518 side chain, which influence cell migration and proliferation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
EBP50
Endothelial cells
Merlin
Protein phosphatase 1
TIMAP
Megjelenés:The International Journal of Biochemistry and Cell Biology 82 (2017), p. 10-17. -
További szerzők:Péter Margit (1987-) (Ph.D. hallgató) Csortos Csilla (1956-) (biokémikus)
Pályázati támogatás:PD116262
OTKA
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4.

001-es BibID:BIBFORM062307
Első szerző:Boratkó Anita (biokémikus, molekuláris biológus)
Cím:TIMAP-protein phosphatase 1-complex controls endothelin-1 production via ECE-1 dephosphorylation / Anita Boratkó, Zoltán Veréb, Goran Petrovski, Csilla Csortos
Dátum:2016
ISSN:1357-2725
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:International Journal Of Biochemistry & Cell Biology 73 (2016), p. 11-18. -
További szerzők:Veréb Zoltán (1980-) (immunológus, mikrobiológus, molekuláris biológus) Petrovski, Goran (1975-) (orvos) Csortos Csilla (1956-) (biokémikus)
Pályázati támogatás:TÁMOP-4.2.2.A-11/1/KONV-2012-0025
TÁMOP
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5.

001-es BibID:BIBFORM061016
Első szerző:Boratkó Anita (biokémikus, molekuláris biológus)
Cím:Elongation factor-1A1 is a novel substrate of the protein phosphatase 1-TIMAP complex / Anita Boratkó, Margit Péter, Zsófia Thalwieser, Előd Kovács, Csilla Csortos
Dátum:2015
ISSN:1357-2725
Megjegyzések:TIMAP (TGF- inhibited membrane associated protein) is a protein phosphatase 1 (PP1) regulatory subunit highly abundant in endothelial cells and it is involved in the maintenance of pulmonary endothelial barrier function. It localizes mainly in the plasma membrane, but it is also present in the nuclei and cytoplasm. Direct interaction of TIMAP with the eukaryotic elongation factor 1 A1 (eEF1A1) is shown by pull-down, LC-MS/MS, Far-Western and immunoprecipitations. In connection with the so called moonlighting functions of the elongation factor, eEF1A is thought to establish protein-protein interactions through a transcription-dependent nuclear export motif, TD-NEM, and to aid nuclear export of TD-NEM containing proteins. We found that a TD-NEM-like motif of TIMAP has a critical role in its specific binding to eEF1A1. However, eEF1A1 is not or not exclusively responsible for the nuclear export of TIMAP. On the contrary, TIMAP seems to regulate membrane localization of eEF1A1 as the elongation factor co-localized with TIMAP in the plasma membrane fraction of control endothelial cells, but it has disappeared from the membrane in TIMAP depleted cells. It is demonstrated that membrane localization of eEF1A1 depends on the phosphorylation state of its Thr residue(s); and ROCK phosphorylated eEF1A1 is a novel substrate for TIMAP-PP1 underlining the complex regulatory role of TIMAP in the endothelium. The elongation factor seems to be involved in the regulation of endothelial cell attachment and spreading as silencing of eEF1A1 positively affected these processes which were monitored by transendothelial resistance measurements.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Endothelial cell
eEF1A1
Protein phosphatase 1
TIMAP
Megjelenés:International Journal Of Biochemistry & Cell Biology 69 (2015), p. 105-113. -
További szerzők:Péter Margit (1987-) (Ph.D. hallgató) Thalwieser Zsófia (1993-) (biológus) Kovács Előd Csortos Csilla (1956-) (biokémikus)
Pályázati támogatás:TÁMOP-4.2.2.A-11/1/KONV-2012-0025
TÁMOP
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6.

001-es BibID:BIBFORM028260
Első szerző:Dévay Piroska
Cím:Differences in protein phosphorylation in vivo and in vitro between wild type and dunce mutant strains of Drosophila melanogaster / Piroska Dévay, Magda Solti, István Kiss, Viktor Dombrádi, Péter Friedrich
Dátum:1984
Megjegyzések:The protein phosphorylation patterns of wild type and dunce mutant strains of Drosophila melanogaster, as detected by sodium dodecylsulfate-gel electrophoresis and autoradiography, have been compared. After labelling in vivo with 32Pi or in vitro in homogenates with [gamma-32P]ATP, radioactive bands at and above apparent polypeptide mol. wt approximately 110,000 were more pronounced in dunce fly heads than in wild type heads. When labelling in vitro, in dunceM11 there appeared a radioactive band at apparent mol. wt approximately equal to 53,000 that was faintly visible in the wild strain. The same band could be intensified in both strains by adding cyclic AMP to the homogenate or by performing homogenization in the presence of theophylline. The data suggest that the mol. wt approximately equal to 53,000 protein is a substrate for cyclic AMP-dependent protein kinase.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
protein phosphorylation
Drosophila melanogaster
dunce mutant
egyetemen (Magyarországon) készült közlemény
Megjelenés:International Journal of Biochemistry. - 16 : 12 (1984), p. 1401-1408. -
További szerzők:Solti Magda Kiss István (Szeged) Friedrich Péter Dombrádi Viktor (1953-) (biokémikus)
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7.

001-es BibID:BIBFORM027860
Első szerző:Dombrádi Viktor (biokémikus)
Cím:Structure and function of protein phosphatase / Viktor Dombrádi
Dátum:2002
ISSN:1432-1033
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
protein phosphatases
Megjelenés:European Journal of Biochemistry. - 269 (2002), p. 1049. -
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8.

001-es BibID:BIBFORM028278
Első szerző:Dombrádi Viktor (biokémikus)
Cím:Interaction of ligands with glycogen phosphorylase as revealed by affinity chromatography / Viktor Dombrádi, György Vereb, György Bot
Dátum:1979
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
glycogen phosphorylase
affinity chromatography
egyetemen (Magyarországon) készült közlemény
Megjelenés:The International Journal of Biochemistry. - 10 : 11 (1979), p. 905-908. -
További szerzők:Vereb György (1938-) (biokémikus, sejtbiológus) Bot György (1917-1998) (biokémikus, vegyész)
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9.

001-es BibID:BIBFORM028276
Első szerző:Dombrádi Viktor (biokémikus)
Cím:Structural changes in glycogen phosphorylase as revealed by cross-linking with bifunctional diimidates : phospho-dephospho hybrid and phosphorylase a / Viktor Dombrádi, János Hajdu, György Bot, Péter Friedrich
Dátum:1980
ISSN:0006-2960
Megjegyzések:The technique of cross-linking with a series of bifunctional diimidates (maximal effective length ranging from 3.7 to 14.5 A), followed by dodecyl sulfate gel electrophoresis, was applied to compare the subunit contact areas of phosphorylases b, ab (the phospho-dephospho hybrid), and a and to study the structure and ligand-induced structural changes in phosphorylases ab and a. Similarly to phosphorylase b, the nearest cross-linkable lysyl-NH2 groups are about 3.7 A apart across the intradimer subunit interface (contact m) and about 8 A apart across the interdimer interface (contact d) in both phosphorylases ab and a. The activation of phosphorylase b induced by phosphorylation and that elicited by AMP binding are distinguishable at both contacts m and d. Phosphorylases ab and a tend to form tetramers whose structures are not identical, but AMP renders phosphorylase ab similar to phosphorylase a. Glucose, caffeine, and glycogen are able to dissociate both a and ab tetramers to dimers, whereas glucose 6-phosphate can only dissociate phosphorylase ab. The structure around the nucleotide site of phosphorylase a is rigid so that ligands binding here, such as AMP, ATP, ADP, inosine monophosphate, and glucose 6-phosphate, fail to influence the cross-link pattern. In control, in phosphorylase ab contact m is markedly affected by AMP, ATP, and glucose 1-phosphate; hence, in this respect phosphorylase ab resembles phosphorylase b.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
glycogen phosphorylase
phosphorylase a
egyetemen (Magyarországon) készült közlemény
Megjelenés:Biochemistry. - 19 : 11 (1980), p. 2295-2299. -
További szerzők:Hajdu János Friedrich Péter Bot György (1917-1998) (biokémikus, vegyész)
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10.

001-es BibID:BIBFORM028272
Első szerző:Dombrádi Viktor (biokémikus)
Cím:Structural aspects of the catalytic and regulatory function of glycogen phosphorylase / Viktor Dombrádi
Dátum:1980
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
glycogen phosphorylase
egyetemen (Magyarországon) készült közlemény
Megjelenés:The International Journal of Biochemistry. - 13 : 2 (1981), p. 125-139. -
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11.

001-es BibID:BIBFORM028271
Első szerző:Dombrádi Viktor (biokémikus)
Cím:Interaction of ligands in phosphorylase A as monitored by crosslinking and enzymatic modifications : synergism of glucose and caffeine manifested in the exposure of N-terminal segment / V. Dombrádi, B. Tóth, G. Bot, J. Hajdú, P. Friedrich
Dátum:1982
Megjegyzések:Glycogen, caffeine and glucose dissociate phosphorylase a tetramer to dimers with half-maximum effect at 0.16%, 1.1 and 71 mM concentration, respectively, as monitored by crosslinking with dimethyl suberimidate at 18 degrees C. The above ligands increase the rate of dephosphorylation and tryptic digestion of phosphorylase alpha at 18 degrees C in the same way with half-maximum effect at 0.04%, 0.1 and 9 mM concentration, respectively. Caffeine and glucose acted synergistically in tetramer dissociation as well as in the enzymic modifications. The alpha-anomer of D-glucose was twice as effective as its mutarotational equilibrium solution.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
phosphorylase a
glycogen phosphorylase
glucose
egyetemen (Magyarországon) készült közlemény
Megjelenés:The International Journal of Biochemistry. - 14 : 4 (1982), p. 277-284. -
További szerzők:Hajdu János Friedrich Péter Tóth Béla (1954-) (vegyész, biokémikus) Bot György (1917-1998) (biokémikus, vegyész)
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12.

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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