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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:BIBFORM060741
Első szerző:Ambrus Attila
Cím:Polyethylene glycol enhanced refolding of the recombinant human tissue transglutaminase / Ambrus, Attila, Fésüs, László
Dátum:2001
ISSN:1082-6068
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Preparative Biochemistry & Biotechnology. - 31 : 1 (2001), p. 59-70. -
További szerzők:Fésüs László (1947-) (orvos biokémikus)
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3.

001-es BibID:BIBFORM111915
035-os BibID:(cikkazonosító)109385 (scopus)85161297715
Első szerző:Arianti, Rini (biokémikus)
Cím:Availability of abundant thiamine determines efficiency of thermogenic activation in human neck area derived adipocytes / Arianti Rini, Vinnai Boglárka Ágnes, Győry Ferenc, Guba Andrea, Csősz Éva, Kristóf Endre, Fésüs László
Dátum:2023
ISSN:0955-2863
Megjegyzések:Brown/beige adipocytes express uncoupling protein-1 (UCP1) that enables them to dissipate energy as heat. Systematic activation of this process can alleviate obesity. Human brown adipose tissues are interspersed in distinct anatomical regions including deep neck. We found that UCP1 enriched adipocytes differentiated from precursors of this depot highly expressed ThTr2 transporter of thiamine and consumed thiamine during thermogenic activation of these adipocytes by cAMP which mimics adrenergic stimulation. Inhibition of ThTr2 led to lower thiamine consumption with decreased proton leak respiration reflecting reduced uncoupling. In the absence of thiamine, cAMP-induced uncoupling was diminished but restored by thiamine addition reaching the highest levels at thiamine concentrations larger than present in human blood plasma. Thiamine is converted to thiamine pyrophosphate (TPP) in cells; the addition of TPP to permeabilized adipocytes increased uncoupling fueled by TPP-dependent pyruvate dehydrogenase. ThTr2 inhibition also hampered cAMP-dependent induction of UCP1, PGC1a, and other browning marker genes, and thermogenic induction of these genes was potentiated by thiamine in a concentration dependent manner. Our study reveals the importance of amply supplied thiamine during thermogenic activation in human adipocytes which provides TPP for TPP-dependent enzymes not fully saturated with this cofactor and by potentiating the induction of thermogenic genes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
human adipocytes
thiamine
thiamine transporter
pyruvate dehydrogenase
thermogenesis
UCP1 expression
Megjelenés:Journal Of Nutritional Biochemistry. - 119 (2023), p. 1-13. -
További szerzők:Vinnai Boglárka Ágnes (1996-) (molekuláris biológus) Győry Ferenc (1964-) (sebész) Guba Andrea (1975-) (Okleveles vegyész) Csősz Éva (1977-) (biokémikus, molekuláris biológus) Kristóf Endre (1987-) (általános orvos) Fésüs László (1947-) (orvos biokémikus)
Pályázati támogatás:GINOP-2.3.2-15-2016-00006
GINOP
FK131424
OTKA
K129139
OTKA
ÚNKP-22-3-I
Egyéb
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Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM073493
Első szerző:Balogh László (kardiológus)
Cím:Effect of factor XIII levels and polymorphisms on the risk of myocardial infarction in young patients / Balogh László, Katona Éva, Mezei Zoltán A., Kállai Judit, Gindele Réka, Édes István, Muszbek László, Papp Zoltán, Bereczky Zsuzsanna
Dátum:2018
ISSN:0300-8177
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Molecular And Cellular Biochemistry. - 448 : 1-2 (2018), p. 199-209. -
További szerzők:Katona Éva (1961-) (klinikai biokémikus) Mezei Zoltán András (1980-) (orvos) Kállai Judit (1983-) (molekuláris biológus) Gindele Réka (1987-) (molekuláris biológus) Édes István (1952-) (kardiológus) Muszbek László (1942-) (haematológus, kutató orvos) Papp Zoltán (1965-) (kardiológus, élettanász) Bereczky Zsuzsanna (1974-) (orvosi laboratóriumi diagnosztika szakorvos)
Pályázati támogatás:EFOP-3.6.2-16-2017-00006
EFOP
K 113097
OTKA
K 109783
OTKA
K 116228
OTKA
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5.

001-es BibID:BIBFORM015742
Első szerző:Barta Judit (kardiológus)
Cím:Calpain-1-sensitive myofibrillar proteins of the human myocardium / Barta Judit, Tóth Attila, Édes István, Vaszily Miklós, Papp Gy. Julius, Varró András, Papp Zoltán
Dátum:2005
Megjegyzések:Calpain-1 is a ubiquitous intracellular Ca2+-activated protease, which has been implicated in the pathogenesis of reversible myocardial depression (i.e. myocardial stunning) that follows ischemia and reperfusion via myofibrillar protein degradation. However, the target proteins of this degradative process in the human myocardium have not yet been identified. In order to compare the levels of Calpain-1 susceptibility within a set of human myofibrillar proteins (titin, alpha-fodrin, desmin, troponin T (cTnT), troponin I (cTnI) and alpha-actinin), crude left ventricular tissue homogenates were incubated for 0.5, 15, 30, 60 or 120 min in the presence of Calpain-1 (1 U or 5 U). Differences in the kinetics and extents of protein degradation were subsequently evaluated by using silver-stained SDS-polyacrylamide gels and Western immunoblot analyses. These assays revealed myofibrillar proteins with high (titin and alpha-fodrin), moderate (desmin and cTnT), or low (cTnI and alpha-actinin) relative Calpain-1 susceptibilities. The level of phosphorylation of cTnI did not explain its relatively low Calpain-1 susceptibility. Moreover, the molecular mass distributions of the truncated alpha-fodrin, desmin and cTnI fragments resulting from Ca2+-dependent autoproteolysis exhibited marked similarities with those of their Calpain-1-clipped products. These in vitro results shed light on a number of structural (titin, alpha-fodrin, desmin and alpha-actinin) and regulatory (cTnT and cTnI) proteins within the contractile apparatus as potential targets of Calpain-1. Their degradation may contribute to the development of postischemic stunning in the human myocardium.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
calpain
desmin
stunning
titin
troponin I
troponin T
Megjelenés:Molecular and Cellular Biochemistry. - 278 : 1-2 (2005), p. 1-8. -
További szerzők:Tóth Attila (1971-) (biológus) Édes István (1952-) (kardiológus) Vaszily Miklós (1949-) (szívsebész) Papp Gy. Julius (Szeged) Varró András (1954-) (farmakológus, klinikai farmakológus) Papp Zoltán (1965-) (kardiológus, élettanász)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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6.

001-es BibID:BIBFORM015741
Első szerző:Barta Judit (kardiológus)
Cím:Calpain-1-dependent degradation of troponin I mutants found in familial hypertrophic cardiomyopathy / Barta Judit, Tóth Attila, Jaquet Kornelia, Redlich Alexander, Édes István, Papp Zoltán
Dátum:2003
Megjegyzések:The mechanism by which mutations of the cardiac troponin I (cTnI) gene evoke familial hypertrophic cardiomyopathy (fHCM)is unknown. In this investigation the potential effects of three fHCM-related cTnI mutations on Calpain-1-induced cTnI degradation were tested, and a study was made of whether additional conformational changes due to troponin complex formation and protein kinase A-induced phosphorylation affect the intensity of cTnI proteolysis. Purified recombinant wild-type cTnI and three of its fHCM-related missense mutants (R145G, G203S and K206Q), alone or in the troponin complex (i.e. together with troponin C and troponin T), in the non-phosphorylated or protein kinase A-bisphosphorylated forms were proteolyzed invitro in the presence of Calpain-1 (0.05?2.5 U) at 30?C. Following incubation with Calpain-1 for 0.5, 30, 60 or 120 min, the extent of protein degradation was evaluated through the use of Western immunoblotting and densitometry. The results indicated that both the wild-type and the mutant cTnI molecules were susceptible to Calpain-1. However, the degradation of the cTnI molecules in the troponin complex was less intense than that of the non-complexed forms. Moreover, phosphorylation by protein kinase A conferred effective protection against cTnI proteolysis. The data suggested that mutations in the central inhibitory domain (R145G) and in the C-terminal region (G203S and K206Q) of cTnI do not affect its Calpain-1-mediated degradation, or the phosphorylation-induced protection against proteolysis.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
hypertrophic cardiomyopathy
calpain
troponin I
mutation
Megjelenés:Molecular and Cellular Biochemistry. - 251 : 1-2 (2003), p. 83-88. -
További szerzők:Tóth Attila (1971-) (biológus) Jaquet, Kornelia Redlich, Alexander Édes István (1952-) (kardiológus) Papp Zoltán (1965-) (kardiológus, élettanász)
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7.

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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Intézményi repozitóriumban (DEA) tárolt változat
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8.

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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Intézményi repozitóriumban (DEA) tárolt változat
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9.

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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10.

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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Intézményi repozitóriumban (DEA) tárolt változat
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11.

001-es BibID:BIBFORM072540
Első szerző:Bozóki Beáta (molekuláris biológus)
Cím:A recombinant fusion protein-based, fluorescent protease assay for high throughput-compatible substrate screening / Beáta Bozóki, Lívia Gazda, Ferenc Tóth, Márió Miczi, János András Mótyán, József Tőzsér
Dátum:2018
ISSN:0003-2697
Megjegyzések:In connection with the intensive investigation of proteases, several methods have been developed for analysis of the substrate specificity. Due to the great number of proteases and the expected target molecules to be analyzed, time- and cost-efficient high-throughput screening (HTS) methods are preferred. Here we describe the development and application of a separation-based HTS-compatible fluorescent protease assay, which is based on the use of recombinant fusion proteins as substrates of proteases. The protein substrates used in this assay consists of N-terminal (hexahistidine and maltose binding protein) fusion tags, cleavage sequences of the tobacco etch virus (TEV) and HIV-1 proteases, and a C-terminal fluorescent protein (mApple or mTurquoise2). The assay is based on the fluorimetric detection of the fluorescent proteins, which are released from the magnetic bead-attached substrates by the proteolytic cleavage. The protease assay has been applied for activity measurements of TEV and HIV-1 proteases to test the suitability of the system for enzyme kinetic measurements, inhibition studies, and determination of pH optimum. We also found that denatured fluorescent proteins can be renatured after SDS-PAGE of denaturing conditions, but showed differences in their renaturation abilities. After in-gel renaturation both substrates and cleavage products can be identified by in-gel UV detection.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Analytical Biochemistry. - 540-541 (2018), p. 52-63. -
További szerzők:Gazda Lívia Diána (1989-) Tóth Ferenc (1980-) (molekuláris biológus) Miczi Márió Mótyán János András (1981-) (biokémikus, molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
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Intézményi repozitóriumban (DEA) tárolt változat
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12.

001-es BibID:BIBFORM040114
Első szerző:Collet, Claude
Cím:Calcium Signaling in Isolated Skeletal Muscle Fibers Investigated Under "Silicone Voltage-Clamp" Conditions / Collet Claude, Pouvreau Sandrine, Csernoch Laszlo, Allard Bruno, Jacquemond Vincent
Dátum:2004
ISSN:1085-9195
Megjegyzések:In skeletal muscle, release of calcium from the sarcoplasmic reticulum (SR) represents the major source of cytoplasmic Ca2+ elevation. SR calcium release is under the strict command of the membrane potential, which drives the interaction between the voltage sensors in the t-tubule membrane and the calcium-release channels. Either detection or control of the membrane voltage is thus essential when studying intracellular calcium signaling in an intact muscle fiber preparation. The silicone-clamp technique used in combination with intracellular calcium measurements represents an efficient tool for such studies. This article reviews some properties of the plasma membrane and intracellular signals measured with this methodology in mouse skeletal muscle fibers. Focus is given to the potency of this approach to investigate both fundamental aspects of excitation-contraction coupling and potential alterations of intracellular calcium handling in some muscle diseases.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cell Biochemistry And Biophysics. - 40 : 2 (2004), p. 225-236. -
További szerzők:Pouvreau, Sandrine Csernoch László (1961-) (élettanász) Allard, Bruno Jacquemond, Vincent
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