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1.

001-es BibID:BIBFORM086411
Első szerző:Csősz Éva (biokémikus, molekuláris biológus)
Cím:An in silico study of substrate preference for transglutaminase 2 / Csősz Éva, Bagossi Péter, Fésüs László
Dátum:2005
ISSN:1742-464X
Tárgyszavak:Orvostudományok Klinikai orvostudományok idézhető absztrakt
folyóiratcikk
Megjelenés:Febs Journal. - 272 : Suppl1 (2005), p. 410-410. -
További szerzők:Bagossi Péter (1966-2011) (biokémikus, vegyész) Fésüs László (1947-) (orvos biokémikus)
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DOI
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2.

001-es BibID:BIBFORM028040
Első szerző:Fésüs László (orvos biokémikus)
Cím:Cellular biochemistry of the multifunctional transglutaminase 2 : challenging issues and novel concepts / Fésüs László
Dátum:2011
ISSN:1742-464X
Megjegyzések:The transglutaminase TG2 can do a lot more than just transamidation: it has multiple biochemical activities, appears in various cell compartments, and has been implicated in a broad range of cellular processes and pathologies. Decades after its discovery, this enigmatic protein still intrigues researchers. Some of the most recent and compelling findings concerning TG2 are reviewed in four minireivews in this issue of FEBS Journal
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Minireview series
Megjelenés:Febs Journal. - 278 : 24 (2011), p. 4703. -
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DOI
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3.

001-es BibID:BIBFORM098103
Első szerző:Király Róbert (biológus)
Cím:Ca2+-binding sites of transglutaminase 2 revealed by site directed mutagenesis / R. Kiraly, E. Csosz, T. Kurtan, Z. Keresztessy, L. Fesus
Dátum:2007
ISSN:1742-464X
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
folyóiratcikk
Megjelenés:FEBS Journal. - 274 : 1. Suppl. (2007), p. 167. -
További szerzők:Csősz Éva (1977-) (biokémikus, molekuláris biológus) Kurtán Tibor (1973-) (vegyész, angol szakfordító) Keresztessy Zsolt Fésüs László (1947-) (orvos biokémikus)
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4.

001-es BibID:BIBFORM086442
Első szerző:Király Róbert (biológus)
Cím:Coeliac autoantibodies can enhance transamidating and inhibit GTPase activity of tissue transglutaminase / Király Róbert, Simon-Vecsei Zsófia Judit, Deményi T., Korponay-Szabó Ilma Rita, Fésüs László
Dátum:2005
ISSN:1742-464X
Tárgyszavak:Orvostudományok Klinikai orvostudományok idézhető absztrakt
folyóiratcikk
Megjelenés:Febs Journal. - 272 : Suppl1 (2005), p. 411. -
További szerzők:Simon-Vecsei Zsófia (1980-) (biológus) Deményi Tamás Korponay-Szabó Ilma (1959-) (gyermekgyógyász) Fésüs László (1947-) (orvos biokémikus)
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DOI
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5.

001-es BibID:BIBFORM028037
Első szerző:Király Róbert (biológus)
Cím:Protein transamidation by transglutaminase 2 in cells : a disputed Ca2+ -dependent action of a multifunctional protein / Király Róbert, Demény Máté Á., Fésüs László
Dátum:2011
ISSN:1742-464X
Megjegyzések:Transglutaminase 2 (TG2) is the first described cellular member of an enzyme family catalyzing Ca2+-dependent transamidation of proteins. During the last two decades its additional enzymatic (GTP binding and hydrolysis, protein disulfide isomerase, protein kinase) and non-enzymatic (multiple interactions in protein scaffolds) activities, which do not require Ca2+, have been recognized. It became a prevailing view that TG2 is silent as a transamidase, except in extreme stress conditions, in the intracellular environment characterized by low Ca2+ and high GTP concentrations. To counter this presumption a critical review of the experimental evidence supporting the role of this enzymatic activity in cellular processes is provided. It includes the structural basis of TG2 regulation through non-canonical Ca2+ binding sites, mechanisms making it sensitive to low Ca2+ concentrations, techniques developed for the detection of protein transamidation in cells and examples of basic cellular phenomena as well as pathological conditions influenced by this irreversible post-translational protein modification.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Molekuláris Medicina
Megjelenés:Febs Journal. - 278 : 24 (2011), p. 4717-4739. -
További szerzők:Demény Máté Ágoston (1976-) (molekuláris biológus) Fésüs László (1947-) (orvos biokémikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Az apoptózis molekuláris mechanizmusa
MRTNCT-2006-036032
EGYÉB
MRTNCT-2006-035624
EGYÉB
LSHB-CT-2007-037730
EGYÉB
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6.

001-es BibID:BIBFORM007895
Első szerző:Király Róbert (biológus)
Cím:Functional significance of five noncanonical Ca2+-binding sites of human transglutaminase 2 characterized by site-directed mutagenesis / Király Róbert, Csősz Éva, Kurtán Tibor, Antus Sándor, Szigeti Krisztián, Simon-Vecsei Zsófia, Korponay-Szabó Ilma Rita, Keresztessy Zsolt, Fésüs László
Dátum:2009
Megjegyzések:The multifunctional tissue transglutaminase 2 (TG2) has a four-domain structure with several Ca2+-regulated biochemical activities, including transglutamylation and GTP hydrolysis. The structure of the Ca2+-binding form of the human enzyme is not known, and its Ca2+-binding sites have not been fully characterized. By mutagenesis, we have targeted its active site Cys, three sites based on homology to Ca2+-binding residues of epidermal transglutaminase and factor XIIIa (S1?S3), and two regions with negative surface potentials (S4 and S5). CD spectroscopy, antibody-binding assay and GTPase activity measurements indicated that the amino acid substitutions did not cause major structural alterations. Calcium-45 equilibrium dialysis and isothermal calorimetric titration showed that both wildtype and active site-deleted enzymes (C277S) bind six Ca2+. Each of the S1?S5 mutants binds fewer than six Ca2+, S1 is a strong Ca2+-binding site, and mutation of one site resulted in the loss of more than one bound Ca2+, suggesting cooperativity among sites. All mutants were deficient in transglutaminase activity, and GTP inhibited remnant activities. Like those of the wild-type enzyme, the GTPase activities of the mutants were inhibited by Ca2+, except in the case of the S4 and S5 mutants, which exhibited increased activity. TG2 is the major autoantigen in celiac disease, and testing the reactivity of mutants with autoantibodies from celiac disease patients revealed that S4 strongly determines antigenicity. It can be concluded that five of the Ca2+-binding sites of TG2 influence its transglutaminase activity, two sites are involved in the regulation of GTPase activity, and one determines antigenicity for autoantibodies in celiac patients.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
calcium binding
celiac epitope
GTPase activity
transglutaminase activity
transglutaminase 2 (tissue transglutaminase)
Megjelenés:The FEBS Journal. - 276 : 23 (2009), p. 7083-7096. -
További szerzők:Csősz Éva (1977-) (biokémikus, molekuláris biológus) Kurtán Tibor (1973-) (vegyész, angol szakfordító) Antus Sándor (1944-2022) (vegyészmérnök) Szigeti Krisztián Simon-Vecsei Zsófia (1980-) (biológus) Korponay-Szabó Ilma (1959-) (gyermekgyógyász) Keresztessy Zsolt Fésüs László (1947-) (orvos biokémikus)
Internet cím:DOI
elektronikus változat
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7.

001-es BibID:BIBFORM066424
Első szerző:Kristóf Endre (általános orvos)
Cím:Role of ICAM3 in the interaction between human macrophages and apoptotic neutrophil granulocytes / E. K. Kristóf, G. Zahuczky, L. Fésüs
Dátum:2011
ISSN:1742-464X
Megjegyzések:The daily clearance of billions of physiologically dying cells in the human body is performed safely mainly by the mononuclear phagocyte system Bridging molecules and receptors ? which recognize the dying cells ? show high redundancy and are linked to several intracellular signaling pathways. Our previous ♭Taq-Man Low Density Array' measurements predicted important role of many genes in phagocytosis, because their expression level heavily elevated during the early stage of the phagocytosis process. The four genes (ADORA2A, FPRL1, ICAM3, THBS1)with the most enhanced expression in human macrophages wereknocked-down by RNA interference which was controlled byWestern-blot and surface immunostaining at translational level. Significant decrease in phagocytic capacity was observed only after silencing ICAM3. Our goal was to investigate the role and interacting partners of ICAM3 transmembrane protein from both sides. Human monocytes were isolated from ♭buffy coats' of healthy blood by magnetic separation using CD14 human microbeads. To examine the phagocytic capacity of 5 day differentiated macrophages, apoptotic neutrophil granulocytes were isolated from human blood by Histopaque density-gradient centrifugation. The phagocytosis assay was performed using fluorescent labeled cells and the incorporated cell-rate was measured by flow cytometry, immediately after pre-incubation of macrophages or apoptotic cells with blocking antibodies. Significant reduction of phagocytosis was noticed after blocking ICAM3 from both sides while that of DC-SIGN, which is a cited receptor for ICAM3, did not influence the engulfment of apoptotic cells. ICAM-3 participates in the recognition of apoptotic neutrophils by macrophages from both sides not only as an adhesion molecule but also as an initiator of signaling pathways mediated by intracellular thyrosin kinases. To examine its interacting partners in this process further investigations have to be performed in the future.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Molekuláris Medicina
Megjelenés:FEBS Journal 278 : Suppl. 1 (2011), p. 138. -
További szerzők:Zahuczky Gábor (1975-) (molekuláris biológus, biokémikus, vegyész) Fésüs László (1947-) (orvos biokémikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Az apoptózis molekuláris mechanizmusa
NI 67877
OTKA
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8.

001-es BibID:BIBFORM066410
Első szerző:Kristóf Endre (általános orvos)
Cím:Role of ICAM3 and its interacting partners in the phagocytosis of apoptotic neutrophils by macrophages / E. K. Kristóf, G. Zahuczky, L. Fésüs
Dátum:2012
ISSN:1742-464X
Megjegyzések:Apoptotic cells express eat-me signals which are recognized by several receptors mainly on professional phagocytes that can define their safe and effective clearance in order to maintain tissue homeostasis in the entire body. TLDA measurements predicted important role of some apopto-phagocytic genes in phagocytosis of apoptotic neutrophils by macrophages, because their expression level heavily elevated during the early stage of phagocytosis. After they were silenced by RNA interference, significant decrease in phagocytosis was observed only after silencing ICAM3. Our goal was to investigate the role and interacting partners of ICAM3 from both sides. Monocytes were isolated from buffy coats of healthy blood by CD14 specific magnetic separation. To examine phagocytic capacity of differentiated macrophages, apoptotic neutrophils were isolated from human blood by density-gradient centrifugation. Phagocytosis assay was performed using fluorescent labeled cells and the incorporated cell-rate was measured by flow cytometry, immediately after preincubation of macrophages or apoptotic cells with blocking antibodies. Localization of the investigated receptors was visualized by indirect immunostaining. Significant reduction of phagocytosis was noticed after blocking of ICAM3 from both sides. In macrophages but not in neutrophils silencing and blocking components of LFA-1, which can strongly bind ICAM3, resulted in a decreased phagocytosis of apoptotic cells. Engulfing caps formed in macrophages during phagocytosis are characterized by accumulation of ICAM3 and the subunits of LFA-1 which show colocalization on the surface of phagocytes showing that ICAM3 and LFA-1 act as recognition receptors in the phagocytosis portals of macrophages for engulfment of apoptotic neutrophils.
Tárgyszavak:Orvostudományok Elméleti orvostudományok poszter
Molekuláris Medicina
Doktori iskola
Megjelenés:FEBS Journal 279 : Suppl. 1 (2012), p. 52. -
További szerzők:Zahuczky Gábor (1975-) (molekuláris biológus, biokémikus, vegyész) Fésüs László (1947-) (orvos biokémikus)
Pályázati támogatás:NK 105046
OTKA
K 61868
OTKA
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Az apoptózis molekuláris mechanizmusa
TÁMOP-4.2.2/B-10/1-2010-0024
TÁMOP
Molekuláris Sejt- és Immunbiológia Doktori Iskola
TRANSCOM IAPP251506
FP7
TRANSPATH ITN 289964
FP7
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9.

001-es BibID:BIBFORM066382
Első szerző:Kristóf Endre (általános orvos)
Cím:Irisin modifies the differentiation program of subcutaneous human adipocytes and induces "browning" / E. K. Kristof, Q. M. Doan-Xuan, P. Bai, Z. Bacsó, L. Fésüs
Dátum:2014
ISSN:1742-464X
Megjegyzések:Although brown adipose tissue (BAT) can be found only in small amounts in the human body after infancy, recent studies revealed that it has a major importance in regulating the energy balance of the entire body. Its oxidative metabolism contributes to energy expenditure during cold exposure and diet or physical exercise induced thermogenesis by triggering the differentiation of"brown adipocyte-like" or "beige" cells interspersed in subcutaneous white adipose tissue depots in a process called "browning". A very strong negative correlation has been found between obesity and BAT amount in humans. Targeting the currently known and unknown regulatory systems of "browning" might open up better strategies to specifically stimulate BAT in obese individuals to aidweight reduction.Irisin is a recently identified peptide hormone which is cleaved from the Fndc5 transmembrane protein and induces a "browning" program in subcutaneous white adipose tissue in mouse models. In humans, however, an escalating debate revolves around the secretion and metabolic effects of irisin. Our aim was to clarify whether human recombinant irsin was able to induce a browning program on differentiating human adipocytes.Human primary preadipocytes obtained from herniotomy were differentiated into white or brown adipocytes with or without long or short-term irisin treatment. Expression of white, brown and general adipocyte markers were determined by RT Q-PCR,immunoblotting or immunocytochemistry and changes in morphology (size and number of lipid droplets, expression of Ucp1 and Cidea in situ) were visualized and quantified by Laser Scanning Cytometry. Functional analysis was carried out using a Seahorse Bioscience XF-96 Analyzer.Irisin administration during white adipogenic differentiation resulted in a significant overexpression of several brown adipocyte marker genes (UCP1, ELOVL3, CIDEA, CYC1, PGC1A). Irisin treated cells had more and smaller lipid droplets, more mitochondrial DNA, higher functional mitochondrial respiration and expressed more Ucp1 and Cidea in situ than the in vitro differentiated white adipocytes. We conclude that irisin treatment is able to induce a browning program in differentiating human subcutaneous white adipocytes in culture conditions.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Browning
Irisin
Laser Scanning Cytometry
Megjelenés:Febs Journal 281 : Suppl. 1 (2014), p. 230. -
További szerzők:Doan-Xuan, Quang-Minh (1986-) (biofizikus) Bai Péter (1976-) (biokémikus) Bacsó Zsolt (1963-) (biofizikus) Fésüs László (1947-) (orvos biokémikus)
Pályázati támogatás:TÁMOP-4.2.2.A-11/1/KONV-2012-0023
TÁMOP
TÁMOP-4.2.4.A/2-11/1-2012-0001
TÁMOP
MTA-DE
MTA
Apoptózis és Genomika Kutatócsoport
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10.

001-es BibID:BIBFORM060597
Első szerző:Kristóf Endre (általános orvos)
Cím:Second generation antipsychotic (SGA) drugs modify the differentiation program of human adipocytes inducing 'browning' markers / E. Kristof, D. Minh, A. Sarvari, Z. Balajthy, Z. Bacso, L. Fesus
Dátum:2013
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:FEBS journal 280 : 1 (2013), p. 289. -
További szerzők:Doan-Xuan, Quang-Minh (1986-) (biofizikus) Sárvári Anitta Kinga (1984-) (biológus) Balajthy Zoltán (1957-) (biokémikus, sejtbiológus) Bacsó Zsolt (1963-) (biofizikus) Fésüs László (1947-) (orvos biokémikus)
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