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1.

001-es BibID:BIBFORM060771
Első szerző:Fésüs László (orvos biokémikus)
Cím:Apoptosis : molecular mechanisms in programmed cell death / L. Fésüs, P. J. A. Davies, M. Piacentini
Dátum:1991
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:European Journal of Cell Biology 56 : 2 (1991), p. 170-177. -
További szerzők:Davies, Peter J. A. Piacentini, Mauro
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2.

001-es BibID:BIBFORM060622
Első szerző:Gentile, Vittorio
Cím:Expression of tissue transglutaminase in Balb-C 3T3 fibroblasts : effects on cellular morphology and adhesion / Vittorio Gentile, Vilmos Thomazy, Mauro Piacentini, Laszlo Fesus, Peter J. A. Davies
Dátum:1992
ISSN:0021-9525
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Cell Biology 119 : 2 (1992), p. 463-474. -
További szerzők:Thomázy Vilmos Piacentini, Mauro Fésüs László (1947-) (orvos biokémikus) Davies, Peter J. A.
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3.

001-es BibID:BIBFORM096180
035-os BibID:(WoS)000709464800005 (Scopus)85107471683
Első szerző:Hardenberg, Maarten
Cím:Observation of an α-synuclein liquid droplet state and its maturation into Lewy body-like assemblies / Maarten C. Hardenberg, Tessa Sinnige, Sam Casford, Samuel T. Dada, Chetan Poudel, Elizabeth A. Robinson, Monika Fuxreiter, Clemens F. Kaminksi, Gabriele S. Kaminski-Schierle, Ellen A. A. Nollen, Christopher M. Dobson, Michele Vendruscolo
Dátum:2021
ISSN:1674-2788 1759-4685
Megjegyzések:Misfolded α-synuclein is a major component of Lewy bodies, which are a hallmark of Parkinson's disease (PD). A large body of evidence shows that α-synuclein can aggregate into amyloid fibrils, but the relationship between α-synuclein self-assembly and Lewy body formation remains unclear. Here, we show, both in vitro and in a Caenorhabditis elegans model of PD, that α-synuclein undergoes liquid?liquid phase separation by forming a liquid droplet state, which converts into an amyloid-rich hydrogel with Lewy-body-like properties. This maturation process towards the amyloid state is delayed in the presence of model synaptic vesicles in vitro. Taken together, these results suggest that the formation of Lewy bodies may be linked to the arrested maturation of α-synuclein condensates in the presence of lipids and other cellular components.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Parkinson's disease
liquid?liquid phase separation
α-synuclein
Megjelenés:Journal of Molecular Cell Biology. - 13 : 4 (2021), p. 282-294. -
További szerzők:Sinnige, Tessa Casford, Sam Dada, Samuel T. Poudel, Chetan Robinson, Elizabeth A. Fuxreiter Mónika (1969-) (kutató vegyész) Kaminksi, Clemens F. Kaminski-Schierle, Gabriele S. Nollen, Ellen A. A. Dobson, Christopher M. Vendruscolo, Michele
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4.

001-es BibID:BIBFORM074369
035-os BibID:(WoS)000446007700011 (Scopus)85054070208
Első szerző:Karányi Zsolt (biostatisztikus, bioinformatikus)
Cím:Nuclear dynamics of the Set1C subunit Spp1 prepares meiotic recombination sites for break formation / Zsolt Karányi, László Halász, Laurent Acquaviva, Dávid Jónás, Szabolcs Hetey, Beáta Boros-Oláh, Feng Peng, Doris Chen, Franz Klein, Vincent Géli, Lóránt Székvölgyi
Dátum:2018
ISSN:0021-9525
Megjegyzések:Spp1 is the H3K4me3 reader subunit of the Set1 complex (COMPASS/Set1C) that contributes to the mechanism by which meiotic DNA break sites (DSBs) are mechanistically selected. We previously proposed a model in which Spp1 interacts with H3K4me3 and the chromosome axis protein Mer2 that leads to DSB formation. Here we show that spatial interactions of Spp1 and Mer2 occur independently of Set1C. Spp1 exhibits dynamic chromatin binding features during meiosis with many de novo appearing and disappearing binding sites. Spp1 chromatin binding dynamics depends on its PHD finger and Mer2-interacting domain, and on modifiable histone residues (H3R2/K4). Remarkably, association of Spp1 with Mer2 axial sites reduces the effective turnover rate and diffusion coefficient of Spp1 upon chromatin binding, compared to other Set1C subunits. Our results indicate that "chromosomal turnover rate" is a major molecular determinant of Spp1 function in the framework of meiotic chromatin structure that prepares recombination initiation sites for break formation.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
recombination
meiosis
COMPASS/Set1C
ChIP
chromatin structure
Megjelenés:Journal of Cell Biology. - 217 : 10 (2018), p. 3398-3415. -
További szerzők:Halász László (1989-) (molekuláris biológus) Acquaviva, Laurent Jonás Dávid Hetey Szabolcs Boros-Oláh Beáta (1989-) (molekuláris biológus) Peng, Feng Chen, Doris Klein, Franz Géli, Vincent Székvölgyi Lóránt (1977-) (biofizikus, biokémikus, sejtbiológus)
Pályázati támogatás:NKFIH-ERC-HU-117670
NKFIH
GINOP-2.3.2-15-2016-00024
GINOP
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5.

001-es BibID:BIBFORM060767
Első szerző:Nemes Z.
Cím:Expression and activation of tissue transglutaminase in apoptotic cells of involuting rodent mammary tissue / Z. Nemes, R. R. Friis, D. Aeschlimann, S. Saurer, M. Paulsson, L. Fésüs
Dátum:1996
ISSN:0171-9335
Megjegyzések:Apoptosis is a form of cell death in which cellular integrity is maintained and neither cytoplasmic nor nuclear content is released. The Ca(2+)-dependent tissue transglutaminase (tTG) is an enzyme that forms protein cross-links between specific glutamyl and lysyl side-chains of intra- and extracellular proteins, therefore it may be responsible for the structural stabilization observed during the death process. In this study, the expression of tTG was investigated following the physiological process of forced weaning which results in an almost complete elimination of secretory epithelium by apoptosis and remodelling of the tissue structure. A dramatic induction of tTG was detected by immunoblotting of total mammary gland homogenates prepared from the involuting glands. The concentration of epsilon(gamma-glutamyl)-lysine crosslinks was also elevated in these samples, showing that the enzyme is activated during apoptosis. To determine the distribution of tTG and its relationship to apoptotic cells, paraffin-embedded specimens were studied by RNA in situ hybridization and immunohistochemical methods as well as using in situ labeling for nuclear fragmentation. All of these approaches indicated that mammary secretory epithelium expressed tissue transglutaminase coincident with the onset of apoptosis. The apoptotic and tTG-expressing cells were found to be identical as demonstrated by a histological double-labeling technique.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:European Journal of Cell Biology 70 : 2 (1996), p. 125-133. -
További szerzők:Friis, Bob R. R. Aeschlimann, Daniel Saurer, S. Paulsson, M. Fésüs László (1947-) (orvos biokémikus)
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6.

001-es BibID:BIBFORM060772
Első szerző:Piacentini, Mauro
Cím:The expression of "tissue" transglutaminase in two human cancer cell lines is related with the programmed cell death (apoptosis) / M. Piacentini, L. Fésüs, M. G. Farrace, L. Ghibelli, G. Melino
Dátum:1991
ISSN:0171-9335
Megjegyzések:The expression of "tissue" transglutaminase (tTG) in two human tumor cell lines (the cervix adenocarcinoma line HeLa-TV and the neuroblastoma cells SK-N-BE-2) was found to be in correlation with the rate of physiological cell death (apoptosis) in culture. We investigated the effect of retinoic acid (RA) and alpha-difluoromethylornithine (DFMO) in order to elucidate the relationship between tTG expression and apoptosis. RA led to a 6-fold increase of tTG activity in HeLa-TV cells and to a 12-fold increase in SK-N-BE(2) cells, which was paralleled in both cell lines by a proportional increase in the number of apoptotic bodies recovered from the cultures. On the contrary, DFMO determined a dramatic reduction of tTG expression and of the apoptotic index. Immunohistochemical analysis using an anti-tTG antibody showed that the enzyme was accumulated in both cell lines within typical apoptotic bodies. Immunocytochemistry and cell cloning of SK-N-BE(2) line demonstrated that tTG was absent in cells showing neurite outgrowth, indicating that the enzyme expression is not associated with neural differentiation, even though both phenomena are elicited by retinoic acid. On the whole, these data indicate that also in tumors tTG activation takes place in cells undergoing apoptosis. The enzyme is activated in apoptotic cells to form cross-linked protein envelopes which are insoluble in detergents and chaotropic agents. The number of insoluble protein envelopes as well as the N,N-bis(gamma-glutamyl)polyamine cross-links is related with both tTG expression and apoptotic index, strongly suggesting the participation of the enzyme in the apoptotic program.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:European Journal of Cell Biology 54 : 2 (1991), p. 246-254. -
További szerzők:Fésüs László (1947-) (orvos biokémikus) Farrace, Maria Grazia Ghibelli, L. Melino, Gerry
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