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001-es BibID:BIBFORM057539
035-os BibID:(scopus)84896847673 (wos)000332354700009
Első szerző:Mocanu, Maria-Magdalena
Cím:Epigallocatechin 3-O-gallate induces 67 kDa laminin receptor-mediated cell death accompanied by downregulation of ErbB proteins and altered lipid raft clustering in mammary and epidermoid carcinoma cells / Maria-Magdalena Mocanu, Constanta Ganea, Laura Georgescu, Tímea Váradi, Dilip Shrestha, Irina Baran, Eva Katona, Peter Nagy, János Szöllősi
Dátum:2014
ISSN:0163-3864
Megjegyzések:Since the administration of synthetic medicines is associated with drug resistance and undesired side effects, utilization of natural compounds could be an alternative and complementary modality to inhibit or prevent the development of tumors. Epigallocatechin 3-O-gallate (EGCG, 1), the major flavan component of green tea, and genistein (2), a soy isoflavonoid, are known to have chemopreventive and chemotherapeutic effects against cancer. This study demonstrated that both flavonoids inhibit cell proliferation, an effect enhanced under serum-free conditions. Compound 1, but not 2, induced downregulation of ErbB1 and ErbB2 in mammary and epidermoid carcinoma cells, and its inhibitory effect on cell viability was mediated by the 67 kDa laminin receptor (67LR). While 1 was superior in inducing cell death, 2 was more efficient in arresting the tumor cells in the G2/M phase. Furthermore, number and brightness analysis revealed that 1 decreased the homoclustering of a lipid raft marker, glycosylphosphatidylinositol-anchored GFP, and it also reduced the co-localization between lipid rafts and 67LR. The main conclusion made is that the primary target of 1 may be the lipid raft component of the plasma membrane followed by secondary changes in the expression of ErbB proteins. Compound 2, on the other hand, must have other unidentified targets.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Epigallocatechin
Molekuláris Medicina
Megjelenés:Journal Of Natural Products. - 77 : 2 (2014), p. 250-257. -
További szerzők:Ganea, Constanta Georgescu, Laura Váradi Tímea (1982-) (okleveles vegyész) Shrestha, Dilip (1980-) (biológus) Baran, Irina Katona Éva (1961-) (klinikai biokémikus) Nagy Péter (1971-) (biofizikus) Szöllősi János (1953-) (biofizikus)
Pályázati támogatás:TÁMOP-4.2.2-08/1-2008-0019
TÁMOP
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Receptor tirozin kinázok mint terápiás célpontok: működésük szabályozásának, és a közöttük fellépő molekuláris kölcsönhatások vizsgálata
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM062699
035-os BibID:(scopus)84925853989 (wos)000354040400007
Első szerző:Shrestha, Dilip (biológus)
Cím:Understanding FRET as a Research Tool for Cellular Studies / Dilip Shrestha, Attila Jenei, Péter Nagy, György Vereb, János Szöllősi
Dátum:2015
ISSN:1661-6596 1422-0067
Megjegyzések:Communication of molecular species through dynamic association and/or dissociation at various cellular sites governs biological functions. Understanding these physiological processes require delineation of molecular events occurring at the level of individual complexes in a living cell. Among the few non-invasive approaches with nanometer resolution are methods based on Förster Resonance Energy Transfer (FRET). FRET is effective at a distance of 1?10 nm which is equivalent to the size of macromolecules, thus providing an unprecedented level of detail on molecular interactions. The emergence of fluorescent proteins and SNAP- and CLIP- tag proteins provided FRET with the capability to monitor changes in a molecular complex in real-time making it possible to establish the functional significance of the studied molecules in a native environment. Now, FRET is widely used in biological sciences, including the field of proteomics, signal transduction, diagnostics and drug development to address questions almost unimaginable with biochemical methods and conventional microscopies. However, the underlying physics of FRET often scares biologists. Therefore, in this review, our goal is to introduce FRET to non-physicists in a lucid manner. We will also discuss our contributions to various FRET methodologies based on microscopy and flow cytometry, while describing its application for determining the molecular heterogeneity of the plasma membrane in various cell types.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
FRET
Megjelenés:International Journal Of Molecular Sciences. - 16 : 4 (2015), p. 6718-6756. -
További szerzők:Jenei Attila (1966-) (biofizikus) Nagy Péter (1971-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Szöllősi János (1953-) (biofizikus)
Pályázati támogatás:MTA-DE
MTA
Sejtbiológiai és Jelátvitel Kutatócsoport
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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