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001-es BibID:BIBFORM050051
Első szerző:Schwartz, Elisabeth F.
Cím:OcyKTx2, a new K+-channel toxin characterized from the venom of the scorpion Opisthacanthus cayaporum / Elisabeth F. Schwartz, Adam Bartok, Carlos Alberto Schwartz, Ferenc Papp, Froylan Gomez-Lagunas, Gyorgy Panyi, Lourival D. Possani
Dátum:2013
Megjegyzések:Opisthacanthus cayaporum belongs to the Liochelidae family, and the scorpions from this genus occur in southern Africa, Central America and South America and, therefore, can be considered a true Gondwana heritage. In this communication, the isolation, primary structure characterization, and K(+)-channel blocking activity of new peptide from this scorpion venom are reported. OcyKTx2 is a 34 amino acid long peptide with four disulfide bridges and molecular mass of 3807 Da. Electrophysiological assays conducted with pure OcyKTx2 showed that this toxin reversibly blocks Shaker B K(+)-channels with a Kd of 82 nM, and presents an even better affinity toward hKv1.3, blocking it with a Kd of approximately 18 nM. OcyKTx2 shares high sequence identity with peptides belonging to subfamily 6 of alpha-KTxs that clustered very closely in the phylogenetic tree included here. Sequence comparison, chain length and number of disulfide bridges analysis classify OcyKTx2 into subfamily 6 of the alpha-KTx scorpion toxins (systematic name, alpha-KTx6.17)
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
article
Brazil
Peptides
Research
Research Support
Scorpions
Support
Toxins
Megjelenés:Peptides. - 46 (2013), p. 40-46. -
További szerzők:Bartók Ádám (1984-) (biotechnológus) Schwartz, Carlos Alberto Papp Ferenc (1979-) (biofizikus) Gomez-Lagunas, Froylan Panyi György (1966-) (biofizikus) Possani, Lourival Domingos
Internet cím:DOI
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2.

001-es BibID:BIBFORM051008
Első szerző:Szentandrássy Norbert (élettanász)
Cím:Tetrodotoxin blocks native cardiac L-type calcium channels but not CaV1.2 channels expressed in HEK cells / N. Szentandrassy, F. Papp, B. Hegyi, A. Bartok, Z. Krasznai, P. P. Nanasi
Dátum:2013
ISSN:0867-5910 1899-1505
Megjegyzések:Tetrodotoxin (TTX) has been believed for a long time to be a selective inhibitor of voltage-gated fast Na(+) channels in excitable tissues, including mammalian myocardium. Recently TTX has been shown to block cardiac L-type Ca(2+) current (ICa,L). Furthermore, this inhibition was ascribed to binding of TTX to the outer pore of the Ca(2+) channel, contributing to the selectivity filter region. In this study the TTX-sensitivity of Cav1.2 channels, expressed in HEK cells, was tested using the whole cell version of the patch clamp technique and compared to the TTX-sensitivity of native canine ICa,L. Cav1.2 channels mediate Ca(2+) current in ventricular myocardium of various mammalian species. Surprisingly, TTX failed to inhibit Cav1.2 current up to the concentration of 100 muM - in contrast to ICa,L - in spite of the fact that the kinetic properties of the ICa,L and Cav1.2 currents were similar. The possible reasons for this discrepancy are discussed. Present results may question the suitability of a single pore-forming channel subunit, expressed in a transfection system, for electrophysiological or pharmacological studies
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
article
Calcium
Calcium Channels
Cells
Hungary
physiology
Research
Research Support
Support
Tetrodotoxin
time
Transfection
Megjelenés:Journal of Physiology and Pharmacology. - 64 : 6 (2013), p. 807-810. -
További szerzők:Papp Ferenc (1979-) (biofizikus) Hegyi Bence (1987-) (élettanász) Bartók Ádám (1984-) (biotechnológus) Krasznai Zoltán (1950-) (biofizikus) Nánási Péter Pál (1956-) (élettanász)
Pályázati támogatás:100151
OTKA
NK104331
OTKA
K101196
OTKA
PD101171
OTKA
TÁMOP-4.2.2.A-11/1/KONV-2012-0045
TÁMOP
Élettan Kutatócsoport
TÁMOP-4.2.4. A/2-11-1-2012-0001
TÁMOP
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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