CCL

Összesen 8 találat.
#/oldal:
Részletezés:
Rendezés:

1.

001-es BibID:BIBFORM052924
Első szerző:Bartók Ádám (biotechnológus)
Cím:Margatoxin is a non-selective inhibitor of human Kv1.3 K+ channels / Adam Bartok, Agnes Toth, Sandor Somodi, Tibor G. Szanto, Peter Hajdu, Gyorgy Panyi, Zoltan Varga
Dátum:2014
ISSN:0041-0101
Megjegyzések:Margatoxin (MgTx), an alpha-KTx scorpion toxin, is considered a selective inhibitor of the Kv1.3 K+ channel. This peptide is widely used in ion channel research; however, a comprehensive study of its selectivity with electrophysiological methods has not been published yet. The lack of selectivity might lead to undesired side effects upon therapeutic application or may lead to incorrect conclusion regarding the role of a particular ion channel in a physiological or pathophysiological response either in vitro or in vivo. Using the patch-clamp technique we characterized the selectivity profile of MgTx using L929 cells expressing mKv1.1 channels, human peripheral lymphocytes expressing Kv1.3 channels and transiently transfected tsA201 cells expressing hKv1.1, hKv1.2, hKv1.3, hKv1.4-IR, hKv1.5, hKv1.6, hKv1.7, rKv2.1, Shaker-IR, hERG, hKCa1.1, hKCa3.1 and hNav1.5 channels. MgTx is indeed a high affinity inhibitor of Kv1.3 (Kd = 11.7 pM) but is not selective, it inhibits the Kv1.2 channel with similar affinity (Kd = 6.4 pM) and Kv1.1 in the nanomolar range (Kd = 4.2 nM). Based on our comprehensive data MgTX has to be considered a non-selective Kv1.3 inhibitor, and thus, experiments aiming at elucidating the significance of Kv1.3 in in vitro or in vivo physiological responses have to be carefully evaluated.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
ion channel
potassium channel
scorpion toxin
margatoxin
Megjelenés:Toxicon. - 87 (2014), p. 6-16. -
További szerzők:Tóth Ágnes (1983-) (biofizikus) Somodi Sándor (1977-) (belgyógyász) Szántó Gábor Tibor (1980-) (vegyész) Hajdu Péter (1975-) (biofizikus) Panyi György (1966-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:

2.

001-es BibID:BIBFORM007283
Első szerző:Beyer Dániel (molekuláris biológus)
Cím:Cylindrospermopsin induces alterations of root histology and microtubule organization in common reed (Phragmites australis) plantlets cultured in vitro / Beyer D., Surányi G., Vasas G., Roszik J., Erdődi F., M-Hamvas M., Bácsi I., Bátori R., Serfőző Z., Szigeti Zs., Vereb Gy., Demeter Z., Gonda S., Máthé C.
Dátum:2009
ISSN:0041-0101
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
cylindrospermopsin
microtubules
chromatin
cell swelling
necrosis
Phragmites australis
Megjelenés:Toxicon 54 : 4 (2009), p. 440-449. -
További szerzők:Surányi Gyula (1957-) (biológus) Vasas Gábor (1975-) (biológus-vegyész) Roszik János (1979-) (biofizikus) Erdődi Ferenc (1953-) (biokémikus) Mikóné Hamvas Márta (1963-) (biológus) Bácsi István (1977-) (biológus) Bátori Róbert Károly (1983-) (biológus, biotechnológus) Serfőző Zoltán Máthéné Szigeti Zsuzsa (1976-) (biológus-ökológus) Vereb György (1965-) (biofizikus, orvos) Demeter Zita (1985-) (biológia-kémia szakos tanár) Gonda Sándor (1984-) (gyógyszerész) Máthé Csaba (1966-) (biológus)
Internet cím:DOI
elektronikus változat
Borító:

3.

001-es BibID:BIBFORM076189
Első szerző:Krishnarjuna, Bankala
Cím:Synthesis, folding, structure and activity of a predicted peptide from the sea anemone Oulactis sp. with an ShKT fold / Krishnarjuna Bankala, Villegas-Moreno Jessica, Mitchell Michela L., Csoti Agota, Peigneur Steve, Amero Carlos, Pennington Michael W., Tytgat Jan, Panyi Gyorgy, Norton Raymond S.
Dátum:2018
ISSN:0041-0101
Megjegyzések:Sea anemone venom is rich in bioactive compounds, including peptides containing multiple disul?de bridges. In a transcriptomic study on Oulactis sp., we identi?ed the putative 36-residue peptide, OspTx2b, which is an isoform of the K channel blocker OspTx2a (Sunanda P et al. [2018] Identi?cation, chemical synthesis, structure and function of a new K V 1 channel blocking peptide from Oulactis sp. Peptide Science, in press). As OspTx2b contains a ShK/BgK-like cysteine framework, with high amino acid sequence similarity to BgK, we were interested to investigate its structure and function. The solution structure of OspTx2b was determined using nuclear magnetic resonance spectroscopy. OspTx2b does indeed possess a BgK-like sca?old, with the same disul?de bond connectivities. The orientation of the Lys-Tyr dyad in OspTx2b is more similar to that in ShK than in BgK. However, it failed to show against a range of voltage-gated potassium channels in Xenopus oocytes and human T lymphocytes. OspTx2b also showed no growth inhibitory activity against several strains of bacteria and fungi. Having a BgK-like fold with the Lys-Tyr dyad but no BgK-like activity highlights the importance of key amino acid residues in BgK that are missing in OspTx2b. The lack of activity against the KV channels assessed in this study emphasises that the ShK/BgK sca?old is capable of supporting functional activity beyond potassium channel blockade.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
OspTx2b
Cysteine-rich peptide
Sea anemone
Structure
NMR spectroscopy
Potassium channel
Megjelenés:Toxicon. - 150 (2018), p. 50-59. -
További szerzők:Villegas-Moreno, Jessica Mitchell, Michela L. Csóti Ágota (1989-) (biológus) Peigneur, Steve Amero, Carlos Pennington, Michael W. Tytgat, Jan Panyi György (1966-) (biofizikus) Norton, Raymond S.
Pályázati támogatás:Australian Research Council LP150100621
Egyéb
Australian Government Research Training Program Scholarship and a Monash University?Museum Victoria Scholarship top-up
Egyéb
CELSA/17/047 - BOF/ISP
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

4.

001-es BibID:BIBFORM069801
Első szerző:Olamendi-Portugal, Timoteo
Cím:Pi5 and Pi6, two undescribed peptides from the venom of the scorpion Pandinus imperator and their effects on K + -channels / Olamendi-Portugal T., Csoti A., Jimenez-Vargas J. M., Gomez-Lagunas F., Panyi G., Possani L. D.
Dátum:2017
ISSN:0041-0101
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Toxicon 133 (2017), p. 136-144. -
További szerzők:Csóti Ágota (1989-) (biológus) Jimenez-Vargas, J. M. Gómez-Lagunas, Froylan Panyi György (1966-) (biofizikus) Possani, Lourival Domingos
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

5.

001-es BibID:BIBFORM063758
Első szerző:Olamendi-Portugal, Timoteo
Cím:Isolation, chemical and functional characterization of several new K+-channel blocking peptides from the venom of the scorpion Centruroides tecomanus / Timoteo Olamendi-Portugal, Adam Bartok, Fernando Zamudio-Zuniga, Andras Balajthy, Baltazar Becerril, Gyorgy Panyi, Lourival D. Possani
Dátum:2016
ISSN:0041-0101
Megjegyzések:AbstractSix new peptides were isolated from the venom of the Mexican scorpion Centruroides tecomanus; their primary structures were determined and the effects on ion channels were verified by patch-clamp experiments. Four are K(+)-channel blockers of the ?-KTx family, containing 32 to 39 amino acid residues, cross-linked by three disulfide bonds. They all block Kv1.2 in nanomolar concentrations and show various degree of selectivity over Kv1.1, Kv1.3, Shaker and KCa3.1 channels. One peptide has 42 amino acids cross-linked by four disulfides; it blocks ERG-channels and belongs to the ?-KTx family. The sixth peptide has only 32 amino acid residues, three disulfide bonds and has no effect on the ion-channels assayed. It also does not have antimicrobial activity. Systematic numbers were assigned (time of elution on HPLC): ?-KTx 10.4 (time 24.1); ?-KTx 2.15 (time 26.2); ?-KTx 2.16 (time 23.8); ?-KTx 2.17 (time 26.7) and ?-KTx 1.9 (elution time 29.6). A partial proteomic analysis of the short chain basic peptides of this venom, which elutes on carboxy-methyl-cellulose column fractionation, is included. The pharmacological properties of the peptides described in this study may provide valuable tools for understanding the structure-function relationship of K(+) channel blocking scorpion toxins.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Toxicon 115 (2016), p. 1-12. -
További szerzők:Bartók Ádám (1984-) (biotechnológus) Zamudio, Fernando Z. Balajthy András (1988-) (általános orvos) Becerril, Baltazar Panyi György (1966-) (biofizikus) Possani, Lourival Domingos
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

6.

001-es BibID:BIBFORM004881
Első szerző:Olamendi-Portugal, Timoteo
Cím:Novel alpha-KTx peptides from the venom of the scorpion Centruroides elegans selectively blockade Kv1.3 over IKCa1 K+ channels of T cells / Olamendi-Portugal, T., Somodi, S., Fernandez, J. A., Zamudio, F. Z., Becerril, B., Varga, Z., Panyi, G., Gaspar, R., Possani, L. D.
Dátum:2005
ISSN:0041-0101
Megjegyzések:From the venom of the Mexican scorpion Centruroides elegans Thorell five peptides were isolated to homogeneity by chromatographic procedures and their full amino acid sequence was determined by automatic Edman degradation. They all belong to the Noxiustoxin subfamily of scorpion toxins and were given the systematic names alpha-KTx 2.8 to 2.12, with trivial names Ce1 to Ce5, respectively. They have 39 amino acid residues, except for Ce3 which has only 38, but all of them have three disulfide bridges, and have molecular weights of 4255, 4267, 4249, 4295 and 4255 atomic mass units, respectively for Ce1 to Ce5. The C-terminal residues of Ce2, Ce4 and Ce5 were found to be amidated. The electrophysiological assay (whole-cell patch-clamp) showed that out of the five peptides, Ce1 (alpha-KTx 2.8), Ce2 (alpha-KTX2.9) and Ce4 (alpha-KTx 2.11) were effective blockers of Kv1.3 channels of human T lymphocytes, whereas these peptides did not inhibit the Ca2+-activated K+ channels (IKCa1) of the same cells. The equilibrium dissociation constants of these peptides for Kv1.3 were 0.70, 0.25 and 0.98nM for Ce1, Ce2 and Ce4, respectively. Furthermore, toxins Ce1, Ce2 and Ce4 practically did not inhibit the related voltage gated Shaker K+ channels, and rKv2.1 channels of the Shab family. The high affinity blockage of Kv1.3 channels by these peptides and their selectivity for Kv1.3 over IKCa1 may have significance in the development of novel tools for suppressing the function of those T cell subsets whose proliferation critically depends on the activity of Kv1.3 channels.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Amino Acid Sequence
Animals
antagonists & inhibitors
Bayes Theorem
Cell Line
Cells
chemistry
Chromatography,High Pressure Liquid
Comparative Study
Electrophysiology
Enzyme-Linked Immunosorbent Assay
genetics
Human
Humans
Intermediate-Conductance Calcium-Activated Potassium Channels
Kv1.3 Potassium Channel
Lymphocytes
Mass Spectrometry
metabolism
Mexico
Models,Genetic
Molecular Sequence Data
Molecular Weight
Organophosphorus Compounds
Peptides
Phylogeny
Potassium
Potassium Channels
Research
Scorpion Venoms
Scorpions
Sequence Analysis,Protein
Support
T-Lymphocytes
toxicity
Toxins
Megjelenés:Toxicon. - 46 : 4 (2005), p. 418-429. -
További szerzők:Somodi Sándor (1977-) (belgyógyász) Fernandez, Juan Antonio Zamudio, Fernando Z. Becerril, Baltazar Varga Zoltán (1969-) (biofizikus, szakfordító) Panyi György (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Possani, Lourival Domingos
Internet cím:elektronikus változat
DOI
Borító:

7.

001-es BibID:BIBFORM010358
Első szerző:Papp Ferenc (biofizikus)
Cím:Tst26, a novel peptide blocker of Kv1.2 and Kv1.3 channels from the venom of Tityus stigmurus / Papp, F., Batista, C. V. F., Varga, Z., Herceg, M., Roman-Gonzalez, S. A., Gaspar, R., Possani, L. D., Panyi, G.
Dátum:2009
ISSN:0041-0101 (Print)
Megjegyzések:Using high-performance liquid chromatography Tst26, a novel potassium channel blocker peptide, was purified from the venom of the Brazilian scorpion Tityus stigmurus. its primary structure was determined by means of automatic Edman degradation and mass spectrometry analysis. The peptide is composed of 37 amino acid residues and tightly folded through three disulfide bridges, similar to other K+ channel blocking peptides purified from scorpion venoms. It contains the "essential dyad" for K+ channel recognition comprised of a lysine at position 27 and a tyrosine at position 36. Electrophysiological assays revealed that Tst26 blocked hKv1.2 and hKv1.3 channels with high affinity (K-d = 1.9 nM and 10.7 nM, respectively) while it did not affect several other ion channels (mKv1.1, hKv1.4, hKv1.5, hERG, hIKCa1, hBK, hNav1.5) tested at 10 nM concentration. The voltage-dependent steady-state parameters of K+ channel gating were unaffected by the toxin in both channels, but due to the fast association and dissociation kinetics Tst26 slowed the rate of inactivation of Kv1.3 channels. Based on the primary structure, the systematic nomenclature proposed for this peptide is alpha-KTx 4.6.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Chromatography
Ion Channels
Kinetics
Lysine
Mass Spectrometry
Peptides
Potassium
Scorpion Venoms
Spectrometry
Tyrosine
Megjelenés:Toxicon. - 54 : 4 (2009), p. 379-389. -
További szerzők:Batista, Cesar V. F. Varga Zoltán (1969-) (biofizikus, szakfordító) Herceg Mónika (biofizikus) Roman-Gonzalez, Sergio A. Gáspár Rezső (1944-) (biofizikus) Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

8.

001-es BibID:BIBFORM100131
Első szerző:Reddiar, Sanjeevini Babu
Cím:Lipopolysaccharide influences the plasma and brain pharmacokinetics of subcutaneously-administered HsTX1[R14A], a KV1.3-blocking peptide / Reddiar Sanjeevini Babu, Jin Liang, Wai Dorothy C. C., Csoti Agota, Panyi Gyorgy, Norton Raymond S., Nicolazzo Joseph A.
Dátum:2021
ISSN:0041-0101
Megjegyzések:KV1.3 is a voltage-gated potassium channel that is upregulated in neuroinflammatory conditions, such as Alzheimer's disease and Parkinson's disease. HsTX1[R14A] is a potent and selective peptide blocker of KV1.3 with the potential to block microglial KV1.3, but its brain uptake is expected to be limited owing to the restrictive nature of the blood-brain barrier. To assess its peripheral and brain exposure, a LC-MS/MS assay was developed to quantify HsTX1[R14A] concentrations in mouse plasma and brain homogenate that was reliable and reproducible in the range of 6.7?66.7 nM (r2 = 0.9765) and 15?150 pmol/g (r2 = 0.9984), respectively. To assess if neuroinflammation affected HsTX1[R14A] disposition, C57BL/6 mice were administered HsTX1[R14A] subcutaneously (2 mg/kg) 24 h after an intraperitoneal dose of Escherichia coli lipopolysaccharide (LPS), which is commonly used to induce neuroinflammation; brain and plasma concentrations of HsTX1[R14A] were then quantified over 120 min. LPS treatment significantly retarded the decline in HsTX1[R14A] plasma concentrations, presumably as a result of reducing renal clearance, and led to substantial brain uptake of HsTX1[R14A], presumably through disruption of brain inter-endothelial tight junctions. This study suggests that HsTX1[R14A] may reach microglia in sufficient concentrations to block KV1.3 in neuroinflammatory conditions, and therefore has the potential to reduce neurodegenerative diseases.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Toxicon. - 195 (2021), p. 29-36. -
További szerzők:Jin, Liang Wai, Dorothy C. C. Csóti Ágota (1989-) (biológus) Panyi György (1966-) (biofizikus) Norton, Raymond S. Nicolazzo, Joseph A.
Pályázati támogatás:K119417
OTKA
EFOP-3.6.1-16-2016-00022
EFOP
GINOP-2.3.2-15-2016-00015
GINOP
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Rekordok letöltése1 
Corvina könyvtári katalógus v8.2.27 © 2023 Monguz kft. Minden jog fenntartva.