Találati lista | Tudóstér

001-es BibID:	BIBFORM106364
035-os BibID:	(WoS)000916020800001 (Scopus)85146824862
Első szerző:	Naseem, Muhammad Umair (biofizikus, molekuláris biológus)
Cím:	Characterization and Chemical Synthesis of Cm39 (α-KTx 4.8) : a Scorpion Toxin That Inhibits Voltage-Gated K+ Channel KV1.2 and Small- and Intermediate-Conductance Ca2+-Activated K+ Channels KCa2.2 and KCa3.1 / Muhammad Umair Naseem, Georgina Gurrola-Briones, Margarita R. Romero-Imbachi, Jesus Borrego, Edson Carcamo-Noriega, José Beltrán-Vidal, Fernando Z. Zamudio, Kashmala Shakeel, Lourival Domingos Possani, Gyorgy Panyi
Dátum:	2023
ISSN:	2072-6651
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Cm39 scorpion toxin Centruroides margaritatus KV1.2 KCa2.2 KCa3.1 electrophysiology Ca2+-activated channel
Megjelenés:	Toxins. - 15 : 1 (2023), p. 1-21. -
További szerzők:	Gurrola-Briones, Georgina Romero-Imbachi, Margarita R. Borrego, Jesús Carcamo-Noriega, Edson Beltrán-Vidal, José Zamudio, Fernando Z. Shakeel, Kashmala (1997-) (Molekuláris biológus) Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Pályázati támogatás:	K143071 OTKA
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:

001-es BibID:	BIBFORM130666
035-os BibID:	(scopus)105009253388 (wos)001515421700001
Első szerző:	Shakeel, Kashmala (Molekuláris biológus)
Cím:	Cvill6 and Cvill7: Potent and Selective Peptide Blockers of Kv1.2 Ion Channel Isolated from Mexican Scorpion Centruroides villegasi / Shakeel Kashmala, Naseem Muhammad Umair, Olamendi-Portugal Timoteo, Zamudio Fernando Z., Possani Lourival Domingos, Panyi Gyorgy
Dátum:	2025
ISSN:	2072-6651
Megjegyzések:	Scorpion venoms are a rich source of peptides that modulate the activity of ion channels and can serve as a new drug for channelopathies. Cvill6 and Cvill7 are two new peptides isolated from the venom of Centruroides villegasi with MW of 4277 Da and 4287 Da and they consist of 38 and 39 amino acids, respectively, including six cysteines. Sequence alignment revealed high similarity with members of the ?-KTx2 subfamily of potassium channel toxins. In electrophysiology, Cvill7 potently inhibited Kv1.2 ion channels with an IC50 of 16 pM and Kv1.3 with an IC50 of 7.2 nM. In addition, it exhibited partial activity on KCa3.1 and Kv1.1, with ~16% and ~34% inhibition at 100 nM, respectively. In contrast, Cvill6 blocked Kv1.2 with low affinity (IC50 of 3.9 nM) and showed modest inhibition of Kv1.3 (~11%) and KCa3.1 (~27%) at 100 nM concentration. Neither peptide showed any activity against other K channels tested in this study (Kv1.5, Kv11.1, KCa1.1, and KCa2.2). Notably, Cvill7 has a remarkable affinity for Kv1.2 and high selectivity of 450-fold over Kv1.3 and 12,000-fold over Kv1.1. These pharmacological properties make Cvill7 a potential candidate to target Kv1.2 gain of function (GOF)-related channelopathies such as epilepsy.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk ?-KTx Centruroides villegasi peptides Kv1.2 Kv1.3 KCa3.1 patch-clamp electrophysiology scorpion toxin
Megjelenés:	Toxins. - 17 : 6 (2025), p. 1-19. -
További szerzők:	Naseem, Muhammad Umair (1993-) (biofizikus, molekuláris biológus) Olamendi-Portugal, Timoteo Zamudio, Fernando Z. Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:

001-es BibID:	BIBFORM114858
035-os BibID:	(scopus)85168734722 (wos)001056214900001
Első szerző:	Shakeel, Kashmala (Molekuláris biológus)
Cím:	Of Seven New K⁺ Channel Inhibitor Peptides of Centruroides bonito, α-KTx 2.24 Has a Picomolar Affinity for Kv1.2 / Shakeel Kashmala, Olamendi-Portugal Timoteo, Naseem Muhammad Umair, Becerril Baltazar, Zamudio Fernando Z., Delgado-Prudencio Gustavo, Possani Lourival Domingos, Panyi Gyorgy
Dátum:	2023
ISSN:	2072-6651
Megjegyzések:	Seven new peptides denominated CboK1 to CboK7 were isolated from the venom of the Mexican scorpion Centruroides bonito and their primary structures were determined. The molecular weights ranged between 3760.4 Da and 4357.9 Da, containing 32 to 39 amino acid residues with three putative disulfide bridges. The comparison of amino acid sequences with known potassium scorpion toxins (KTx) and phylogenetic analysis revealed that CboK1 (?-KTx 10.5) and CboK2 (?-KTx 10.6) belong to the ?-KTx 10.x subfamily, whereas CboK3 (?-KTx 2.22), CboK4 (?-KTx 2.23), CboK6 (?-KTx 2.21), and CboK7 (?-KTx 2.24) bear > 95% amino acid similarity with members of the ?-KTx 2.x subfamily, and CboK5 is identical to Ce3 toxin (?-KTx 2.10). Electrophysiological assays demonstrated that except CboK1, all six other peptides blocked the Kv1.2 channel with Kd values in the picomolar range (24?763 pM) and inhibited the Kv1.3 channel with comparatively less potency (Kd values between 20?171 nM). CboK3 and CboK4 inhibited less than 10% and CboK7 inhibited about 42% of Kv1.1 currents at 100 nM concentration. Among all, CboK7 showed out-standing affinity for Kv1.2 (Kd = 24 pM), as well as high selectivity over Kv1.3 (850-fold) and Kv1.1 (~6000-fold). These characteristics of CboK7 may provide a framework for developing tools to treat Kv1.2-related channelopathies.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk CboK Centruroides bonito scorpion toxin Kv1.2 Kv1.3 Kv1.2 channelopathies electrophysiology
Megjelenés:	Toxins. - 15 : 8 (2023), p. 1-20. -
További szerzők:	Olamendi-Portugal, Timoteo Naseem, Muhammad Umair (1993-) (biofizikus, molekuláris biológus) Becerril, Baltazar Zamudio, Fernando Z. Delgado-Prudencio, Gustavo Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Pályázati támogatás:	K143071 OTKA
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon: