Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Jesús, Borrego"'
Autor:
Ferenc Papp, Gilman E. S. Toombes, Zoltán Pethő, Adrienn Bagosi, Adam Feher, János Almássy, Jesús Borrego, Ákos Kuki, Sándor Kéki, Gyorgy Panyi, Zoltan Varga
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-12 (2022)
Fluorometry signals indicating conformational change in an ion channel are generated by quenching amino acids and lipid effects during movement of the dye relative to the plane of the membrane.
Externí odkaz:
https://doaj.org/article/7f7b2f17186c408295029866185e676f
Autor:
Jesús Borrego, Muhammad Umair Naseem, Al Nasar Ahmed Sehgal, Lipsa Rani Panda, Kashmala Shakeel, Attila Gaspar, Cynthia Nagy, Zoltan Varga, Gyorgy Panyi
Publikováno v:
Journal of Fungi, Vol 8, Iss 11, p 1215 (2022)
The Kv1.3 channel has become a therapeutic target for the treatment of various diseases. Several Kv1.3 channel blockers have been characterized from scorpion venom; however, extensive studies require amounts of toxin that cannot be readily obtained d
Externí odkaz:
https://doaj.org/article/e66c946cc5fc41abb7997fb4015c7f54
Autor:
Muhammad Umair Naseem, Gabor Tajti, Attila Gaspar, Tibor G. Szanto, Jesús Borrego, Gyorgy Panyi
Publikováno v:
Frontiers in Pharmacology, Vol 12 (2021)
Margatoxin (MgTx) is a high-affinity blocker of voltage-gated potassium (Kv) channels. It inhibits Kv1.1–Kv1.3 ion channels in picomolar concentrations. This toxin is widely used to study physiological function of Kv ion channels in various cell ty
Externí odkaz:
https://doaj.org/article/b4c80743087e4d37a5242da8909296c6
Autor:
Diana Alvarado, Samuel Cardoso-Arenas, Ligia-Luz Corrales-García, Herlinda Clement, Iván Arenas, Pavel Andrei Montero-Dominguez, Timoteo Olamendi-Portugal, Fernando Zamudio, Agota Csoti, Jesús Borrego, Gyorgy Panyi, Ferenc Papp, Gerardo Corzo
Publikováno v:
Frontiers in Pharmacology, Vol 11 (2021)
Spider venoms include various peptide toxins that modify the ion currents, mainly of excitable insect cells. Consequently, scientific research on spider venoms has revealed a broad range of peptide toxins with different pharmacological properties, ev
Externí odkaz:
https://doaj.org/article/f876414bce1e4318b0f8d8ae2745b2ad
Publikováno v:
Pharmaceuticals, Vol 14, Iss 12, p 1303 (2021)
The human voltage gated potassium channel Kv1.5 that conducts the IKur current is a key determinant of the atrial action potential. Its mutations have been linked to hereditary forms of atrial fibrillation (AF), and the channel is an attractive targe
Externí odkaz:
https://doaj.org/article/7a8b7a19ab9449b59051c4ee818fb8a4
Autor:
Jesús Borrego Jiménez, Aurora Martínez Romero, José Luis Ortega Sánchez, Jesús Eduardo Luna Martínez, José de Jesús Alba-Romero
Publikováno v:
Brazilian Journal of Animal and Environmental Research. 4:6246-6253
El objetivo del presente proyecto fue diagnosticar brucelosis bovina en tanque de leche con la Prueba Anillo de Leche (PAL) y ELISA indirecto (iELISA), así el índice de frecuencias para determinar una comparativa entre ambas pruebas para establecer
Autor:
Panyi, Jesús Borrego, Muhammad Umair Naseem, Al Nasar Ahmed Sehgal, Lipsa Rani Panda, Kashmala Shakeel, Attila Gaspar, Cynthia Nagy, Zoltan Varga, Gyorgy
Publikováno v:
Journal of Fungi; Volume 8; Issue 11; Pages: 1215
The Kv1.3 channel has become a therapeutic target for the treatment of various diseases. Several Kv1.3 channel blockers have been characterized from scorpion venom; however, extensive studies require amounts of toxin that cannot be readily obtained d
Autor:
Jesús, Borrego, Muhammad Umair, Naseem, Al Nasar Ahmed, Sehgal, Lipsa Rani, Panda, Kashmala, Shakeel, Attila, Gaspar, Cynthia, Nagy, Zoltan, Varga, Gyorgy, Panyi
Publikováno v:
Journal of fungi (Basel, Switzerland). 8(11)
The Kv1.3 channel has become a therapeutic target for the treatment of various diseases. Several Kv1.3 channel blockers have been characterized from scorpion venom; however, extensive studies require amounts of toxin that cannot be readily obtained d
Publikováno v:
Amino Acids. 52:465-475
δ-Atracotoxins, also known as δ-hexatoxins, are spider neurotoxic peptides, lethal to both vertebrates and insects. Their mechanism of action involves the binding to of the S3/S4 loop of the domain IV of the voltage-gated sodium channels (Nav). Bec
Autor:
Herlinda Clement, Samuel Cardoso-Arenas, Ferenc Papp, Diana Alvarado, Gerardo Corzo, Ligia-Luz Corrales-García, Agota Csoti, Fernando Z. Zamudio, Timoteo Olamendi-Portugal, Pavel Andrei Montero-Dominguez, Gyorgy Panyi, Iván Arenas, Jesús Borrego
Publikováno v:
Frontiers in Pharmacology
Frontiers in Pharmacology, Vol 11 (2021)
Frontiers in Pharmacology, Vol 11 (2021)
Spider venoms include various peptide toxins that modify the ion currents, mainly of excitable insect cells. Consequently, scientific research on spider venoms has revealed a broad range of peptide toxins with different pharmacological properties, ev