Szerző szerinti böngészés "Naseem, Muhammad Umair"
Megjelenítve 1 - 12 (Összesen 12)
Találat egy oldalon
Rendezési lehetőségek
Tétel Szabadon hozzáférhető 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(2023) Naseem, Muhammad Umair; Gurrola-Briones, Georgina; Romero-Imbachi, Margarita R.; Borrego, Jesús; Carcamo-Noriega, Edson; Beltrán-Vidal, José; Zamudio, Fernando Z.; Shakeel, Kashmala; Possani, Lourival Domingos; Panyi, GyörgyTétel Szabadon hozzáférhető Cm28, a scorpion toxin having a unique primary structure, inhibits KV1.2 and KV1.3 with high affinity(2022) Naseem, Muhammad Umair; Carcamo-Noriega, Edson; Beltrán-Vidal, José; Borrego, Jesús; Szántó, Gábor Tibor; Zamudio, Fernando Z.; Delgado-Prudencio, Gustavo; Possani, Lourival Domingos; Panyi, GyörgyTétel Szabadon hozzáférhető Doxorubicin impacts chromatin binding of HMGB1, Histone H1 and retinoic acid receptor(2022) Bosire, Rosevalentine; Fadel, Lina; Mocsár, Gábor; Nánási, Péter Pál ifj.; Sen, Pialy; Sharma, Anshu Kumar; Naseem, Muhammad Umair; Kovács, Attila; Kugel, Jennifer; Kroemer, Guido; Vámosi, György; Szabó, GáborTétel Szabadon hozzáférhető Genomic, functional and structural analyses elucidate evolutionary innovation within the sea anemone 8 toxin family(2023) Ashwood, Lauren M.; Elnahriry, Khaled A.; Stewart, Zachary K.; Shafee, Thomas; Naseem, Muhammad Umair; Szántó, Gábor Tibor; van der Burg, Chloé A.; Smith, Hayden L.; Surm, Joachim M.; Undheim, Eivind A. B.; Madio, Bruno; Hamilton, Brett R.; Guo, Shaodong; Wai, Dorothy C. C.; Coyne, Victoria L.; Phillips, Matthew J.; Dudley, Kevin J.; Hurwood, David A.; Panyi, György; King, Glenn F.; Pavasovic, Ana; Norton, Raymond S.; Prentis, PeterTétel Korlátozottan hozzáférhető Molecular cloning of Anuroctoxin gene into pPICZαA: A yeast expression vectorGembiczki, Júlia; Panyi, György; Naseem, Muhammad Umair; DE--Természettudományi és Technológiai Kar--Biológiai és Ökológiai IntézetAnuroctoxin gene was amplified from source plasmid and cloned into pPICZαA vector using the restriction ligation approach. The recombinant vector was transformed into bacterial strain E. coli using heat shock method. Finally, the correct cloning of gene into desired vector was authenticated by DNA sequencing. In conclusion, I successfully constructed pPICZαA-AnTx vector for the expression of Anuroctoxin in Pichia pastoris expression system.Tétel Szabadon hozzáférhető Of Seven New K Channel Inhibitor Peptides of Centruroides bonito, α-KTx 2.24 Has a Picomolar Affinity for Kv1.2(2023) Shakeel, Kashmala; Olamendi-Portugal, Timoteo; Naseem, Muhammad Umair; Becerril, Baltazar; Zamudio, Fernando Z.; Delgado-Prudencio, Gustavo; Possani, Lourival Domingos; Panyi, GyörgyTétel Szabadon hozzáférhető Optimization of Pichia pastoris Expression System for High-Level Production of Margatoxin(2021) Naseem, Muhammad Umair; Tajti, Gábor; Gáspár, Attila; Szántó, Gábor Tibor; Borrego, Jesús; Panyi, GyörgyTétel Szabadon hozzáférhető Recombinant Expression in Pichia pastoris System of Three Potent Kv1.3 Channel Blockers: Vm24, Anuroctoxin, and Ts6(2022) Borrego, Jesús; Naseem, Muhammad Umair; Sehgal, Al Nasar Ahmed; Panda, Lipsa Rani; Shakeel, Kashmala; Gáspár, Attila; Nagy, Cynthia; Varga, Zoltán; Panyi, GyörgyTétel Szabadon hozzáférhető Structural and functional characterisation of Tst2, a novel TRPV1 inhibitory peptide from the Australian sea anemone Telmatactis stephensoni(2024) Elnahriry, Khaled A.; Wai, Dorothy C. C.; Ashwood, Lauren M.; Naseem, Muhammad Umair; Szántó, Gábor Tibor; Guo, Shaodong; Panyi, György; Prentis, Peter; Norton, Raymond S.Tétel Szabadon hozzáférhető Structure-function relationships in domain peptides: from the sea anemone(2024) Sanches, Karoline; Ashwood, Lauren M.; Olushola-Siedoks, Abisola Ave-Maria; Wai, Dorothy C. C.; Rahman, Arfatur; Shakeel, Kashmala; Naseem, Muhammad Umair; Panyi, György; Prentis, Peter; Norton, Raymond S.Tétel Szabadon hozzáférhető Studying interactions between peptide toxins and voltage-gated K+ channels at the molecular levelNaseem, Muhammad Umair; Panyi, György; Molekuláris Orvostudomány Doktori Iskola; Debreceni Egyetem::Általános Orvostudományi Kar::Biofizikai és Sejtbiológiai IntézetThe voltage-gated Kv1.3 potassium ion channels express in immune cells and are implicated in a range of autoimmune diseases and neuroinflammatory disorders. Selective blocking of Kv1.3 using peptides isolated from scorpion venom holds a great potential in developing immunomodulatory therapies. We discovered and characterized a novel short peptide in the venom of C. margaritatus (Cm28). Cm28 obeys a unique primary structure, consists of 27 amino acid residues and has <40% similarity with other known α-KTxs from scorpions. Cm28 reversibly inhibited Kv1.2 and Kv1.3 channels with Kd values of 0.96 and 1.3 nM, respectively. The biophysical characterization of the block revealed that Cm28 is not a gating modifier, but rather a pore blocker. Cm28 is ~400-fold selective for Kv1.2 and Kv1.3 over Kv1.1 and did not inhibit a variety of other K+, Na+ and H+ channels at 150 nM concentration. Cm28 strongly downregulated the expression of two key early activation markers IL2R and CD40 ligand in stimulated human effector memory T cells. Cm28, due to its unique structure, may serve as a template for the generation of novel peptides targeting Kv1.3. The high affinity and selectivity of peptide toxins for Kv1.3 make them suitable for the development of visualization tools to study the expression and the pharmacokinetics of peptide toxins. We developed a fluorescent analogue of HsTX1[R14A] having an N-terminus Cy5 tag. We showed that Cy5-HsTX1[R14A] retained high affinity and selectivity for Kv1.3 (Kd ~0.9 nM), even against channels formed by Kv1.3-Kv1.5 tandem dimers. Furthermore, flow cytometry demonstrated that Cy5-HsTX1[R14A] can identify Kv1.3-expressing CHO cells. To generate ample amounts of Kv1.3 inhibitor toxins for pharmacology and therapeutic development processes we optimized Pichia pastoris expression system to produce ~36 mg/L of His-tagged margatoxin with >98% purity. This yield, which is 3-fold higher than has been previously reported, was achieved by optimizing the codon, the selection process, and the culturing conditions. Moreover, we showed that the His-tagged MgTx inhibited Kv1.2 and Kv1.3 channels with similar potency to the untagged MgTx, and significantly inhibited the IL2R and CD40 ligand in activated human effector memory T cells, thus, elimination of the tag removal reduces the cost of the production. These results suggest that Pichia expression system is a powerful method to produce the disulfide-rich peptide MgTx, the overexpression of similar peptides could be enhanced noticeably through optimization strategies, making it more cost-effective. In summary, the data presented in the PhD dissertation resulted in a novel ion channel inhibitor peptide (Cm28), a new visualization tool for Kv1.3 (Cy5-HsTX1[R14A]) and an optimized method to produce MgTx in the Pichia expression system.Tétel Szabadon hozzáférhető The Voltage-Gated Hv1 H Channel Is Expressed in Tumor-Infiltrating Myeloid-Derived Suppressor Cells(2023) Cozzolino, Marco; Gyöngyösi, Adrienn; Korpos, Éva; Gogolák, Péter; Naseem, Muhammad Umair; Kállai, Judit; Lányi, Árpád; Panyi, György